HEADER MEMBRANE PROTEIN 18-JUN-20 6ZG4
TITLE STRUCTURE OF M1-STAR-T4L IN COMPLEX WITH HTL0009936 AT 2.35A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M1,ENDOLYSIN,MUSCARINIC
COMPND 3 ACETYLCHOLINE RECEPTOR M1;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE;
COMPND 6 EC: 3.2.1.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: CHRM1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, 7TM, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.RUCKTOOA,R.M.COOKE
REVDAT 3 08-DEC-21 6ZG4 1 JRNL
REVDAT 2 01-DEC-21 6ZG4 1 JRNL
REVDAT 1 06-OCT-21 6ZG4 0
JRNL AUTH A.J.H.BROWN,S.J.BRADLEY,F.H.MARSHALL,G.A.BROWN,K.A.BENNETT,
JRNL AUTH 2 J.BROWN,J.E.CANSFIELD,D.M.CROSS,C.DE GRAAF,B.D.HUDSON,
JRNL AUTH 3 L.DWOMOH,J.M.DIAS,J.C.ERREY,E.HURRELL,J.LIPTROT,G.MATTEDI,
JRNL AUTH 4 C.MOLLOY,P.J.NATHAN,K.OKRASA,G.OSBORNE,J.C.PATEL,
JRNL AUTH 5 M.PICKWORTH,N.ROBERTSON,S.SHAHABI,C.BUNDGAARD,K.PHILLIPS,
JRNL AUTH 6 L.M.BROAD,A.V.GOONAWARDENA,S.R.MORAIRTY,M.BROWNING,F.PERINI,
JRNL AUTH 7 G.R.DAWSON,J.F.W.DEAKIN,R.T.SMITH,P.M.SEXTON,J.WARNECK,
JRNL AUTH 8 M.VINSON,T.TASKER,B.G.TEHAN,B.TEOBALD,A.CHRISTOPOULOS,
JRNL AUTH 9 C.J.LANGMEAD,A.JAZAYERI,R.M.COOKE,P.RUCKTOOA,M.S.CONGREVE,
JRNL AUTH10 M.WEIR,A.B.TOBIN
JRNL TITL FROM STRUCTURE TO CLINIC: DESIGN OF A MUSCARINIC M1 RECEPTOR
JRNL TITL 2 AGONIST WITH POTENTIAL TO TREATMENT OF ALZHEIMER'S DISEASE.
JRNL REF CELL V. 184 5886 2021
JRNL REFN ISSN 1097-4172
JRNL PMID 34822784
JRNL DOI 10.1016/J.CELL.2021.11.001
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.0
REMARK 3 NUMBER OF REFLECTIONS : 20579
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.45
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 10.92
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2283
REMARK 3 BIN FREE R VALUE : 0.2842
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 18
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 271
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.26560
REMARK 3 B22 (A**2) : 8.65800
REMARK 3 B33 (A**2) : -5.39230
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) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.464
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.258
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.463
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.261
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 : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3894 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5220 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1432 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 609 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3894 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 489 ; 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 : 4518 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.47
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.66
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|20 - A|219 A|354 - A|439 }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0442 18.0776 -5.9288
REMARK 3 T TENSOR
REMARK 3 T11: -0.12 T22: 0.0277
REMARK 3 T33: -0.1697 T12: 0.0115
REMARK 3 T13: -0.019 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 1.6493 L22: 0.5913
REMARK 3 L33: 2.3764 L12: 0.0767
REMARK 3 L13: -0.1055 L23: 0.2744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: -0.0252 S13: -0.0005
REMARK 3 S21: -0.0252 S22: 0.0201 S23: 0.0823
REMARK 3 S31: -0.0005 S32: 0.0823 S33: 0.0102
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1002 - A|1161 }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3869 -3.3031 -41.5044
REMARK 3 T TENSOR
REMARK 3 T11: -0.0839 T22: -0.093
REMARK 3 T33: -0.3298 T12: -0.0416
REMARK 3 T13: 0.0162 T23: -0.1041
REMARK 3 L TENSOR
REMARK 3 L11: 5.5623 L22: 2.9849
REMARK 3 L33: 3.2862 L12: -1.1915
REMARK 3 L13: -0.7673 L23: 0.4394
REMARK 3 S TENSOR
REMARK 3 S11: -0.3797 S12: 0.053 S13: 0.2568
REMARK 3 S21: 0.053 S22: 0.0597 S23: -0.0163
REMARK 3 S31: 0.2568 S32: -0.0163 S33: 0.3201
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1292109488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4-7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03319
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.353
REMARK 200 RESOLUTION RANGE LOW (A) : 49.982
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2Y00
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAHEPES PH 7.4-7.8, 0.1M DI
REMARK 280 -AMMONIUM HYDROGENPHOSPHATE, 30-38% PEG300, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.41500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.41500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.72500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 HIS A 440
REMARK 465 HIS A 441
REMARK 465 HIS A 442
REMARK 465 HIS A 443
REMARK 465 HIS A 444
REMARK 465 HIS A 445
REMARK 465 HIS A 446
REMARK 465 HIS A 447
REMARK 465 HIS A 448
REMARK 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 PHE A 77 -72.64 -93.74
REMARK 500 ARG A 134 34.78 -80.41
REMARK 500 PHE A 197 -73.08 -124.55
REMARK 500 PRO A1037 47.01 -84.26
REMARK 500 ARG A1125 74.86 -100.63
REMARK 500 THR A1142 68.66 -119.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue QK8 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1216
DBREF 6ZG4 A 27 219 UNP P11229 ACM1_HUMAN 27 219
DBREF 6ZG4 A 1002 1161 UNP P00720 ENLYS_BPT4 2 161
DBREF 6ZG4 A 354 438 UNP P11229 ACM1_HUMAN 354 438
SEQADV 6ZG4 MET A 20 UNP P11229 INITIATING METHIONINE
SEQADV 6ZG4 GLU A 21 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 THR A 22 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 VAL A 23 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 GLU A 24 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 MET A 25 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 VAL A 26 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 ALA A 27 UNP P11229 PHE 27 ENGINEERED MUTATION
SEQADV 6ZG4 ALA A 29 UNP P11229 GLY 29 CONFLICT
SEQADV 6ZG4 THR A 30 UNP P11229 ILE 30 CONFLICT
SEQADV 6ZG4 VAL A 31 UNP P11229 THR 31 CONFLICT
SEQADV 6ZG4 ALA A 32 UNP P11229 THR 32 ENGINEERED MUTATION
SEQADV 6ZG4 ILE A 44 UNP P11229 LEU 44 ENGINEERED MUTATION
SEQADV 6ZG4 LEU A 46 UNP P11229 VAL 46 ENGINEERED MUTATION
SEQADV 6ZG4 MET A 47 UNP P11229 LEU 47 CONFLICT
SEQADV 6ZG4 LEU A 48 UNP P11229 ILE 48 CONFLICT
SEQADV 6ZG4 ILE A 50 UNP P11229 PHE 50 CONFLICT
SEQADV 6ZG4 ARG A 54 UNP P11229 THR 54 CONFLICT
SEQADV 6ZG4 GLN A 55 UNP P11229 GLU 55 CONFLICT
SEQADV 6ZG4 GLN A 57 UNP P11229 LYS 57 CONFLICT
SEQADV 6ZG4 ALA A 64 UNP P11229 LEU 64 ENGINEERED MUTATION
SEQADV 6ZG4 PHE A 65 UNP P11229 LEU 65 CONFLICT
SEQADV 6ZG4 ALA A 76 UNP P11229 THR 76 ENGINEERED MUTATION
SEQADV 6ZG4 VAL A 84 UNP P11229 THR 84 ENGINEERED MUTATION
SEQADV 6ZG4 ILE A 86 UNP P11229 LEU 86 CONFLICT
SEQADV 6ZG4 ILE A 87 UNP P11229 LEU 87 CONFLICT
SEQADV 6ZG4 ALA A 95 UNP P11229 THR 95 ENGINEERED MUTATION
SEQADV 6ZG4 ALA A 101 UNP P11229 TRP 101 ENGINEERED MUTATION
SEQADV 6ZG4 ALA A 112 UNP P11229 SER 112 ENGINEERED MUTATION
SEQADV 6ZG4 LEU A 143 UNP P11229 ALA 143 ENGINEERED MUTATION
SEQADV 6ZG4 THR A 196 UNP P11229 ALA 196 ENGINEERED MUTATION
SEQADV 6ZG4 GLY A 1012 UNP P00720 ARG 12 CONFLICT
SEQADV 6ZG4 THR A 1054 UNP P00720 CYS 54 CONFLICT
SEQADV 6ZG4 ALA A 1097 UNP P00720 CYS 97 CONFLICT
SEQADV 6ZG4 ARG A 1137 UNP P00720 ILE 137 CONFLICT
SEQADV 6ZG4 ALA A 362 UNP P11229 LYS 362 ENGINEERED MUTATION
SEQADV 6ZG4 LEU A 364 UNP P11229 ALA 364 ENGINEERED MUTATION
SEQADV 6ZG4 ALA A 411 UNP P11229 SER 411 ENGINEERED MUTATION
SEQADV 6ZG4 ALA A 435 UNP P11229 CYS 435 CONFLICT
SEQADV 6ZG4 HIS A 439 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 440 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 441 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 442 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 443 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 444 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 445 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 446 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 447 UNP P11229 EXPRESSION TAG
SEQADV 6ZG4 HIS A 448 UNP P11229 EXPRESSION TAG
SEQRES 1 A 455 MET GLU THR VAL GLU MET VAL ALA ILE ALA THR VAL ALA
SEQRES 2 A 455 GLY LEU LEU SER LEU ALA THR VAL THR GLY ASN ILE LEU
SEQRES 3 A 455 LEU MET LEU SER ILE LYS VAL ASN ARG GLN LEU GLN THR
SEQRES 4 A 455 VAL ASN ASN TYR PHE ALA PHE SER LEU ALA CYS ALA ASP
SEQRES 5 A 455 LEU ILE ILE GLY ALA PHE SER MET ASN LEU TYR THR VAL
SEQRES 6 A 455 TYR ILE ILE MET GLY HIS TRP ALA LEU GLY ALA LEU ALA
SEQRES 7 A 455 CYS ASP LEU ALA LEU ALA LEU ASP TYR VAL ALA SER ASN
SEQRES 8 A 455 ALA ALA VAL MET ASN LEU LEU LEU ILE SER PHE ASP ARG
SEQRES 9 A 455 TYR PHE SER VAL THR ARG PRO LEU SER TYR ARG ALA LYS
SEQRES 10 A 455 ARG THR PRO ARG ARG ALA LEU LEU MET ILE GLY LEU ALA
SEQRES 11 A 455 TRP LEU VAL SER PHE VAL LEU TRP ALA PRO ALA ILE LEU
SEQRES 12 A 455 PHE TRP GLN TYR LEU VAL GLY GLU ARG THR VAL LEU ALA
SEQRES 13 A 455 GLY GLN CYS TYR ILE GLN PHE LEU SER GLN PRO ILE ILE
SEQRES 14 A 455 THR PHE GLY THR ALA MET ALA THR PHE TYR LEU PRO VAL
SEQRES 15 A 455 THR VAL MET CYS THR LEU TYR TRP ARG ILE TYR ARG GLU
SEQRES 16 A 455 THR GLU ASN ARG ALA ASN ILE PHE GLU MET LEU ARG ILE
SEQRES 17 A 455 ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU
SEQRES 18 A 455 GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS
SEQRES 19 A 455 SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS
SEQRES 20 A 455 ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP
SEQRES 21 A 455 GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA
SEQRES 22 A 455 VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL
SEQRES 23 A 455 TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE
SEQRES 24 A 455 ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY
SEQRES 25 A 455 PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP
SEQRES 26 A 455 ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR
SEQRES 27 A 455 ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR
SEQRES 28 A 455 PHE ARG THR GLY THR TRP ASP ALA TYR THR PHE SER LEU
SEQRES 29 A 455 VAL LYS GLU LYS ALA ALA LEU ARG THR LEU SER ALA ILE
SEQRES 30 A 455 LEU LEU ALA PHE ILE LEU THR TRP THR PRO TYR ASN ILE
SEQRES 31 A 455 MET VAL LEU VAL SER THR PHE CYS LYS ASP CYS VAL PRO
SEQRES 32 A 455 GLU THR LEU TRP GLU LEU GLY TYR TRP LEU CYS TYR VAL
SEQRES 33 A 455 ASN ALA THR ILE ASN PRO MET CYS TYR ALA LEU CYS ASN
SEQRES 34 A 455 LYS ALA PHE ARG ASP THR PHE ARG LEU LEU LEU LEU ALA
SEQRES 35 A 455 ARG TRP ASP HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET QK8 A1201 26
HET OLA A1202 20
HET OLA A1203 20
HET OLA A1204 20
HET OLA A1205 20
HET OLA A1206 20
HET OLA A1207 20
HET PGE A1208 10
HET PO4 A1209 5
HET PO4 A1210 5
HET OLA A1211 20
HET OLA A1212 20
HET OLA A1213 20
HET OLA A1214 20
HET OLA A1215 20
HET PO4 A1216 5
HETNAM QK8 ETHYL (4~{S})-4-[4-[(1-METHYLCYCLOBUTYL)
HETNAM 2 QK8 CARBAMOYL]PIPERIDIN-1-YL]AZEPANE-1-CARBOXYLATE
HETNAM OLA OLEIC ACID
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PO4 PHOSPHATE ION
FORMUL 2 QK8 C20 H35 N3 O3
FORMUL 3 OLA 11(C18 H34 O2)
FORMUL 9 PGE C6 H14 O4
FORMUL 10 PO4 3(O4 P 3-)
FORMUL 18 HOH *72(H2 O)
HELIX 1 AA1 GLU A 21 ASN A 53 1 33
HELIX 2 AA2 ARG A 54 GLN A 57 5 4
HELIX 3 AA3 THR A 58 PHE A 77 1 20
HELIX 4 AA4 PHE A 77 GLY A 89 1 13
HELIX 5 AA5 GLY A 94 ARG A 129 1 36
HELIX 6 AA6 ARG A 129 ARG A 134 1 6
HELIX 7 AA7 THR A 138 GLY A 169 1 32
HELIX 8 AA8 GLN A 181 SER A 184 5 4
HELIX 9 AA9 GLN A 185 PHE A 197 1 13
HELIX 10 AB1 PHE A 197 GLU A 1011 1 33
HELIX 11 AB2 SER A 1038 GLY A 1051 1 14
HELIX 12 AB3 THR A 1059 ASN A 1081 1 23
HELIX 13 AB4 LEU A 1084 LEU A 1091 1 8
HELIX 14 AB5 ASP A 1092 GLY A 1107 1 16
HELIX 15 AB6 GLY A 1107 GLY A 1113 1 7
HELIX 16 AB7 PHE A 1114 GLN A 1123 1 10
HELIX 17 AB8 ARG A 1125 LYS A 1135 1 11
HELIX 18 AB9 SER A 1136 THR A 1142 1 7
HELIX 19 AC1 THR A 1142 GLY A 1156 1 15
HELIX 20 AC2 LYS A 361 CYS A 391 1 31
HELIX 21 AC3 PRO A 396 ASN A 422 1 27
HELIX 22 AC4 ASN A 422 ASP A 438 1 17
SHEET 1 AA1 3 ARG A1014 LYS A1019 0
SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018
SHEET 3 AA1 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025
SSBOND 1 CYS A 98 CYS A 178 1555 1555 2.04
SSBOND 2 CYS A 391 CYS A 394 1555 1555 2.03
SITE 1 AC1 15 LEU A 81 TYR A 82 TYR A 85 ALA A 101
SITE 2 AC1 15 LEU A 102 ASP A 105 TYR A 106 SER A 109
SITE 3 AC1 15 ASN A 110 CYS A 178 TRP A 378 TYR A 404
SITE 4 AC1 15 TYR A 408 HOH A1327 HOH A1347
SITE 1 AC2 8 LEU A 104 VAL A 107 LEU A 143 GLY A 147
SITE 2 AC2 8 TRP A 150 PHE A 154 CYS A 394 OLA A1203
SITE 1 AC3 2 TRP A 150 OLA A1202
SITE 1 AC4 3 GLU A 401 TRP A 405 OLA A1211
SITE 1 AC5 4 MET A 114 LEU A 118 ARG A 141 MET A 145
SITE 1 AC6 4 ALA A 76 PHE A 77 LEU A 81 LEU A 93
SITE 1 AC7 6 GLU A1011 ILE A1029 GLY A1030 VAL A1103
SITE 2 AC7 6 PHE A1104 GLN A1105
SITE 1 AC8 2 TYR A 85 GLU A 401
SITE 1 AC9 5 PHE A1114 THR A1115 ASN A1116 SER A1117
SITE 2 AC9 5 ASN A1132
SITE 1 AD1 4 THR A1142 PRO A1143 ASN A1144 ARG A1145
SITE 1 AD2 1 OLA A1204
SITE 1 AD3 1 GLU A 24
SITE 1 AD4 8 LEU A 93 ALA A 95 LEU A 96 ALA A 175
SITE 2 AD4 8 CYS A 205 TYR A 208 TRP A 209 TYR A 212
SITE 1 AD5 5 ALA A 38 TYR A 166 LEU A 167 LEU A 420
SITE 2 AD5 5 HOH A1332
SITE 1 AD6 4 LEU A 156 PHE A 163 ILE A 413 LEU A 420
SITE 1 AD7 5 ARG A 123 ARG A 134 LYS A1065 HOH A1326
SITE 2 AD7 5 HOH A1351
CRYST1 62.470 65.450 154.830 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016008 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006459 0.00000
ATOM 1 N MET A 20 -16.166 37.188 18.153 1.00 70.03 N
ANISOU 1 N MET A 20 8948 9920 7741 -806 -277 -1926 N
ATOM 2 CA MET A 20 -15.453 37.516 16.917 1.00 69.72 C
ANISOU 2 CA MET A 20 8950 9744 7795 -905 -278 -1843 C
ATOM 3 C MET A 20 -15.398 39.030 16.672 1.00 72.62 C
ANISOU 3 C MET A 20 9476 9856 8260 -1007 -253 -1960 C
ATOM 4 O MET A 20 -16.406 39.725 16.832 1.00 72.08 O
ANISOU 4 O MET A 20 9520 9619 8247 -914 -224 -2032 O
ATOM 5 CB MET A 20 -16.072 36.783 15.713 1.00 72.08 C
ANISOU 5 CB MET A 20 9250 9973 8164 -783 -267 -1652 C
ATOM 6 CG MET A 20 -15.152 36.730 14.499 1.00 75.71 C
ANISOU 6 CG MET A 20 9704 10384 8678 -884 -274 -1541 C
ATOM 7 SD MET A 20 -15.719 35.627 13.180 1.00 79.68 S
ANISOU 7 SD MET A 20 10173 10874 9227 -750 -269 -1325 S
ATOM 8 CE MET A 20 -16.819 36.656 12.369 1.00 76.22 C
ANISOU 8 CE MET A 20 9899 10146 8916 -681 -235 -1310 C
ATOM 9 N GLU A 21 -14.213 39.524 16.271 1.00 68.44 N
ANISOU 9 N GLU A 21 8955 9299 7750 -1197 -263 -1975 N
ATOM 10 CA GLU A 21 -13.956 40.936 15.986 1.00 68.02 C
ANISOU 10 CA GLU A 21 9059 8997 7788 -1335 -238 -2073 C
ATOM 11 C GLU A 21 -14.622 41.392 14.692 1.00 70.73 C
ANISOU 11 C GLU A 21 9541 9065 8268 -1265 -208 -1949 C
ATOM 12 O GLU A 21 -14.698 40.623 13.732 1.00 69.93 O
ANISOU 12 O GLU A 21 9386 9000 8185 -1203 -212 -1774 O
ATOM 13 CB GLU A 21 -12.447 41.217 15.941 1.00 69.51 C
ANISOU 13 CB GLU A 21 9192 9279 7940 -1579 -257 -2120 C
ATOM 14 CG GLU A 21 -11.829 41.395 17.319 1.00 81.56 C
ANISOU 14 CG GLU A 21 10645 10992 9351 -1688 -281 -2312 C
ATOM 15 CD GLU A 21 -10.321 41.558 17.364 1.00105.97 C
ANISOU 15 CD GLU A 21 13646 14233 12386 -1930 -305 -2364 C
ATOM 16 OE1 GLU A 21 -9.746 42.137 16.413 1.00103.50 O
ANISOU 16 OE1 GLU A 21 13404 13768 12154 -2080 -285 -2326 O
ATOM 17 OE2 GLU A 21 -9.715 41.120 18.368 1.00100.44 O
ANISOU 17 OE2 GLU A 21 12798 13813 11551 -1972 -345 -2444 O
ATOM 18 N THR A 22 -15.083 42.662 14.672 1.00 66.33 N
ANISOU 18 N THR A 22 9168 8232 7802 -1275 -179 -2044 N
ATOM 19 CA THR A 22 -15.763 43.322 13.547 1.00 65.29 C
ANISOU 19 CA THR A 22 9199 7808 7801 -1201 -152 -1943 C
ATOM 20 C THR A 22 -14.906 43.319 12.255 1.00 66.82 C
ANISOU 20 C THR A 22 9401 7951 8037 -1339 -150 -1788 C
ATOM 21 O THR A 22 -15.466 43.220 11.161 1.00 65.91 O
ANISOU 21 O THR A 22 9335 7720 7986 -1235 -140 -1631 O
ATOM 22 CB THR A 22 -16.260 44.727 13.958 1.00 72.45 C
ANISOU 22 CB THR A 22 10308 8433 8787 -1201 -123 -2100 C
ATOM 23 OG1 THR A 22 -16.920 45.346 12.854 1.00 71.82 O
ANISOU 23 OG1 THR A 22 10388 8071 8828 -1111 -102 -1986 O
ATOM 24 CG2 THR A 22 -15.148 45.636 14.501 1.00 71.38 C
ANISOU 24 CG2 THR A 22 10234 8246 8643 -1458 -119 -2263 C
ATOM 25 N VAL A 23 -13.562 43.389 12.397 1.00 61.96 N
ANISOU 25 N VAL A 23 8722 7448 7374 -1570 -159 -1835 N
ATOM 26 CA VAL A 23 -12.585 43.342 11.298 1.00 61.17 C
ANISOU 26 CA VAL A 23 8598 7354 7289 -1729 -154 -1709 C
ATOM 27 C VAL A 23 -12.685 41.961 10.604 1.00 63.72 C
ANISOU 27 C VAL A 23 8765 7876 7568 -1603 -173 -1531 C
ATOM 28 O VAL A 23 -12.688 41.887 9.371 1.00 63.29 O
ANISOU 28 O VAL A 23 8744 7739 7563 -1596 -159 -1377 O
ATOM 29 CB VAL A 23 -11.143 43.629 11.810 1.00 65.08 C
ANISOU 29 CB VAL A 23 9019 7988 7719 -1999 -163 -1825 C
ATOM 30 CG1 VAL A 23 -10.135 43.664 10.662 1.00 64.79 C
ANISOU 30 CG1 VAL A 23 8956 7966 7696 -2175 -150 -1702 C
ATOM 31 CG2 VAL A 23 -11.083 44.927 12.617 1.00 64.97 C
ANISOU 31 CG2 VAL A 23 9159 7786 7742 -2128 -146 -2026 C
ATOM 32 N GLU A 24 -12.803 40.883 11.416 1.00 58.68 N
ANISOU 32 N GLU A 24 7968 7492 6836 -1501 -202 -1555 N
ATOM 33 CA GLU A 24 -12.938 39.494 10.968 1.00 57.49 C
ANISOU 33 CA GLU A 24 7675 7531 6639 -1372 -221 -1411 C
ATOM 34 C GLU A 24 -14.298 39.243 10.323 1.00 58.13 C
ANISOU 34 C GLU A 24 7825 7478 6783 -1163 -207 -1303 C
ATOM 35 O GLU A 24 -14.361 38.512 9.339 1.00 57.74 O
ANISOU 35 O GLU A 24 7729 7468 6743 -1104 -208 -1154 O
ATOM 36 CB GLU A 24 -12.700 38.510 12.130 1.00 59.12 C
ANISOU 36 CB GLU A 24 7720 8017 6727 -1324 -254 -1472 C
ATOM 37 CG GLU A 24 -11.273 38.512 12.661 1.00 72.00 C
ANISOU 37 CG GLU A 24 9237 9848 8272 -1511 -279 -1554 C
ATOM 38 CD GLU A 24 -11.001 37.551 13.802 1.00 95.31 C
ANISOU 38 CD GLU A 24 12029 13086 11098 -1450 -318 -1594 C
ATOM 39 OE1 GLU A 24 -10.667 38.029 14.911 1.00 86.83 O
ANISOU 39 OE1 GLU A 24 10935 12099 9957 -1532 -334 -1749 O
ATOM 40 OE2 GLU A 24 -11.115 36.321 13.589 1.00 92.53 O
ANISOU 40 OE2 GLU A 24 11578 12870 10709 -1321 -334 -1471 O
ATOM 41 N MET A 25 -15.376 39.864 10.859 1.00 52.53 N
ANISOU 41 N MET A 25 7222 6622 6114 -1051 -194 -1385 N
ATOM 42 CA MET A 25 -16.753 39.754 10.352 1.00 51.56 C
ANISOU 42 CA MET A 25 7160 6382 6048 -846 -183 -1306 C
ATOM 43 C MET A 25 -16.876 40.226 8.891 1.00 51.76 C
ANISOU 43 C MET A 25 7292 6213 6163 -848 -168 -1167 C
ATOM 44 O MET A 25 -17.399 39.484 8.065 1.00 51.08 O
ANISOU 44 O MET A 25 7160 6167 6081 -735 -172 -1030 O
ATOM 45 CB MET A 25 -17.756 40.507 11.255 1.00 54.44 C
ANISOU 45 CB MET A 25 7620 6628 6437 -741 -169 -1446 C
ATOM 46 CG MET A 25 -17.803 40.005 12.691 1.00 58.80 C
ANISOU 46 CG MET A 25 8067 7388 6888 -717 -180 -1574 C
ATOM 47 SD MET A 25 -19.470 39.880 13.386 1.00 63.59 S
ANISOU 47 SD MET A 25 8681 7995 7487 -478 -164 -1629 S
ATOM 48 CE MET A 25 -19.128 38.965 14.865 1.00 60.36 C
ANISOU 48 CE MET A 25 8112 7895 6929 -502 -182 -1722 C
ATOM 49 N VAL A 26 -16.359 41.436 8.578 1.00 45.82 N
ANISOU 49 N VAL A 26 6682 5255 5473 -989 -150 -1201 N
ATOM 50 CA VAL A 26 -16.361 42.060 7.246 1.00 44.33 C
ANISOU 50 CA VAL A 26 6618 4863 5363 -1020 -133 -1070 C
ATOM 51 C VAL A 26 -15.498 41.264 6.244 1.00 45.09 C
ANISOU 51 C VAL A 26 6603 5110 5419 -1113 -137 -928 C
ATOM 52 O VAL A 26 -15.924 41.076 5.104 1.00 44.63 O
ANISOU 52 O VAL A 26 6569 5000 5389 -1033 -134 -779 O
ATOM 53 CB VAL A 26 -15.957 43.564 7.324 1.00 48.18 C
ANISOU 53 CB VAL A 26 7296 5089 5922 -1170 -109 -1155 C
ATOM 54 CG1 VAL A 26 -15.924 44.221 5.945 1.00 47.79 C
ANISOU 54 CG1 VAL A 26 7385 4826 5945 -1214 -89 -1001 C
ATOM 55 CG2 VAL A 26 -16.891 44.335 8.253 1.00 48.02 C
ANISOU 55 CG2 VAL A 26 7394 4906 5946 -1047 -101 -1300 C
ATOM 56 N ALA A 27 -14.307 40.788 6.679 1.00 39.33 N
ANISOU 56 N ALA A 27 5744 4583 4617 -1270 -147 -979 N
ATOM 57 CA ALA A 27 -13.363 40.019 5.856 1.00 38.08 C
ANISOU 57 CA ALA A 27 5462 4597 4410 -1360 -150 -870 C
ATOM 58 C ALA A 27 -13.913 38.648 5.434 1.00 40.43 C
ANISOU 58 C ALA A 27 5638 5056 4670 -1183 -167 -762 C
ATOM 59 O ALA A 27 -13.832 38.305 4.248 1.00 40.74 O
ANISOU 59 O ALA A 27 5663 5102 4715 -1174 -159 -628 O
ATOM 60 CB ALA A 27 -12.030 39.867 6.575 1.00 38.69 C
ANISOU 60 CB ALA A 27 5418 4869 4412 -1543 -160 -971 C
ATOM 61 N ILE A 28 -14.485 37.874 6.393 1.00 34.27 N
ANISOU 61 N ILE A 28 4774 4401 3845 -1050 -188 -822 N
ATOM 62 CA ILE A 28 -15.095 36.571 6.113 1.00 32.33 C
ANISOU 62 CA ILE A 28 4427 4290 3566 -889 -202 -732 C
ATOM 63 C ILE A 28 -16.281 36.807 5.176 1.00 34.28 C
ANISOU 63 C ILE A 28 4772 4373 3880 -755 -190 -634 C
ATOM 64 O ILE A 28 -16.382 36.116 4.169 1.00 34.81 O
ANISOU 64 O ILE A 28 4794 4493 3941 -706 -191 -515 O
ATOM 65 CB ILE A 28 -15.498 35.797 7.408 1.00 34.82 C
ANISOU 65 CB ILE A 28 4652 4760 3818 -792 -221 -812 C
ATOM 66 CG1 ILE A 28 -14.260 35.367 8.204 1.00 35.09 C
ANISOU 66 CG1 ILE A 28 4566 4999 3769 -906 -242 -881 C
ATOM 67 CG2 ILE A 28 -16.377 34.573 7.091 1.00 34.95 C
ANISOU 67 CG2 ILE A 28 4600 4863 3816 -625 -228 -717 C
ATOM 68 CD1 ILE A 28 -14.506 35.129 9.711 1.00 41.39 C
ANISOU 68 CD1 ILE A 28 5316 5910 4501 -859 -259 -998 C
ATOM 69 N ALA A 29 -17.139 37.808 5.479 1.00 28.78 N
ANISOU 69 N ALA A 29 4207 3483 3243 -693 -181 -689 N
ATOM 70 CA ALA A 29 -18.309 38.147 4.665 1.00 28.30 C
ANISOU 70 CA ALA A 29 4240 3272 3243 -549 -175 -603 C
ATOM 71 C ALA A 29 -17.949 38.439 3.203 1.00 30.67 C
ANISOU 71 C ALA A 29 4596 3486 3572 -611 -166 -462 C
ATOM 72 O ALA A 29 -18.606 37.897 2.320 1.00 29.76 O
ANISOU 72 O ALA A 29 4454 3399 3454 -500 -173 -351 O
ATOM 73 CB ALA A 29 -19.061 39.323 5.266 1.00 29.07 C
ANISOU 73 CB ALA A 29 4478 3166 3401 -485 -165 -698 C
ATOM 74 N THR A 30 -16.896 39.257 2.956 1.00 26.29 N
ANISOU 74 N THR A 30 4110 2845 3035 -797 -150 -467 N
ATOM 75 CA THR A 30 -16.418 39.635 1.615 1.00 25.66 C
ANISOU 75 CA THR A 30 4089 2689 2972 -889 -134 -334 C
ATOM 76 C THR A 30 -15.894 38.424 0.845 1.00 29.96 C
ANISOU 76 C THR A 30 4481 3453 3449 -904 -139 -241 C
ATOM 77 O THR A 30 -16.378 38.162 -0.255 1.00 29.51 O
ANISOU 77 O THR A 30 4435 3385 3392 -827 -139 -117 O
ATOM 78 CB THR A 30 -15.398 40.784 1.691 1.00 30.35 C
ANISOU 78 CB THR A 30 4786 3151 3592 -1109 -110 -378 C
ATOM 79 OG1 THR A 30 -15.942 41.843 2.476 1.00 28.22 O
ANISOU 79 OG1 THR A 30 4663 2672 3387 -1081 -106 -484 O
ATOM 80 CG2 THR A 30 -15.026 41.323 0.323 1.00 29.18 C
ANISOU 80 CG2 THR A 30 4729 2895 3464 -1204 -88 -231 C
ATOM 81 N VAL A 31 -14.938 37.671 1.436 1.00 26.92 N
ANISOU 81 N VAL A 31 3954 3272 3001 -989 -145 -306 N
ATOM 82 CA VAL A 31 -14.346 36.471 0.829 1.00 26.18 C
ANISOU 82 CA VAL A 31 3710 3393 2842 -994 -150 -240 C
ATOM 83 C VAL A 31 -15.409 35.385 0.577 1.00 29.17 C
ANISOU 83 C VAL A 31 4032 3844 3209 -797 -167 -187 C
ATOM 84 O VAL A 31 -15.522 34.923 -0.559 1.00 29.57 O
ANISOU 84 O VAL A 31 4057 3934 3244 -764 -163 -81 O
ATOM 85 CB VAL A 31 -13.114 35.943 1.610 1.00 29.55 C
ANISOU 85 CB VAL A 31 4001 4021 3206 -1108 -157 -327 C
ATOM 86 CG1 VAL A 31 -12.526 34.702 0.945 1.00 28.83 C
ANISOU 86 CG1 VAL A 31 3763 4139 3052 -1087 -160 -259 C
ATOM 87 CG2 VAL A 31 -12.043 37.026 1.722 1.00 29.57 C
ANISOU 87 CG2 VAL A 31 4052 3968 3215 -1328 -137 -378 C
ATOM 88 N ALA A 32 -16.203 35.012 1.605 1.00 24.69 N
ANISOU 88 N ALA A 32 3444 3295 2641 -679 -184 -261 N
ATOM 89 CA ALA A 32 -17.257 34.002 1.469 1.00 24.34 C
ANISOU 89 CA ALA A 32 3346 3318 2584 -512 -197 -219 C
ATOM 90 C ALA A 32 -18.347 34.469 0.502 1.00 28.90 C
ANISOU 90 C ALA A 32 4014 3760 3206 -414 -194 -132 C
ATOM 91 O ALA A 32 -18.858 33.659 -0.282 1.00 28.65 O
ANISOU 91 O ALA A 32 3932 3799 3154 -333 -201 -55 O
ATOM 92 CB ALA A 32 -17.850 33.657 2.819 1.00 24.92 C
ANISOU 92 CB ALA A 32 3386 3440 2643 -429 -208 -317 C
ATOM 93 N GLY A 33 -18.625 35.777 0.520 1.00 25.41 N
ANISOU 93 N GLY A 33 3708 3127 2821 -427 -187 -144 N
ATOM 94 CA GLY A 33 -19.591 36.433 -0.360 1.00 25.00 C
ANISOU 94 CA GLY A 33 3760 2926 2813 -328 -188 -57 C
ATOM 95 C GLY A 33 -19.169 36.401 -1.814 1.00 27.71 C
ANISOU 95 C GLY A 33 4115 3276 3140 -383 -182 78 C
ATOM 96 O GLY A 33 -19.992 36.097 -2.677 1.00 27.56 O
ANISOU 96 O GLY A 33 4088 3273 3110 -272 -194 165 O
ATOM 97 N LEU A 34 -17.878 36.687 -2.097 1.00 23.61 N
ANISOU 97 N LEU A 34 3602 2764 2605 -563 -162 92 N
ATOM 98 CA LEU A 34 -17.331 36.653 -3.459 1.00 23.34 C
ANISOU 98 CA LEU A 34 3568 2760 2540 -639 -149 216 C
ATOM 99 C LEU A 34 -17.272 35.214 -3.965 1.00 25.35 C
ANISOU 99 C LEU A 34 3672 3230 2729 -588 -157 247 C
ATOM 100 O LEU A 34 -17.571 34.970 -5.138 1.00 24.24 O
ANISOU 100 O LEU A 34 3530 3119 2563 -548 -157 351 O
ATOM 101 CB LEU A 34 -15.956 37.330 -3.559 1.00 23.53 C
ANISOU 101 CB LEU A 34 3621 2762 2557 -857 -120 211 C
ATOM 102 CG LEU A 34 -15.944 38.865 -3.495 1.00 28.16 C
ANISOU 102 CG LEU A 34 4392 3099 3208 -941 -104 219 C
ATOM 103 CD1 LEU A 34 -14.635 39.377 -2.914 1.00 27.85 C
ANISOU 103 CD1 LEU A 34 4348 3068 3164 -1163 -80 137 C
ATOM 104 CD2 LEU A 34 -16.182 39.483 -4.866 1.00 31.25 C
ANISOU 104 CD2 LEU A 34 4894 3377 3603 -946 -92 380 C
ATOM 105 N LEU A 35 -16.955 34.255 -3.060 1.00 20.31 N
ANISOU 105 N LEU A 35 2916 2737 2064 -579 -165 155 N
ATOM 106 CA LEU A 35 -16.930 32.822 -3.383 1.00 18.91 C
ANISOU 106 CA LEU A 35 2609 2744 1834 -519 -172 169 C
ATOM 107 C LEU A 35 -18.337 32.376 -3.806 1.00 21.68 C
ANISOU 107 C LEU A 35 2967 3081 2191 -358 -190 213 C
ATOM 108 O LEU A 35 -18.475 31.736 -4.840 1.00 22.77 O
ANISOU 108 O LEU A 35 3062 3299 2292 -329 -190 281 O
ATOM 109 CB LEU A 35 -16.398 31.986 -2.196 1.00 18.51 C
ANISOU 109 CB LEU A 35 2455 2820 1757 -526 -181 68 C
ATOM 110 CG LEU A 35 -16.249 30.468 -2.436 1.00 22.35 C
ANISOU 110 CG LEU A 35 2820 3477 2192 -465 -187 78 C
ATOM 111 CD1 LEU A 35 -15.186 30.146 -3.497 1.00 21.72 C
ANISOU 111 CD1 LEU A 35 2681 3503 2068 -547 -169 129 C
ATOM 112 CD2 LEU A 35 -15.990 29.730 -1.139 1.00 23.08 C
ANISOU 112 CD2 LEU A 35 2841 3664 2265 -441 -201 -8 C
ATOM 113 N SER A 36 -19.373 32.776 -3.045 1.00 17.06 N
ANISOU 113 N SER A 36 2433 2404 1647 -260 -203 169 N
ATOM 114 CA SER A 36 -20.777 32.506 -3.341 1.00 16.35 C
ANISOU 114 CA SER A 36 2343 2308 1562 -110 -220 199 C
ATOM 115 C SER A 36 -21.139 33.089 -4.709 1.00 22.47 C
ANISOU 115 C SER A 36 3186 3016 2337 -85 -224 315 C
ATOM 116 O SER A 36 -21.694 32.383 -5.543 1.00 21.17 O
ANISOU 116 O SER A 36 2968 2940 2135 -20 -235 369 O
ATOM 117 CB SER A 36 -21.670 33.110 -2.265 1.00 17.71 C
ANISOU 117 CB SER A 36 2564 2388 1777 -23 -227 125 C
ATOM 118 OG SER A 36 -23.031 32.872 -2.581 1.00 23.31 O
ANISOU 118 OG SER A 36 3259 3113 2486 121 -243 153 O
ATOM 119 N LEU A 37 -20.772 34.362 -4.955 1.00 22.37 N
ANISOU 119 N LEU A 37 3293 2849 2359 -146 -214 355 N
ATOM 120 CA LEU A 37 -21.015 35.050 -6.227 1.00 23.04 C
ANISOU 120 CA LEU A 37 3462 2854 2439 -131 -217 482 C
ATOM 121 C LEU A 37 -20.386 34.295 -7.413 1.00 26.16 C
ANISOU 121 C LEU A 37 3783 3394 2762 -199 -209 561 C
ATOM 122 O LEU A 37 -21.051 34.123 -8.430 1.00 26.10 O
ANISOU 122 O LEU A 37 3773 3425 2720 -122 -224 647 O
ATOM 123 CB LEU A 37 -20.505 36.501 -6.156 1.00 23.49 C
ANISOU 123 CB LEU A 37 3672 2706 2546 -220 -201 507 C
ATOM 124 CG LEU A 37 -20.621 37.352 -7.425 1.00 29.26 C
ANISOU 124 CG LEU A 37 4516 3330 3269 -225 -200 656 C
ATOM 125 CD1 LEU A 37 -22.090 37.579 -7.823 1.00 29.51 C
ANISOU 125 CD1 LEU A 37 4591 3307 3313 -21 -234 716 C
ATOM 126 CD2 LEU A 37 -19.885 38.671 -7.251 1.00 32.41 C
ANISOU 126 CD2 LEU A 37 5068 3528 3718 -359 -174 671 C
ATOM 127 N ALA A 38 -19.126 33.827 -7.258 1.00 21.53 N
ANISOU 127 N ALA A 38 3128 2904 2147 -335 -185 523 N
ATOM 128 CA ALA A 38 -18.377 33.075 -8.268 1.00 20.81 C
ANISOU 128 CA ALA A 38 2955 2967 1986 -403 -170 573 C
ATOM 129 C ALA A 38 -19.007 31.702 -8.519 1.00 23.11 C
ANISOU 129 C ALA A 38 3136 3408 2236 -298 -187 551 C
ATOM 130 O ALA A 38 -18.921 31.187 -9.640 1.00 22.63 O
ANISOU 130 O ALA A 38 3033 3449 2116 -300 -182 610 O
ATOM 131 CB ALA A 38 -16.929 32.912 -7.830 1.00 21.58 C
ANISOU 131 CB ALA A 38 2994 3139 2067 -554 -142 518 C
ATOM 132 N THR A 39 -19.639 31.115 -7.474 1.00 17.94 N
ANISOU 132 N THR A 39 2439 2768 1610 -215 -203 464 N
ATOM 133 CA THR A 39 -20.306 29.809 -7.535 1.00 16.58 C
ANISOU 133 CA THR A 39 2175 2717 1409 -127 -216 433 C
ATOM 134 C THR A 39 -21.691 29.923 -8.184 1.00 19.39 C
ANISOU 134 C THR A 39 2554 3055 1758 -12 -240 486 C
ATOM 135 O THR A 39 -22.054 29.077 -8.993 1.00 19.48 O
ANISOU 135 O THR A 39 2507 3174 1722 21 -248 507 O
ATOM 136 CB THR A 39 -20.334 29.159 -6.147 1.00 18.26 C
ANISOU 136 CB THR A 39 2338 2954 1645 -103 -219 331 C
ATOM 137 OG1 THR A 39 -19.024 29.218 -5.599 1.00 12.87 O
ANISOU 137 OG1 THR A 39 1635 2296 960 -206 -202 290 O
ATOM 138 CG2 THR A 39 -20.779 27.713 -6.186 1.00 16.80 C
ANISOU 138 CG2 THR A 39 2068 2887 1429 -44 -225 301 C
ATOM 139 N VAL A 40 -22.455 30.962 -7.830 1.00 15.28 N
ANISOU 139 N VAL A 40 2115 2407 1284 53 -254 500 N
ATOM 140 CA VAL A 40 -23.781 31.215 -8.376 1.00 15.13 C
ANISOU 140 CA VAL A 40 2112 2376 1258 179 -282 550 C
ATOM 141 C VAL A 40 -23.660 31.530 -9.880 1.00 20.78 C
ANISOU 141 C VAL A 40 2860 3113 1923 163 -288 670 C
ATOM 142 O VAL A 40 -24.291 30.833 -10.676 1.00 21.22 O
ANISOU 142 O VAL A 40 2853 3286 1925 218 -306 696 O
ATOM 143 CB VAL A 40 -24.551 32.284 -7.553 1.00 18.38 C
ANISOU 143 CB VAL A 40 2604 2645 1734 268 -293 526 C
ATOM 144 CG1 VAL A 40 -25.771 32.810 -8.304 1.00 17.79 C
ANISOU 144 CG1 VAL A 40 2560 2550 1650 405 -325 601 C
ATOM 145 CG2 VAL A 40 -24.958 31.731 -6.194 1.00 17.88 C
ANISOU 145 CG2 VAL A 40 2481 2617 1695 303 -290 409 C
ATOM 146 N THR A 41 -22.779 32.498 -10.262 1.00 17.22 N
ANISOU 146 N THR A 41 2500 2565 1479 71 -270 737 N
ATOM 147 CA THR A 41 -22.504 32.895 -11.655 1.00 16.69 C
ANISOU 147 CA THR A 41 2474 2515 1353 34 -268 864 C
ATOM 148 C THR A 41 -22.106 31.693 -12.536 1.00 20.58 C
ANISOU 148 C THR A 41 2855 3205 1762 -11 -259 863 C
ATOM 149 O THR A 41 -22.690 31.486 -13.608 1.00 20.16 O
ANISOU 149 O THR A 41 2781 3236 1642 42 -278 931 O
ATOM 150 CB THR A 41 -21.419 34.004 -11.719 1.00 21.53 C
ANISOU 150 CB THR A 41 3197 2995 1989 -98 -237 920 C
ATOM 151 OG1 THR A 41 -21.768 35.081 -10.849 1.00 23.27 O
ANISOU 151 OG1 THR A 41 3531 3018 2293 -58 -244 902 O
ATOM 152 CG2 THR A 41 -21.202 34.544 -13.136 1.00 17.51 C
ANISOU 152 CG2 THR A 41 2747 2493 1414 -141 -232 1068 C
ATOM 153 N GLY A 42 -21.111 30.939 -12.081 1.00 16.62 N
ANISOU 153 N GLY A 42 2282 2776 1257 -102 -231 783 N
ATOM 154 CA GLY A 42 -20.568 29.807 -12.820 1.00 16.70 C
ANISOU 154 CA GLY A 42 2192 2958 1195 -144 -216 764 C
ATOM 155 C GLY A 42 -21.569 28.723 -13.146 1.00 20.77 C
ANISOU 155 C GLY A 42 2632 3582 1675 -46 -241 728 C
ATOM 156 O GLY A 42 -21.554 28.190 -14.254 1.00 21.08 O
ANISOU 156 O GLY A 42 2628 3743 1639 -53 -240 758 O
ATOM 157 N ASN A 43 -22.426 28.372 -12.180 1.00 16.91 N
ANISOU 157 N ASN A 43 2125 3063 1237 33 -260 658 N
ATOM 158 CA ASN A 43 -23.407 27.317 -12.371 1.00 16.21 C
ANISOU 158 CA ASN A 43 1964 3075 1121 105 -280 613 C
ATOM 159 C ASN A 43 -24.600 27.823 -13.172 1.00 21.63 C
ANISOU 159 C ASN A 43 2667 3778 1773 194 -316 686 C
ATOM 160 O ASN A 43 -25.145 27.060 -13.966 1.00 21.27 O
ANISOU 160 O ASN A 43 2559 3859 1665 218 -331 680 O
ATOM 161 CB ASN A 43 -23.765 26.652 -11.056 1.00 11.39 C
ANISOU 161 CB ASN A 43 1290 2413 624 127 -248 488 C
ATOM 162 CG ASN A 43 -22.591 25.869 -10.533 1.00 21.39 C
ANISOU 162 CG ASN A 43 2549 3740 1837 63 -251 450 C
ATOM 163 OD1 ASN A 43 -22.304 24.771 -10.998 1.00 17.33 O
ANISOU 163 OD1 ASN A 43 1979 3323 1284 46 -241 416 O
ATOM 164 ND2 ASN A 43 -21.848 26.423 -9.584 1.00 9.30 N
ANISOU 164 ND2 ASN A 43 963 2036 535 3 -156 364 N
ATOM 165 N ILE A 44 -24.917 29.133 -13.067 1.00 19.58 N
ANISOU 165 N ILE A 44 2496 3395 1547 240 -331 759 N
ATOM 166 CA ILE A 44 -25.937 29.794 -13.888 1.00 19.88 C
ANISOU 166 CA ILE A 44 2562 3442 1549 339 -369 851 C
ATOM 167 C ILE A 44 -25.472 29.830 -15.363 1.00 23.28 C
ANISOU 167 C ILE A 44 2997 3962 1885 289 -367 948 C
ATOM 168 O ILE A 44 -26.261 29.505 -16.247 1.00 23.54 O
ANISOU 168 O ILE A 44 2981 4118 1846 349 -398 979 O
ATOM 169 CB ILE A 44 -26.331 31.183 -13.310 1.00 23.29 C
ANISOU 169 CB ILE A 44 3104 3696 2050 414 -382 900 C
ATOM 170 CG1 ILE A 44 -27.382 30.992 -12.195 1.00 23.25 C
ANISOU 170 CG1 ILE A 44 3057 3678 2098 517 -398 808 C
ATOM 171 CG2 ILE A 44 -26.851 32.146 -14.415 1.00 24.98 C
ANISOU 171 CG2 ILE A 44 3390 3884 2219 491 -413 1042 C
ATOM 172 CD1 ILE A 44 -27.616 32.159 -11.330 1.00 30.54 C
ANISOU 172 CD1 ILE A 44 4079 4426 3101 583 -399 809 C
ATOM 173 N LEU A 45 -24.190 30.170 -15.613 1.00 20.18 N
ANISOU 173 N LEU A 45 2651 3531 1485 172 -330 986 N
ATOM 174 CA LEU A 45 -23.590 30.173 -16.959 1.00 20.58 C
ANISOU 174 CA LEU A 45 2700 3681 1438 104 -317 1072 C
ATOM 175 C LEU A 45 -23.673 28.784 -17.598 1.00 25.82 C
ANISOU 175 C LEU A 45 3245 4542 2025 96 -317 1000 C
ATOM 176 O LEU A 45 -24.035 28.666 -18.771 1.00 24.57 O
ANISOU 176 O LEU A 45 3062 4504 1769 116 -335 1060 O
ATOM 177 CB LEU A 45 -22.119 30.629 -16.931 1.00 20.34 C
ANISOU 177 CB LEU A 45 2715 3598 1416 -39 -268 1099 C
ATOM 178 CG LEU A 45 -21.843 32.123 -16.780 1.00 24.80 C
ANISOU 178 CG LEU A 45 3420 3976 2027 -73 -261 1202 C
ATOM 179 CD1 LEU A 45 -20.370 32.355 -16.490 1.00 25.16 C
ANISOU 179 CD1 LEU A 45 3480 3990 2090 -236 -209 1184 C
ATOM 180 CD2 LEU A 45 -22.275 32.905 -18.013 1.00 25.43 C
ANISOU 180 CD2 LEU A 45 3573 4056 2032 -38 -280 1362 C
ATOM 181 N LEU A 46 -23.362 27.740 -16.808 1.00 23.90 N
ANISOU 181 N LEU A 46 2934 4327 1822 70 -298 871 N
ATOM 182 CA LEU A 46 -23.420 26.348 -17.228 1.00 24.22 C
ANISOU 182 CA LEU A 46 2877 4518 1809 62 -293 782 C
ATOM 183 C LEU A 46 -24.854 25.965 -17.674 1.00 27.76 C
ANISOU 183 C LEU A 46 3281 5051 2216 151 -338 773 C
ATOM 184 O LEU A 46 -25.024 25.498 -18.798 1.00 27.77 O
ANISOU 184 O LEU A 46 3236 5193 2121 144 -347 781 O
ATOM 185 CB LEU A 46 -22.899 25.449 -16.088 1.00 24.63 C
ANISOU 185 CB LEU A 46 2891 4538 1929 34 -268 661 C
ATOM 186 CG LEU A 46 -22.398 24.049 -16.483 1.00 30.20 C
ANISOU 186 CG LEU A 46 3521 5365 2589 1 -246 569 C
ATOM 187 CD1 LEU A 46 -21.217 24.126 -17.432 1.00 30.42 C
ANISOU 187 CD1 LEU A 46 3536 5477 2545 -72 -212 601 C
ATOM 188 CD2 LEU A 46 -21.977 23.266 -15.259 1.00 33.87 C
ANISOU 188 CD2 LEU A 46 3968 5776 3127 -4 -228 470 C
ATOM 189 N MET A 47 -25.877 26.247 -16.831 1.00 23.62 N
ANISOU 189 N MET A 47 2764 4455 1754 233 -367 757 N
ATOM 190 CA MET A 47 -27.298 25.992 -17.096 1.00 23.33 C
ANISOU 190 CA MET A 47 2673 4507 1684 319 -411 745 C
ATOM 191 C MET A 47 -27.829 26.763 -18.323 1.00 27.70 C
ANISOU 191 C MET A 47 3242 5135 2149 377 -450 865 C
ATOM 192 O MET A 47 -28.553 26.187 -19.138 1.00 25.98 O
ANISOU 192 O MET A 47 2950 5076 1847 400 -478 849 O
ATOM 193 CB MET A 47 -28.133 26.363 -15.870 1.00 25.70 C
ANISOU 193 CB MET A 47 2982 4712 2070 396 -426 714 C
ATOM 194 CG MET A 47 -28.267 25.257 -14.876 1.00 29.80 C
ANISOU 194 CG MET A 47 3447 5238 2637 364 -406 590 C
ATOM 195 SD MET A 47 -29.106 25.851 -13.388 1.00 34.25 S
ANISOU 195 SD MET A 47 4026 5696 3292 446 -414 559 S
ATOM 196 CE MET A 47 -27.759 26.137 -12.405 1.00 30.90 C
ANISOU 196 CE MET A 47 3673 5125 2942 376 -373 539 C
ATOM 197 N LEU A 48 -27.493 28.066 -18.429 1.00 25.97 N
ANISOU 197 N LEU A 48 3123 4799 1947 399 -452 986 N
ATOM 198 CA LEU A 48 -27.913 28.919 -19.537 1.00 26.96 C
ANISOU 198 CA LEU A 48 3286 4967 1991 461 -488 1126 C
ATOM 199 C LEU A 48 -27.240 28.564 -20.838 1.00 27.86 C
ANISOU 199 C LEU A 48 3379 5221 1987 379 -473 1171 C
ATOM 200 O LEU A 48 -27.880 28.691 -21.869 1.00 27.06 O
ANISOU 200 O LEU A 48 3250 5248 1782 434 -513 1240 O
ATOM 201 CB LEU A 48 -27.686 30.403 -19.237 1.00 28.47 C
ANISOU 201 CB LEU A 48 3613 4962 2241 501 -489 1245 C
ATOM 202 CG LEU A 48 -28.663 31.094 -18.290 1.00 35.20 C
ANISOU 202 CG LEU A 48 4499 5694 3180 636 -519 1237 C
ATOM 203 CD1 LEU A 48 -28.191 32.507 -18.011 1.00 36.34 C
ANISOU 203 CD1 LEU A 48 4799 5617 3391 649 -508 1339 C
ATOM 204 CD2 LEU A 48 -30.088 31.138 -18.874 1.00 38.63 C
ANISOU 204 CD2 LEU A 48 4869 6260 3547 784 -583 1275 C
ATOM 205 N SER A 49 -25.961 28.132 -20.806 1.00 23.93 N
ANISOU 205 N SER A 49 2883 4715 1494 255 -418 1129 N
ATOM 206 CA SER A 49 -25.212 27.721 -22.004 1.00 23.32 C
ANISOU 206 CA SER A 49 2774 4787 1300 171 -394 1151 C
ATOM 207 C SER A 49 -25.913 26.562 -22.705 1.00 27.19 C
ANISOU 207 C SER A 49 3154 5476 1700 193 -418 1063 C
ATOM 208 O SER A 49 -26.108 26.621 -23.923 1.00 26.46 O
ANISOU 208 O SER A 49 3040 5532 1482 197 -437 1128 O
ATOM 209 CB SER A 49 -23.771 27.346 -21.665 1.00 25.53 C
ANISOU 209 CB SER A 49 3051 5038 1611 51 -330 1091 C
ATOM 210 OG SER A 49 -22.982 28.505 -21.456 1.00 32.04 O
ANISOU 210 OG SER A 49 3974 5726 2474 -4 -305 1194 O
ATOM 211 N ILE A 50 -26.335 25.541 -21.924 1.00 23.82 N
ANISOU 211 N ILE A 50 2664 5053 1335 202 -418 919 N
ATOM 212 CA ILE A 50 -27.055 24.362 -22.413 1.00 24.56 C
ANISOU 212 CA ILE A 50 2660 5309 1363 206 -438 811 C
ATOM 213 C ILE A 50 -28.445 24.781 -22.966 1.00 31.43 C
ANISOU 213 C ILE A 50 3495 6280 2165 302 -505 872 C
ATOM 214 O ILE A 50 -28.849 24.307 -24.029 1.00 31.10 O
ANISOU 214 O ILE A 50 3388 6423 2004 296 -528 854 O
ATOM 215 CB ILE A 50 -27.100 23.248 -21.320 1.00 27.68 C
ANISOU 215 CB ILE A 50 3019 5647 1852 180 -415 657 C
ATOM 216 CG1 ILE A 50 -25.659 22.850 -20.880 1.00 27.82 C
ANISOU 216 CG1 ILE A 50 3063 5589 1919 102 -355 607 C
ATOM 217 CG2 ILE A 50 -27.901 22.014 -21.786 1.00 28.41 C
ANISOU 217 CG2 ILE A 50 3023 5887 1884 166 -433 539 C
ATOM 218 CD1 ILE A 50 -25.529 22.207 -19.469 1.00 27.86 C
ANISOU 218 CD1 ILE A 50 3070 5473 2042 96 -335 507 C
ATOM 219 N LYS A 51 -29.121 25.734 -22.285 1.00 29.35 N
ANISOU 219 N LYS A 51 3275 5904 1971 397 -535 945 N
ATOM 220 CA LYS A 51 -30.428 26.272 -22.668 1.00 29.34 C
ANISOU 220 CA LYS A 51 3242 5987 1918 517 -602 1012 C
ATOM 221 C LYS A 51 -30.392 27.078 -23.989 1.00 33.64 C
ANISOU 221 C LYS A 51 3820 6623 2337 554 -633 1168 C
ATOM 222 O LYS A 51 -31.217 26.850 -24.870 1.00 33.87 O
ANISOU 222 O LYS A 51 3773 6844 2254 604 -683 1181 O
ATOM 223 CB LYS A 51 -31.005 27.123 -21.509 1.00 31.79 C
ANISOU 223 CB LYS A 51 3602 6132 2346 618 -616 1041 C
ATOM 224 CG LYS A 51 -32.372 27.756 -21.801 1.00 44.91 C
ANISOU 224 CG LYS A 51 5225 7875 3964 770 -686 1108 C
ATOM 225 CD LYS A 51 -32.602 29.031 -21.006 1.00 51.20 C
ANISOU 225 CD LYS A 51 6120 8478 4857 885 -696 1193 C
ATOM 226 CE LYS A 51 -33.857 29.746 -21.447 1.00 56.43 C
ANISOU 226 CE LYS A 51 6754 9226 5462 1059 -767 1283 C
ATOM 227 NZ LYS A 51 -34.045 31.032 -20.724 1.00 63.72 N
ANISOU 227 NZ LYS A 51 7786 9943 6482 1187 -775 1360 N
ATOM 228 N VAL A 52 -29.435 28.006 -24.107 1.00 30.83 N
ANISOU 228 N VAL A 52 3577 6139 1997 523 -603 1287 N
ATOM 229 CA VAL A 52 -29.229 28.975 -25.201 1.00 30.68 C
ANISOU 229 CA VAL A 52 3629 6152 1876 546 -621 1468 C
ATOM 230 C VAL A 52 -28.481 28.416 -26.448 1.00 35.21 C
ANISOU 230 C VAL A 52 4164 6909 2306 439 -595 1475 C
ATOM 231 O VAL A 52 -28.626 28.979 -27.530 1.00 35.26 O
ANISOU 231 O VAL A 52 4192 7017 2187 470 -623 1612 O
ATOM 232 CB VAL A 52 -28.508 30.202 -24.562 1.00 34.08 C
ANISOU 232 CB VAL A 52 4211 6328 2411 540 -590 1577 C
ATOM 233 CG1 VAL A 52 -27.319 30.724 -25.364 1.00 33.70 C
ANISOU 233 CG1 VAL A 52 4242 6265 2299 425 -544 1690 C
ATOM 234 CG2 VAL A 52 -29.490 31.301 -24.187 1.00 33.57 C
ANISOU 234 CG2 VAL A 52 4216 6145 2392 702 -644 1683 C
ATOM 235 N ASN A 53 -27.680 27.350 -26.301 1.00 32.38 N
ANISOU 235 N ASN A 53 3752 6591 1960 324 -541 1333 N
ATOM 236 CA ASN A 53 -26.904 26.777 -27.406 1.00 32.04 C
ANISOU 236 CA ASN A 53 3668 6721 1786 227 -508 1314 C
ATOM 237 C ASN A 53 -27.365 25.354 -27.737 1.00 37.86 C
ANISOU 237 C ASN A 53 4281 7641 2463 206 -517 1139 C
ATOM 238 O ASN A 53 -27.358 24.479 -26.869 1.00 38.07 O
ANISOU 238 O ASN A 53 4272 7605 2588 182 -497 989 O
ATOM 239 CB ASN A 53 -25.402 26.835 -27.073 1.00 30.24 C
ANISOU 239 CB ASN A 53 3488 6390 1611 110 -430 1303 C
ATOM 240 CG ASN A 53 -24.441 26.380 -28.136 1.00 41.01 C
ANISOU 240 CG ASN A 53 4811 7924 2847 10 -383 1287 C
ATOM 241 OD1 ASN A 53 -24.812 25.848 -29.180 1.00 38.74 O
ANISOU 241 OD1 ASN A 53 4456 7844 2420 15 -404 1262 O
ATOM 242 ND2 ASN A 53 -23.164 26.585 -27.881 1.00 28.76 N
ANISOU 242 ND2 ASN A 53 3293 6302 1334 -85 -318 1292 N
ATOM 243 N ARG A 54 -27.757 25.137 -29.004 1.00 35.49 N
ANISOU 243 N ARG A 54 3923 7564 1998 211 -548 1161 N
ATOM 244 CA ARG A 54 -28.250 23.861 -29.534 1.00 35.63 C
ANISOU 244 CA ARG A 54 3829 7777 1933 183 -562 998 C
ATOM 245 C ARG A 54 -27.193 22.748 -29.502 1.00 37.77 C
ANISOU 245 C ARG A 54 4074 8057 2218 76 -491 839 C
ATOM 246 O ARG A 54 -27.518 21.619 -29.138 1.00 37.01 O
ANISOU 246 O ARG A 54 3924 7975 2165 54 -487 669 O
ATOM 247 CB ARG A 54 -28.827 24.056 -30.958 1.00 38.65 C
ANISOU 247 CB ARG A 54 4160 8409 2116 211 -613 1074 C
ATOM 248 CG ARG A 54 -29.655 22.881 -31.515 1.00 52.83 C
ANISOU 248 CG ARG A 54 5835 10422 3818 191 -646 908 C
ATOM 249 CD ARG A 54 -30.968 22.670 -30.778 1.00 67.52 C
ANISOU 249 CD ARG A 54 7638 12264 5751 259 -702 846 C
ATOM 250 NE ARG A 54 -32.064 23.452 -31.350 1.00 79.60 N
ANISOU 250 NE ARG A 54 9132 13932 7181 370 -785 974 N
ATOM 251 CZ ARG A 54 -33.239 23.636 -30.754 1.00 95.69 C
ANISOU 251 CZ ARG A 54 11122 15965 9271 462 -841 971 C
ATOM 252 NH1 ARG A 54 -33.470 23.121 -29.550 1.00 81.52 N
ANISOU 252 NH1 ARG A 54 9316 14029 7628 443 -818 851 N
ATOM 253 NH2 ARG A 54 -34.185 24.350 -31.348 1.00 83.88 N
ANISOU 253 NH2 ARG A 54 9586 14615 7671 578 -919 1091 N
ATOM 254 N GLN A 55 -25.936 23.072 -29.858 1.00 33.78 N
ANISOU 254 N GLN A 55 3611 7543 1681 12 -434 895 N
ATOM 255 CA GLN A 55 -24.798 22.139 -29.861 1.00 33.49 C
ANISOU 255 CA GLN A 55 3549 7525 1652 -71 -364 757 C
ATOM 256 C GLN A 55 -24.535 21.533 -28.473 1.00 35.88 C
ANISOU 256 C GLN A 55 3866 7634 2132 -73 -336 640 C
ATOM 257 O GLN A 55 -23.929 20.463 -28.375 1.00 36.21 O
ANISOU 257 O GLN A 55 3875 7692 2192 -112 -294 488 O
ATOM 258 CB GLN A 55 -23.517 22.842 -30.340 1.00 34.99 C
ANISOU 258 CB GLN A 55 3777 7732 1785 -134 -308 866 C
ATOM 259 CG GLN A 55 -23.507 23.271 -31.802 1.00 49.54 C
ANISOU 259 CG GLN A 55 5601 9794 3429 -156 -316 967 C
ATOM 260 CD GLN A 55 -22.160 23.828 -32.191 1.00 73.21 C
ANISOU 260 CD GLN A 55 8629 12811 6376 -241 -247 1055 C
ATOM 261 OE1 GLN A 55 -21.545 24.629 -31.467 1.00 69.12 O
ANISOU 261 OE1 GLN A 55 8186 12122 5955 -267 -223 1160 O
ATOM 262 NE2 GLN A 55 -21.668 23.413 -33.350 1.00 67.44 N
ANISOU 262 NE2 GLN A 55 7836 12301 5486 -295 -211 1007 N
ATOM 263 N LEU A 56 -24.957 22.231 -27.408 1.00 30.20 N
ANISOU 263 N LEU A 56 3201 6733 1540 -25 -359 712 N
ATOM 264 CA LEU A 56 -24.769 21.778 -26.033 1.00 28.20 C
ANISOU 264 CA LEU A 56 2966 6303 1447 -24 -338 620 C
ATOM 265 C LEU A 56 -25.938 20.947 -25.533 1.00 30.96 C
ANISOU 265 C LEU A 56 3273 6650 1842 11 -374 506 C
ATOM 266 O LEU A 56 -25.796 20.254 -24.534 1.00 30.42 O
ANISOU 266 O LEU A 56 3209 6470 1881 0 -351 404 O
ATOM 267 CB LEU A 56 -24.482 22.964 -25.103 1.00 27.64 C
ANISOU 267 CB LEU A 56 2976 6042 1483 -4 -335 741 C
ATOM 268 CG LEU A 56 -23.162 23.698 -25.354 1.00 31.38 C
ANISOU 268 CG LEU A 56 3497 6491 1937 -70 -287 835 C
ATOM 269 CD1 LEU A 56 -23.065 24.956 -24.515 1.00 31.04 C
ANISOU 269 CD1 LEU A 56 3545 6257 1993 -55 -292 955 C
ATOM 270 CD2 LEU A 56 -21.970 22.796 -25.113 1.00 32.45 C
ANISOU 270 CD2 LEU A 56 3595 6641 2095 -133 -226 714 C
ATOM 271 N GLN A 57 -27.077 20.976 -26.244 1.00 27.73 N
ANISOU 271 N GLN A 57 2816 6379 1342 46 -429 522 N
ATOM 272 CA GLN A 57 -28.282 20.224 -25.888 1.00 27.47 C
ANISOU 272 CA GLN A 57 2726 6380 1332 62 -464 414 C
ATOM 273 C GLN A 57 -28.162 18.715 -26.211 1.00 30.48 C
ANISOU 273 C GLN A 57 3061 6840 1680 -12 -437 229 C
ATOM 274 O GLN A 57 -28.909 18.199 -27.044 1.00 30.70 O
ANISOU 274 O GLN A 57 3024 7039 1602 -31 -468 164 O
ATOM 275 CB GLN A 57 -29.515 20.860 -26.548 1.00 28.86 C
ANISOU 275 CB GLN A 57 2855 6698 1413 129 -536 498 C
ATOM 276 CG GLN A 57 -30.175 21.937 -25.701 1.00 38.05 C
ANISOU 276 CG GLN A 57 4053 7742 2664 224 -572 611 C
ATOM 277 CD GLN A 57 -30.905 22.962 -26.531 1.00 52.88 C
ANISOU 277 CD GLN A 57 5918 9738 4435 314 -635 757 C
ATOM 278 OE1 GLN A 57 -31.689 22.639 -27.436 1.00 48.43 O
ANISOU 278 OE1 GLN A 57 5271 9385 3745 324 -680 732 O
ATOM 279 NE2 GLN A 57 -30.665 24.230 -26.234 1.00 42.40 N
ANISOU 279 NE2 GLN A 57 4678 8277 3155 384 -641 913 N
ATOM 280 N THR A 58 -27.227 18.018 -25.529 1.00 25.08 N
ANISOU 280 N THR A 58 2413 6028 1088 -48 -381 141 N
ATOM 281 CA THR A 58 -26.942 16.583 -25.669 1.00 24.31 C
ANISOU 281 CA THR A 58 2300 5950 987 -104 -346 -35 C
ATOM 282 C THR A 58 -27.318 15.842 -24.383 1.00 28.25 C
ANISOU 282 C THR A 58 2823 6288 1622 -113 -337 -121 C
ATOM 283 O THR A 58 -27.300 16.458 -23.312 1.00 26.76 O
ANISOU 283 O THR A 58 2670 5961 1537 -77 -338 -45 O
ATOM 284 CB THR A 58 -25.446 16.378 -25.920 1.00 34.34 C
ANISOU 284 CB THR A 58 3597 7204 2249 -121 -286 -57 C
ATOM 285 OG1 THR A 58 -24.721 16.921 -24.812 1.00 40.27 O
ANISOU 285 OG1 THR A 58 4398 7783 3119 -98 -263 14 O
ATOM 286 CG2 THR A 58 -24.965 17.006 -27.235 1.00 31.34 C
ANISOU 286 CG2 THR A 58 3191 6998 1720 -132 -283 21 C
ATOM 287 N VAL A 59 -27.602 14.513 -24.481 1.00 24.87 N
ANISOU 287 N VAL A 59 2384 5873 1191 -166 -323 -280 N
ATOM 288 CA VAL A 59 -27.951 13.633 -23.352 1.00 24.16 C
ANISOU 288 CA VAL A 59 2327 5634 1217 -192 -309 -367 C
ATOM 289 C VAL A 59 -27.001 13.794 -22.149 1.00 29.35 C
ANISOU 289 C VAL A 59 3050 6103 2001 -154 -273 -322 C
ATOM 290 O VAL A 59 -27.480 14.001 -21.033 1.00 30.01 O
ANISOU 290 O VAL A 59 3149 6079 2173 -141 -283 -286 O
ATOM 291 CB VAL A 59 -28.076 12.147 -23.774 1.00 27.64 C
ANISOU 291 CB VAL A 59 2774 6093 1635 -262 -286 -545 C
ATOM 292 CG1 VAL A 59 -28.181 11.221 -22.559 1.00 27.07 C
ANISOU 292 CG1 VAL A 59 2762 5833 1689 -289 -260 -616 C
ATOM 293 CG2 VAL A 59 -29.250 11.934 -24.720 1.00 27.49 C
ANISOU 293 CG2 VAL A 59 2682 6260 1502 -317 -328 -604 C
ATOM 294 N ASN A 60 -25.669 13.700 -22.355 1.00 25.40 N
ANISOU 294 N ASN A 60 2575 5577 1499 -136 -232 -330 N
ATOM 295 CA ASN A 60 -24.738 13.826 -21.226 1.00 24.67 C
ANISOU 295 CA ASN A 60 2530 5329 1513 -101 -203 -295 C
ATOM 296 C ASN A 60 -24.800 15.207 -20.574 1.00 25.91 C
ANISOU 296 C ASN A 60 2692 5439 1712 -68 -225 -150 C
ATOM 297 O ASN A 60 -24.601 15.293 -19.368 1.00 26.83 O
ANISOU 297 O ASN A 60 2843 5422 1927 -49 -217 -129 O
ATOM 298 CB ASN A 60 -23.289 13.419 -21.575 1.00 26.63 C
ANISOU 298 CB ASN A 60 2787 5584 1745 -83 -155 -341 C
ATOM 299 CG ASN A 60 -22.432 13.162 -20.337 1.00 44.58 C
ANISOU 299 CG ASN A 60 5103 7705 4129 -45 -129 -343 C
ATOM 300 OD1 ASN A 60 -21.905 14.092 -19.717 1.00 39.81 O
ANISOU 300 OD1 ASN A 60 4502 7059 3566 -26 -129 -245 O
ATOM 301 ND2 ASN A 60 -22.275 11.904 -19.934 1.00 28.79 N
ANISOU 301 ND2 ASN A 60 3142 5619 2178 -34 -106 -453 N
ATOM 302 N ASN A 61 -25.148 16.261 -21.333 1.00 19.75 N
ANISOU 302 N ASN A 61 1885 4761 856 -60 -253 -51 N
ATOM 303 CA ASN A 61 -25.260 17.614 -20.786 1.00 18.00 C
ANISOU 303 CA ASN A 61 1685 4479 674 -25 -275 85 C
ATOM 304 C ASN A 61 -26.543 17.824 -19.987 1.00 20.74 C
ANISOU 304 C ASN A 61 2027 4776 1078 2 -312 100 C
ATOM 305 O ASN A 61 -26.668 18.840 -19.301 1.00 20.81 O
ANISOU 305 O ASN A 61 2062 4705 1140 42 -326 190 O
ATOM 306 CB ASN A 61 -25.061 18.672 -21.850 1.00 17.20 C
ANISOU 306 CB ASN A 61 1576 4483 477 -20 -288 197 C
ATOM 307 CG ASN A 61 -23.609 18.927 -22.183 1.00 34.59 C
ANISOU 307 CG ASN A 61 3791 6695 2655 -48 -243 225 C
ATOM 308 OD1 ASN A 61 -22.674 18.501 -21.484 1.00 30.14 O
ANISOU 308 OD1 ASN A 61 3242 6050 2160 -57 -206 176 O
ATOM 309 ND2 ASN A 61 -23.383 19.638 -23.261 1.00 25.16 N
ANISOU 309 ND2 ASN A 61 2588 5616 1355 -63 -245 309 N
ATOM 310 N TYR A 62 -27.465 16.838 -20.007 1.00 17.04 N
ANISOU 310 N TYR A 62 1525 4350 599 -25 -323 1 N
ATOM 311 CA TYR A 62 -28.653 16.852 -19.147 1.00 17.37 C
ANISOU 311 CA TYR A 62 1548 4357 693 -13 -348 -6 C
ATOM 312 C TYR A 62 -28.137 16.601 -17.713 1.00 19.97 C
ANISOU 312 C TYR A 62 1930 4517 1140 -11 -316 -22 C
ATOM 313 O TYR A 62 -28.600 17.248 -16.777 1.00 19.87 O
ANISOU 313 O TYR A 62 1924 4439 1186 24 -328 27 O
ATOM 314 CB TYR A 62 -29.676 15.771 -19.559 1.00 18.90 C
ANISOU 314 CB TYR A 62 1689 4651 839 -70 -362 -116 C
ATOM 315 CG TYR A 62 -30.629 16.195 -20.657 1.00 22.16 C
ANISOU 315 CG TYR A 62 2029 5251 1141 -59 -411 -90 C
ATOM 316 CD1 TYR A 62 -30.155 16.603 -21.903 1.00 24.06 C
ANISOU 316 CD1 TYR A 62 2259 5605 1278 -47 -421 -47 C
ATOM 317 CD2 TYR A 62 -32.007 16.150 -20.467 1.00 24.14 C
ANISOU 317 CD2 TYR A 62 2212 5585 1376 -61 -448 -109 C
ATOM 318 CE1 TYR A 62 -31.025 17.003 -22.915 1.00 23.93 C
ANISOU 318 CE1 TYR A 62 2173 5772 1145 -28 -472 -13 C
ATOM 319 CE2 TYR A 62 -32.889 16.549 -21.473 1.00 25.70 C
ANISOU 319 CE2 TYR A 62 2329 5976 1461 -38 -501 -83 C
ATOM 320 CZ TYR A 62 -32.391 16.972 -22.698 1.00 31.57 C
ANISOU 320 CZ TYR A 62 3070 6823 2101 -19 -515 -32 C
ATOM 321 OH TYR A 62 -33.247 17.330 -23.709 1.00 32.00 O
ANISOU 321 OH TYR A 62 3046 7082 2033 8 -571 -1 O
ATOM 322 N PHE A 63 -27.107 15.727 -17.572 1.00 15.32 N
ANISOU 322 N PHE A 63 1379 3865 578 -38 -276 -87 N
ATOM 323 CA PHE A 63 -26.475 15.416 -16.293 1.00 14.92 C
ANISOU 323 CA PHE A 63 1376 3670 622 -29 -248 -98 C
ATOM 324 C PHE A 63 -25.621 16.574 -15.805 1.00 19.78 C
ANISOU 324 C PHE A 63 2014 4227 1273 10 -245 -4 C
ATOM 325 O PHE A 63 -25.589 16.838 -14.612 1.00 20.32 O
ANISOU 325 O PHE A 63 2107 4199 1414 28 -242 18 O
ATOM 326 CB PHE A 63 -25.675 14.118 -16.366 1.00 16.28 C
ANISOU 326 CB PHE A 63 1579 3801 805 -51 -211 -194 C
ATOM 327 CG PHE A 63 -26.438 12.924 -16.886 1.00 17.71 C
ANISOU 327 CG PHE A 63 1755 4020 954 -105 -210 -301 C
ATOM 328 CD1 PHE A 63 -27.539 12.428 -16.201 1.00 20.67 C
ANISOU 328 CD1 PHE A 63 2132 4356 1364 -147 -217 -333 C
ATOM 329 CD2 PHE A 63 -26.021 12.259 -18.034 1.00 20.26 C
ANISOU 329 CD2 PHE A 63 2071 4417 1209 -124 -196 -379 C
ATOM 330 CE1 PHE A 63 -28.250 11.320 -16.690 1.00 21.80 C
ANISOU 330 CE1 PHE A 63 2274 4532 1478 -220 -213 -438 C
ATOM 331 CE2 PHE A 63 -26.731 11.149 -18.522 1.00 22.88 C
ANISOU 331 CE2 PHE A 63 2406 4776 1511 -187 -193 -493 C
ATOM 332 CZ PHE A 63 -27.838 10.686 -17.845 1.00 20.51 C
ANISOU 332 CZ PHE A 63 2112 4431 1251 -241 -202 -521 C
ATOM 333 N ALA A 64 -24.969 17.296 -16.732 1.00 17.25 N
ANISOU 333 N ALA A 64 1686 3973 896 14 -244 52 N
ATOM 334 CA ALA A 64 -24.156 18.486 -16.446 1.00 16.48 C
ANISOU 334 CA ALA A 64 1613 3827 820 28 -239 144 C
ATOM 335 C ALA A 64 -25.068 19.587 -15.873 1.00 19.86 C
ANISOU 335 C ALA A 64 2057 4205 1285 65 -271 220 C
ATOM 336 O ALA A 64 -24.684 20.227 -14.899 1.00 20.26 O
ANISOU 336 O ALA A 64 2142 4155 1401 76 -265 254 O
ATOM 337 CB ALA A 64 -23.479 18.974 -17.723 1.00 16.97 C
ANISOU 337 CB ALA A 64 1662 3991 796 9 -231 193 C
ATOM 338 N PHE A 65 -26.293 19.758 -16.449 1.00 15.93 N
ANISOU 338 N PHE A 65 1529 3783 742 88 -306 236 N
ATOM 339 CA PHE A 65 -27.320 20.721 -16.016 1.00 15.53 C
ANISOU 339 CA PHE A 65 1480 3706 715 146 -341 298 C
ATOM 340 C PHE A 65 -27.844 20.331 -14.627 1.00 19.72 C
ANISOU 340 C PHE A 65 2009 4158 1325 155 -335 242 C
ATOM 341 O PHE A 65 -28.019 21.203 -13.775 1.00 18.27 O
ANISOU 341 O PHE A 65 1853 3893 1196 198 -341 283 O
ATOM 342 CB PHE A 65 -28.482 20.741 -17.022 1.00 17.12 C
ANISOU 342 CB PHE A 65 1626 4047 832 172 -381 311 C
ATOM 343 CG PHE A 65 -29.488 21.859 -16.852 1.00 18.26 C
ANISOU 343 CG PHE A 65 1766 4190 982 258 -422 389 C
ATOM 344 CD1 PHE A 65 -30.473 21.789 -15.871 1.00 20.13 C
ANISOU 344 CD1 PHE A 65 1973 4405 1270 294 -433 351 C
ATOM 345 CD2 PHE A 65 -29.527 22.920 -17.749 1.00 20.59 C
ANISOU 345 CD2 PHE A 65 2082 4523 1219 307 -450 501 C
ATOM 346 CE1 PHE A 65 -31.424 22.801 -15.735 1.00 20.70 C
ANISOU 346 CE1 PHE A 65 2032 4487 1344 393 -470 413 C
ATOM 347 CE2 PHE A 65 -30.493 23.923 -17.627 1.00 23.39 C
ANISOU 347 CE2 PHE A 65 2436 4872 1577 409 -492 574 C
ATOM 348 CZ PHE A 65 -31.433 23.858 -16.615 1.00 20.94 C
ANISOU 348 CZ PHE A 65 2091 4539 1324 458 -502 524 C
ATOM 349 N SER A 66 -28.103 19.015 -14.414 1.00 17.01 N
ANISOU 349 N SER A 66 1640 3838 985 110 -320 148 N
ATOM 350 CA SER A 66 -28.554 18.463 -13.144 1.00 16.59 C
ANISOU 350 CA SER A 66 1589 3720 995 101 -307 98 C
ATOM 351 C SER A 66 -27.509 18.715 -12.065 1.00 20.22 C
ANISOU 351 C SER A 66 2102 4058 1523 108 -282 113 C
ATOM 352 O SER A 66 -27.878 19.057 -10.945 1.00 20.91 O
ANISOU 352 O SER A 66 2198 4089 1659 130 -282 118 O
ATOM 353 CB SER A 66 -28.815 16.966 -13.267 1.00 19.84 C
ANISOU 353 CB SER A 66 1985 4159 1393 37 -290 3 C
ATOM 354 OG SER A 66 -29.173 16.436 -11.998 1.00 25.35 O
ANISOU 354 OG SER A 66 2696 4789 2148 19 -273 -29 O
ATOM 355 N LEU A 67 -26.211 18.544 -12.404 1.00 15.48 N
ANISOU 355 N LEU A 67 1527 3436 917 88 -262 115 N
ATOM 356 CA LEU A 67 -25.094 18.774 -11.489 1.00 14.62 C
ANISOU 356 CA LEU A 67 1454 3241 859 90 -242 125 C
ATOM 357 C LEU A 67 -24.998 20.269 -11.158 1.00 18.50 C
ANISOU 357 C LEU A 67 1969 3684 1374 115 -254 198 C
ATOM 358 O LEU A 67 -24.753 20.621 -9.998 1.00 18.38 O
ANISOU 358 O LEU A 67 1977 3594 1410 123 -249 197 O
ATOM 359 CB LEU A 67 -23.785 18.251 -12.112 1.00 14.35 C
ANISOU 359 CB LEU A 67 1421 3232 800 67 -218 105 C
ATOM 360 CG LEU A 67 -22.467 18.466 -11.338 1.00 18.44 C
ANISOU 360 CG LEU A 67 1955 3698 1353 66 -199 112 C
ATOM 361 CD1 LEU A 67 -22.506 17.835 -9.952 1.00 18.08 C
ANISOU 361 CD1 LEU A 67 1927 3581 1361 81 -194 76 C
ATOM 362 CD2 LEU A 67 -21.269 17.927 -12.124 1.00 18.81 C
ANISOU 362 CD2 LEU A 67 1982 3804 1361 54 -176 84 C
ATOM 363 N ALA A 68 -25.231 21.142 -12.181 1.00 13.57 N
ANISOU 363 N ALA A 68 1347 3102 709 128 -273 262 N
ATOM 364 CA ALA A 68 -25.205 22.599 -12.065 1.00 12.32 C
ANISOU 364 CA ALA A 68 1223 2870 588 152 -274 335 C
ATOM 365 C ALA A 68 -26.269 23.112 -11.117 1.00 16.67 C
ANISOU 365 C ALA A 68 1788 3379 1166 212 -303 336 C
ATOM 366 O ALA A 68 -25.990 24.067 -10.404 1.00 16.78 O
ANISOU 366 O ALA A 68 1849 3299 1228 226 -301 359 O
ATOM 367 CB ALA A 68 -25.336 23.253 -13.438 1.00 12.93 C
ANISOU 367 CB ALA A 68 1310 3016 588 162 -299 415 C
ATOM 368 N CYS A 69 -27.474 22.469 -11.093 1.00 14.59 N
ANISOU 368 N CYS A 69 1473 3184 886 240 -318 296 N
ATOM 369 CA CYS A 69 -28.627 22.746 -10.216 1.00 15.04 C
ANISOU 369 CA CYS A 69 1509 3231 972 295 -330 276 C
ATOM 370 C CYS A 69 -28.219 22.492 -8.743 1.00 19.08 C
ANISOU 370 C CYS A 69 2042 3666 1542 275 -305 227 C
ATOM 371 O CYS A 69 -28.483 23.335 -7.878 1.00 19.06 O
ANISOU 371 O CYS A 69 2062 3603 1578 319 -307 231 O
ATOM 372 CB CYS A 69 -29.833 21.884 -10.606 1.00 16.01 C
ANISOU 372 CB CYS A 69 1557 3475 1052 296 -344 234 C
ATOM 373 SG CYS A 69 -30.736 22.441 -12.084 1.00 20.18 S
ANISOU 373 SG CYS A 69 2041 4124 1503 354 -390 292 S
ATOM 374 N ALA A 70 -27.579 21.324 -8.465 1.00 15.09 N
ANISOU 374 N ALA A 70 1531 3165 1038 214 -281 180 N
ATOM 375 CA ALA A 70 -27.079 20.949 -7.130 1.00 14.67 C
ANISOU 375 CA ALA A 70 1497 3053 1024 195 -259 144 C
ATOM 376 C ALA A 70 -26.028 21.951 -6.661 1.00 20.00 C
ANISOU 376 C ALA A 70 2218 3651 1731 196 -256 169 C
ATOM 377 O ALA A 70 -26.060 22.371 -5.503 1.00 19.75 O
ANISOU 377 O ALA A 70 2203 3572 1731 210 -251 150 O
ATOM 378 CB ALA A 70 -26.484 19.546 -7.148 1.00 14.78 C
ANISOU 378 CB ALA A 70 1508 3080 1028 146 -239 105 C
ATOM 379 N ASP A 71 -25.121 22.361 -7.576 1.00 17.02 N
ANISOU 379 N ASP A 71 1860 3270 1338 173 -256 209 N
ATOM 380 CA ASP A 71 -24.052 23.304 -7.267 1.00 16.44 C
ANISOU 380 CA ASP A 71 1827 3131 1288 147 -250 232 C
ATOM 381 C ASP A 71 -24.570 24.737 -7.116 1.00 18.89 C
ANISOU 381 C ASP A 71 2185 3367 1627 184 -264 269 C
ATOM 382 O ASP A 71 -23.986 25.500 -6.345 1.00 19.06 O
ANISOU 382 O ASP A 71 2246 3314 1682 164 -257 260 O
ATOM 383 CB ASP A 71 -22.901 23.182 -8.273 1.00 18.70 C
ANISOU 383 CB ASP A 71 2109 3455 1541 96 -238 259 C
ATOM 384 CG ASP A 71 -22.076 21.905 -8.159 1.00 30.77 C
ANISOU 384 CG ASP A 71 3601 5035 3055 73 -220 210 C
ATOM 385 OD1 ASP A 71 -22.162 21.228 -7.107 1.00 31.36 O
ANISOU 385 OD1 ASP A 71 3669 5094 3152 87 -217 166 O
ATOM 386 OD2 ASP A 71 -21.324 21.596 -9.111 1.00 36.70 O
ANISOU 386 OD2 ASP A 71 4333 5843 3768 45 -208 218 O
ATOM 387 N LEU A 72 -25.703 25.077 -7.771 1.00 14.49 N
ANISOU 387 N LEU A 72 1622 2829 1053 245 -285 303 N
ATOM 388 CA LEU A 72 -26.355 26.385 -7.621 1.00 14.17 C
ANISOU 388 CA LEU A 72 1632 2712 1041 311 -301 337 C
ATOM 389 C LEU A 72 -26.985 26.498 -6.210 1.00 19.09 C
ANISOU 389 C LEU A 72 2249 3302 1704 355 -297 271 C
ATOM 390 O LEU A 72 -26.947 27.570 -5.617 1.00 18.75 O
ANISOU 390 O LEU A 72 2264 3160 1700 383 -297 268 O
ATOM 391 CB LEU A 72 -27.405 26.611 -8.724 1.00 14.19 C
ANISOU 391 CB LEU A 72 1615 2772 1004 381 -330 393 C
ATOM 392 CG LEU A 72 -28.247 27.906 -8.672 1.00 18.59 C
ANISOU 392 CG LEU A 72 2222 3256 1586 485 -353 436 C
ATOM 393 CD1 LEU A 72 -27.371 29.174 -8.792 1.00 18.66 C
ANISOU 393 CD1 LEU A 72 2341 3120 1628 460 -347 497 C
ATOM 394 CD2 LEU A 72 -29.346 27.885 -9.713 1.00 17.96 C
ANISOU 394 CD2 LEU A 72 2096 3276 1452 565 -388 484 C
ATOM 395 N ILE A 73 -27.528 25.387 -5.662 1.00 16.81 N
ANISOU 395 N ILE A 73 1894 3093 1400 354 -290 216 N
ATOM 396 CA ILE A 73 -28.102 25.343 -4.303 1.00 16.09 C
ANISOU 396 CA ILE A 73 1786 2998 1329 383 -279 154 C
ATOM 397 C ILE A 73 -26.969 25.503 -3.291 1.00 16.93 C
ANISOU 397 C ILE A 73 1932 3041 1462 330 -262 122 C
ATOM 398 O ILE A 73 -27.104 26.282 -2.350 1.00 16.41 O
ANISOU 398 O ILE A 73 1894 2919 1421 359 -258 87 O
ATOM 399 CB ILE A 73 -28.963 24.071 -4.035 1.00 19.27 C
ANISOU 399 CB ILE A 73 2113 3507 1701 372 -271 115 C
ATOM 400 CG1 ILE A 73 -30.204 24.014 -4.966 1.00 19.55 C
ANISOU 400 CG1 ILE A 73 2092 3631 1704 422 -291 133 C
ATOM 401 CG2 ILE A 73 -29.368 23.981 -2.557 1.00 19.53 C
ANISOU 401 CG2 ILE A 73 2131 3545 1745 382 -252 57 C
ATOM 402 CD1 ILE A 73 -30.695 22.590 -5.290 1.00 25.05 C
ANISOU 402 CD1 ILE A 73 2725 4432 2362 364 -283 106 C
ATOM 403 N ILE A 74 -25.845 24.807 -3.509 1.00 11.95 N
ANISOU 403 N ILE A 74 1298 2425 818 258 -253 129 N
ATOM 404 CA ILE A 74 -24.667 24.919 -2.642 1.00 11.57 C
ANISOU 404 CA ILE A 74 1271 2343 783 206 -242 101 C
ATOM 405 C ILE A 74 -24.153 26.379 -2.606 1.00 18.83 C
ANISOU 405 C ILE A 74 2255 3165 1733 192 -246 111 C
ATOM 406 O ILE A 74 -23.928 26.906 -1.522 1.00 19.94 O
ANISOU 406 O ILE A 74 2419 3265 1893 184 -241 63 O
ATOM 407 CB ILE A 74 -23.579 23.874 -3.018 1.00 13.71 C
ANISOU 407 CB ILE A 74 1514 2665 1028 151 -234 108 C
ATOM 408 CG1 ILE A 74 -24.058 22.448 -2.703 1.00 13.72 C
ANISOU 408 CG1 ILE A 74 1477 2727 1009 161 -227 86 C
ATOM 409 CG2 ILE A 74 -22.242 24.166 -2.346 1.00 13.17 C
ANISOU 409 CG2 ILE A 74 1455 2583 964 99 -229 88 C
ATOM 410 CD1 ILE A 74 -23.422 21.367 -3.556 1.00 20.16 C
ANISOU 410 CD1 ILE A 74 2274 3584 1801 136 -221 97 C
ATOM 411 N GLY A 75 -24.031 27.019 -3.774 1.00 16.54 N
ANISOU 411 N GLY A 75 2000 2840 1445 187 -253 174 N
ATOM 412 CA GLY A 75 -23.572 28.402 -3.897 1.00 16.31 C
ANISOU 412 CA GLY A 75 2050 2700 1447 163 -253 199 C
ATOM 413 C GLY A 75 -24.507 29.427 -3.284 1.00 20.27 C
ANISOU 413 C GLY A 75 2606 3107 1988 242 -261 175 C
ATOM 414 O GLY A 75 -24.081 30.252 -2.473 1.00 19.10 O
ANISOU 414 O GLY A 75 2514 2869 1872 213 -253 132 O
ATOM 415 N ALA A 76 -25.794 29.369 -3.661 1.00 17.72 N
ANISOU 415 N ALA A 76 2262 2811 1658 344 -275 195 N
ATOM 416 CA ALA A 76 -26.817 30.300 -3.205 1.00 17.64 C
ANISOU 416 CA ALA A 76 2292 2731 1681 450 -284 173 C
ATOM 417 C ALA A 76 -27.251 30.104 -1.746 1.00 22.57 C
ANISOU 417 C ALA A 76 2883 3381 2312 478 -271 73 C
ATOM 418 O ALA A 76 -27.272 31.079 -0.988 1.00 21.12 O
ANISOU 418 O ALA A 76 2762 3099 2165 507 -265 23 O
ATOM 419 CB ALA A 76 -28.020 30.257 -4.141 1.00 18.21 C
ANISOU 419 CB ALA A 76 2331 2857 1729 554 -307 228 C
ATOM 420 N PHE A 77 -27.593 28.859 -1.354 1.00 21.39 N
ANISOU 420 N PHE A 77 2641 3360 2125 467 -263 42 N
ATOM 421 CA PHE A 77 -28.091 28.550 -0.014 1.00 22.32 C
ANISOU 421 CA PHE A 77 2719 3529 2233 489 -248 -39 C
ATOM 422 C PHE A 77 -27.028 28.115 0.957 1.00 25.65 C
ANISOU 422 C PHE A 77 3140 3962 2644 400 -233 -84 C
ATOM 423 O PHE A 77 -26.729 28.864 1.889 1.00 26.76 O
ANISOU 423 O PHE A 77 3320 4047 2800 397 -226 -145 O
ATOM 424 CB PHE A 77 -29.220 27.510 -0.066 1.00 25.30 C
ANISOU 424 CB PHE A 77 3002 4041 2571 524 -245 -42 C
ATOM 425 CG PHE A 77 -29.998 27.344 1.221 1.00 28.72 C
ANISOU 425 CG PHE A 77 3389 4539 2986 558 -225 -117 C
ATOM 426 CD1 PHE A 77 -29.631 26.378 2.158 1.00 32.72 C
ANISOU 426 CD1 PHE A 77 3864 5108 3459 487 -205 -147 C
ATOM 427 CD2 PHE A 77 -31.132 28.119 1.476 1.00 32.19 C
ANISOU 427 CD2 PHE A 77 3812 4986 3432 670 -225 -154 C
ATOM 428 CE1 PHE A 77 -30.371 26.203 3.336 1.00 34.34 C
ANISOU 428 CE1 PHE A 77 4025 5389 3635 511 -182 -209 C
ATOM 429 CE2 PHE A 77 -31.869 27.949 2.657 1.00 35.44 C
ANISOU 429 CE2 PHE A 77 4170 5481 3816 699 -201 -229 C
ATOM 430 CZ PHE A 77 -31.481 26.994 3.583 1.00 33.71 C
ANISOU 430 CZ PHE A 77 3921 5329 3559 612 -178 -254 C
ATOM 431 N SER A 78 -26.507 26.885 0.788 1.00 20.15 N
ANISOU 431 N SER A 78 2397 3343 1916 337 -230 -60 N
ATOM 432 CA SER A 78 -25.528 26.266 1.687 1.00 19.31 C
ANISOU 432 CA SER A 78 2277 3271 1787 269 -221 -91 C
ATOM 433 C SER A 78 -24.378 27.190 2.082 1.00 22.67 C
ANISOU 433 C SER A 78 2755 3627 2232 215 -224 -119 C
ATOM 434 O SER A 78 -24.201 27.421 3.272 1.00 22.32 O
ANISOU 434 O SER A 78 2713 3592 2177 205 -219 -184 O
ATOM 435 CB SER A 78 -25.012 24.948 1.116 1.00 21.38 C
ANISOU 435 CB SER A 78 2503 3599 2024 226 -221 -48 C
ATOM 436 OG SER A 78 -26.086 24.048 0.898 1.00 24.92 O
ANISOU 436 OG SER A 78 2909 4109 2453 255 -215 -35 O
ATOM 437 N MET A 79 -23.655 27.773 1.103 1.00 18.73 N
ANISOU 437 N MET A 79 2295 3065 1756 173 -231 -74 N
ATOM 438 CA MET A 79 -22.533 28.676 1.365 1.00 18.41 C
ANISOU 438 CA MET A 79 2303 2960 1734 95 -230 -100 C
ATOM 439 C MET A 79 -22.907 29.897 2.207 1.00 21.79 C
ANISOU 439 C MET A 79 2795 3293 2193 118 -227 -169 C
ATOM 440 O MET A 79 -22.190 30.222 3.151 1.00 21.50 O
ANISOU 440 O MET A 79 2765 3257 2147 58 -225 -237 O
ATOM 441 CB MET A 79 -21.889 29.151 0.060 1.00 20.70 C
ANISOU 441 CB MET A 79 2629 3197 2040 43 -232 -29 C
ATOM 442 CG MET A 79 -20.863 28.214 -0.483 1.00 24.53 C
ANISOU 442 CG MET A 79 3055 3775 2489 -22 -230 2 C
ATOM 443 SD MET A 79 -20.039 28.996 -1.881 1.00 28.49 S
ANISOU 443 SD MET A 79 3602 4224 3000 -101 -223 77 S
ATOM 444 CE MET A 79 -19.471 27.612 -2.711 1.00 25.03 C
ANISOU 444 CE MET A 79 3076 3923 2513 -114 -219 112 C
ATOM 445 N ASN A 80 -23.991 30.597 1.835 1.00 18.00 N
ANISOU 445 N ASN A 80 2361 2734 1746 207 -229 -157 N
ATOM 446 CA ASN A 80 -24.412 31.820 2.521 1.00 17.68 C
ANISOU 446 CA ASN A 80 2395 2581 1742 249 -224 -226 C
ATOM 447 C ASN A 80 -24.958 31.561 3.926 1.00 21.68 C
ANISOU 447 C ASN A 80 2858 3160 2220 293 -214 -324 C
ATOM 448 O ASN A 80 -24.686 32.352 4.830 1.00 21.26 O
ANISOU 448 O ASN A 80 2852 3048 2178 274 -207 -413 O
ATOM 449 CB ASN A 80 -25.374 32.622 1.662 1.00 14.92 C
ANISOU 449 CB ASN A 80 2107 2128 1433 352 -232 -177 C
ATOM 450 CG ASN A 80 -24.691 33.172 0.432 1.00 27.31 C
ANISOU 450 CG ASN A 80 3746 3603 3027 291 -238 -84 C
ATOM 451 OD1 ASN A 80 -23.568 33.680 0.489 1.00 14.93 O
ANISOU 451 OD1 ASN A 80 2230 1970 1472 175 -230 -93 O
ATOM 452 ND2 ASN A 80 -25.341 33.069 -0.713 1.00 15.10 N
ANISOU 452 ND2 ASN A 80 2196 2065 1477 360 -252 8 N
ATOM 453 N LEU A 81 -25.651 30.428 4.126 1.00 17.71 N
ANISOU 453 N LEU A 81 2265 2790 1673 335 -210 -312 N
ATOM 454 CA LEU A 81 -26.144 30.040 5.443 1.00 17.55 C
ANISOU 454 CA LEU A 81 2195 2862 1610 363 -196 -390 C
ATOM 455 C LEU A 81 -24.978 29.631 6.364 1.00 19.74 C
ANISOU 455 C LEU A 81 2454 3201 1845 265 -196 -429 C
ATOM 456 O LEU A 81 -24.984 29.983 7.544 1.00 19.15 O
ANISOU 456 O LEU A 81 2381 3151 1744 264 -188 -518 O
ATOM 457 CB LEU A 81 -27.192 28.938 5.321 1.00 18.01 C
ANISOU 457 CB LEU A 81 2170 3040 1632 416 -188 -355 C
ATOM 458 CG LEU A 81 -28.238 28.895 6.429 1.00 24.13 C
ANISOU 458 CG LEU A 81 2901 3898 2371 481 -167 -429 C
ATOM 459 CD1 LEU A 81 -29.112 30.138 6.448 1.00 23.90 C
ANISOU 459 CD1 LEU A 81 2910 3791 2380 590 -163 -485 C
ATOM 460 CD2 LEU A 81 -29.131 27.730 6.230 1.00 29.62 C
ANISOU 460 CD2 LEU A 81 3512 4714 3026 497 -157 -386 C
ATOM 461 N TYR A 82 -23.949 28.953 5.799 1.00 14.57 N
ANISOU 461 N TYR A 82 1778 2576 1181 189 -208 -367 N
ATOM 462 CA TYR A 82 -22.733 28.560 6.502 1.00 13.11 C
ANISOU 462 CA TYR A 82 1567 2462 955 107 -216 -391 C
ATOM 463 C TYR A 82 -21.976 29.796 6.954 1.00 20.04 C
ANISOU 463 C TYR A 82 2499 3264 1851 42 -219 -468 C
ATOM 464 O TYR A 82 -21.473 29.799 8.077 1.00 20.68 O
ANISOU 464 O TYR A 82 2558 3415 1886 3 -223 -539 O
ATOM 465 CB TYR A 82 -21.860 27.643 5.639 1.00 12.98 C
ANISOU 465 CB TYR A 82 1513 2490 929 61 -226 -310 C
ATOM 466 CG TYR A 82 -20.641 27.066 6.334 1.00 13.88 C
ANISOU 466 CG TYR A 82 1581 2703 992 1 -238 -326 C
ATOM 467 CD1 TYR A 82 -20.721 26.571 7.633 1.00 15.74 C
ANISOU 467 CD1 TYR A 82 1782 3032 1167 16 -240 -367 C
ATOM 468 CD2 TYR A 82 -19.425 26.952 5.668 1.00 14.29 C
ANISOU 468 CD2 TYR A 82 1612 2772 1043 -63 -249 -293 C
ATOM 469 CE1 TYR A 82 -19.614 26.017 8.266 1.00 16.30 C
ANISOU 469 CE1 TYR A 82 1806 3207 1182 -23 -258 -372 C
ATOM 470 CE2 TYR A 82 -18.310 26.396 6.290 1.00 15.13 C
ANISOU 470 CE2 TYR A 82 1662 2990 1097 -101 -264 -307 C
ATOM 471 CZ TYR A 82 -18.411 25.925 7.588 1.00 25.22 C
ANISOU 471 CZ TYR A 82 2911 4356 2317 -75 -272 -344 C
ATOM 472 OH TYR A 82 -17.321 25.371 8.208 1.00 27.73 O
ANISOU 472 OH TYR A 82 3168 4794 2574 -98 -294 -349 O
ATOM 473 N THR A 83 -21.963 30.874 6.122 1.00 18.07 N
ANISOU 473 N THR A 83 2329 2873 1665 29 -218 -456 N
ATOM 474 CA THR A 83 -21.313 32.164 6.432 1.00 18.06 C
ANISOU 474 CA THR A 83 2405 2763 1695 -46 -216 -530 C
ATOM 475 C THR A 83 -21.964 32.836 7.630 1.00 22.65 C
ANISOU 475 C THR A 83 3019 3317 2271 2 -207 -648 C
ATOM 476 O THR A 83 -21.251 33.211 8.557 1.00 23.44 O
ANISOU 476 O THR A 83 3122 3441 2343 -75 -209 -740 O
ATOM 477 CB THR A 83 -21.250 33.076 5.200 1.00 24.26 C
ANISOU 477 CB THR A 83 3281 3388 2547 -66 -214 -468 C
ATOM 478 OG1 THR A 83 -20.693 32.340 4.115 1.00 26.58 O
ANISOU 478 OG1 THR A 83 3529 3739 2830 -105 -219 -364 O
ATOM 479 CG2 THR A 83 -20.431 34.346 5.446 1.00 18.47 C
ANISOU 479 CG2 THR A 83 2639 2531 1849 -176 -209 -535 C
ATOM 480 N VAL A 84 -23.312 32.957 7.628 1.00 19.58 N
ANISOU 480 N VAL A 84 2642 2897 1900 130 -196 -652 N
ATOM 481 CA VAL A 84 -24.096 33.530 8.737 1.00 19.46 C
ANISOU 481 CA VAL A 84 2645 2874 1873 202 -181 -769 C
ATOM 482 C VAL A 84 -23.773 32.762 10.026 1.00 24.16 C
ANISOU 482 C VAL A 84 3157 3642 2379 163 -179 -831 C
ATOM 483 O VAL A 84 -23.517 33.396 11.044 1.00 25.07 O
ANISOU 483 O VAL A 84 3297 3757 2471 133 -174 -949 O
ATOM 484 CB VAL A 84 -25.631 33.570 8.456 1.00 22.88 C
ANISOU 484 CB VAL A 84 3071 3295 2327 358 -169 -751 C
ATOM 485 CG1 VAL A 84 -26.393 34.213 9.615 1.00 22.08 C
ANISOU 485 CG1 VAL A 84 2981 3200 2208 439 -149 -885 C
ATOM 486 CG2 VAL A 84 -25.946 34.291 7.144 1.00 22.51 C
ANISOU 486 CG2 VAL A 84 3105 3089 2358 410 -178 -675 C
ATOM 487 N TYR A 85 -23.728 31.410 9.960 1.00 20.75 N
ANISOU 487 N TYR A 85 2636 3354 1895 159 -185 -750 N
ATOM 488 CA TYR A 85 -23.419 30.527 11.089 1.00 20.84 C
ANISOU 488 CA TYR A 85 2573 3533 1815 130 -186 -776 C
ATOM 489 C TYR A 85 -22.023 30.806 11.673 1.00 26.02 C
ANISOU 489 C TYR A 85 3228 4222 2436 18 -206 -831 C
ATOM 490 O TYR A 85 -21.925 30.980 12.882 1.00 25.93 O
ANISOU 490 O TYR A 85 3199 4291 2362 2 -205 -926 O
ATOM 491 CB TYR A 85 -23.625 29.049 10.694 1.00 22.09 C
ANISOU 491 CB TYR A 85 2659 3793 1939 149 -188 -661 C
ATOM 492 CG TYR A 85 -23.555 28.021 11.808 1.00 25.26 C
ANISOU 492 CG TYR A 85 2996 4356 2245 142 -186 -660 C
ATOM 493 CD1 TYR A 85 -23.727 28.388 13.143 1.00 27.80 C
ANISOU 493 CD1 TYR A 85 3307 4754 2501 142 -177 -760 C
ATOM 494 CD2 TYR A 85 -23.397 26.669 11.525 1.00 26.67 C
ANISOU 494 CD2 TYR A 85 3131 4608 2394 140 -191 -557 C
ATOM 495 CE1 TYR A 85 -23.637 27.448 14.172 1.00 28.39 C
ANISOU 495 CE1 TYR A 85 3327 4985 2476 133 -176 -744 C
ATOM 496 CE2 TYR A 85 -23.341 25.715 12.545 1.00 27.81 C
ANISOU 496 CE2 TYR A 85 3232 4885 2449 136 -188 -539 C
ATOM 497 CZ TYR A 85 -23.456 26.112 13.865 1.00 34.55 C
ANISOU 497 CZ TYR A 85 4074 5824 3231 132 -182 -626 C
ATOM 498 OH TYR A 85 -23.395 25.181 14.868 1.00 37.54 O
ANISOU 498 OH TYR A 85 4413 6340 3511 128 -180 -595 O
ATOM 499 N ILE A 86 -20.975 30.928 10.821 1.00 23.90 N
ANISOU 499 N ILE A 86 2974 3902 2205 -63 -223 -782 N
ATOM 500 CA ILE A 86 -19.583 31.237 11.218 1.00 24.37 C
ANISOU 500 CA ILE A 86 3019 4006 2234 -183 -243 -832 C
ATOM 501 C ILE A 86 -19.465 32.647 11.827 1.00 29.71 C
ANISOU 501 C ILE A 86 3772 4584 2932 -238 -236 -969 C
ATOM 502 O ILE A 86 -18.874 32.800 12.902 1.00 28.69 O
ANISOU 502 O ILE A 86 3613 4553 2737 -299 -247 -1066 O
ATOM 503 CB ILE A 86 -18.589 31.061 10.027 1.00 27.24 C
ANISOU 503 CB ILE A 86 3374 4344 2634 -256 -255 -745 C
ATOM 504 CG1 ILE A 86 -18.458 29.592 9.604 1.00 27.40 C
ANISOU 504 CG1 ILE A 86 3313 4478 2619 -210 -264 -634 C
ATOM 505 CG2 ILE A 86 -17.212 31.673 10.328 1.00 27.16 C
ANISOU 505 CG2 ILE A 86 3352 4365 2602 -396 -270 -812 C
ATOM 506 CD1 ILE A 86 -18.084 29.467 8.188 1.00 32.23 C
ANISOU 506 CD1 ILE A 86 3934 5031 3281 -232 -263 -544 C
ATOM 507 N ILE A 87 -20.004 33.666 11.117 1.00 27.64 N
ANISOU 507 N ILE A 87 3613 4128 2760 -215 -219 -977 N
ATOM 508 CA ILE A 87 -19.969 35.068 11.535 1.00 28.17 C
ANISOU 508 CA ILE A 87 3783 4053 2868 -259 -208 -1103 C
ATOM 509 C ILE A 87 -20.708 35.280 12.887 1.00 31.45 C
ANISOU 509 C ILE A 87 4193 4525 3232 -189 -196 -1235 C
ATOM 510 O ILE A 87 -20.121 35.871 13.798 1.00 31.29 O
ANISOU 510 O ILE A 87 4188 4527 3176 -274 -199 -1364 O
ATOM 511 CB ILE A 87 -20.442 36.021 10.389 1.00 31.74 C
ANISOU 511 CB ILE A 87 4357 4273 3429 -226 -194 -1055 C
ATOM 512 CG1 ILE A 87 -19.296 36.217 9.374 1.00 32.14 C
ANISOU 512 CG1 ILE A 87 4431 4269 3513 -363 -203 -978 C
ATOM 513 CG2 ILE A 87 -20.948 37.394 10.923 1.00 33.00 C
ANISOU 513 CG2 ILE A 87 4643 4257 3639 -198 -176 -1187 C
ATOM 514 CD1 ILE A 87 -19.671 36.898 8.080 1.00 42.59 C
ANISOU 514 CD1 ILE A 87 5861 5396 4925 -337 -192 -885 C
ATOM 515 N MET A 88 -21.957 34.773 13.022 1.00 26.65 N
ANISOU 515 N MET A 88 3553 3961 2611 -47 -180 -1208 N
ATOM 516 CA MET A 88 -22.759 34.912 14.247 1.00 25.65 C
ANISOU 516 CA MET A 88 3409 3911 2427 28 -161 -1326 C
ATOM 517 C MET A 88 -22.196 34.129 15.432 1.00 28.19 C
ANISOU 517 C MET A 88 3634 4453 2626 -31 -173 -1366 C
ATOM 518 O MET A 88 -22.490 34.458 16.582 1.00 28.02 O
ANISOU 518 O MET A 88 3605 4502 2541 -15 -161 -1493 O
ATOM 519 CB MET A 88 -24.223 34.529 14.005 1.00 27.89 C
ANISOU 519 CB MET A 88 3664 4212 2720 183 -139 -1277 C
ATOM 520 CG MET A 88 -24.999 35.564 13.227 1.00 31.00 C
ANISOU 520 CG MET A 88 4157 4405 3217 279 -127 -1286 C
ATOM 521 SD MET A 88 -26.769 35.218 13.274 1.00 34.87 S
ANISOU 521 SD MET A 88 4585 4971 3692 466 -100 -1271 S
ATOM 522 CE MET A 88 -27.202 35.950 14.861 1.00 31.39 C
ANISOU 522 CE MET A 88 4151 4585 3191 514 -71 -1476 C
ATOM 523 N GLY A 89 -21.403 33.106 15.138 1.00 23.36 N
ANISOU 523 N GLY A 89 2949 3950 1977 -88 -198 -1256 N
ATOM 524 CA GLY A 89 -20.761 32.270 16.141 1.00 22.46 C
ANISOU 524 CA GLY A 89 2745 4046 1745 -134 -218 -1262 C
ATOM 525 C GLY A 89 -21.662 31.211 16.731 1.00 25.53 C
ANISOU 525 C GLY A 89 3066 4577 2055 -43 -202 -1210 C
ATOM 526 O GLY A 89 -21.200 30.403 17.537 1.00 24.90 O
ANISOU 526 O GLY A 89 2917 4671 1872 -67 -219 -1189 O
ATOM 527 N HIS A 90 -22.954 31.214 16.343 1.00 22.39 N
ANISOU 527 N HIS A 90 2688 4117 1703 58 -171 -1185 N
ATOM 528 CA HIS A 90 -23.973 30.278 16.824 1.00 23.22 C
ANISOU 528 CA HIS A 90 2731 4351 1742 133 -147 -1138 C
ATOM 529 C HIS A 90 -25.185 30.215 15.859 1.00 27.13 C
ANISOU 529 C HIS A 90 3237 4756 2313 225 -123 -1075 C
ATOM 530 O HIS A 90 -25.293 31.049 14.955 1.00 27.08 O
ANISOU 530 O HIS A 90 3296 4587 2407 250 -125 -1085 O
ATOM 531 CB HIS A 90 -24.411 30.656 18.265 1.00 24.62 C
ANISOU 531 CB HIS A 90 2886 4646 1820 151 -125 -1271 C
ATOM 532 CG HIS A 90 -25.285 31.869 18.346 1.00 28.30 C
ANISOU 532 CG HIS A 90 3407 5008 2338 224 -95 -1400 C
ATOM 533 ND1 HIS A 90 -24.802 33.127 18.050 1.00 30.17 N
ANISOU 533 ND1 HIS A 90 3735 5071 2658 197 -104 -1494 N
ATOM 534 CD2 HIS A 90 -26.592 31.968 18.676 1.00 30.35 C
ANISOU 534 CD2 HIS A 90 3642 5315 2576 324 -55 -1446 C
ATOM 535 CE1 HIS A 90 -25.831 33.946 18.183 1.00 29.62 C
ANISOU 535 CE1 HIS A 90 3703 4931 2620 298 -72 -1591 C
ATOM 536 NE2 HIS A 90 -26.928 33.294 18.562 1.00 30.08 N
ANISOU 536 NE2 HIS A 90 3684 5130 2615 382 -42 -1570 N
ATOM 537 N TRP A 91 -26.080 29.222 16.048 1.00 22.95 N
ANISOU 537 N TRP A 91 2647 4341 1734 270 -101 -1007 N
ATOM 538 CA TRP A 91 -27.284 29.059 15.231 1.00 22.17 C
ANISOU 538 CA TRP A 91 2534 4202 1686 349 -78 -955 C
ATOM 539 C TRP A 91 -28.438 29.712 15.978 1.00 27.19 C
ANISOU 539 C TRP A 91 3151 4887 2292 433 -41 -1068 C
ATOM 540 O TRP A 91 -28.791 29.256 17.066 1.00 27.71 O
ANISOU 540 O TRP A 91 3160 5112 2255 429 -16 -1099 O
ATOM 541 CB TRP A 91 -27.565 27.572 14.932 1.00 20.23 C
ANISOU 541 CB TRP A 91 2231 4049 1404 331 -74 -821 C
ATOM 542 CG TRP A 91 -28.723 27.377 13.997 1.00 20.74 C
ANISOU 542 CG TRP A 91 2274 4085 1521 393 -56 -771 C
ATOM 543 CD1 TRP A 91 -30.019 27.122 14.342 1.00 23.61 C
ANISOU 543 CD1 TRP A 91 2577 4551 1842 444 -19 -788 C
ATOM 544 CD2 TRP A 91 -28.711 27.545 12.575 1.00 20.32 C
ANISOU 544 CD2 TRP A 91 2252 3907 1563 412 -75 -708 C
ATOM 545 NE1 TRP A 91 -30.813 27.104 13.222 1.00 22.83 N
ANISOU 545 NE1 TRP A 91 2463 4405 1808 494 -18 -742 N
ATOM 546 CE2 TRP A 91 -30.036 27.351 12.119 1.00 24.19 C
ANISOU 546 CE2 TRP A 91 2694 4435 2062 479 -54 -689 C
ATOM 547 CE3 TRP A 91 -27.704 27.829 11.632 1.00 21.40 C
ANISOU 547 CE3 TRP A 91 2445 3919 1768 375 -108 -664 C
ATOM 548 CZ2 TRP A 91 -30.379 27.418 10.761 1.00 23.14 C
ANISOU 548 CZ2 TRP A 91 2571 4222 2001 514 -69 -627 C
ATOM 549 CZ3 TRP A 91 -28.045 27.903 10.291 1.00 22.69 C
ANISOU 549 CZ3 TRP A 91 2622 3997 2001 407 -118 -599 C
ATOM 550 CH2 TRP A 91 -29.368 27.696 9.867 1.00 23.47 C
ANISOU 550 CH2 TRP A 91 2676 4138 2105 479 -101 -581 C
ATOM 551 N ALA A 92 -28.992 30.811 15.432 1.00 23.71 N
ANISOU 551 N ALA A 92 2760 4315 1935 516 -36 -1131 N
ATOM 552 CA ALA A 92 -30.063 31.566 16.111 1.00 23.49 C
ANISOU 552 CA ALA A 92 2716 4325 1884 619 0 -1256 C
ATOM 553 C ALA A 92 -31.457 31.435 15.480 1.00 25.83 C
ANISOU 553 C ALA A 92 2960 4646 2209 732 21 -1220 C
ATOM 554 O ALA A 92 -32.391 32.118 15.910 1.00 24.94 O
ANISOU 554 O ALA A 92 2830 4555 2089 842 49 -1325 O
ATOM 555 CB ALA A 92 -29.669 33.037 16.221 1.00 24.21 C
ANISOU 555 CB ALA A 92 2909 4255 2036 646 -7 -1387 C
ATOM 556 N LEU A 93 -31.603 30.529 14.503 1.00 22.10 N
ANISOU 556 N LEU A 93 2451 4187 1758 706 9 -1081 N
ATOM 557 CA LEU A 93 -32.839 30.338 13.743 1.00 21.29 C
ANISOU 557 CA LEU A 93 2289 4120 1681 796 21 -1038 C
ATOM 558 C LEU A 93 -33.773 29.209 14.236 1.00 24.43 C
ANISOU 558 C LEU A 93 2566 4730 1985 776 58 -1005 C
ATOM 559 O LEU A 93 -34.876 29.074 13.715 1.00 24.14 O
ANISOU 559 O LEU A 93 2461 4754 1956 843 70 -986 O
ATOM 560 CB LEU A 93 -32.491 30.153 12.263 1.00 21.04 C
ANISOU 560 CB LEU A 93 2297 3964 1734 780 -17 -919 C
ATOM 561 CG LEU A 93 -32.014 31.424 11.545 1.00 26.17 C
ANISOU 561 CG LEU A 93 3058 4403 2481 828 -45 -940 C
ATOM 562 CD1 LEU A 93 -31.654 31.138 10.080 1.00 26.01 C
ANISOU 562 CD1 LEU A 93 3067 4290 2524 798 -78 -812 C
ATOM 563 CD2 LEU A 93 -33.084 32.516 11.585 1.00 30.02 C
ANISOU 563 CD2 LEU A 93 3557 4847 3002 988 -32 -1028 C
ATOM 564 N GLY A 94 -33.364 28.467 15.263 1.00 20.21 N
ANISOU 564 N GLY A 94 2007 4314 1359 685 76 -1003 N
ATOM 565 CA GLY A 94 -34.161 27.380 15.823 1.00 19.05 C
ANISOU 565 CA GLY A 94 1763 4360 1116 642 116 -964 C
ATOM 566 C GLY A 94 -33.801 26.026 15.255 1.00 22.83 C
ANISOU 566 C GLY A 94 2240 4844 1591 537 103 -818 C
ATOM 567 O GLY A 94 -33.145 25.942 14.215 1.00 23.11 O
ANISOU 567 O GLY A 94 2330 4744 1707 519 64 -749 O
ATOM 568 N ALA A 95 -34.216 24.961 15.956 1.00 18.93 N
ANISOU 568 N ALA A 95 1688 4503 1001 464 139 -772 N
ATOM 569 CA ALA A 95 -33.972 23.551 15.647 1.00 18.41 C
ANISOU 569 CA ALA A 95 1628 4450 917 359 138 -638 C
ATOM 570 C ALA A 95 -34.630 23.058 14.366 1.00 23.06 C
ANISOU 570 C ALA A 95 2189 5003 1570 353 133 -573 C
ATOM 571 O ALA A 95 -34.037 22.236 13.667 1.00 24.02 O
ANISOU 571 O ALA A 95 2356 5043 1728 291 109 -479 O
ATOM 572 CB ALA A 95 -34.385 22.674 16.824 1.00 18.73 C
ANISOU 572 CB ALA A 95 1622 4661 831 285 185 -612 C
ATOM 573 N LEU A 96 -35.857 23.512 14.073 1.00 19.80 N
ANISOU 573 N LEU A 96 1695 4665 1162 420 155 -628 N
ATOM 574 CA LEU A 96 -36.558 23.120 12.848 1.00 20.44 C
ANISOU 574 CA LEU A 96 1734 4739 1292 419 146 -578 C
ATOM 575 C LEU A 96 -35.823 23.693 11.640 1.00 23.31 C
ANISOU 575 C LEU A 96 2172 4923 1762 470 90 -555 C
ATOM 576 O LEU A 96 -35.493 22.932 10.733 1.00 24.75 O
ANISOU 576 O LEU A 96 2380 5045 1980 409 70 -472 O
ATOM 577 CB LEU A 96 -38.030 23.572 12.861 1.00 21.11 C
ANISOU 577 CB LEU A 96 1700 4972 1349 495 178 -650 C
ATOM 578 CG LEU A 96 -39.073 22.480 12.770 1.00 26.77 C
ANISOU 578 CG LEU A 96 2318 5847 2007 401 216 -606 C
ATOM 579 CD1 LEU A 96 -39.520 22.046 14.122 1.00 25.89 C
ANISOU 579 CD1 LEU A 96 2151 5904 1782 333 277 -627 C
ATOM 580 CD2 LEU A 96 -40.260 22.954 12.003 1.00 31.85 C
ANISOU 580 CD2 LEU A 96 2853 6579 2669 491 214 -651 C
ATOM 581 N ALA A 97 -35.500 25.010 11.669 1.00 16.76 N
ANISOU 581 N ALA A 97 1386 4002 979 572 69 -628 N
ATOM 582 CA ALA A 97 -34.751 25.705 10.628 1.00 15.90 C
ANISOU 582 CA ALA A 97 1359 3719 965 614 21 -605 C
ATOM 583 C ALA A 97 -33.384 25.037 10.420 1.00 21.00 C
ANISOU 583 C ALA A 97 2079 4274 1626 513 -3 -528 C
ATOM 584 O ALA A 97 -32.926 24.919 9.281 1.00 20.39 O
ANISOU 584 O ALA A 97 2038 4103 1607 500 -34 -466 O
ATOM 585 CB ALA A 97 -34.569 27.170 11.004 1.00 16.28 C
ANISOU 585 CB ALA A 97 1459 3680 1048 715 13 -702 C
ATOM 586 N CYS A 98 -32.772 24.554 11.523 1.00 18.13 N
ANISOU 586 N CYS A 98 1730 3957 1201 447 11 -533 N
ATOM 587 CA CYS A 98 -31.495 23.860 11.557 1.00 18.55 C
ANISOU 587 CA CYS A 98 1840 3957 1251 367 -10 -468 C
ATOM 588 C CYS A 98 -31.591 22.534 10.798 1.00 22.56 C
ANISOU 588 C CYS A 98 2339 4468 1763 302 -10 -366 C
ATOM 589 O CYS A 98 -30.842 22.330 9.839 1.00 20.62 O
ANISOU 589 O CYS A 98 2136 4126 1573 286 -41 -315 O
ATOM 590 CB CYS A 98 -31.043 23.654 13.004 1.00 19.55 C
ANISOU 590 CB CYS A 98 1968 4168 1292 329 5 -496 C
ATOM 591 SG CYS A 98 -29.639 22.521 13.207 1.00 23.86 S
ANISOU 591 SG CYS A 98 2562 4694 1809 246 -20 -400 S
ATOM 592 N ASP A 99 -32.520 21.646 11.225 1.00 20.39 N
ANISOU 592 N ASP A 99 2011 4307 1429 258 27 -342 N
ATOM 593 CA ASP A 99 -32.736 20.320 10.635 1.00 20.81 C
ANISOU 593 CA ASP A 99 2064 4363 1480 180 35 -256 C
ATOM 594 C ASP A 99 -33.116 20.376 9.161 1.00 22.18 C
ANISOU 594 C ASP A 99 2223 4484 1722 199 14 -242 C
ATOM 595 O ASP A 99 -32.634 19.542 8.390 1.00 20.97 O
ANISOU 595 O ASP A 99 2108 4265 1596 151 0 -180 O
ATOM 596 CB ASP A 99 -33.751 19.501 11.460 1.00 24.12 C
ANISOU 596 CB ASP A 99 2430 4919 1816 114 86 -242 C
ATOM 597 CG ASP A 99 -33.217 18.987 12.808 1.00 40.43 C
ANISOU 597 CG ASP A 99 4526 7035 3799 70 104 -217 C
ATOM 598 OD1 ASP A 99 -32.274 19.602 13.352 1.00 41.51 O
ANISOU 598 OD1 ASP A 99 4700 7140 3933 112 80 -246 O
ATOM 599 OD2 ASP A 99 -33.758 17.980 13.321 1.00 48.42 O
ANISOU 599 OD2 ASP A 99 5525 8127 4746 -11 144 -166 O
ATOM 600 N LEU A 100 -33.933 21.385 8.756 1.00 17.88 N
ANISOU 600 N LEU A 100 1626 3967 1199 281 11 -300 N
ATOM 601 CA LEU A 100 -34.333 21.587 7.350 1.00 16.60 C
ANISOU 601 CA LEU A 100 1445 3773 1091 315 -14 -285 C
ATOM 602 C LEU A 100 -33.153 22.086 6.482 1.00 20.13 C
ANISOU 602 C LEU A 100 1971 4072 1604 341 -57 -257 C
ATOM 603 O LEU A 100 -33.028 21.660 5.342 1.00 19.68 O
ANISOU 603 O LEU A 100 1923 3978 1576 319 -77 -211 O
ATOM 604 CB LEU A 100 -35.552 22.525 7.227 1.00 16.27 C
ANISOU 604 CB LEU A 100 1322 3813 1045 414 -9 -347 C
ATOM 605 CG LEU A 100 -36.856 22.100 7.949 1.00 20.22 C
ANISOU 605 CG LEU A 100 1714 4494 1473 389 37 -381 C
ATOM 606 CD1 LEU A 100 -37.902 23.196 7.893 1.00 19.08 C
ANISOU 606 CD1 LEU A 100 1490 4433 1329 520 37 -454 C
ATOM 607 CD2 LEU A 100 -37.408 20.783 7.412 1.00 22.79 C
ANISOU 607 CD2 LEU A 100 1997 4888 1775 275 50 -329 C
ATOM 608 N ALA A 101 -32.283 22.970 7.030 1.00 16.88 N
ANISOU 608 N ALA A 101 1616 3588 1211 376 -69 -289 N
ATOM 609 CA ALA A 101 -31.090 23.510 6.350 1.00 16.04 C
ANISOU 609 CA ALA A 101 1581 3353 1160 381 -103 -266 C
ATOM 610 C ALA A 101 -30.021 22.440 6.189 1.00 19.82 C
ANISOU 610 C ALA A 101 2094 3805 1632 301 -111 -207 C
ATOM 611 O ALA A 101 -29.318 22.441 5.181 1.00 20.98 O
ANISOU 611 O ALA A 101 2274 3880 1818 291 -134 -170 O
ATOM 612 CB ALA A 101 -30.523 24.685 7.123 1.00 16.45 C
ANISOU 612 CB ALA A 101 1677 3350 1224 419 -108 -330 C
ATOM 613 N LEU A 102 -29.895 21.529 7.178 1.00 14.72 N
ANISOU 613 N LEU A 102 1441 3218 932 250 -90 -195 N
ATOM 614 CA LEU A 102 -28.955 20.412 7.122 1.00 13.30 C
ANISOU 614 CA LEU A 102 1297 3014 742 194 -96 -136 C
ATOM 615 C LEU A 102 -29.406 19.446 6.018 1.00 16.12 C
ANISOU 615 C LEU A 102 1647 3361 1118 161 -93 -90 C
ATOM 616 O LEU A 102 -28.580 19.014 5.204 1.00 14.79 O
ANISOU 616 O LEU A 102 1512 3131 978 148 -111 -55 O
ATOM 617 CB LEU A 102 -28.846 19.695 8.478 1.00 12.65 C
ANISOU 617 CB LEU A 102 1217 2999 591 160 -75 -124 C
ATOM 618 CG LEU A 102 -28.035 20.413 9.568 1.00 15.73 C
ANISOU 618 CG LEU A 102 1619 3407 949 177 -86 -165 C
ATOM 619 CD1 LEU A 102 -28.357 19.842 10.930 1.00 14.95 C
ANISOU 619 CD1 LEU A 102 1507 3408 765 152 -59 -159 C
ATOM 620 CD2 LEU A 102 -26.532 20.363 9.290 1.00 14.84 C
ANISOU 620 CD2 LEU A 102 1544 3236 857 172 -120 -141 C
ATOM 621 N ALA A 103 -30.737 19.175 5.961 1.00 11.86 N
ANISOU 621 N ALA A 103 1056 2893 558 147 -69 -101 N
ATOM 622 CA ALA A 103 -31.378 18.339 4.950 1.00 10.68 C
ANISOU 622 CA ALA A 103 844 2709 506 105 -48 -73 C
ATOM 623 C ALA A 103 -31.100 18.906 3.557 1.00 15.57 C
ANISOU 623 C ALA A 103 1512 3319 1085 144 -98 -73 C
ATOM 624 O ALA A 103 -30.614 18.150 2.716 1.00 15.60 O
ANISOU 624 O ALA A 103 1544 3280 1104 108 -107 -43 O
ATOM 625 CB ALA A 103 -32.874 18.251 5.202 1.00 11.00 C
ANISOU 625 CB ALA A 103 826 2884 472 87 -31 -102 C
ATOM 626 N LEU A 104 -31.299 20.241 3.333 1.00 11.93 N
ANISOU 626 N LEU A 104 1034 2851 647 221 -116 -102 N
ATOM 627 CA LEU A 104 -31.014 20.851 2.028 1.00 12.05 C
ANISOU 627 CA LEU A 104 1064 2814 701 257 -147 -83 C
ATOM 628 C LEU A 104 -29.538 20.715 1.628 1.00 17.08 C
ANISOU 628 C LEU A 104 1763 3365 1361 233 -162 -52 C
ATOM 629 O LEU A 104 -29.241 20.299 0.517 1.00 18.86 O
ANISOU 629 O LEU A 104 1996 3574 1595 214 -174 -24 O
ATOM 630 CB LEU A 104 -31.504 22.308 1.937 1.00 12.13 C
ANISOU 630 CB LEU A 104 1064 2814 733 350 -162 -109 C
ATOM 631 CG LEU A 104 -31.375 23.012 0.560 1.00 17.08 C
ANISOU 631 CG LEU A 104 1709 3391 1389 394 -194 -73 C
ATOM 632 CD1 LEU A 104 -31.916 22.153 -0.587 1.00 16.73 C
ANISOU 632 CD1 LEU A 104 1620 3414 1323 363 -203 -46 C
ATOM 633 CD2 LEU A 104 -32.107 24.337 0.549 1.00 19.62 C
ANISOU 633 CD2 LEU A 104 2026 3702 1729 500 -207 -93 C
ATOM 634 N ASP A 105 -28.637 20.983 2.552 1.00 13.35 N
ANISOU 634 N ASP A 105 1325 2858 890 229 -160 -62 N
ATOM 635 CA ASP A 105 -27.198 20.911 2.375 1.00 12.98 C
ANISOU 635 CA ASP A 105 1319 2757 856 207 -174 -42 C
ATOM 636 C ASP A 105 -26.692 19.513 2.010 1.00 16.91 C
ANISOU 636 C ASP A 105 1826 3257 1341 167 -169 -9 C
ATOM 637 O ASP A 105 -25.930 19.400 1.065 1.00 18.67 O
ANISOU 637 O ASP A 105 2063 3453 1580 161 -180 10 O
ATOM 638 CB ASP A 105 -26.519 21.433 3.657 1.00 15.15 C
ANISOU 638 CB ASP A 105 1610 3026 1118 208 -173 -73 C
ATOM 639 CG ASP A 105 -25.014 21.547 3.585 1.00 25.06 C
ANISOU 639 CG ASP A 105 2891 4251 2381 185 -189 -63 C
ATOM 640 OD1 ASP A 105 -24.492 21.832 2.491 1.00 26.11 O
ANISOU 640 OD1 ASP A 105 3034 4347 2541 177 -201 -41 O
ATOM 641 OD2 ASP A 105 -24.364 21.378 4.626 1.00 32.47 O
ANISOU 641 OD2 ASP A 105 3830 5217 3290 173 -191 -77 O
ATOM 642 N TYR A 106 -27.093 18.460 2.757 1.00 12.22 N
ANISOU 642 N TYR A 106 1232 2694 718 140 -149 -2 N
ATOM 643 CA TYR A 106 -26.667 17.065 2.544 1.00 10.39 C
ANISOU 643 CA TYR A 106 994 2398 556 108 -111 25 C
ATOM 644 C TYR A 106 -27.298 16.422 1.308 1.00 12.98 C
ANISOU 644 C TYR A 106 1351 2765 817 81 -137 29 C
ATOM 645 O TYR A 106 -26.631 15.674 0.613 1.00 12.14 O
ANISOU 645 O TYR A 106 1272 2621 719 74 -140 40 O
ATOM 646 CB TYR A 106 -26.904 16.215 3.811 1.00 10.28 C
ANISOU 646 CB TYR A 106 992 2399 513 83 -94 42 C
ATOM 647 CG TYR A 106 -25.825 16.419 4.853 1.00 11.63 C
ANISOU 647 CG TYR A 106 1223 2622 575 111 -132 56 C
ATOM 648 CD1 TYR A 106 -25.842 17.527 5.698 1.00 13.51 C
ANISOU 648 CD1 TYR A 106 1437 2900 797 130 -137 21 C
ATOM 649 CD2 TYR A 106 -24.758 15.535 4.961 1.00 11.91 C
ANISOU 649 CD2 TYR A 106 1296 2627 603 126 -141 93 C
ATOM 650 CE1 TYR A 106 -24.826 17.743 6.626 1.00 14.15 C
ANISOU 650 CE1 TYR A 106 1524 3002 849 146 -152 20 C
ATOM 651 CE2 TYR A 106 -23.741 15.737 5.889 1.00 12.32 C
ANISOU 651 CE2 TYR A 106 1349 2708 624 156 -159 101 C
ATOM 652 CZ TYR A 106 -23.774 16.846 6.715 1.00 19.51 C
ANISOU 652 CZ TYR A 106 2229 3670 1514 158 -165 63 C
ATOM 653 OH TYR A 106 -22.769 17.029 7.637 1.00 18.89 O
ANISOU 653 OH TYR A 106 2144 3638 1396 178 -186 62 O
ATOM 654 N VAL A 107 -28.580 16.695 1.052 1.00 10.50 N
ANISOU 654 N VAL A 107 917 2410 660 68 -67 7 N
ATOM 655 CA VAL A 107 -29.323 16.190 -0.107 1.00 9.91 C
ANISOU 655 CA VAL A 107 796 2329 640 35 -43 -1 C
ATOM 656 C VAL A 107 -28.716 16.753 -1.398 1.00 14.98 C
ANISOU 656 C VAL A 107 1538 3075 1080 68 -156 5 C
ATOM 657 O VAL A 107 -28.499 15.976 -2.324 1.00 14.87 O
ANISOU 657 O VAL A 107 1538 3049 1064 40 -156 1 O
ATOM 658 CB VAL A 107 -30.847 16.462 0.022 1.00 12.91 C
ANISOU 658 CB VAL A 107 1206 2920 777 21 -120 -24 C
ATOM 659 CG1 VAL A 107 -31.596 16.176 -1.280 1.00 12.62 C
ANISOU 659 CG1 VAL A 107 1130 2935 732 -7 -131 -40 C
ATOM 660 CG2 VAL A 107 -31.443 15.658 1.175 1.00 12.29 C
ANISOU 660 CG2 VAL A 107 1127 2872 670 -38 -85 -24 C
ATOM 661 N ALA A 108 -28.387 18.074 -1.440 1.00 12.14 N
ANISOU 661 N ALA A 108 1171 2706 735 122 -175 12 N
ATOM 662 CA ALA A 108 -27.766 18.716 -2.612 1.00 12.08 C
ANISOU 662 CA ALA A 108 1171 2681 738 144 -195 31 C
ATOM 663 C ALA A 108 -26.333 18.214 -2.864 1.00 16.50 C
ANISOU 663 C ALA A 108 1766 3201 1303 129 -193 41 C
ATOM 664 O ALA A 108 -25.988 17.923 -4.004 1.00 17.12 O
ANISOU 664 O ALA A 108 1843 3289 1372 120 -198 46 O
ATOM 665 CB ALA A 108 -27.786 20.230 -2.469 1.00 12.77 C
ANISOU 665 CB ALA A 108 1261 2747 843 195 -211 41 C
ATOM 666 N SER A 109 -25.522 18.073 -1.795 1.00 13.38 N
ANISOU 666 N SER A 109 1394 2778 914 132 -187 41 N
ATOM 667 CA SER A 109 -24.145 17.559 -1.846 1.00 12.34 C
ANISOU 667 CA SER A 109 1280 2627 781 133 -187 47 C
ATOM 668 C SER A 109 -24.098 16.105 -2.340 1.00 17.02 C
ANISOU 668 C SER A 109 1892 3210 1365 121 -174 40 C
ATOM 669 O SER A 109 -23.190 15.744 -3.094 1.00 17.40 O
ANISOU 669 O SER A 109 1943 3257 1410 132 -175 36 O
ATOM 670 CB SER A 109 -23.498 17.651 -0.473 1.00 13.00 C
ANISOU 670 CB SER A 109 1374 2705 861 144 -188 47 C
ATOM 671 OG SER A 109 -23.469 18.998 -0.032 1.00 17.20 O
ANISOU 671 OG SER A 109 1898 3236 1403 148 -197 38 O
ATOM 672 N ASN A 110 -25.076 15.280 -1.917 1.00 13.01 N
ANISOU 672 N ASN A 110 1397 2694 852 95 -160 33 N
ATOM 673 CA ASN A 110 -25.194 13.884 -2.327 1.00 12.69 C
ANISOU 673 CA ASN A 110 1391 2621 809 69 -144 20 C
ATOM 674 C ASN A 110 -25.713 13.810 -3.759 1.00 17.53 C
ANISOU 674 C ASN A 110 1982 3265 1414 44 -147 -9 C
ATOM 675 O ASN A 110 -25.276 12.948 -4.520 1.00 17.96 O
ANISOU 675 O ASN A 110 2062 3295 1465 40 -140 -33 O
ATOM 676 CB ASN A 110 -26.117 13.131 -1.378 1.00 9.90 C
ANISOU 676 CB ASN A 110 1044 2231 485 26 -113 25 C
ATOM 677 CG ASN A 110 -25.973 11.640 -1.440 1.00 24.54 C
ANISOU 677 CG ASN A 110 2985 4034 2307 3 -105 24 C
ATOM 678 OD1 ASN A 110 -25.270 11.033 -0.636 1.00 23.21 O
ANISOU 678 OD1 ASN A 110 2868 3813 2139 33 -100 54 O
ATOM 679 ND2 ASN A 110 -26.657 11.010 -2.376 1.00 15.37 N
ANISOU 679 ND2 ASN A 110 1829 2866 1144 -51 -95 -13 N
ATOM 680 N ALA A 111 -26.618 14.729 -4.142 1.00 14.60 N
ANISOU 680 N ALA A 111 1562 2951 1033 36 -160 -9 N
ATOM 681 CA ALA A 111 -27.167 14.777 -5.501 1.00 14.55 C
ANISOU 681 CA ALA A 111 1523 2999 1005 18 -170 -28 C
ATOM 682 C ALA A 111 -26.069 15.142 -6.486 1.00 18.97 C
ANISOU 682 C ALA A 111 2086 3565 1557 47 -179 -21 C
ATOM 683 O ALA A 111 -26.135 14.721 -7.639 1.00 19.34 O
ANISOU 683 O ALA A 111 2123 3648 1577 29 -180 -46 O
ATOM 684 CB ALA A 111 -28.310 15.775 -5.594 1.00 14.88 C
ANISOU 684 CB ALA A 111 1510 3108 1034 29 -187 -18 C
ATOM 685 N ALA A 112 -25.050 15.908 -6.029 1.00 14.33 N
ANISOU 685 N ALA A 112 1505 2954 984 82 -184 10 N
ATOM 686 CA ALA A 112 -23.915 16.286 -6.873 1.00 13.39 C
ANISOU 686 CA ALA A 112 1381 2854 853 96 -186 20 C
ATOM 687 C ALA A 112 -23.041 15.051 -7.171 1.00 18.07 C
ANISOU 687 C ALA A 112 1993 3434 1440 104 -169 -16 C
ATOM 688 O ALA A 112 -22.703 14.823 -8.337 1.00 18.35 O
ANISOU 688 O ALA A 112 2016 3511 1446 101 -165 -36 O
ATOM 689 CB ALA A 112 -23.109 17.399 -6.226 1.00 13.33 C
ANISOU 689 CB ALA A 112 1372 2829 862 112 -193 53 C
ATOM 690 N VAL A 113 -22.767 14.211 -6.134 1.00 14.50 N
ANISOU 690 N VAL A 113 1575 2925 1009 120 -160 -24 N
ATOM 691 CA VAL A 113 -21.984 12.960 -6.189 1.00 13.92 C
ANISOU 691 CA VAL A 113 1536 2815 938 150 -145 -54 C
ATOM 692 C VAL A 113 -22.708 11.950 -7.077 1.00 20.67 C
ANISOU 692 C VAL A 113 2417 3654 1783 117 -132 -104 C
ATOM 693 O VAL A 113 -22.081 11.275 -7.898 1.00 20.18 O
ANISOU 693 O VAL A 113 2366 3593 1708 140 -121 -147 O
ATOM 694 CB VAL A 113 -21.705 12.367 -4.781 1.00 17.16 C
ANISOU 694 CB VAL A 113 1988 3163 1369 180 -142 -33 C
ATOM 695 CG1 VAL A 113 -20.906 11.071 -4.880 1.00 16.82 C
ANISOU 695 CG1 VAL A 113 1991 3069 1330 233 -129 -57 C
ATOM 696 CG2 VAL A 113 -20.991 13.375 -3.863 1.00 16.81 C
ANISOU 696 CG2 VAL A 113 1911 3151 1325 204 -157 3 C
ATOM 697 N MET A 114 -24.035 11.875 -6.929 1.00 19.71 N
ANISOU 697 N MET A 114 2298 3529 1662 61 -132 -108 N
ATOM 698 CA MET A 114 -24.865 10.968 -7.713 1.00 20.25 C
ANISOU 698 CA MET A 114 2385 3594 1717 5 -122 -163 C
ATOM 699 C MET A 114 -24.962 11.379 -9.172 1.00 20.68 C
ANISOU 699 C MET A 114 2390 3740 1728 -6 -132 -193 C
ATOM 700 O MET A 114 -25.141 10.513 -10.022 1.00 20.02 O
ANISOU 700 O MET A 114 2324 3659 1625 -37 -122 -257 O
ATOM 701 CB MET A 114 -26.237 10.799 -7.067 1.00 23.65 C
ANISOU 701 CB MET A 114 2815 4020 2152 -63 -118 -159 C
ATOM 702 CG MET A 114 -26.175 9.997 -5.793 1.00 28.82 C
ANISOU 702 CG MET A 114 3536 4579 2836 -69 -99 -137 C
ATOM 703 SD MET A 114 -27.782 9.276 -5.454 1.00 35.43 S
ANISOU 703 SD MET A 114 4381 5416 3666 -185 -80 -157 S
ATOM 704 CE MET A 114 -27.504 7.620 -6.040 1.00 32.50 C
ANISOU 704 CE MET A 114 4107 4936 3307 -231 -54 -221 C
ATOM 705 N ASN A 115 -24.806 12.688 -9.462 1.00 16.24 N
ANISOU 705 N ASN A 115 1775 3248 1149 16 -152 -145 N
ATOM 706 CA ASN A 115 -24.824 13.228 -10.821 1.00 16.36 C
ANISOU 706 CA ASN A 115 1747 3358 1113 11 -164 -149 C
ATOM 707 C ASN A 115 -23.513 12.968 -11.548 1.00 19.22 C
ANISOU 707 C ASN A 115 2112 3739 1453 43 -149 -172 C
ATOM 708 O ASN A 115 -23.529 12.710 -12.757 1.00 18.77 O
ANISOU 708 O ASN A 115 2035 3752 1345 27 -146 -212 O
ATOM 709 CB ASN A 115 -25.228 14.698 -10.850 1.00 16.69 C
ANISOU 709 CB ASN A 115 1747 3449 1144 24 -189 -80 C
ATOM 710 CG ASN A 115 -26.727 14.863 -10.873 1.00 41.56 C
ANISOU 710 CG ASN A 115 4866 6644 4281 -1 -207 -81 C
ATOM 711 OD1 ASN A 115 -27.436 14.246 -11.680 1.00 30.87 O
ANISOU 711 OD1 ASN A 115 3489 5350 2887 -41 -211 -129 O
ATOM 712 ND2 ASN A 115 -27.253 15.707 -9.998 1.00 37.48 N
ANISOU 712 ND2 ASN A 115 4339 6111 3792 23 -219 -37 N
ATOM 713 N LEU A 116 -22.385 12.984 -10.792 1.00 13.56 N
ANISOU 713 N LEU A 116 1410 2975 767 88 -139 -153 N
ATOM 714 CA LEU A 116 -21.057 12.667 -11.300 1.00 12.31 C
ANISOU 714 CA LEU A 116 1241 2847 589 129 -121 -180 C
ATOM 715 C LEU A 116 -21.039 11.192 -11.671 1.00 15.48 C
ANISOU 715 C LEU A 116 1685 3205 990 143 -101 -265 C
ATOM 716 O LEU A 116 -20.410 10.832 -12.658 1.00 16.33 O
ANISOU 716 O LEU A 116 1777 3369 1059 163 -86 -317 O
ATOM 717 CB LEU A 116 -19.957 12.959 -10.251 1.00 12.26 C
ANISOU 717 CB LEU A 116 1231 2813 615 175 -120 -144 C
ATOM 718 CG LEU A 116 -19.667 14.411 -9.927 1.00 16.79 C
ANISOU 718 CG LEU A 116 1768 3423 1188 155 -134 -77 C
ATOM 719 CD1 LEU A 116 -18.867 14.522 -8.661 1.00 17.30 C
ANISOU 719 CD1 LEU A 116 1834 3456 1285 187 -137 -57 C
ATOM 720 CD2 LEU A 116 -18.937 15.110 -11.066 1.00 19.95 C
ANISOU 720 CD2 LEU A 116 2120 3922 1537 138 -124 -65 C
ATOM 721 N LEU A 117 -21.741 10.344 -10.889 1.00 11.98 N
ANISOU 721 N LEU A 117 1303 2661 589 128 -99 -281 N
ATOM 722 CA LEU A 117 -21.859 8.903 -11.135 1.00 12.05 C
ANISOU 722 CA LEU A 117 1379 2593 608 128 -78 -361 C
ATOM 723 C LEU A 117 -22.666 8.644 -12.415 1.00 17.04 C
ANISOU 723 C LEU A 117 1996 3287 1192 62 -76 -431 C
ATOM 724 O LEU A 117 -22.307 7.753 -13.194 1.00 17.33 O
ANISOU 724 O LEU A 117 2060 3316 1210 77 -57 -517 O
ATOM 725 CB LEU A 117 -22.478 8.161 -9.934 1.00 11.50 C
ANISOU 725 CB LEU A 117 1385 2395 590 108 -73 -344 C
ATOM 726 CG LEU A 117 -21.564 7.868 -8.735 1.00 15.25 C
ANISOU 726 CG LEU A 117 1900 2792 1103 189 -71 -298 C
ATOM 727 CD1 LEU A 117 -22.402 7.507 -7.488 1.00 15.12 C
ANISOU 727 CD1 LEU A 117 1939 2687 1120 147 -70 -250 C
ATOM 728 CD2 LEU A 117 -20.561 6.753 -9.040 1.00 14.36 C
ANISOU 728 CD2 LEU A 117 1844 2611 1000 274 -52 -355 C
ATOM 729 N LEU A 118 -23.729 9.446 -12.643 1.00 13.03 N
ANISOU 729 N LEU A 118 1440 2854 659 -3 -98 -399 N
ATOM 730 CA LEU A 118 -24.545 9.374 -13.859 1.00 12.80 C
ANISOU 730 CA LEU A 118 1375 2921 568 -65 -106 -455 C
ATOM 731 C LEU A 118 -23.730 9.793 -15.101 1.00 17.31 C
ANISOU 731 C LEU A 118 1899 3606 1072 -32 -104 -472 C
ATOM 732 O LEU A 118 -23.831 9.121 -16.117 1.00 17.39 O
ANISOU 732 O LEU A 118 1912 3662 1035 -56 -94 -561 O
ATOM 733 CB LEU A 118 -25.824 10.225 -13.738 1.00 12.75 C
ANISOU 733 CB LEU A 118 1314 2985 545 -115 -136 -403 C
ATOM 734 CG LEU A 118 -26.921 9.745 -12.766 1.00 16.52 C
ANISOU 734 CG LEU A 118 1816 3399 1064 -175 -135 -406 C
ATOM 735 CD1 LEU A 118 -28.029 10.783 -12.657 1.00 15.80 C
ANISOU 735 CD1 LEU A 118 1650 3404 950 -194 -165 -352 C
ATOM 736 CD2 LEU A 118 -27.513 8.415 -13.201 1.00 18.25 C
ANISOU 736 CD2 LEU A 118 2076 3586 1273 -258 -117 -509 C
ATOM 737 N ILE A 119 -22.902 10.869 -15.007 1.00 14.34 N
ANISOU 737 N ILE A 119 1483 3277 689 14 -110 -391 N
ATOM 738 CA ILE A 119 -22.035 11.355 -16.097 1.00 14.14 C
ANISOU 738 CA ILE A 119 1409 3368 595 35 -102 -389 C
ATOM 739 C ILE A 119 -21.051 10.245 -16.510 1.00 20.73 C
ANISOU 739 C ILE A 119 2267 4190 1421 80 -67 -487 C
ATOM 740 O ILE A 119 -20.950 9.941 -17.708 1.00 21.44 O
ANISOU 740 O ILE A 119 2335 4375 1439 68 -56 -556 O
ATOM 741 CB ILE A 119 -21.292 12.684 -15.733 1.00 16.57 C
ANISOU 741 CB ILE A 119 1683 3705 909 58 -108 -283 C
ATOM 742 CG1 ILE A 119 -22.277 13.860 -15.610 1.00 16.74 C
ANISOU 742 CG1 ILE A 119 1688 3745 929 27 -142 -194 C
ATOM 743 CG2 ILE A 119 -20.169 13.018 -16.753 1.00 16.80 C
ANISOU 743 CG2 ILE A 119 1666 3851 868 70 -87 -285 C
ATOM 744 CD1 ILE A 119 -21.773 15.105 -14.826 1.00 21.82 C
ANISOU 744 CD1 ILE A 119 2327 4354 1608 42 -149 -97 C
ATOM 745 N SER A 120 -20.351 9.642 -15.503 1.00 16.67 N
ANISOU 745 N SER A 120 1796 3563 973 140 -53 -494 N
ATOM 746 CA SER A 120 -19.361 8.568 -15.627 1.00 15.94 C
ANISOU 746 CA SER A 120 1735 3432 890 215 -23 -578 C
ATOM 747 C SER A 120 -19.913 7.305 -16.261 1.00 20.30 C
ANISOU 747 C SER A 120 2349 3931 1434 195 -7 -698 C
ATOM 748 O SER A 120 -19.306 6.806 -17.209 1.00 20.39 O
ANISOU 748 O SER A 120 2349 4002 1397 231 17 -788 O
ATOM 749 CB SER A 120 -18.753 8.243 -14.268 1.00 19.04 C
ANISOU 749 CB SER A 120 2168 3709 1357 286 -22 -540 C
ATOM 750 OG SER A 120 -18.253 9.428 -13.676 1.00 28.73 O
ANISOU 750 OG SER A 120 3337 4992 2588 290 -37 -444 O
ATOM 751 N PHE A 121 -21.061 6.794 -15.760 1.00 17.71 N
ANISOU 751 N PHE A 121 2082 3500 1146 129 -18 -708 N
ATOM 752 CA PHE A 121 -21.720 5.590 -16.286 1.00 18.12 C
ANISOU 752 CA PHE A 121 2203 3487 1196 80 -3 -826 C
ATOM 753 C PHE A 121 -22.220 5.773 -17.721 1.00 23.76 C
ANISOU 753 C PHE A 121 2858 4353 1815 14 -7 -896 C
ATOM 754 O PHE A 121 -22.029 4.871 -18.540 1.00 24.45 O
ANISOU 754 O PHE A 121 2979 4439 1872 18 16 -1021 O
ATOM 755 CB PHE A 121 -22.861 5.130 -15.374 1.00 19.64 C
ANISOU 755 CB PHE A 121 2463 3553 1447 0 -10 -808 C
ATOM 756 CG PHE A 121 -22.444 4.167 -14.290 1.00 20.44 C
ANISOU 756 CG PHE A 121 2673 3463 1630 56 9 -804 C
ATOM 757 CD1 PHE A 121 -22.342 2.802 -14.551 1.00 22.10 C
ANISOU 757 CD1 PHE A 121 2991 3543 1865 65 37 -911 C
ATOM 758 CD2 PHE A 121 -22.179 4.618 -13.001 1.00 21.43 C
ANISOU 758 CD2 PHE A 121 2802 3537 1804 100 -2 -691 C
ATOM 759 CE1 PHE A 121 -21.961 1.910 -13.546 1.00 22.38 C
ANISOU 759 CE1 PHE A 121 3141 3390 1973 127 53 -891 C
ATOM 760 CE2 PHE A 121 -21.797 3.725 -11.996 1.00 23.84 C
ANISOU 760 CE2 PHE A 121 3210 3676 2172 158 12 -674 C
ATOM 761 CZ PHE A 121 -21.691 2.376 -12.277 1.00 21.86 C
ANISOU 761 CZ PHE A 121 3071 3289 1947 175 38 -766 C
ATOM 762 N ASP A 122 -22.838 6.939 -18.029 1.00 19.94 N
ANISOU 762 N ASP A 122 2292 4003 1282 -36 -38 -817 N
ATOM 763 CA ASP A 122 -23.332 7.280 -19.369 1.00 19.62 C
ANISOU 763 CA ASP A 122 2185 4133 1136 -91 -51 -857 C
ATOM 764 C ASP A 122 -22.160 7.288 -20.357 1.00 26.70 C
ANISOU 764 C ASP A 122 3047 5133 1963 -30 -25 -905 C
ATOM 765 O ASP A 122 -22.244 6.664 -21.413 1.00 27.29 O
ANISOU 765 O ASP A 122 3119 5280 1968 -55 -12 -1022 O
ATOM 766 CB ASP A 122 -24.010 8.651 -19.348 1.00 20.85 C
ANISOU 766 CB ASP A 122 2267 4394 1260 -120 -91 -733 C
ATOM 767 CG ASP A 122 -24.444 9.133 -20.709 1.00 29.93 C
ANISOU 767 CG ASP A 122 3346 5734 2292 -159 -111 -746 C
ATOM 768 OD1 ASP A 122 -25.449 8.600 -21.233 1.00 31.34 O
ANISOU 768 OD1 ASP A 122 3516 5963 2429 -231 -125 -826 O
ATOM 769 OD2 ASP A 122 -23.779 10.038 -21.256 1.00 32.71 O
ANISOU 769 OD2 ASP A 122 3650 6193 2587 -124 -112 -675 O
ATOM 770 N ARG A 123 -21.049 7.954 -19.976 1.00 24.65 N
ANISOU 770 N ARG A 123 2759 4887 1720 44 -15 -825 N
ATOM 771 CA ARG A 123 -19.814 8.040 -20.743 1.00 24.42 C
ANISOU 771 CA ARG A 123 2682 4968 1627 103 16 -856 C
ATOM 772 C ARG A 123 -19.188 6.641 -20.898 1.00 29.61 C
ANISOU 772 C ARG A 123 3398 5551 2304 169 54 -1003 C
ATOM 773 O ARG A 123 -18.661 6.326 -21.968 1.00 29.45 O
ANISOU 773 O ARG A 123 3344 5645 2201 190 80 -1097 O
ATOM 774 CB ARG A 123 -18.851 9.029 -20.066 1.00 25.11 C
ANISOU 774 CB ARG A 123 2728 5069 1743 150 17 -737 C
ATOM 775 CG ARG A 123 -17.695 9.515 -20.944 1.00 41.06 C
ANISOU 775 CG ARG A 123 4670 7256 3677 177 46 -735 C
ATOM 776 CD ARG A 123 -18.155 10.294 -22.166 1.00 53.69 C
ANISOU 776 CD ARG A 123 6214 9026 5161 105 36 -699 C
ATOM 777 NE ARG A 123 -18.662 11.623 -21.822 1.00 63.67 N
ANISOU 777 NE ARG A 123 7464 10295 6435 55 1 -547 N
ATOM 778 CZ ARG A 123 -19.483 12.328 -22.593 1.00 79.69 C
ANISOU 778 CZ ARG A 123 9469 12422 8387 -2 -25 -489 C
ATOM 779 NH1 ARG A 123 -19.911 11.834 -23.748 1.00 67.83 N
ANISOU 779 NH1 ARG A 123 7947 11040 6787 -28 -23 -571 N
ATOM 780 NH2 ARG A 123 -19.872 13.540 -22.222 1.00 67.07 N
ANISOU 780 NH2 ARG A 123 7870 10808 6808 -27 -55 -352 N
ATOM 781 N TYR A 124 -19.311 5.786 -19.855 1.00 26.87 N
ANISOU 781 N TYR A 124 3142 5008 2059 203 56 -1025 N
ATOM 782 CA TYR A 124 -18.814 4.409 -19.862 1.00 26.99 C
ANISOU 782 CA TYR A 124 3240 4905 2111 277 89 -1154 C
ATOM 783 C TYR A 124 -19.520 3.549 -20.900 1.00 31.96 C
ANISOU 783 C TYR A 124 3910 5544 2691 211 101 -1303 C
ATOM 784 O TYR A 124 -18.849 2.866 -21.670 1.00 31.23 O
ANISOU 784 O TYR A 124 3824 5484 2556 272 134 -1429 O
ATOM 785 CB TYR A 124 -18.900 3.778 -18.456 1.00 28.30 C
ANISOU 785 CB TYR A 124 3507 4851 2394 315 85 -1115 C
ATOM 786 CG TYR A 124 -18.590 2.299 -18.412 1.00 30.30 C
ANISOU 786 CG TYR A 124 3877 4939 2695 386 115 -1238 C
ATOM 787 CD1 TYR A 124 -17.274 1.842 -18.427 1.00 32.52 C
ANISOU 787 CD1 TYR A 124 4160 5214 2983 540 141 -1285 C
ATOM 788 CD2 TYR A 124 -19.607 1.356 -18.312 1.00 31.53 C
ANISOU 788 CD2 TYR A 124 4146 4941 2893 302 118 -1306 C
ATOM 789 CE1 TYR A 124 -16.981 0.478 -18.392 1.00 34.06 C
ANISOU 789 CE1 TYR A 124 4475 5239 3226 626 168 -1399 C
ATOM 790 CE2 TYR A 124 -19.328 -0.009 -18.271 1.00 33.06 C
ANISOU 790 CE2 TYR A 124 4470 4954 3137 365 148 -1418 C
ATOM 791 CZ TYR A 124 -18.013 -0.444 -18.318 1.00 43.64 C
ANISOU 791 CZ TYR A 124 5819 6276 4485 536 172 -1463 C
ATOM 792 OH TYR A 124 -17.733 -1.786 -18.264 1.00 49.50 O
ANISOU 792 OH TYR A 124 6702 6823 5282 617 201 -1571 O
ATOM 793 N PHE A 125 -20.865 3.570 -20.909 1.00 29.83 N
ANISOU 793 N PHE A 125 3658 5255 2420 86 75 -1298 N
ATOM 794 CA PHE A 125 -21.665 2.767 -21.828 1.00 29.84 C
ANISOU 794 CA PHE A 125 3693 5274 2372 -4 80 -1443 C
ATOM 795 C PHE A 125 -21.646 3.293 -23.258 1.00 34.46 C
ANISOU 795 C PHE A 125 4176 6099 2817 -34 77 -1489 C
ATOM 796 O PHE A 125 -21.578 2.489 -24.185 1.00 34.13 O
ANISOU 796 O PHE A 125 4157 6092 2718 -43 101 -1647 O
ATOM 797 CB PHE A 125 -23.092 2.600 -21.307 1.00 31.81 C
ANISOU 797 CB PHE A 125 3980 5444 2660 -133 54 -1423 C
ATOM 798 CG PHE A 125 -23.238 1.906 -19.971 1.00 33.59 C
ANISOU 798 CG PHE A 125 4322 5431 3010 -127 64 -1392 C
ATOM 799 CD1 PHE A 125 -22.819 0.591 -19.802 1.00 36.68 C
ANISOU 799 CD1 PHE A 125 4843 5634 3461 -84 100 -1501 C
ATOM 800 CD2 PHE A 125 -23.889 2.530 -18.914 1.00 35.90 C
ANISOU 800 CD2 PHE A 125 4600 5686 3354 -170 38 -1258 C
ATOM 801 CE1 PHE A 125 -22.985 -0.060 -18.575 1.00 37.58 C
ANISOU 801 CE1 PHE A 125 5074 5523 3681 -82 108 -1457 C
ATOM 802 CE2 PHE A 125 -24.056 1.877 -17.689 1.00 38.74 C
ANISOU 802 CE2 PHE A 125 5066 5840 3813 -173 49 -1224 C
ATOM 803 CZ PHE A 125 -23.606 0.586 -17.529 1.00 36.73 C
ANISOU 803 CZ PHE A 125 4944 5398 3613 -132 84 -1316 C
ATOM 804 N SER A 126 -21.648 4.630 -23.446 1.00 31.13 N
ANISOU 804 N SER A 126 3651 5841 2338 -43 50 -1354 N
ATOM 805 CA SER A 126 -21.613 5.248 -24.773 1.00 31.01 C
ANISOU 805 CA SER A 126 3540 6063 2180 -71 45 -1365 C
ATOM 806 C SER A 126 -20.321 4.935 -25.579 1.00 37.40 C
ANISOU 806 C SER A 126 4323 6966 2923 15 92 -1455 C
ATOM 807 O SER A 126 -20.323 5.009 -26.815 1.00 37.59 O
ANISOU 807 O SER A 126 4289 7177 2817 -14 100 -1522 O
ATOM 808 CB SER A 126 -21.859 6.752 -24.663 1.00 33.87 C
ANISOU 808 CB SER A 126 3821 6539 2509 -91 8 -1182 C
ATOM 809 OG SER A 126 -20.672 7.518 -24.528 1.00 43.17 O
ANISOU 809 OG SER A 126 4955 7768 3680 -19 27 -1090 O
ATOM 810 N VAL A 127 -19.229 4.584 -24.879 1.00 35.11 N
ANISOU 810 N VAL A 127 4067 6561 2711 125 124 -1457 N
ATOM 811 CA VAL A 127 -17.931 4.274 -25.489 1.00 35.00 C
ANISOU 811 CA VAL A 127 4017 6638 2644 226 172 -1542 C
ATOM 812 C VAL A 127 -17.767 2.755 -25.663 1.00 39.14 C
ANISOU 812 C VAL A 127 4638 7033 3201 282 206 -1739 C
ATOM 813 O VAL A 127 -17.375 2.308 -26.749 1.00 38.61 O
ANISOU 813 O VAL A 127 4545 7089 3039 304 239 -1879 O
ATOM 814 CB VAL A 127 -16.755 4.932 -24.704 1.00 38.94 C
ANISOU 814 CB VAL A 127 4469 7136 3190 319 183 -1424 C
ATOM 815 CG1 VAL A 127 -15.394 4.499 -25.250 1.00 39.09 C
ANISOU 815 CG1 VAL A 127 4440 7258 3157 433 236 -1524 C
ATOM 816 CG2 VAL A 127 -16.867 6.456 -24.715 1.00 38.51 C
ANISOU 816 CG2 VAL A 127 4329 7212 3092 252 156 -1247 C
ATOM 817 N THR A 128 -18.088 1.974 -24.601 1.00 35.62 N
ANISOU 817 N THR A 128 4310 6336 2887 303 200 -1750 N
ATOM 818 CA THR A 128 -17.975 0.507 -24.569 1.00 35.33 C
ANISOU 818 CA THR A 128 4400 6117 2908 360 232 -1918 C
ATOM 819 C THR A 128 -19.053 -0.192 -25.395 1.00 40.24 C
ANISOU 819 C THR A 128 5075 6732 3482 234 230 -2067 C
ATOM 820 O THR A 128 -18.739 -1.170 -26.075 1.00 41.06 O
ANISOU 820 O THR A 128 5235 6807 3561 277 267 -2249 O
ATOM 821 CB THR A 128 -17.920 -0.035 -23.121 1.00 40.88 C
ANISOU 821 CB THR A 128 5218 6554 3760 419 226 -1855 C
ATOM 822 OG1 THR A 128 -19.134 0.267 -22.437 1.00 37.76 O
ANISOU 822 OG1 THR A 128 4856 6078 3414 287 188 -1758 O
ATOM 823 CG2 THR A 128 -16.720 0.500 -22.326 1.00 39.24 C
ANISOU 823 CG2 THR A 128 4955 6363 3592 558 228 -1736 C
ATOM 824 N ARG A 129 -20.311 0.293 -25.340 1.00 36.75 N
ANISOU 824 N ARG A 129 4612 6324 3025 83 188 -2000 N
ATOM 825 CA ARG A 129 -21.454 -0.271 -26.083 1.00 36.72 C
ANISOU 825 CA ARG A 129 4639 6345 2968 -60 178 -2131 C
ATOM 826 C ARG A 129 -22.136 0.841 -26.938 1.00 41.14 C
ANISOU 826 C ARG A 129 5058 7181 3392 -159 138 -2064 C
ATOM 827 O ARG A 129 -23.300 1.162 -26.663 1.00 40.27 O
ANISOU 827 O ARG A 129 4932 7078 3288 -275 97 -2002 O
ATOM 828 CB ARG A 129 -22.495 -0.888 -25.113 1.00 37.21 C
ANISOU 828 CB ARG A 129 4812 6182 3143 -160 162 -2119 C
ATOM 829 CG ARG A 129 -21.959 -1.785 -23.995 1.00 49.07 C
ANISOU 829 CG ARG A 129 6463 7393 4789 -69 191 -2122 C
ATOM 830 CD ARG A 129 -23.089 -2.223 -23.079 1.00 61.56 C
ANISOU 830 CD ARG A 129 8140 8789 6460 -198 176 -2089 C
ATOM 831 NE ARG A 129 -23.104 -3.672 -22.855 1.00 74.60 N
ANISOU 831 NE ARG A 129 9971 10181 8192 -201 214 -2227 N
ATOM 832 CZ ARG A 129 -23.747 -4.554 -23.618 1.00 88.01 C
ANISOU 832 CZ ARG A 129 11737 11844 9859 -320 230 -2410 C
ATOM 833 NH1 ARG A 129 -24.433 -4.150 -24.680 1.00 70.43 N
ANISOU 833 NH1 ARG A 129 9399 9849 7511 -441 208 -2480 N
ATOM 834 NH2 ARG A 129 -23.707 -5.847 -23.326 1.00 77.47 N
ANISOU 834 NH2 ARG A 129 10586 10240 8611 -318 267 -2523 N
ATOM 835 N PRO A 130 -21.466 1.455 -27.962 1.00 37.99 N
ANISOU 835 N PRO A 130 4554 7016 2864 -114 148 -2067 N
ATOM 836 CA PRO A 130 -22.123 2.545 -28.715 1.00 38.03 C
ANISOU 836 CA PRO A 130 4439 7269 2741 -198 106 -1977 C
ATOM 837 C PRO A 130 -23.426 2.183 -29.441 1.00 42.21 C
ANISOU 837 C PRO A 130 4958 7890 3188 -339 74 -2083 C
ATOM 838 O PRO A 130 -24.336 3.002 -29.456 1.00 41.48 O
ANISOU 838 O PRO A 130 4795 7915 3052 -412 23 -1970 O
ATOM 839 CB PRO A 130 -21.037 3.015 -29.693 1.00 39.72 C
ANISOU 839 CB PRO A 130 4566 7695 2830 -123 137 -1984 C
ATOM 840 CG PRO A 130 -20.088 1.884 -29.786 1.00 43.85 C
ANISOU 840 CG PRO A 130 5158 8115 3388 -27 195 -2156 C
ATOM 841 CD PRO A 130 -20.078 1.264 -28.432 1.00 39.30 C
ANISOU 841 CD PRO A 130 4699 7244 2991 18 198 -2135 C
ATOM 842 N LEU A 131 -23.521 0.972 -30.016 1.00 39.02 N
ANISOU 842 N LEU A 131 4624 7436 2766 -376 103 -2301 N
ATOM 843 CA LEU A 131 -24.693 0.507 -30.757 1.00 39.16 C
ANISOU 843 CA LEU A 131 4631 7549 2699 -523 77 -2435 C
ATOM 844 C LEU A 131 -25.915 0.211 -29.863 1.00 46.25 C
ANISOU 844 C LEU A 131 5579 8295 3696 -642 44 -2407 C
ATOM 845 O LEU A 131 -26.975 0.802 -30.084 1.00 47.52 O
ANISOU 845 O LEU A 131 5651 8613 3791 -737 -9 -2340 O
ATOM 846 CB LEU A 131 -24.314 -0.712 -31.629 1.00 38.86 C
ANISOU 846 CB LEU A 131 4663 7487 2615 -524 125 -2693 C
ATOM 847 CG LEU A 131 -25.348 -1.277 -32.589 1.00 43.20 C
ANISOU 847 CG LEU A 131 5194 8173 3047 -676 105 -2874 C
ATOM 848 CD1 LEU A 131 -25.485 -0.413 -33.828 1.00 43.40 C
ANISOU 848 CD1 LEU A 131 5068 8555 2868 -691 76 -2848 C
ATOM 849 CD2 LEU A 131 -24.965 -2.673 -33.010 1.00 45.76 C
ANISOU 849 CD2 LEU A 131 5642 8355 3391 -674 160 -3134 C
ATOM 850 N SER A 132 -25.777 -0.702 -28.881 1.00 43.23 N
ANISOU 850 N SER A 132 5337 7621 3465 -634 76 -2456 N
ATOM 851 CA SER A 132 -26.863 -1.132 -27.993 1.00 43.38 C
ANISOU 851 CA SER A 132 5422 7478 3584 -756 59 -2442 C
ATOM 852 C SER A 132 -27.281 -0.118 -26.919 1.00 49.57 C
ANISOU 852 C SER A 132 6150 8252 4432 -747 22 -2215 C
ATOM 853 O SER A 132 -28.412 -0.195 -26.435 1.00 50.46 O
ANISOU 853 O SER A 132 6259 8341 4574 -871 -4 -2195 O
ATOM 854 CB SER A 132 -26.521 -2.466 -27.343 1.00 46.93 C
ANISOU 854 CB SER A 132 6053 7610 4167 -742 110 -2552 C
ATOM 855 OG SER A 132 -25.274 -2.397 -26.673 1.00 57.05 O
ANISOU 855 OG SER A 132 7385 8758 5534 -562 140 -2467 O
ATOM 856 N TYR A 133 -26.384 0.804 -26.521 1.00 46.19 N
ANISOU 856 N TYR A 133 5681 7843 4027 -608 22 -2055 N
ATOM 857 CA TYR A 133 -26.708 1.809 -25.505 1.00 45.62 C
ANISOU 857 CA TYR A 133 5563 7757 4016 -590 -11 -1851 C
ATOM 858 C TYR A 133 -27.318 3.070 -26.121 1.00 50.51 C
ANISOU 858 C TYR A 133 6036 8638 4519 -616 -64 -1744 C
ATOM 859 O TYR A 133 -28.230 3.639 -25.526 1.00 50.23 O
ANISOU 859 O TYR A 133 5957 8620 4509 -663 -101 -1640 O
ATOM 860 CB TYR A 133 -25.498 2.123 -24.591 1.00 46.11 C
ANISOU 860 CB TYR A 133 5665 7680 4174 -442 14 -1735 C
ATOM 861 CG TYR A 133 -25.766 3.127 -23.486 1.00 46.63 C
ANISOU 861 CG TYR A 133 5696 7715 4306 -423 -15 -1540 C
ATOM 862 CD1 TYR A 133 -26.514 2.778 -22.364 1.00 48.21 C
ANISOU 862 CD1 TYR A 133 5958 7755 4606 -485 -20 -1505 C
ATOM 863 CD2 TYR A 133 -25.232 4.412 -23.539 1.00 47.14 C
ANISOU 863 CD2 TYR A 133 5673 7903 4334 -346 -33 -1396 C
ATOM 864 CE1 TYR A 133 -26.746 3.692 -21.337 1.00 48.16 C
ANISOU 864 CE1 TYR A 133 5918 7728 4655 -461 -43 -1340 C
ATOM 865 CE2 TYR A 133 -25.454 5.332 -22.515 1.00 47.76 C
ANISOU 865 CE2 TYR A 133 5729 7941 4477 -326 -58 -1233 C
ATOM 866 CZ TYR A 133 -26.229 4.973 -21.424 1.00 53.69 C
ANISOU 866 CZ TYR A 133 6533 8547 5319 -379 -63 -1210 C
ATOM 867 OH TYR A 133 -26.468 5.885 -20.423 1.00 53.50 O
ANISOU 867 OH TYR A 133 6483 8496 5351 -356 -85 -1062 O
ATOM 868 N ARG A 134 -26.873 3.486 -27.323 1.00 47.82 N
ANISOU 868 N ARG A 134 5620 8504 4044 -583 -67 -1771 N
ATOM 869 CA ARG A 134 -27.428 4.690 -27.951 1.00 47.66 C
ANISOU 869 CA ARG A 134 5474 8728 3907 -597 -120 -1656 C
ATOM 870 C ARG A 134 -28.780 4.404 -28.649 1.00 50.47 C
ANISOU 870 C ARG A 134 5770 9241 4166 -729 -162 -1751 C
ATOM 871 O ARG A 134 -29.116 5.010 -29.669 1.00 49.66 O
ANISOU 871 O ARG A 134 5567 9384 3918 -743 -200 -1729 O
ATOM 872 CB ARG A 134 -26.405 5.397 -28.859 1.00 48.97 C
ANISOU 872 CB ARG A 134 5583 9060 3964 -512 -108 -1607 C
ATOM 873 CG ARG A 134 -25.213 5.982 -28.089 1.00 62.90 C
ANISOU 873 CG ARG A 134 7372 10712 5815 -397 -79 -1476 C
ATOM 874 CD ARG A 134 -24.600 7.184 -28.789 1.00 78.60 C
ANISOU 874 CD ARG A 134 9278 12893 7693 -346 -84 -1352 C
ATOM 875 NE ARG A 134 -23.135 7.187 -28.713 1.00 89.15 N
ANISOU 875 NE ARG A 134 10632 14184 9056 -256 -31 -1343 N
ATOM 876 CZ ARG A 134 -22.374 8.278 -28.789 1.00102.35 C
ANISOU 876 CZ ARG A 134 12257 15933 10698 -209 -25 -1194 C
ATOM 877 NH1 ARG A 134 -22.930 9.477 -28.914 1.00 92.49 N
ANISOU 877 NH1 ARG A 134 10960 14781 9402 -232 -70 -1033 N
ATOM 878 NH2 ARG A 134 -21.053 8.179 -28.719 1.00 83.26 N
ANISOU 878 NH2 ARG A 134 9843 13493 8301 -137 25 -1206 N
ATOM 879 N ALA A 135 -29.560 3.491 -28.038 1.00 47.01 N
ANISOU 879 N ALA A 135 5393 8661 3808 -830 -156 -1847 N
ATOM 880 CA ALA A 135 -30.918 3.049 -28.383 1.00 46.90 C
ANISOU 880 CA ALA A 135 5331 8753 3735 -982 -190 -1950 C
ATOM 881 C ALA A 135 -31.749 3.154 -27.090 1.00 50.60 C
ANISOU 881 C ALA A 135 5811 9093 4321 -1031 -203 -1859 C
ATOM 882 O ALA A 135 -32.979 3.059 -27.117 1.00 50.93 O
ANISOU 882 O ALA A 135 5788 9236 4326 -1152 -237 -1897 O
ATOM 883 CB ALA A 135 -30.895 1.608 -28.880 1.00 47.61 C
ANISOU 883 CB ALA A 135 5509 8761 3818 -1080 -150 -2188 C
ATOM 884 N LYS A 136 -31.035 3.345 -25.958 1.00 45.53 N
ANISOU 884 N LYS A 136 5244 8242 3812 -936 -175 -1742 N
ATOM 885 CA LYS A 136 -31.535 3.550 -24.599 1.00 44.85 C
ANISOU 885 CA LYS A 136 5180 8019 3842 -948 -178 -1633 C
ATOM 886 C LYS A 136 -31.240 5.014 -24.233 1.00 47.20 C
ANISOU 886 C LYS A 136 5406 8386 4142 -821 -208 -1431 C
ATOM 887 O LYS A 136 -31.987 5.626 -23.472 1.00 46.96 O
ANISOU 887 O LYS A 136 5328 8368 4147 -829 -235 -1328 O
ATOM 888 CB LYS A 136 -30.794 2.635 -23.594 1.00 47.26 C
ANISOU 888 CB LYS A 136 5640 8027 4290 -924 -121 -1658 C
ATOM 889 CG LYS A 136 -31.023 1.137 -23.760 1.00 60.44 C
ANISOU 889 CG LYS A 136 7418 9557 5991 -1050 -84 -1842 C
ATOM 890 CD LYS A 136 -30.425 0.355 -22.585 1.00 69.88 C
ANISOU 890 CD LYS A 136 8769 10448 7332 -1010 -35 -1822 C
ATOM 891 CE LYS A 136 -31.477 -0.385 -21.785 1.00 80.70 C
ANISOU 891 CE LYS A 136 10214 11679 8768 -1172 -18 -1873 C
ATOM 892 NZ LYS A 136 -30.954 -0.876 -20.479 1.00 87.28 N
ANISOU 892 NZ LYS A 136 11184 12241 9736 -1121 19 -1794 N
ATOM 893 N ARG A 137 -30.147 5.565 -24.799 1.00 41.78 N
ANISOU 893 N ARG A 137 4715 7746 3415 -710 -200 -1382 N
ATOM 894 CA ARG A 137 -29.628 6.915 -24.575 1.00 40.41 C
ANISOU 894 CA ARG A 137 4496 7616 3242 -596 -218 -1201 C
ATOM 895 C ARG A 137 -30.498 8.034 -25.195 1.00 42.46 C
ANISOU 895 C ARG A 137 4635 8104 3394 -594 -280 -1107 C
ATOM 896 O ARG A 137 -30.117 8.663 -26.185 1.00 42.27 O
ANISOU 896 O ARG A 137 4561 8239 3260 -552 -296 -1070 O
ATOM 897 CB ARG A 137 -28.174 6.987 -25.061 1.00 37.61 C
ANISOU 897 CB ARG A 137 4173 7251 2868 -505 -182 -1202 C
ATOM 898 CG ARG A 137 -27.346 7.985 -24.316 1.00 32.13 C
ANISOU 898 CG ARG A 137 3486 6484 2239 -403 -176 -1040 C
ATOM 899 CD ARG A 137 -25.895 7.930 -24.716 1.00 28.13 C
ANISOU 899 CD ARG A 137 3002 5971 1715 -328 -135 -1056 C
ATOM 900 NE ARG A 137 -25.206 9.051 -24.093 1.00 33.48 N
ANISOU 900 NE ARG A 137 3668 6617 2437 -253 -136 -894 N
ATOM 901 CZ ARG A 137 -24.778 10.119 -24.748 1.00 51.39 C
ANISOU 901 CZ ARG A 137 5879 9023 4622 -224 -146 -793 C
ATOM 902 NH1 ARG A 137 -24.881 10.180 -26.071 1.00 43.44 N
ANISOU 902 NH1 ARG A 137 4820 8208 3477 -250 -154 -833 N
ATOM 903 NH2 ARG A 137 -24.200 11.115 -24.094 1.00 39.77 N
ANISOU 903 NH2 ARG A 137 4410 7500 3202 -174 -146 -654 N
ATOM 904 N THR A 138 -31.660 8.284 -24.576 1.00 37.37 N
ANISOU 904 N THR A 138 3945 7476 2779 -633 -313 -1062 N
ATOM 905 CA THR A 138 -32.631 9.302 -24.983 1.00 36.23 C
ANISOU 905 CA THR A 138 3686 7533 2546 -614 -376 -971 C
ATOM 906 C THR A 138 -32.697 10.409 -23.905 1.00 38.65 C
ANISOU 906 C THR A 138 3990 7756 2940 -522 -390 -802 C
ATOM 907 O THR A 138 -32.352 10.127 -22.748 1.00 38.95 O
ANISOU 907 O THR A 138 4101 7596 3102 -517 -354 -790 O
ATOM 908 CB THR A 138 -34.027 8.654 -25.219 1.00 42.34 C
ANISOU 908 CB THR A 138 4385 8437 3265 -738 -406 -1084 C
ATOM 909 OG1 THR A 138 -34.505 8.058 -24.012 1.00 44.12 O
ANISOU 909 OG1 THR A 138 4652 8504 3607 -805 -381 -1115 O
ATOM 910 CG2 THR A 138 -34.027 7.626 -26.339 1.00 36.48 C
ANISOU 910 CG2 THR A 138 3641 7795 2425 -837 -397 -1262 C
ATOM 911 N PRO A 139 -33.155 11.653 -24.221 1.00 33.11 N
ANISOU 911 N PRO A 139 3212 7194 2174 -446 -442 -673 N
ATOM 912 CA PRO A 139 -33.291 12.673 -23.156 1.00 32.01 C
ANISOU 912 CA PRO A 139 3079 6961 2123 -360 -453 -533 C
ATOM 913 C PRO A 139 -34.303 12.249 -22.083 1.00 34.89 C
ANISOU 913 C PRO A 139 3420 7275 2562 -415 -452 -576 C
ATOM 914 O PRO A 139 -34.135 12.597 -20.915 1.00 34.97 O
ANISOU 914 O PRO A 139 3474 7137 2678 -373 -433 -512 O
ATOM 915 CB PRO A 139 -33.755 13.923 -23.905 1.00 33.77 C
ANISOU 915 CB PRO A 139 3226 7360 2246 -273 -513 -410 C
ATOM 916 CG PRO A 139 -33.464 13.649 -25.361 1.00 38.71 C
ANISOU 916 CG PRO A 139 3823 8153 2732 -304 -525 -461 C
ATOM 917 CD PRO A 139 -33.617 12.178 -25.524 1.00 34.30 C
ANISOU 917 CD PRO A 139 3272 7591 2169 -430 -495 -650 C
ATOM 918 N ARG A 140 -35.315 11.446 -22.472 1.00 30.47 N
ANISOU 918 N ARG A 140 2792 6843 1941 -522 -468 -693 N
ATOM 919 CA ARG A 140 -36.338 10.889 -21.579 1.00 30.05 C
ANISOU 919 CA ARG A 140 2706 6773 1940 -609 -461 -751 C
ATOM 920 C ARG A 140 -35.700 9.991 -20.509 1.00 30.70 C
ANISOU 920 C ARG A 140 2910 6606 2149 -663 -396 -796 C
ATOM 921 O ARG A 140 -36.094 10.063 -19.356 1.00 30.73 O
ANISOU 921 O ARG A 140 2920 6525 2231 -666 -381 -757 O
ATOM 922 CB ARG A 140 -37.388 10.095 -22.386 1.00 32.89 C
ANISOU 922 CB ARG A 140 2974 7325 2197 -741 -485 -888 C
ATOM 923 CG ARG A 140 -38.763 10.026 -21.725 1.00 46.98 C
ANISOU 923 CG ARG A 140 4659 9203 3988 -810 -501 -911 C
ATOM 924 CD ARG A 140 -39.840 9.498 -22.659 1.00 59.79 C
ANISOU 924 CD ARG A 140 6158 11075 5485 -927 -540 -1030 C
ATOM 925 NE ARG A 140 -41.175 9.947 -22.253 1.00 71.32 N
ANISOU 925 NE ARG A 140 7470 12716 6912 -923 -580 -1001 N
ATOM 926 CZ ARG A 140 -42.290 9.740 -22.950 1.00 91.04 C
ANISOU 926 CZ ARG A 140 9820 15479 9291 -1005 -626 -1082 C
ATOM 927 NH1 ARG A 140 -42.250 9.083 -24.104 1.00 81.66 N
ANISOU 927 NH1 ARG A 140 8618 14405 8004 -1107 -640 -1203 N
ATOM 928 NH2 ARG A 140 -43.455 10.189 -22.499 1.00 78.95 N
ANISOU 928 NH2 ARG A 140 8146 14118 7735 -983 -660 -1051 N
ATOM 929 N ARG A 141 -34.726 9.156 -20.889 1.00 25.13 N
ANISOU 929 N ARG A 141 2299 5791 1456 -697 -357 -875 N
ATOM 930 CA ARG A 141 -34.055 8.256 -19.963 1.00 24.16 C
ANISOU 930 CA ARG A 141 2301 5432 1447 -730 -299 -913 C
ATOM 931 C ARG A 141 -33.076 9.013 -19.061 1.00 27.24 C
ANISOU 931 C ARG A 141 2749 5678 1923 -605 -283 -785 C
ATOM 932 O ARG A 141 -32.856 8.585 -17.926 1.00 26.40 O
ANISOU 932 O ARG A 141 2717 5403 1913 -616 -249 -774 O
ATOM 933 CB ARG A 141 -33.371 7.086 -20.698 1.00 23.84 C
ANISOU 933 CB ARG A 141 2341 5326 1390 -789 -265 -1049 C
ATOM 934 CG ARG A 141 -33.181 5.869 -19.792 1.00 36.27 C
ANISOU 934 CG ARG A 141 4038 6676 3069 -863 -212 -1119 C
ATOM 935 CD ARG A 141 -32.245 4.819 -20.346 1.00 47.49 C
ANISOU 935 CD ARG A 141 5565 7981 4497 -872 -172 -1236 C
ATOM 936 NE ARG A 141 -31.974 3.776 -19.360 1.00 59.24 N
ANISOU 936 NE ARG A 141 7186 9226 6095 -911 -124 -1269 N
ATOM 937 CZ ARG A 141 -30.935 3.782 -18.533 1.00 83.73 C
ANISOU 937 CZ ARG A 141 10375 12155 9283 -805 -97 -1196 C
ATOM 938 NH1 ARG A 141 -30.042 4.764 -18.585 1.00 76.03 N
ANISOU 938 NH1 ARG A 141 9363 11223 8301 -669 -110 -1098 N
ATOM 939 NH2 ARG A 141 -30.774 2.802 -17.653 1.00 76.29 N
ANISOU 939 NH2 ARG A 141 9557 10999 8430 -839 -58 -1219 N
ATOM 940 N ALA A 142 -32.494 10.136 -19.562 1.00 23.18 N
ANISOU 940 N ALA A 142 2205 5234 1369 -496 -308 -688 N
ATOM 941 CA ALA A 142 -31.581 10.994 -18.796 1.00 21.96 C
ANISOU 941 CA ALA A 142 2095 4963 1285 -391 -297 -570 C
ATOM 942 C ALA A 142 -32.392 11.621 -17.654 1.00 25.35 C
ANISOU 942 C ALA A 142 2494 5368 1771 -370 -311 -495 C
ATOM 943 O ALA A 142 -32.038 11.438 -16.488 1.00 24.91 O
ANISOU 943 O ALA A 142 2500 5161 1805 -361 -281 -473 O
ATOM 944 CB ALA A 142 -30.993 12.076 -19.690 1.00 22.38 C
ANISOU 944 CB ALA A 142 2118 5116 1269 -308 -321 -485 C
ATOM 945 N LEU A 143 -33.542 12.257 -17.995 1.00 21.71 N
ANISOU 945 N LEU A 143 1933 5069 1248 -364 -355 -469 N
ATOM 946 CA LEU A 143 -34.485 12.864 -17.051 1.00 20.88 C
ANISOU 946 CA LEU A 143 1775 4982 1177 -337 -371 -415 C
ATOM 947 C LEU A 143 -34.939 11.855 -15.980 1.00 24.27 C
ANISOU 947 C LEU A 143 2232 5319 1671 -435 -333 -481 C
ATOM 948 O LEU A 143 -34.985 12.217 -14.796 1.00 23.86 O
ANISOU 948 O LEU A 143 2199 5179 1687 -399 -317 -427 O
ATOM 949 CB LEU A 143 -35.684 13.487 -17.784 1.00 20.55 C
ANISOU 949 CB LEU A 143 1608 5160 1041 -315 -427 -401 C
ATOM 950 CG LEU A 143 -35.394 14.730 -18.648 1.00 24.93 C
ANISOU 950 CG LEU A 143 2140 5797 1535 -194 -471 -294 C
ATOM 951 CD1 LEU A 143 -36.554 15.025 -19.569 1.00 24.83 C
ANISOU 951 CD1 LEU A 143 2004 6022 1407 -183 -529 -300 C
ATOM 952 CD2 LEU A 143 -35.074 15.953 -17.797 1.00 26.40 C
ANISOU 952 CD2 LEU A 143 2363 5875 1793 -76 -473 -174 C
ATOM 953 N LEU A 144 -35.183 10.579 -16.379 1.00 19.71 N
ANISOU 953 N LEU A 144 1670 4747 1072 -562 -313 -598 N
ATOM 954 CA LEU A 144 -35.549 9.495 -15.459 1.00 20.07 C
ANISOU 954 CA LEU A 144 1763 4687 1175 -677 -270 -659 C
ATOM 955 C LEU A 144 -34.443 9.238 -14.440 1.00 24.58 C
ANISOU 955 C LEU A 144 2460 5035 1843 -635 -228 -616 C
ATOM 956 O LEU A 144 -34.712 9.258 -13.248 1.00 25.36 O
ANISOU 956 O LEU A 144 2575 5066 1996 -644 -207 -577 O
ATOM 957 CB LEU A 144 -35.911 8.198 -16.218 1.00 20.52 C
ANISOU 957 CB LEU A 144 1834 4773 1190 -824 -256 -798 C
ATOM 958 CG LEU A 144 -36.098 6.900 -15.391 1.00 25.51 C
ANISOU 958 CG LEU A 144 2558 5249 1886 -959 -203 -865 C
ATOM 959 CD1 LEU A 144 -37.269 6.995 -14.411 1.00 25.12 C
ANISOU 959 CD1 LEU A 144 2439 5259 1846 -1034 -196 -843 C
ATOM 960 CD2 LEU A 144 -36.305 5.724 -16.304 1.00 28.98 C
ANISOU 960 CD2 LEU A 144 3032 5694 2285 -1092 -191 -1008 C
ATOM 961 N MET A 145 -33.208 9.036 -14.905 1.00 21.62 N
ANISOU 961 N MET A 145 2163 4569 1482 -583 -215 -624 N
ATOM 962 CA MET A 145 -32.042 8.777 -14.064 1.00 21.49 C
ANISOU 962 CA MET A 145 2255 4365 1546 -528 -181 -587 C
ATOM 963 C MET A 145 -31.710 9.934 -13.151 1.00 22.50 C
ANISOU 963 C MET A 145 2368 4466 1714 -427 -191 -472 C
ATOM 964 O MET A 145 -31.305 9.697 -12.012 1.00 22.29 O
ANISOU 964 O MET A 145 2405 4312 1752 -413 -166 -439 O
ATOM 965 CB MET A 145 -30.828 8.354 -14.909 1.00 24.79 C
ANISOU 965 CB MET A 145 2733 4733 1954 -487 -168 -631 C
ATOM 966 CG MET A 145 -30.965 6.963 -15.511 1.00 30.40 C
ANISOU 966 CG MET A 145 3500 5400 2650 -584 -144 -763 C
ATOM 967 SD MET A 145 -31.460 5.718 -14.273 1.00 37.13 S
ANISOU 967 SD MET A 145 4454 6072 3581 -690 -101 -795 S
ATOM 968 CE MET A 145 -32.632 4.714 -15.259 1.00 34.11 C
ANISOU 968 CE MET A 145 4050 5775 3136 -866 -100 -947 C
ATOM 969 N ILE A 146 -31.915 11.181 -13.628 1.00 16.99 N
ANISOU 969 N ILE A 146 1593 3888 975 -357 -229 -411 N
ATOM 970 CA ILE A 146 -31.681 12.418 -12.867 1.00 15.78 C
ANISOU 970 CA ILE A 146 1428 3712 855 -262 -241 -310 C
ATOM 971 C ILE A 146 -32.644 12.522 -11.661 1.00 20.50 C
ANISOU 971 C ILE A 146 1998 4307 1485 -284 -235 -294 C
ATOM 972 O ILE A 146 -32.196 12.754 -10.536 1.00 21.18 O
ANISOU 972 O ILE A 146 2128 4293 1628 -249 -217 -251 O
ATOM 973 CB ILE A 146 -31.730 13.665 -13.812 1.00 17.44 C
ANISOU 973 CB ILE A 146 1578 4038 1009 -187 -283 -249 C
ATOM 974 CG1 ILE A 146 -30.441 13.739 -14.676 1.00 16.64 C
ANISOU 974 CG1 ILE A 146 1521 3915 889 -155 -276 -238 C
ATOM 975 CG2 ILE A 146 -31.999 14.993 -13.042 1.00 15.78 C
ANISOU 975 CG2 ILE A 146 1345 3821 829 -101 -301 -159 C
ATOM 976 CD1 ILE A 146 -30.540 14.533 -15.902 1.00 16.85 C
ANISOU 976 CD1 ILE A 146 1498 4070 835 -120 -310 -199 C
ATOM 977 N GLY A 147 -33.938 12.334 -11.919 1.00 16.61 N
ANISOU 977 N GLY A 147 1424 3941 948 -345 -249 -335 N
ATOM 978 CA GLY A 147 -34.994 12.409 -10.920 1.00 15.98 C
ANISOU 978 CA GLY A 147 1290 3901 878 -377 -240 -332 C
ATOM 979 C GLY A 147 -34.817 11.383 -9.827 1.00 20.27 C
ANISOU 979 C GLY A 147 1913 4315 1474 -457 -192 -353 C
ATOM 980 O GLY A 147 -34.913 11.716 -8.635 1.00 20.55 O
ANISOU 980 O GLY A 147 1954 4311 1544 -432 -176 -310 O
ATOM 981 N LEU A 148 -34.513 10.132 -10.228 1.00 16.00 N
ANISOU 981 N LEU A 148 1442 3700 937 -549 -168 -417 N
ATOM 982 CA LEU A 148 -34.248 9.045 -9.286 1.00 15.68 C
ANISOU 982 CA LEU A 148 1502 3509 946 -621 -122 -427 C
ATOM 983 C LEU A 148 -32.986 9.338 -8.481 1.00 19.47 C
ANISOU 983 C LEU A 148 2065 3850 1482 -519 -112 -358 C
ATOM 984 O LEU A 148 -32.949 9.004 -7.313 1.00 20.10 O
ANISOU 984 O LEU A 148 2195 3847 1595 -538 -85 -325 O
ATOM 985 CB LEU A 148 -34.122 7.695 -10.001 1.00 15.82 C
ANISOU 985 CB LEU A 148 1592 3459 960 -726 -101 -516 C
ATOM 986 CG LEU A 148 -35.385 7.103 -10.623 1.00 20.50 C
ANISOU 986 CG LEU A 148 2116 4174 1499 -871 -102 -604 C
ATOM 987 CD1 LEU A 148 -35.047 5.876 -11.461 1.00 20.17 C
ANISOU 987 CD1 LEU A 148 2160 4050 1454 -956 -85 -704 C
ATOM 988 CD2 LEU A 148 -36.426 6.749 -9.550 1.00 21.70 C
ANISOU 988 CD2 LEU A 148 2245 4342 1656 -984 -71 -596 C
ATOM 989 N ALA A 149 -31.982 10.015 -9.071 1.00 16.00 N
ANISOU 989 N ALA A 149 1632 3401 1044 -415 -134 -332 N
ATOM 990 CA ALA A 149 -30.749 10.366 -8.347 1.00 15.75 C
ANISOU 990 CA ALA A 149 1662 3265 1059 -324 -128 -272 C
ATOM 991 C ALA A 149 -31.037 11.391 -7.260 1.00 20.84 C
ANISOU 991 C ALA A 149 2267 3933 1717 -276 -134 -208 C
ATOM 992 O ALA A 149 -30.492 11.274 -6.165 1.00 21.78 O
ANISOU 992 O ALA A 149 2438 3966 1869 -253 -117 -172 O
ATOM 993 CB ALA A 149 -29.674 10.880 -9.302 1.00 16.01 C
ANISOU 993 CB ALA A 149 1694 3308 1080 -246 -146 -264 C
ATOM 994 N TRP A 150 -31.914 12.369 -7.550 1.00 16.77 N
ANISOU 994 N TRP A 150 1662 3539 1173 -254 -160 -197 N
ATOM 995 CA TRP A 150 -32.337 13.403 -6.603 1.00 16.09 C
ANISOU 995 CA TRP A 150 1533 3485 1096 -200 -166 -153 C
ATOM 996 C TRP A 150 -33.265 12.818 -5.543 1.00 17.49 C
ANISOU 996 C TRP A 150 1694 3680 1271 -273 -137 -167 C
ATOM 997 O TRP A 150 -33.234 13.267 -4.406 1.00 15.50 O
ANISOU 997 O TRP A 150 1446 3409 1035 -239 -126 -135 O
ATOM 998 CB TRP A 150 -33.079 14.514 -7.350 1.00 15.11 C
ANISOU 998 CB TRP A 150 1320 3485 937 -144 -203 -142 C
ATOM 999 CG TRP A 150 -32.174 15.487 -8.030 1.00 15.68 C
ANISOU 999 CG TRP A 150 1412 3532 1013 -58 -229 -97 C
ATOM 1000 CD1 TRP A 150 -31.749 15.452 -9.323 1.00 18.01 C
ANISOU 1000 CD1 TRP A 150 1708 3857 1276 -55 -247 -101 C
ATOM 1001 CD2 TRP A 150 -31.589 16.651 -7.443 1.00 15.76 C
ANISOU 1001 CD2 TRP A 150 1445 3486 1056 26 -237 -44 C
ATOM 1002 NE1 TRP A 150 -30.913 16.510 -9.575 1.00 17.24 N
ANISOU 1002 NE1 TRP A 150 1635 3726 1190 19 -262 -42 N
ATOM 1003 CE2 TRP A 150 -30.790 17.263 -8.436 1.00 18.82 C
ANISOU 1003 CE2 TRP A 150 1853 3865 1434 66 -257 -9 C
ATOM 1004 CE3 TRP A 150 -31.621 17.214 -6.149 1.00 16.99 C
ANISOU 1004 CE3 TRP A 150 1612 3599 1246 62 -226 -28 C
ATOM 1005 CZ2 TRP A 150 -30.056 18.430 -8.193 1.00 17.86 C
ANISOU 1005 CZ2 TRP A 150 1766 3683 1340 130 -266 44 C
ATOM 1006 CZ3 TRP A 150 -30.897 18.376 -5.911 1.00 18.23 C
ANISOU 1006 CZ3 TRP A 150 1802 3697 1430 133 -238 13 C
ATOM 1007 CH2 TRP A 150 -30.122 18.967 -6.923 1.00 18.66 C
ANISOU 1007 CH2 TRP A 150 1880 3732 1479 160 -257 50 C
ATOM 1008 N LEU A 151 -34.119 11.842 -5.929 1.00 14.99 N
ANISOU 1008 N LEU A 151 1357 3412 928 -384 -122 -219 N
ATOM 1009 CA LEU A 151 -35.059 11.184 -5.014 1.00 14.82 C
ANISOU 1009 CA LEU A 151 1318 3419 894 -485 -87 -233 C
ATOM 1010 C LEU A 151 -34.338 10.259 -4.041 1.00 18.40 C
ANISOU 1010 C LEU A 151 1888 3720 1382 -525 -49 -205 C
ATOM 1011 O LEU A 151 -34.616 10.318 -2.851 1.00 17.64 O
ANISOU 1011 O LEU A 151 1791 3626 1284 -537 -26 -172 O
ATOM 1012 CB LEU A 151 -36.168 10.447 -5.770 1.00 14.63 C
ANISOU 1012 CB LEU A 151 1234 3498 828 -610 -84 -302 C
ATOM 1013 CG LEU A 151 -37.400 10.030 -4.968 1.00 19.21 C
ANISOU 1013 CG LEU A 151 1751 4170 1379 -724 -50 -321 C
ATOM 1014 CD1 LEU A 151 -37.935 11.176 -4.097 1.00 18.91 C
ANISOU 1014 CD1 LEU A 151 1623 4236 1327 -637 -55 -286 C
ATOM 1015 CD2 LEU A 151 -38.499 9.561 -5.911 1.00 22.47 C
ANISOU 1015 CD2 LEU A 151 2073 4727 1738 -836 -60 -397 C
ATOM 1016 N VAL A 152 -33.384 9.449 -4.539 1.00 15.40 N
ANISOU 1016 N VAL A 152 1607 3216 1029 -530 -45 -216 N
ATOM 1017 CA VAL A 152 -32.558 8.556 -3.724 1.00 15.24 C
ANISOU 1017 CA VAL A 152 1709 3040 1043 -537 -17 -182 C
ATOM 1018 C VAL A 152 -31.723 9.415 -2.748 1.00 18.19 C
ANISOU 1018 C VAL A 152 2089 3390 1432 -424 -28 -115 C
ATOM 1019 O VAL A 152 -31.605 9.053 -1.586 1.00 19.41 O
ANISOU 1019 O VAL A 152 2292 3495 1589 -437 -4 -71 O
ATOM 1020 CB VAL A 152 -31.704 7.571 -4.593 1.00 18.92 C
ANISOU 1020 CB VAL A 152 2269 3387 1532 -537 -15 -219 C
ATOM 1021 CG1 VAL A 152 -30.691 6.796 -3.749 1.00 18.76 C
ANISOU 1021 CG1 VAL A 152 2373 3208 1548 -497 5 -172 C
ATOM 1022 CG2 VAL A 152 -32.601 6.595 -5.351 1.00 18.36 C
ANISOU 1022 CG2 VAL A 152 2206 3325 1443 -673 2 -296 C
ATOM 1023 N SER A 153 -31.230 10.577 -3.195 1.00 12.86 N
ANISOU 1023 N SER A 153 1364 2762 760 -324 -61 -109 N
ATOM 1024 CA SER A 153 -30.453 11.499 -2.366 1.00 12.41 C
ANISOU 1024 CA SER A 153 1308 2691 717 -230 -74 -61 C
ATOM 1025 C SER A 153 -31.255 12.031 -1.168 1.00 14.65 C
ANISOU 1025 C SER A 153 1546 3039 981 -239 -61 -42 C
ATOM 1026 O SER A 153 -30.705 12.184 -0.082 1.00 13.32 O
ANISOU 1026 O SER A 153 1410 2836 816 -206 -54 -7 O
ATOM 1027 CB SER A 153 -29.948 12.668 -3.206 1.00 16.37 C
ANISOU 1027 CB SER A 153 1765 3232 1223 -149 -108 -62 C
ATOM 1028 OG SER A 153 -28.953 12.226 -4.115 1.00 27.85 O
ANISOU 1028 OG SER A 153 3262 4632 2687 -128 -115 -74 O
ATOM 1029 N PHE A 154 -32.537 12.339 -1.390 1.00 11.51 N
ANISOU 1029 N PHE A 154 1065 2752 558 -279 -59 -72 N
ATOM 1030 CA PHE A 154 -33.467 12.892 -0.410 1.00 11.10 C
ANISOU 1030 CA PHE A 154 934 2780 503 -283 -39 -69 C
ATOM 1031 C PHE A 154 -33.858 11.840 0.611 1.00 16.39 C
ANISOU 1031 C PHE A 154 1655 3446 1128 -384 1 -53 C
ATOM 1032 O PHE A 154 -33.779 12.087 1.808 1.00 15.59 O
ANISOU 1032 O PHE A 154 1560 3352 1011 -365 18 -24 O
ATOM 1033 CB PHE A 154 -34.713 13.459 -1.126 1.00 12.48 C
ANISOU 1033 CB PHE A 154 1007 3108 627 -287 -58 -111 C
ATOM 1034 CG PHE A 154 -35.737 14.078 -0.206 1.00 13.47 C
ANISOU 1034 CG PHE A 154 1046 3351 721 -274 -41 -122 C
ATOM 1035 CD1 PHE A 154 -35.609 15.399 0.216 1.00 15.49 C
ANISOU 1035 CD1 PHE A 154 1273 3626 985 -155 -59 -118 C
ATOM 1036 CD2 PHE A 154 -36.827 13.341 0.246 1.00 15.48 C
ANISOU 1036 CD2 PHE A 154 1249 3698 934 -386 -4 -143 C
ATOM 1037 CE1 PHE A 154 -36.537 15.962 1.098 1.00 15.73 C
ANISOU 1037 CE1 PHE A 154 1225 3769 984 -130 -40 -140 C
ATOM 1038 CE2 PHE A 154 -37.741 13.899 1.146 1.00 17.81 C
ANISOU 1038 CE2 PHE A 154 1455 4120 1192 -371 17 -158 C
ATOM 1039 CZ PHE A 154 -37.599 15.210 1.552 1.00 15.00 C
ANISOU 1039 CZ PHE A 154 1069 3785 844 -234 -2 -161 C
ATOM 1040 N VAL A 155 -34.278 10.668 0.123 1.00 15.07 N
ANISOU 1040 N VAL A 155 1517 3254 956 -497 22 -71 N
ATOM 1041 CA VAL A 155 -34.723 9.511 0.902 1.00 15.40 C
ANISOU 1041 CA VAL A 155 1612 3261 977 -621 69 -50 C
ATOM 1042 C VAL A 155 -33.583 8.956 1.804 1.00 20.40 C
ANISOU 1042 C VAL A 155 2370 3752 1628 -586 79 17 C
ATOM 1043 O VAL A 155 -33.864 8.410 2.873 1.00 20.71 O
ANISOU 1043 O VAL A 155 2449 3781 1640 -651 116 62 O
ATOM 1044 CB VAL A 155 -35.345 8.461 -0.071 1.00 18.98 C
ANISOU 1044 CB VAL A 155 2079 3704 1430 -753 83 -99 C
ATOM 1045 CG1 VAL A 155 -35.600 7.124 0.604 1.00 19.57 C
ANISOU 1045 CG1 VAL A 155 2245 3697 1495 -894 134 -70 C
ATOM 1046 CG2 VAL A 155 -36.638 8.992 -0.686 1.00 18.34 C
ANISOU 1046 CG2 VAL A 155 1851 3806 1311 -793 73 -160 C
ATOM 1047 N LEU A 156 -32.312 9.153 1.381 1.00 16.73 N
ANISOU 1047 N LEU A 156 1958 3198 1202 -480 47 27 N
ATOM 1048 CA LEU A 156 -31.074 8.728 2.038 1.00 16.27 C
ANISOU 1048 CA LEU A 156 2001 3024 1159 -416 44 84 C
ATOM 1049 C LEU A 156 -30.706 9.620 3.211 1.00 18.37 C
ANISOU 1049 C LEU A 156 2236 3343 1399 -343 35 122 C
ATOM 1050 O LEU A 156 -30.350 9.114 4.268 1.00 17.77 O
ANISOU 1050 O LEU A 156 2223 3227 1301 -345 51 180 O
ATOM 1051 CB LEU A 156 -29.924 8.729 0.995 1.00 16.88 C
ANISOU 1051 CB LEU A 156 2110 3027 1275 -332 11 63 C
ATOM 1052 CG LEU A 156 -29.076 7.455 0.772 1.00 22.30 C
ANISOU 1052 CG LEU A 156 2918 3565 1989 -324 20 79 C
ATOM 1053 CD1 LEU A 156 -29.937 6.180 0.652 1.00 23.02 C
ANISOU 1053 CD1 LEU A 156 3080 3587 2081 -457 58 67 C
ATOM 1054 CD2 LEU A 156 -28.227 7.596 -0.477 1.00 24.17 C
ANISOU 1054 CD2 LEU A 156 3150 3779 2254 -253 -7 32 C
ATOM 1055 N TRP A 157 -30.802 10.947 3.047 1.00 15.48 N
ANISOU 1055 N TRP A 157 1781 3066 1034 -278 11 89 N
ATOM 1056 CA TRP A 157 -30.416 11.871 4.112 1.00 14.34 C
ANISOU 1056 CA TRP A 157 1612 2968 868 -210 2 105 C
ATOM 1057 C TRP A 157 -31.542 12.496 4.910 1.00 16.26 C
ANISOU 1057 C TRP A 157 1778 3331 1070 -236 24 86 C
ATOM 1058 O TRP A 157 -31.484 12.457 6.131 1.00 16.82 O
ANISOU 1058 O TRP A 157 1862 3430 1099 -239 41 115 O
ATOM 1059 CB TRP A 157 -29.525 12.975 3.563 1.00 13.14 C
ANISOU 1059 CB TRP A 157 1435 2808 748 -113 -39 83 C
ATOM 1060 CG TRP A 157 -28.158 12.496 3.200 1.00 14.42 C
ANISOU 1060 CG TRP A 157 1662 2881 936 -69 -58 106 C
ATOM 1061 CD1 TRP A 157 -27.715 12.148 1.957 1.00 17.38 C
ANISOU 1061 CD1 TRP A 157 2056 3207 1343 -60 -70 89 C
ATOM 1062 CD2 TRP A 157 -27.053 12.300 4.093 1.00 14.56 C
ANISOU 1062 CD2 TRP A 157 1725 2868 940 -20 -68 146 C
ATOM 1063 NE1 TRP A 157 -26.395 11.771 2.014 1.00 17.24 N
ANISOU 1063 NE1 TRP A 157 2086 3128 1335 -3 -84 112 N
ATOM 1064 CE2 TRP A 157 -25.967 11.835 3.318 1.00 18.63 C
ANISOU 1064 CE2 TRP A 157 2278 3316 1484 25 -86 150 C
ATOM 1065 CE3 TRP A 157 -26.871 12.479 5.477 1.00 15.79 C
ANISOU 1065 CE3 TRP A 157 1885 3063 1052 -5 -65 176 C
ATOM 1066 CZ2 TRP A 157 -24.710 11.563 3.877 1.00 17.53 C
ANISOU 1066 CZ2 TRP A 157 2173 3153 1335 90 -103 184 C
ATOM 1067 CZ3 TRP A 157 -25.628 12.206 6.028 1.00 17.08 C
ANISOU 1067 CZ3 TRP A 157 2087 3202 1202 53 -85 213 C
ATOM 1068 CH2 TRP A 157 -24.562 11.764 5.229 1.00 17.70 C
ANISOU 1068 CH2 TRP A 157 2195 3218 1313 104 -105 217 C
ATOM 1069 N ALA A 158 -32.520 13.125 4.249 1.00 12.29 N
ANISOU 1069 N ALA A 158 1188 2911 569 -241 21 36 N
ATOM 1070 CA ALA A 158 -33.581 13.887 4.918 1.00 11.30 C
ANISOU 1070 CA ALA A 158 954 2898 441 -237 36 3 C
ATOM 1071 C ALA A 158 -34.372 13.110 6.029 1.00 13.24 C
ANISOU 1071 C ALA A 158 1211 3230 589 -336 91 26 C
ATOM 1072 O ALA A 158 -34.491 13.698 7.099 1.00 11.38 O
ANISOU 1072 O ALA A 158 891 3005 429 -301 74 16 O
ATOM 1073 CB ALA A 158 -34.522 14.518 3.901 1.00 11.60 C
ANISOU 1073 CB ALA A 158 917 3037 453 -218 25 -47 C
ATOM 1074 N PRO A 159 -34.836 11.830 5.893 1.00 11.09 N
ANISOU 1074 N PRO A 159 914 2867 432 -458 81 42 N
ATOM 1075 CA PRO A 159 -35.566 11.194 7.016 1.00 11.35 C
ANISOU 1075 CA PRO A 159 936 2951 427 -558 107 64 C
ATOM 1076 C PRO A 159 -34.740 10.988 8.293 1.00 15.50 C
ANISOU 1076 C PRO A 159 1610 3519 761 -538 186 152 C
ATOM 1077 O PRO A 159 -35.247 11.222 9.399 1.00 15.34 O
ANISOU 1077 O PRO A 159 1546 3610 673 -559 219 158 O
ATOM 1078 CB PRO A 159 -36.069 9.873 6.413 1.00 12.94 C
ANISOU 1078 CB PRO A 159 1253 3186 479 -709 204 101 C
ATOM 1079 CG PRO A 159 -36.054 10.087 4.926 1.00 16.10 C
ANISOU 1079 CG PRO A 159 1622 3562 932 -679 166 44 C
ATOM 1080 CD PRO A 159 -34.836 10.938 4.714 1.00 12.11 C
ANISOU 1080 CD PRO A 159 1146 2986 470 -526 117 48 C
ATOM 1081 N ALA A 160 -33.454 10.619 8.145 1.00 11.67 N
ANISOU 1081 N ALA A 160 1157 2812 464 -476 105 170 N
ATOM 1082 CA ALA A 160 -32.564 10.416 9.291 1.00 10.75 C
ANISOU 1082 CA ALA A 160 1052 2603 431 -432 72 208 C
ATOM 1083 C ALA A 160 -32.135 11.733 9.903 1.00 14.52 C
ANISOU 1083 C ALA A 160 1600 3302 617 -337 129 224 C
ATOM 1084 O ALA A 160 -31.934 11.780 11.104 1.00 14.19 O
ANISOU 1084 O ALA A 160 1569 3314 509 -330 141 256 O
ATOM 1085 CB ALA A 160 -31.357 9.581 8.896 1.00 11.17 C
ANISOU 1085 CB ALA A 160 1252 2532 459 -397 76 270 C
ATOM 1086 N ILE A 161 -32.022 12.817 9.104 1.00 11.66 N
ANISOU 1086 N ILE A 161 1115 2882 434 -258 70 139 N
ATOM 1087 CA ILE A 161 -31.670 14.135 9.649 1.00 11.02 C
ANISOU 1087 CA ILE A 161 946 2818 425 -168 43 88 C
ATOM 1088 C ILE A 161 -32.823 14.651 10.546 1.00 18.29 C
ANISOU 1088 C ILE A 161 1887 3992 1068 -190 112 60 C
ATOM 1089 O ILE A 161 -32.586 15.024 11.697 1.00 17.95 O
ANISOU 1089 O ILE A 161 1840 4013 967 -166 120 55 O
ATOM 1090 CB ILE A 161 -31.270 15.150 8.549 1.00 12.67 C
ANISOU 1090 CB ILE A 161 1232 3086 494 -91 32 48 C
ATOM 1091 CG1 ILE A 161 -29.949 14.715 7.844 1.00 12.71 C
ANISOU 1091 CG1 ILE A 161 1310 2971 547 -64 -3 85 C
ATOM 1092 CG2 ILE A 161 -31.167 16.562 9.122 1.00 11.21 C
ANISOU 1092 CG2 ILE A 161 932 2883 444 -15 13 -14 C
ATOM 1093 CD1 ILE A 161 -29.485 15.557 6.632 1.00 5.80 C
ANISOU 1093 CD1 ILE A 161 383 1435 384 -5 0 22 C
ATOM 1094 N LEU A 162 -34.065 14.613 10.030 1.00 17.08 N
ANISOU 1094 N LEU A 162 1662 3910 917 -236 137 27 N
ATOM 1095 CA LEU A 162 -35.238 15.104 10.745 1.00 17.57 C
ANISOU 1095 CA LEU A 162 1624 4133 917 -248 177 -23 C
ATOM 1096 C LEU A 162 -35.742 14.204 11.893 1.00 22.75 C
ANISOU 1096 C LEU A 162 2286 4879 1481 -354 233 27 C
ATOM 1097 O LEU A 162 -36.211 14.738 12.904 1.00 23.18 O
ANISOU 1097 O LEU A 162 2280 5064 1465 -337 262 -10 O
ATOM 1098 CB LEU A 162 -36.410 15.396 9.768 1.00 17.79 C
ANISOU 1098 CB LEU A 162 1555 4235 969 -254 181 -77 C
ATOM 1099 CG LEU A 162 -36.185 16.123 8.421 1.00 22.61 C
ANISOU 1099 CG LEU A 162 2153 4778 1660 -166 130 -113 C
ATOM 1100 CD1 LEU A 162 -37.510 16.398 7.744 1.00 23.07 C
ANISOU 1100 CD1 LEU A 162 2093 4961 1710 -165 138 -165 C
ATOM 1101 CD2 LEU A 162 -35.443 17.438 8.569 1.00 25.67 C
ANISOU 1101 CD2 LEU A 162 2558 5115 2080 -36 95 -152 C
ATOM 1102 N PHE A 163 -35.667 12.861 11.750 1.00 19.12 N
ANISOU 1102 N PHE A 163 1902 4347 1017 -466 252 110 N
ATOM 1103 CA PHE A 163 -36.272 11.962 12.740 1.00 18.87 C
ANISOU 1103 CA PHE A 163 1881 4392 895 -589 312 170 C
ATOM 1104 C PHE A 163 -35.351 11.172 13.690 1.00 24.95 C
ANISOU 1104 C PHE A 163 2773 5087 1619 -609 315 276 C
ATOM 1105 O PHE A 163 -35.883 10.444 14.534 1.00 23.21 O
ANISOU 1105 O PHE A 163 2569 4932 1317 -716 368 338 O
ATOM 1106 CB PHE A 163 -37.205 10.983 12.018 1.00 20.07 C
ANISOU 1106 CB PHE A 163 2024 4543 1059 -731 346 186 C
ATOM 1107 CG PHE A 163 -38.480 11.683 11.621 1.00 20.65 C
ANISOU 1107 CG PHE A 163 1940 4785 1120 -737 363 91 C
ATOM 1108 CD1 PHE A 163 -39.523 11.830 12.531 1.00 23.02 C
ANISOU 1108 CD1 PHE A 163 2138 5281 1327 -798 421 68 C
ATOM 1109 CD2 PHE A 163 -38.614 12.257 10.362 1.00 20.87 C
ANISOU 1109 CD2 PHE A 163 1915 4791 1222 -669 321 25 C
ATOM 1110 CE1 PHE A 163 -40.690 12.500 12.174 1.00 23.61 C
ANISOU 1110 CE1 PHE A 163 2055 5530 1387 -782 434 -24 C
ATOM 1111 CE2 PHE A 163 -39.775 12.934 10.012 1.00 23.29 C
ANISOU 1111 CE2 PHE A 163 2072 5264 1512 -651 330 -57 C
ATOM 1112 CZ PHE A 163 -40.805 13.050 10.918 1.00 21.92 C
ANISOU 1112 CZ PHE A 163 1792 5286 1250 -703 386 -84 C
ATOM 1113 N TRP A 164 -34.013 11.328 13.605 1.00 25.28 N
ANISOU 1113 N TRP A 164 2892 5011 1702 -508 262 300 N
ATOM 1114 CA TRP A 164 -33.088 10.630 14.507 1.00 26.55 C
ANISOU 1114 CA TRP A 164 3158 5118 1812 -502 256 402 C
ATOM 1115 C TRP A 164 -33.358 10.912 15.994 1.00 27.28 C
ANISOU 1115 C TRP A 164 3215 5369 1782 -515 288 417 C
ATOM 1116 O TRP A 164 -33.365 9.974 16.790 1.00 26.18 O
ANISOU 1116 O TRP A 164 3147 5232 1569 -586 318 523 O
ATOM 1117 CB TRP A 164 -31.639 10.949 14.175 1.00 27.34 C
ANISOU 1117 CB TRP A 164 3310 5111 1968 -379 190 403 C
ATOM 1118 CG TRP A 164 -30.685 10.046 14.893 1.00 30.15 C
ANISOU 1118 CG TRP A 164 3776 5402 2280 -363 177 517 C
ATOM 1119 CD1 TRP A 164 -29.935 10.347 15.990 1.00 33.26 C
ANISOU 1119 CD1 TRP A 164 4174 5868 2595 -301 156 546 C
ATOM 1120 CD2 TRP A 164 -30.456 8.661 14.615 1.00 31.03 C
ANISOU 1120 CD2 TRP A 164 4009 5368 2413 -408 186 619 C
ATOM 1121 NE1 TRP A 164 -29.216 9.246 16.386 1.00 33.73 N
ANISOU 1121 NE1 TRP A 164 4347 5844 2625 -291 146 669 N
ATOM 1122 CE2 TRP A 164 -29.521 8.193 15.560 1.00 35.93 C
ANISOU 1122 CE2 TRP A 164 4706 5975 2969 -352 165 717 C
ATOM 1123 CE3 TRP A 164 -30.905 7.782 13.614 1.00 33.11 C
ANISOU 1123 CE3 TRP A 164 4328 5505 2746 -483 205 630 C
ATOM 1124 CZ2 TRP A 164 -29.040 6.877 15.547 1.00 36.13 C
ANISOU 1124 CZ2 TRP A 164 4871 5854 3003 -356 164 834 C
ATOM 1125 CZ3 TRP A 164 -30.436 6.481 13.605 1.00 35.28 C
ANISOU 1125 CZ3 TRP A 164 4745 5627 3033 -500 208 734 C
ATOM 1126 CH2 TRP A 164 -29.515 6.038 14.561 1.00 36.21 C
ANISOU 1126 CH2 TRP A 164 4946 5721 3091 -430 188 838 C
ATOM 1127 N GLN A 165 -33.604 12.195 16.354 1.00 22.95 N
ANISOU 1127 N GLN A 165 2561 4950 1210 -447 284 312 N
ATOM 1128 CA GLN A 165 -33.916 12.665 17.717 1.00 22.38 C
ANISOU 1128 CA GLN A 165 2435 5051 1018 -447 315 292 C
ATOM 1129 C GLN A 165 -35.137 11.921 18.302 1.00 24.76 C
ANISOU 1129 C GLN A 165 2707 5473 1229 -586 392 340 C
ATOM 1130 O GLN A 165 -35.165 11.648 19.497 1.00 23.12 O
ANISOU 1130 O GLN A 165 2511 5371 903 -624 423 394 O
ATOM 1131 CB GLN A 165 -34.138 14.203 17.738 1.00 23.44 C
ANISOU 1131 CB GLN A 165 2463 5277 1166 -348 301 145 C
ATOM 1132 CG GLN A 165 -35.292 14.678 16.841 1.00 25.71 C
ANISOU 1132 CG GLN A 165 2654 5602 1511 -353 321 60 C
ATOM 1133 CD GLN A 165 -35.417 16.169 16.643 1.00 39.23 C
ANISOU 1133 CD GLN A 165 4290 7353 3262 -233 299 -74 C
ATOM 1134 OE1 GLN A 165 -35.517 16.949 17.592 1.00 30.89 O
ANISOU 1134 OE1 GLN A 165 3190 6408 2138 -184 312 -144 O
ATOM 1135 NE2 GLN A 165 -35.474 16.591 15.381 1.00 36.13 N
ANISOU 1135 NE2 GLN A 165 3883 6870 2976 -184 266 -113 N
ATOM 1136 N TYR A 166 -36.117 11.567 17.438 1.00 21.10 N
ANISOU 1136 N TYR A 166 2202 5002 814 -669 422 321 N
ATOM 1137 CA TYR A 166 -37.336 10.859 17.823 1.00 20.26 C
ANISOU 1137 CA TYR A 166 2053 5015 630 -823 498 356 C
ATOM 1138 C TYR A 166 -37.112 9.373 18.016 1.00 23.81 C
ANISOU 1138 C TYR A 166 2640 5350 1056 -950 523 506 C
ATOM 1139 O TYR A 166 -37.739 8.788 18.886 1.00 23.91 O
ANISOU 1139 O TYR A 166 2654 5468 963 -1072 586 572 O
ATOM 1140 CB TYR A 166 -38.479 11.151 16.835 1.00 20.83 C
ANISOU 1140 CB TYR A 166 2008 5152 755 -859 516 263 C
ATOM 1141 CG TYR A 166 -38.772 12.630 16.754 1.00 21.46 C
ANISOU 1141 CG TYR A 166 1959 5346 849 -721 496 124 C
ATOM 1142 CD1 TYR A 166 -39.239 13.328 17.864 1.00 23.92 C
ANISOU 1142 CD1 TYR A 166 2181 5850 1059 -688 533 66 C
ATOM 1143 CD2 TYR A 166 -38.490 13.350 15.602 1.00 21.52 C
ANISOU 1143 CD2 TYR A 166 1949 5258 970 -613 438 54 C
ATOM 1144 CE1 TYR A 166 -39.439 14.705 17.820 1.00 24.85 C
ANISOU 1144 CE1 TYR A 166 2201 6046 1196 -546 513 -67 C
ATOM 1145 CE2 TYR A 166 -38.690 14.726 15.543 1.00 22.52 C
ANISOU 1145 CE2 TYR A 166 1982 5459 1114 -476 418 -63 C
ATOM 1146 CZ TYR A 166 -39.157 15.401 16.660 1.00 30.92 C
ANISOU 1146 CZ TYR A 166 2966 6697 2085 -439 455 -127 C
ATOM 1147 OH TYR A 166 -39.377 16.752 16.612 1.00 33.01 O
ANISOU 1147 OH TYR A 166 3153 7018 2373 -297 437 -249 O
ATOM 1148 N LEU A 167 -36.207 8.765 17.244 1.00 20.84 N
ANISOU 1148 N LEU A 167 2387 4759 773 -919 476 562 N
ATOM 1149 CA LEU A 167 -35.880 7.343 17.399 1.00 20.71 C
ANISOU 1149 CA LEU A 167 2527 4595 746 -1015 494 706 C
ATOM 1150 C LEU A 167 -35.007 7.112 18.657 1.00 25.61 C
ANISOU 1150 C LEU A 167 3233 5224 1272 -961 483 815 C
ATOM 1151 O LEU A 167 -35.225 6.132 19.368 1.00 25.55 O
ANISOU 1151 O LEU A 167 3316 5203 1187 -1069 528 941 O
ATOM 1152 CB LEU A 167 -35.226 6.764 16.120 1.00 20.07 C
ANISOU 1152 CB LEU A 167 2545 4286 795 -985 450 714 C
ATOM 1153 CG LEU A 167 -36.062 6.878 14.835 1.00 23.79 C
ANISOU 1153 CG LEU A 167 2940 4750 1348 -1047 457 617 C
ATOM 1154 CD1 LEU A 167 -35.250 6.502 13.620 1.00 24.06 C
ANISOU 1154 CD1 LEU A 167 3062 4581 1499 -987 406 609 C
ATOM 1155 CD2 LEU A 167 -37.299 6.019 14.897 1.00 25.01 C
ANISOU 1155 CD2 LEU A 167 3088 4954 1458 -1253 531 646 C
ATOM 1156 N VAL A 168 -34.064 8.041 18.947 1.00 22.03 N
ANISOU 1156 N VAL A 168 2749 4805 817 -803 424 766 N
ATOM 1157 CA VAL A 168 -33.174 8.020 20.117 1.00 21.75 C
ANISOU 1157 CA VAL A 168 2766 4815 685 -732 401 844 C
ATOM 1158 C VAL A 168 -33.985 8.392 21.362 1.00 26.32 C
ANISOU 1158 C VAL A 168 3260 5626 1115 -797 458 835 C
ATOM 1159 O VAL A 168 -33.795 7.796 22.425 1.00 27.22 O
ANISOU 1159 O VAL A 168 3440 5791 1111 -833 478 954 O
ATOM 1160 CB VAL A 168 -31.936 8.945 19.902 1.00 25.96 C
ANISOU 1160 CB VAL A 168 3275 5321 1269 -561 319 771 C
ATOM 1161 CG1 VAL A 168 -31.118 9.129 21.172 1.00 25.96 C
ANISOU 1161 CG1 VAL A 168 3291 5423 1150 -491 293 822 C
ATOM 1162 CG2 VAL A 168 -31.047 8.405 18.805 1.00 26.02 C
ANISOU 1162 CG2 VAL A 168 3373 5115 1398 -501 269 801 C
ATOM 1163 N GLY A 169 -34.888 9.354 21.214 1.00 22.37 N
ANISOU 1163 N GLY A 169 2583 5234 683 -799 456 677 N
ATOM 1164 CA GLY A 169 -35.743 9.821 22.300 1.00 22.07 C
ANISOU 1164 CA GLY A 169 2386 5367 631 -839 454 604 C
ATOM 1165 C GLY A 169 -35.316 11.154 22.879 1.00 24.75 C
ANISOU 1165 C GLY A 169 2725 5938 740 -721 512 534 C
ATOM 1166 O GLY A 169 -35.935 11.630 23.842 1.00 23.55 O
ANISOU 1166 O GLY A 169 2429 5925 594 -735 501 459 O
ATOM 1167 N GLU A 170 -34.251 11.769 22.289 1.00 20.38 N
ANISOU 1167 N GLU A 170 2085 5133 527 -578 343 433 N
ATOM 1168 CA GLU A 170 -33.694 13.059 22.706 1.00 20.06 C
ANISOU 1168 CA GLU A 170 1972 5165 487 -461 307 318 C
ATOM 1169 C GLU A 170 -32.993 13.810 21.591 1.00 22.06 C
ANISOU 1169 C GLU A 170 2347 5405 629 -364 328 268 C
ATOM 1170 O GLU A 170 -32.275 13.201 20.799 1.00 21.34 O
ANISOU 1170 O GLU A 170 2340 5145 625 -351 288 340 O
ATOM 1171 CB GLU A 170 -32.650 12.861 23.832 1.00 21.36 C
ANISOU 1171 CB GLU A 170 2211 5405 501 -427 299 395 C
ATOM 1172 CG GLU A 170 -33.223 12.778 25.235 1.00 33.64 C
ANISOU 1172 CG GLU A 170 3833 7296 1654 -495 421 452 C
ATOM 1173 CD GLU A 170 -33.831 14.047 25.790 1.00 53.52 C
ANISOU 1173 CD GLU A 170 6222 10002 4110 -456 448 279 C
ATOM 1174 OE1 GLU A 170 -33.230 15.134 25.618 1.00 64.47 O
ANISOU 1174 OE1 GLU A 170 7578 11367 5549 -351 398 150 O
ATOM 1175 OE2 GLU A 170 -34.911 13.947 26.412 1.00 36.51 O
ANISOU 1175 OE2 GLU A 170 4000 8021 1852 -534 524 270 O
ATOM 1176 N ARG A 171 -33.128 15.148 21.585 1.00 18.54 N
ANISOU 1176 N ARG A 171 1705 4896 443 -283 246 102 N
ATOM 1177 CA ARG A 171 -32.364 16.023 20.699 1.00 17.67 C
ANISOU 1177 CA ARG A 171 1612 4671 431 -189 201 29 C
ATOM 1178 C ARG A 171 -31.117 16.398 21.546 1.00 22.66 C
ANISOU 1178 C ARG A 171 2378 5443 788 -135 207 25 C
ATOM 1179 O ARG A 171 -31.237 17.037 22.600 1.00 21.24 O
ANISOU 1179 O ARG A 171 2151 5412 505 -121 223 -48 O
ATOM 1180 CB ARG A 171 -33.163 17.255 20.243 1.00 14.82 C
ANISOU 1180 CB ARG A 171 1028 4191 413 -135 124 -102 C
ATOM 1181 CG ARG A 171 -32.297 18.258 19.495 1.00 16.62 C
ANISOU 1181 CG ARG A 171 1427 4460 427 -42 164 -184 C
ATOM 1182 CD ARG A 171 -33.103 19.379 18.892 1.00 24.40 C
ANISOU 1182 CD ARG A 171 2431 5531 1307 25 215 -321 C
ATOM 1183 NE ARG A 171 -32.307 20.193 17.971 1.00 27.09 N
ANISOU 1183 NE ARG A 171 2811 5718 1764 93 159 -366 N
ATOM 1184 CZ ARG A 171 -32.106 19.905 16.687 1.00 36.32 C
ANISOU 1184 CZ ARG A 171 4012 6752 3037 92 132 -313 C
ATOM 1185 NH1 ARG A 171 -32.620 18.803 16.158 1.00 20.96 N
ANISOU 1185 NH1 ARG A 171 2070 4795 1099 26 151 -222 N
ATOM 1186 NH2 ARG A 171 -31.378 20.712 15.926 1.00 21.30 N
ANISOU 1186 NH2 ARG A 171 2143 4725 1225 147 86 -353 N
ATOM 1187 N THR A 172 -29.941 15.907 21.129 1.00 20.86 N
ANISOU 1187 N THR A 172 2224 5091 609 -109 152 103 N
ATOM 1188 CA THR A 172 -28.694 16.079 21.889 1.00 20.61 C
ANISOU 1188 CA THR A 172 2216 5104 512 -63 101 111 C
ATOM 1189 C THR A 172 -27.858 17.245 21.340 1.00 23.61 C
ANISOU 1189 C THR A 172 2574 5418 978 4 48 -8 C
ATOM 1190 O THR A 172 -26.867 17.641 21.956 1.00 23.88 O
ANISOU 1190 O THR A 172 2604 5510 958 35 5 -39 O
ATOM 1191 CB THR A 172 -27.939 14.744 21.975 1.00 23.34 C
ANISOU 1191 CB THR A 172 2648 5389 830 -71 76 278 C
ATOM 1192 OG1 THR A 172 -27.556 14.347 20.656 1.00 21.98 O
ANISOU 1192 OG1 THR A 172 2521 5036 793 -51 50 312 O
ATOM 1193 CG2 THR A 172 -28.773 13.638 22.636 1.00 18.09 C
ANISOU 1193 CG2 THR A 172 1839 4605 428 -149 94 354 C
ATOM 1194 N VAL A 173 -28.291 17.806 20.204 1.00 18.06 N
ANISOU 1194 N VAL A 173 1855 4606 400 19 52 -74 N
ATOM 1195 CA VAL A 173 -27.718 18.997 19.580 1.00 17.39 C
ANISOU 1195 CA VAL A 173 1758 4445 405 69 14 -185 C
ATOM 1196 C VAL A 173 -28.239 20.157 20.458 1.00 25.48 C
ANISOU 1196 C VAL A 173 2729 5582 1369 87 37 -327 C
ATOM 1197 O VAL A 173 -29.454 20.307 20.640 1.00 25.71 O
ANISOU 1197 O VAL A 173 2716 5677 1377 82 89 -367 O
ATOM 1198 CB VAL A 173 -28.184 19.152 18.097 1.00 19.02 C
ANISOU 1198 CB VAL A 173 1969 4507 750 80 16 -192 C
ATOM 1199 CG1 VAL A 173 -27.717 20.472 17.502 1.00 18.38 C
ANISOU 1199 CG1 VAL A 173 1882 4347 753 126 -15 -302 C
ATOM 1200 CG2 VAL A 173 -27.725 17.980 17.234 1.00 18.30 C
ANISOU 1200 CG2 VAL A 173 1931 4309 712 62 -2 -70 C
ATOM 1201 N LEU A 174 -27.330 20.940 21.032 1.00 24.13 N
ANISOU 1201 N LEU A 174 2556 5447 1164 105 1 -408 N
ATOM 1202 CA LEU A 174 -27.690 22.064 21.902 1.00 24.79 C
ANISOU 1202 CA LEU A 174 2601 5628 1189 123 20 -560 C
ATOM 1203 C LEU A 174 -28.281 23.237 21.115 1.00 29.82 C
ANISOU 1203 C LEU A 174 3234 6155 1941 170 32 -679 C
ATOM 1204 O LEU A 174 -28.038 23.357 19.914 1.00 30.12 O
ANISOU 1204 O LEU A 174 3302 6040 2102 183 8 -651 O
ATOM 1205 CB LEU A 174 -26.415 22.538 22.610 1.00 25.34 C
ANISOU 1205 CB LEU A 174 2678 5750 1200 116 -29 -616 C
ATOM 1206 CG LEU A 174 -26.197 22.171 24.066 1.00 31.37 C
ANISOU 1206 CG LEU A 174 3415 6714 1790 94 -26 -610 C
ATOM 1207 CD1 LEU A 174 -26.326 20.660 24.310 1.00 32.48 C
ANISOU 1207 CD1 LEU A 174 3571 6914 1855 70 -14 -427 C
ATOM 1208 CD2 LEU A 174 -24.841 22.657 24.517 1.00 33.95 C
ANISOU 1208 CD2 LEU A 174 3740 7084 2075 85 -86 -671 C
ATOM 1209 N ALA A 175 -29.020 24.128 21.796 1.00 26.83 N
ANISOU 1209 N ALA A 175 2819 5854 1519 203 67 -813 N
ATOM 1210 CA ALA A 175 -29.546 25.341 21.168 1.00 26.51 C
ANISOU 1210 CA ALA A 175 2785 5705 1582 269 75 -933 C
ATOM 1211 C ALA A 175 -28.345 26.280 20.920 1.00 32.04 C
ANISOU 1211 C ALA A 175 3544 6283 2348 264 24 -1007 C
ATOM 1212 O ALA A 175 -27.478 26.432 21.791 1.00 32.62 O
ANISOU 1212 O ALA A 175 3621 6432 2342 225 2 -1053 O
ATOM 1213 CB ALA A 175 -30.570 26.001 22.073 1.00 26.83 C
ANISOU 1213 CB ALA A 175 2775 5872 1548 317 127 -1065 C
ATOM 1214 N GLY A 176 -28.277 26.841 19.717 1.00 28.72 N
ANISOU 1214 N GLY A 176 3165 5685 2063 293 6 -1007 N
ATOM 1215 CA GLY A 176 -27.164 27.683 19.288 1.00 28.11 C
ANISOU 1215 CA GLY A 176 3147 5474 2058 269 -37 -1058 C
ATOM 1216 C GLY A 176 -26.148 26.871 18.503 1.00 30.71 C
ANISOU 1216 C GLY A 176 3492 5750 2426 216 -78 -926 C
ATOM 1217 O GLY A 176 -25.114 27.397 18.087 1.00 30.54 O
ANISOU 1217 O GLY A 176 3507 5638 2459 179 -113 -948 O
ATOM 1218 N GLN A 177 -26.425 25.558 18.345 1.00 26.01 N
ANISOU 1218 N GLN A 177 2868 5217 1799 207 -70 -794 N
ATOM 1219 CA GLN A 177 -25.617 24.580 17.608 1.00 25.24 C
ANISOU 1219 CA GLN A 177 2783 5076 1730 175 -101 -663 C
ATOM 1220 C GLN A 177 -26.473 23.957 16.521 1.00 25.24 C
ANISOU 1220 C GLN A 177 2784 5004 1802 197 -81 -577 C
ATOM 1221 O GLN A 177 -27.666 23.716 16.727 1.00 23.44 O
ANISOU 1221 O GLN A 177 2526 4833 1548 217 -41 -576 O
ATOM 1222 CB GLN A 177 -25.121 23.446 18.525 1.00 26.75 C
ANISOU 1222 CB GLN A 177 2954 5405 1807 146 -110 -580 C
ATOM 1223 CG GLN A 177 -23.956 23.798 19.436 1.00 42.55 C
ANISOU 1223 CG GLN A 177 4943 7500 3725 118 -146 -638 C
ATOM 1224 CD GLN A 177 -23.621 22.695 20.423 1.00 56.91 C
ANISOU 1224 CD GLN A 177 6742 9465 5417 108 -157 -543 C
ATOM 1225 OE1 GLN A 177 -24.075 21.543 20.324 1.00 49.35 O
ANISOU 1225 OE1 GLN A 177 5794 8516 4441 115 -138 -420 O
ATOM 1226 NE2 GLN A 177 -22.814 23.034 21.411 1.00 49.54 N
ANISOU 1226 NE2 GLN A 177 5784 8650 4388 89 -188 -598 N
ATOM 1227 N CYS A 178 -25.850 23.668 15.378 1.00 20.73 N
ANISOU 1227 N CYS A 178 2239 4326 1311 187 -108 -508 N
ATOM 1228 CA CYS A 178 -26.507 23.025 14.250 1.00 19.75 C
ANISOU 1228 CA CYS A 178 2117 4137 1250 198 -96 -427 C
ATOM 1229 C CYS A 178 -25.577 22.037 13.594 1.00 22.58 C
ANISOU 1229 C CYS A 178 2496 4456 1629 172 -123 -326 C
ATOM 1230 O CYS A 178 -24.570 22.442 13.003 1.00 23.40 O
ANISOU 1230 O CYS A 178 2617 4494 1780 164 -155 -331 O
ATOM 1231 CB CYS A 178 -27.042 24.041 13.245 1.00 20.10 C
ANISOU 1231 CB CYS A 178 2175 4075 1389 239 -94 -475 C
ATOM 1232 SG CYS A 178 -28.182 23.328 12.030 1.00 23.97 S
ANISOU 1232 SG CYS A 178 2643 4535 1928 256 -76 -399 S
ATOM 1233 N TYR A 179 -25.898 20.734 13.721 1.00 16.68 N
ANISOU 1233 N TYR A 179 1748 3748 842 157 -107 -235 N
ATOM 1234 CA TYR A 179 -25.142 19.620 13.131 1.00 14.86 C
ANISOU 1234 CA TYR A 179 1544 3474 627 147 -127 -137 C
ATOM 1235 C TYR A 179 -26.030 18.359 13.094 1.00 17.98 C
ANISOU 1235 C TYR A 179 1952 3878 1001 123 -94 -56 C
ATOM 1236 O TYR A 179 -27.080 18.351 13.744 1.00 17.43 O
ANISOU 1236 O TYR A 179 1859 3881 884 105 -57 -73 O
ATOM 1237 CB TYR A 179 -23.804 19.383 13.878 1.00 14.46 C
ANISOU 1237 CB TYR A 179 1498 3480 518 151 -162 -118 C
ATOM 1238 CG TYR A 179 -23.936 18.858 15.291 1.00 14.93 C
ANISOU 1238 CG TYR A 179 1552 3659 463 145 -152 -91 C
ATOM 1239 CD1 TYR A 179 -24.064 19.730 16.373 1.00 16.88 C
ANISOU 1239 CD1 TYR A 179 1768 4002 642 139 -148 -179 C
ATOM 1240 CD2 TYR A 179 -23.886 17.489 15.556 1.00 15.20 C
ANISOU 1240 CD2 TYR A 179 1617 3706 450 145 -147 22 C
ATOM 1241 CE1 TYR A 179 -24.182 19.249 17.680 1.00 16.23 C
ANISOU 1241 CE1 TYR A 179 1678 4051 440 131 -138 -152 C
ATOM 1242 CE2 TYR A 179 -24.011 16.998 16.856 1.00 15.81 C
ANISOU 1242 CE2 TYR A 179 1698 3896 413 138 -137 62 C
ATOM 1243 CZ TYR A 179 -24.151 17.881 17.916 1.00 23.01 C
ANISOU 1243 CZ TYR A 179 2568 4926 1249 130 -133 -23 C
ATOM 1244 OH TYR A 179 -24.239 17.390 19.195 1.00 25.09 O
ANISOU 1244 OH TYR A 179 2831 5318 1384 121 -124 21 O
ATOM 1245 N ILE A 180 -25.633 17.316 12.326 1.00 13.63 N
ANISOU 1245 N ILE A 180 1438 3256 483 118 -103 24 N
ATOM 1246 CA ILE A 180 -26.408 16.075 12.245 1.00 13.07 C
ANISOU 1246 CA ILE A 180 1390 3164 410 79 -69 98 C
ATOM 1247 C ILE A 180 -26.144 15.232 13.468 1.00 18.71 C
ANISOU 1247 C ILE A 180 2143 3946 1020 69 -64 169 C
ATOM 1248 O ILE A 180 -25.000 14.871 13.723 1.00 19.34 O
ANISOU 1248 O ILE A 180 2250 4018 1079 107 -98 212 O
ATOM 1249 CB ILE A 180 -26.177 15.283 10.938 1.00 16.04 C
ANISOU 1249 CB ILE A 180 1811 3436 846 76 -78 142 C
ATOM 1250 CG1 ILE A 180 -26.723 16.020 9.711 1.00 15.72 C
ANISOU 1250 CG1 ILE A 180 1738 3355 881 76 -78 85 C
ATOM 1251 CG2 ILE A 180 -26.779 13.885 11.041 1.00 16.66 C
ANISOU 1251 CG2 ILE A 180 1942 3486 902 25 -47 222 C
ATOM 1252 CD1 ILE A 180 -26.430 15.278 8.439 1.00 23.21 C
ANISOU 1252 CD1 ILE A 180 2719 4213 1888 72 -87 117 C
ATOM 1253 N GLN A 181 -27.208 14.910 14.215 1.00 16.63 N
ANISOU 1253 N GLN A 181 1871 3752 694 18 -20 187 N
ATOM 1254 CA GLN A 181 -27.148 14.132 15.440 1.00 17.34 C
ANISOU 1254 CA GLN A 181 1994 3913 681 -3 -6 265 C
ATOM 1255 C GLN A 181 -26.604 12.714 15.260 1.00 24.77 C
ANISOU 1255 C GLN A 181 3025 4760 1625 -4 -13 386 C
ATOM 1256 O GLN A 181 -25.797 12.295 16.090 1.00 25.55 O
ANISOU 1256 O GLN A 181 3159 4893 1656 33 -36 452 O
ATOM 1257 CB GLN A 181 -28.513 14.109 16.137 1.00 18.46 C
ANISOU 1257 CB GLN A 181 2101 4157 756 -71 52 256 C
ATOM 1258 CG GLN A 181 -28.406 13.711 17.604 1.00 22.66 C
ANISOU 1258 CG GLN A 181 2649 4802 1157 -89 66 317 C
ATOM 1259 CD GLN A 181 -29.719 13.735 18.334 1.00 28.46 C
ANISOU 1259 CD GLN A 181 3336 5664 1813 -161 130 301 C
ATOM 1260 OE1 GLN A 181 -30.455 14.722 18.296 1.00 16.67 O
ANISOU 1260 OE1 GLN A 181 1716 4198 419 -152 134 184 O
ATOM 1261 NE2 GLN A 181 -30.032 12.642 19.028 1.00 20.22 N
ANISOU 1261 NE2 GLN A 181 2344 4650 686 -230 165 415 N
ATOM 1262 N PHE A 182 -27.042 11.969 14.209 1.00 22.62 N
ANISOU 1262 N PHE A 182 2795 4372 1428 -41 4 413 N
ATOM 1263 CA PHE A 182 -26.594 10.586 13.988 1.00 23.06 C
ANISOU 1263 CA PHE A 182 2953 4313 1496 -39 2 518 C
ATOM 1264 C PHE A 182 -25.112 10.499 13.583 1.00 30.06 C
ANISOU 1264 C PHE A 182 3864 5139 2417 65 -54 532 C
ATOM 1265 O PHE A 182 -24.498 9.448 13.779 1.00 29.62 O
ANISOU 1265 O PHE A 182 3891 5017 2344 104 -66 625 O
ATOM 1266 CB PHE A 182 -27.513 9.807 13.021 1.00 24.91 C
ANISOU 1266 CB PHE A 182 3227 4446 1793 -122 40 528 C
ATOM 1267 CG PHE A 182 -27.432 10.097 11.538 1.00 26.96 C
ANISOU 1267 CG PHE A 182 3463 4627 2154 -104 23 457 C
ATOM 1268 CD1 PHE A 182 -26.482 9.468 10.737 1.00 30.39 C
ANISOU 1268 CD1 PHE A 182 3960 4942 2645 -48 -5 480 C
ATOM 1269 CD2 PHE A 182 -28.378 10.905 10.919 1.00 28.81 C
ANISOU 1269 CD2 PHE A 182 3615 4912 2421 -144 38 372 C
ATOM 1270 CE1 PHE A 182 -26.420 9.722 9.363 1.00 31.10 C
ANISOU 1270 CE1 PHE A 182 4025 4976 2815 -38 -17 415 C
ATOM 1271 CE2 PHE A 182 -28.305 11.171 9.546 1.00 31.18 C
ANISOU 1271 CE2 PHE A 182 3895 5151 2801 -127 20 317 C
ATOM 1272 CZ PHE A 182 -27.331 10.575 8.779 1.00 29.40 C
ANISOU 1272 CZ PHE A 182 3730 4817 2625 -81 -6 339 C
ATOM 1273 N LEU A 183 -24.527 11.611 13.077 1.00 28.91 N
ANISOU 1273 N LEU A 183 3647 5024 2314 113 -88 442 N
ATOM 1274 CA LEU A 183 -23.111 11.662 12.692 1.00 29.81 C
ANISOU 1274 CA LEU A 183 3758 5114 2452 201 -138 443 C
ATOM 1275 C LEU A 183 -22.170 11.947 13.868 1.00 38.06 C
ANISOU 1275 C LEU A 183 4778 6274 3410 257 -175 461 C
ATOM 1276 O LEU A 183 -20.967 12.080 13.647 1.00 39.28 O
ANISOU 1276 O LEU A 183 4910 6444 3573 328 -219 454 O
ATOM 1277 CB LEU A 183 -22.860 12.684 11.565 1.00 29.35 C
ANISOU 1277 CB LEU A 183 3639 5039 2474 209 -154 347 C
ATOM 1278 CG LEU A 183 -23.419 12.383 10.185 1.00 33.54 C
ANISOU 1278 CG LEU A 183 4188 5467 3089 178 -134 328 C
ATOM 1279 CD1 LEU A 183 -23.112 13.520 9.234 1.00 33.49 C
ANISOU 1279 CD1 LEU A 183 4121 5466 3140 187 -152 247 C
ATOM 1280 CD2 LEU A 183 -22.904 11.059 9.635 1.00 35.41 C
ANISOU 1280 CD2 LEU A 183 4503 5599 3353 213 -137 390 C
ATOM 1281 N SER A 184 -22.692 12.046 15.104 1.00 36.38 N
ANISOU 1281 N SER A 184 4557 6161 3104 223 -158 480 N
ATOM 1282 CA SER A 184 -21.871 12.318 16.287 1.00 37.16 C
ANISOU 1282 CA SER A 184 4625 6391 3100 269 -194 493 C
ATOM 1283 C SER A 184 -20.749 11.265 16.488 1.00 42.90 C
ANISOU 1283 C SER A 184 5405 7101 3795 361 -235 599 C
ATOM 1284 O SER A 184 -19.619 11.648 16.804 1.00 43.41 O
ANISOU 1284 O SER A 184 5416 7259 3819 425 -286 579 O
ATOM 1285 CB SER A 184 -22.733 12.472 17.542 1.00 40.61 C
ANISOU 1285 CB SER A 184 5055 6942 3434 213 -161 503 C
ATOM 1286 OG SER A 184 -23.735 13.467 17.400 1.00 44.31 O
ANISOU 1286 OG SER A 184 5467 7441 3929 152 -127 396 O
ATOM 1287 N GLN A 185 -21.039 9.960 16.256 1.00 38.94 N
ANISOU 1287 N GLN A 185 5006 6478 3313 370 -213 706 N
ATOM 1288 CA GLN A 185 -20.015 8.922 16.385 1.00 38.29 C
ANISOU 1288 CA GLN A 185 4987 6353 3207 479 -250 809 C
ATOM 1289 C GLN A 185 -19.161 8.832 15.100 1.00 40.05 C
ANISOU 1289 C GLN A 185 5197 6487 3531 550 -276 766 C
ATOM 1290 O GLN A 185 -19.726 8.667 14.019 1.00 39.01 O
ANISOU 1290 O GLN A 185 5095 6232 3493 504 -244 731 O
ATOM 1291 CB GLN A 185 -20.616 7.565 16.771 1.00 39.93 C
ANISOU 1291 CB GLN A 185 5328 6457 3388 461 -216 947 C
ATOM 1292 CG GLN A 185 -19.565 6.592 17.314 1.00 61.75 C
ANISOU 1292 CG GLN A 185 8162 9207 6094 594 -260 1071 C
ATOM 1293 CD GLN A 185 -20.129 5.381 18.019 1.00 86.07 C
ANISOU 1293 CD GLN A 185 11383 12203 9118 572 -228 1225 C
ATOM 1294 OE1 GLN A 185 -21.290 5.344 18.451 1.00 82.75 O
ANISOU 1294 OE1 GLN A 185 10991 11786 8666 443 -172 1245 O
ATOM 1295 NE2 GLN A 185 -19.296 4.360 18.166 1.00 78.67 N
ANISOU 1295 NE2 GLN A 185 10537 11191 8162 701 -262 1340 N
ATOM 1296 N PRO A 186 -17.808 8.938 15.216 1.00 35.77 N
ANISOU 1296 N PRO A 186 4602 6027 2961 660 -334 765 N
ATOM 1297 CA PRO A 186 -16.939 8.914 14.019 1.00 35.22 C
ANISOU 1297 CA PRO A 186 4502 5906 2975 728 -355 716 C
ATOM 1298 C PRO A 186 -17.056 7.706 13.063 1.00 38.25 C
ANISOU 1298 C PRO A 186 4993 6102 3437 773 -332 764 C
ATOM 1299 O PRO A 186 -16.894 7.920 11.853 1.00 38.63 O
ANISOU 1299 O PRO A 186 5013 6096 3569 770 -325 691 O
ATOM 1300 CB PRO A 186 -15.531 9.014 14.612 1.00 36.87 C
ANISOU 1300 CB PRO A 186 4636 6263 3109 842 -419 729 C
ATOM 1301 CG PRO A 186 -15.724 9.723 15.908 1.00 40.74 C
ANISOU 1301 CG PRO A 186 5077 6910 3493 792 -432 723 C
ATOM 1302 CD PRO A 186 -17.010 9.184 16.438 1.00 36.52 C
ANISOU 1302 CD PRO A 186 4642 6296 2936 720 -383 795 C
ATOM 1303 N ILE A 187 -17.337 6.470 13.564 1.00 32.50 N
ANISOU 1303 N ILE A 187 4392 5274 2684 808 -319 883 N
ATOM 1304 CA ILE A 187 -17.509 5.284 12.698 1.00 31.93 C
ANISOU 1304 CA ILE A 187 4441 5001 2690 840 -293 920 C
ATOM 1305 C ILE A 187 -18.719 5.408 11.752 1.00 34.00 C
ANISOU 1305 C ILE A 187 4727 5156 3036 699 -237 851 C
ATOM 1306 O ILE A 187 -18.629 4.948 10.607 1.00 33.65 O
ANISOU 1306 O ILE A 187 4718 4994 3072 718 -224 810 O
ATOM 1307 CB ILE A 187 -17.536 3.927 13.441 1.00 35.47 C
ANISOU 1307 CB ILE A 187 5041 5340 3097 905 -290 1068 C
ATOM 1308 CG1 ILE A 187 -18.264 4.015 14.798 1.00 36.70 C
ANISOU 1308 CG1 ILE A 187 5221 5574 3151 825 -275 1153 C
ATOM 1309 CG2 ILE A 187 -16.134 3.333 13.574 1.00 36.14 C
ANISOU 1309 CG2 ILE A 187 5134 5441 3158 1105 -346 1122 C
ATOM 1310 CD1 ILE A 187 -19.763 3.707 14.753 1.00 48.23 C
ANISOU 1310 CD1 ILE A 187 6759 6934 4633 654 -205 1167 C
ATOM 1311 N ILE A 188 -19.847 6.018 12.236 1.00 27.74 N
ANISOU 1311 N ILE A 188 3906 4418 2215 564 -203 834 N
ATOM 1312 CA ILE A 188 -21.071 6.254 11.455 1.00 26.08 C
ANISOU 1312 CA ILE A 188 3694 4149 2067 430 -155 768 C
ATOM 1313 C ILE A 188 -20.746 7.231 10.316 1.00 27.21 C
ANISOU 1313 C ILE A 188 3735 4330 2275 436 -170 649 C
ATOM 1314 O ILE A 188 -21.112 6.977 9.169 1.00 25.65 O
ANISOU 1314 O ILE A 188 3558 4040 2149 400 -149 601 O
ATOM 1315 CB ILE A 188 -22.272 6.712 12.342 1.00 28.92 C
ANISOU 1315 CB ILE A 188 4029 4593 2367 309 -119 776 C
ATOM 1316 CG1 ILE A 188 -22.703 5.572 13.301 1.00 29.57 C
ANISOU 1316 CG1 ILE A 188 4231 4617 2387 277 -92 906 C
ATOM 1317 CG2 ILE A 188 -23.475 7.181 11.477 1.00 28.77 C
ANISOU 1317 CG2 ILE A 188 3968 4558 2407 189 -79 688 C
ATOM 1318 CD1 ILE A 188 -23.351 6.004 14.606 1.00 38.70 C
ANISOU 1318 CD1 ILE A 188 5351 5914 3438 210 -73 940 C
ATOM 1319 N THR A 189 -20.002 8.304 10.647 1.00 22.68 N
ANISOU 1319 N THR A 189 3056 3894 1669 477 -207 604 N
ATOM 1320 CA THR A 189 -19.515 9.346 9.741 1.00 21.94 C
ANISOU 1320 CA THR A 189 2864 3852 1620 481 -225 505 C
ATOM 1321 C THR A 189 -18.569 8.725 8.714 1.00 25.28 C
ANISOU 1321 C THR A 189 3304 4209 2093 569 -240 496 C
ATOM 1322 O THR A 189 -18.610 9.102 7.543 1.00 24.14 O
ANISOU 1322 O THR A 189 3125 4038 2007 543 -231 428 O
ATOM 1323 CB THR A 189 -18.841 10.439 10.564 1.00 26.22 C
ANISOU 1323 CB THR A 189 3313 4548 2102 500 -261 474 C
ATOM 1324 OG1 THR A 189 -19.713 10.767 11.644 1.00 26.35 O
ANISOU 1324 OG1 THR A 189 3331 4621 2060 435 -243 489 O
ATOM 1325 CG2 THR A 189 -18.519 11.686 9.748 1.00 21.33 C
ANISOU 1325 CG2 THR A 189 2602 3976 1526 471 -271 375 C
ATOM 1326 N PHE A 190 -17.751 7.747 9.154 1.00 22.96 N
ANISOU 1326 N PHE A 190 3064 3890 1771 680 -262 569 N
ATOM 1327 CA PHE A 190 -16.834 7.009 8.289 1.00 23.42 C
ANISOU 1327 CA PHE A 190 3143 3886 1869 789 -275 562 C
ATOM 1328 C PHE A 190 -17.622 6.116 7.328 1.00 26.34 C
ANISOU 1328 C PHE A 190 3617 4082 2309 747 -232 552 C
ATOM 1329 O PHE A 190 -17.242 6.010 6.161 1.00 26.41 O
ANISOU 1329 O PHE A 190 3610 4055 2368 778 -228 490 O
ATOM 1330 CB PHE A 190 -15.795 6.210 9.096 1.00 25.49 C
ANISOU 1330 CB PHE A 190 3437 4172 2076 938 -313 645 C
ATOM 1331 CG PHE A 190 -14.842 5.431 8.224 1.00 27.48 C
ANISOU 1331 CG PHE A 190 3705 4369 2368 1072 -325 629 C
ATOM 1332 CD1 PHE A 190 -13.923 6.090 7.407 1.00 31.63 C
ANISOU 1332 CD1 PHE A 190 4107 5003 2907 1110 -344 543 C
ATOM 1333 CD2 PHE A 190 -14.885 4.041 8.187 1.00 29.85 C
ANISOU 1333 CD2 PHE A 190 4147 4504 2693 1156 -313 694 C
ATOM 1334 CE1 PHE A 190 -13.066 5.368 6.564 1.00 33.15 C
ANISOU 1334 CE1 PHE A 190 4304 5162 3131 1237 -349 518 C
ATOM 1335 CE2 PHE A 190 -14.024 3.318 7.351 1.00 33.53 C
ANISOU 1335 CE2 PHE A 190 4630 4914 3197 1293 -321 665 C
ATOM 1336 CZ PHE A 190 -13.117 3.986 6.547 1.00 32.15 C
ANISOU 1336 CZ PHE A 190 4316 4870 3028 1337 -339 574 C
ATOM 1337 N GLY A 191 -18.719 5.530 7.823 1.00 21.23 N
ANISOU 1337 N GLY A 191 3065 3345 1656 664 -199 607 N
ATOM 1338 CA GLY A 191 -19.646 4.722 7.041 1.00 20.69 C
ANISOU 1338 CA GLY A 191 3094 3122 1646 586 -155 593 C
ATOM 1339 C GLY A 191 -20.271 5.528 5.918 1.00 24.58 C
ANISOU 1339 C GLY A 191 3507 3647 2183 491 -138 490 C
ATOM 1340 O GLY A 191 -20.327 5.052 4.786 1.00 24.54 O
ANISOU 1340 O GLY A 191 3534 3559 2231 488 -123 437 O
ATOM 1341 N THR A 192 -20.686 6.788 6.213 1.00 21.37 N
ANISOU 1341 N THR A 192 2999 3368 1754 425 -143 457 N
ATOM 1342 CA THR A 192 -21.272 7.727 5.241 1.00 21.44 C
ANISOU 1342 CA THR A 192 2928 3422 1796 350 -134 372 C
ATOM 1343 C THR A 192 -20.210 8.218 4.249 1.00 25.91 C
ANISOU 1343 C THR A 192 3428 4030 2389 420 -158 314 C
ATOM 1344 O THR A 192 -20.528 8.416 3.088 1.00 26.03 O
ANISOU 1344 O THR A 192 3420 4031 2440 381 -147 255 O
ATOM 1345 CB THR A 192 -22.033 8.888 5.921 1.00 29.87 C
ANISOU 1345 CB THR A 192 3921 4595 2832 277 -130 358 C
ATOM 1346 OG1 THR A 192 -21.113 9.723 6.622 1.00 35.35 O
ANISOU 1346 OG1 THR A 192 4552 5392 3489 336 -164 360 O
ATOM 1347 CG2 THR A 192 -23.145 8.413 6.858 1.00 23.88 C
ANISOU 1347 CG2 THR A 192 3214 3819 2039 196 -98 409 C
ATOM 1348 N ALA A 193 -18.949 8.372 4.702 1.00 23.00 N
ANISOU 1348 N ALA A 193 3024 3724 1992 521 -191 332 N
ATOM 1349 CA ALA A 193 -17.810 8.754 3.868 1.00 23.04 C
ANISOU 1349 CA ALA A 193 2957 3789 2010 587 -212 283 C
ATOM 1350 C ALA A 193 -17.487 7.625 2.877 1.00 29.24 C
ANISOU 1350 C ALA A 193 3804 4475 2832 649 -198 263 C
ATOM 1351 O ALA A 193 -17.144 7.917 1.729 1.00 29.57 O
ANISOU 1351 O ALA A 193 3796 4544 2895 650 -193 200 O
ATOM 1352 CB ALA A 193 -16.598 9.042 4.736 1.00 23.66 C
ANISOU 1352 CB ALA A 193 2976 3976 2038 674 -250 308 C
ATOM 1353 N MET A 194 -17.630 6.337 3.307 1.00 26.09 N
ANISOU 1353 N MET A 194 3520 3955 2437 696 -188 316 N
ATOM 1354 CA MET A 194 -17.402 5.167 2.452 1.00 26.35 C
ANISOU 1354 CA MET A 194 3638 3865 2510 758 -171 291 C
ATOM 1355 C MET A 194 -18.415 5.165 1.314 1.00 29.55 C
ANISOU 1355 C MET A 194 4059 4215 2955 643 -137 222 C
ATOM 1356 O MET A 194 -18.047 4.915 0.169 1.00 30.26 O
ANISOU 1356 O MET A 194 4138 4291 3068 675 -129 152 O
ATOM 1357 CB MET A 194 -17.496 3.842 3.240 1.00 29.29 C
ANISOU 1357 CB MET A 194 4155 4092 2882 813 -164 372 C
ATOM 1358 CG MET A 194 -16.272 3.525 4.114 1.00 34.00 C
ANISOU 1358 CG MET A 194 4750 4732 3438 976 -202 440 C
ATOM 1359 SD MET A 194 -14.654 3.405 3.271 1.00 39.59 S
ANISOU 1359 SD MET A 194 5376 5519 4149 1156 -229 378 S
ATOM 1360 CE MET A 194 -14.857 1.889 2.306 1.00 36.09 C
ANISOU 1360 CE MET A 194 5089 4852 3771 1214 -192 339 C
ATOM 1361 N ALA A 195 -19.679 5.487 1.628 1.00 23.85 N
ANISOU 1361 N ALA A 195 3347 3485 2232 512 -119 235 N
ATOM 1362 CA ALA A 195 -20.783 5.537 0.675 1.00 22.51 C
ANISOU 1362 CA ALA A 195 3177 3288 2087 394 -92 175 C
ATOM 1363 C ALA A 195 -20.837 6.835 -0.178 1.00 24.87 C
ANISOU 1363 C ALA A 195 3354 3714 2382 357 -104 116 C
ATOM 1364 O ALA A 195 -21.404 6.806 -1.271 1.00 23.99 O
ANISOU 1364 O ALA A 195 3234 3596 2286 297 -89 57 O
ATOM 1365 CB ALA A 195 -22.097 5.349 1.416 1.00 23.12 C
ANISOU 1365 CB ALA A 195 3301 3327 2155 276 -69 215 C
ATOM 1366 N THR A 196 -20.294 7.970 0.315 1.00 19.65 N
ANISOU 1366 N THR A 196 2605 3164 1697 385 -129 134 N
ATOM 1367 CA THR A 196 -20.391 9.229 -0.440 1.00 18.67 C
ANISOU 1367 CA THR A 196 2385 3136 1571 343 -137 92 C
ATOM 1368 C THR A 196 -19.062 9.695 -1.085 1.00 20.50 C
ANISOU 1368 C THR A 196 2551 3443 1796 413 -153 65 C
ATOM 1369 O THR A 196 -19.083 10.557 -1.968 1.00 18.33 O
ANISOU 1369 O THR A 196 2215 3230 1520 376 -154 33 O
ATOM 1370 CB THR A 196 -21.007 10.330 0.429 1.00 24.36 C
ANISOU 1370 CB THR A 196 3060 3920 2276 291 -145 117 C
ATOM 1371 OG1 THR A 196 -20.131 10.613 1.516 1.00 22.41 O
ANISOU 1371 OG1 THR A 196 2793 3719 2002 347 -166 152 O
ATOM 1372 CG2 THR A 196 -22.403 9.975 0.938 1.00 21.63 C
ANISOU 1372 CG2 THR A 196 2756 3535 1929 211 -123 134 C
ATOM 1373 N PHE A 197 -17.922 9.122 -0.651 1.00 17.10 N
ANISOU 1373 N PHE A 197 2129 3014 1354 514 -165 82 N
ATOM 1374 CA PHE A 197 -16.610 9.482 -1.180 1.00 15.87 C
ANISOU 1374 CA PHE A 197 1896 2952 1183 580 -178 53 C
ATOM 1375 C PHE A 197 -15.796 8.292 -1.734 1.00 19.50 C
ANISOU 1375 C PHE A 197 2389 3372 1647 691 -170 26 C
ATOM 1376 O PHE A 197 -15.654 8.186 -2.940 1.00 16.29 O
ANISOU 1376 O PHE A 197 1965 2980 1247 690 -153 -32 O
ATOM 1377 CB PHE A 197 -15.786 10.276 -0.142 1.00 16.25 C
ANISOU 1377 CB PHE A 197 1874 3101 1198 605 -207 84 C
ATOM 1378 CG PHE A 197 -14.552 10.914 -0.740 1.00 16.38 C
ANISOU 1378 CG PHE A 197 1789 3241 1193 634 -216 50 C
ATOM 1379 CD1 PHE A 197 -14.662 11.896 -1.728 1.00 17.35 C
ANISOU 1379 CD1 PHE A 197 1857 3417 1319 554 -205 17 C
ATOM 1380 CD2 PHE A 197 -13.281 10.506 -0.349 1.00 17.14 C
ANISOU 1380 CD2 PHE A 197 1842 3411 1261 742 -236 54 C
ATOM 1381 CE1 PHE A 197 -13.524 12.464 -2.300 1.00 17.79 C
ANISOU 1381 CE1 PHE A 197 1819 3592 1349 562 -207 -10 C
ATOM 1382 CE2 PHE A 197 -12.141 11.083 -0.918 1.00 19.52 C
ANISOU 1382 CE2 PHE A 197 2033 3848 1534 757 -240 17 C
ATOM 1383 CZ PHE A 197 -12.270 12.070 -1.878 1.00 17.34 C
ANISOU 1383 CZ PHE A 197 1707 3620 1261 657 -223 -14 C
ATOM 1384 N TYR A 198 -15.264 7.428 -0.844 1.00 18.90 N
ANISOU 1384 N TYR A 198 2363 3254 1566 793 -183 68 N
ATOM 1385 CA TYR A 198 -14.386 6.288 -1.125 1.00 19.41 C
ANISOU 1385 CA TYR A 198 2466 3276 1634 933 -182 51 C
ATOM 1386 C TYR A 198 -14.900 5.338 -2.187 1.00 25.71 C
ANISOU 1386 C TYR A 198 3352 3950 2469 928 -149 -7 C
ATOM 1387 O TYR A 198 -14.165 5.072 -3.133 1.00 25.90 O
ANISOU 1387 O TYR A 198 3341 4011 2489 999 -139 -73 O
ATOM 1388 CB TYR A 198 -14.043 5.533 0.169 1.00 20.47 C
ANISOU 1388 CB TYR A 198 2665 3359 1755 1036 -205 130 C
ATOM 1389 CG TYR A 198 -13.285 6.402 1.150 1.00 22.45 C
ANISOU 1389 CG TYR A 198 2812 3763 1955 1061 -243 170 C
ATOM 1390 CD1 TYR A 198 -11.949 6.733 0.933 1.00 24.42 C
ANISOU 1390 CD1 TYR A 198 2943 4165 2172 1148 -264 139 C
ATOM 1391 CD2 TYR A 198 -13.921 6.950 2.259 1.00 23.06 C
ANISOU 1391 CD2 TYR A 198 2899 3852 2011 984 -255 229 C
ATOM 1392 CE1 TYR A 198 -11.262 7.573 1.807 1.00 25.19 C
ANISOU 1392 CE1 TYR A 198 2937 4416 2218 1149 -299 163 C
ATOM 1393 CE2 TYR A 198 -13.239 7.782 3.146 1.00 23.86 C
ANISOU 1393 CE2 TYR A 198 2905 4101 2061 995 -290 250 C
ATOM 1394 CZ TYR A 198 -11.909 8.089 2.918 1.00 29.83 C
ANISOU 1394 CZ TYR A 198 3546 5001 2786 1073 -314 216 C
ATOM 1395 OH TYR A 198 -11.236 8.909 3.791 1.00 30.21 O
ANISOU 1395 OH TYR A 198 3495 5203 2779 1068 -349 227 O
ATOM 1396 N LEU A 199 -16.132 4.822 -2.043 1.00 23.93 N
ANISOU 1396 N LEU A 199 3232 3588 2271 839 -130 8 N
ATOM 1397 CA LEU A 199 -16.731 3.924 -3.029 1.00 24.30 C
ANISOU 1397 CA LEU A 199 3367 3514 2350 807 -98 -58 C
ATOM 1398 C LEU A 199 -17.066 4.670 -4.321 1.00 25.07 C
ANISOU 1398 C LEU A 199 3383 3705 2439 719 -85 -135 C
ATOM 1399 O LEU A 199 -16.533 4.247 -5.340 1.00 26.49 O
ANISOU 1399 O LEU A 199 3558 3892 2616 775 -71 -211 O
ATOM 1400 CB LEU A 199 -17.941 3.144 -2.474 1.00 25.64 C
ANISOU 1400 CB LEU A 199 3669 3525 2548 718 -79 -20 C
ATOM 1401 CG LEU A 199 -17.736 1.658 -2.088 1.00 32.32 C
ANISOU 1401 CG LEU A 199 4673 4184 3425 804 -66 2 C
ATOM 1402 CD1 LEU A 199 -17.483 0.774 -3.319 1.00 33.14 C
ANISOU 1402 CD1 LEU A 199 4835 4201 3557 847 -41 -105 C
ATOM 1403 CD2 LEU A 199 -16.660 1.474 -1.028 1.00 35.15 C
ANISOU 1403 CD2 LEU A 199 5036 4556 3763 964 -96 83 C
ATOM 1404 N PRO A 200 -17.813 5.814 -4.346 1.00 18.12 N
ANISOU 1404 N PRO A 200 2432 2910 1544 601 -92 -119 N
ATOM 1405 CA PRO A 200 -18.032 6.505 -5.632 1.00 16.99 C
ANISOU 1405 CA PRO A 200 2215 2858 1382 537 -84 -180 C
ATOM 1406 C PRO A 200 -16.760 6.798 -6.433 1.00 20.03 C
ANISOU 1406 C PRO A 200 2516 3356 1739 618 -84 -223 C
ATOM 1407 O PRO A 200 -16.747 6.517 -7.632 1.00 20.32 O
ANISOU 1407 O PRO A 200 2546 3413 1761 612 -65 -296 O
ATOM 1408 CB PRO A 200 -18.765 7.789 -5.225 1.00 18.52 C
ANISOU 1408 CB PRO A 200 2347 3124 1565 441 -99 -133 C
ATOM 1409 CG PRO A 200 -19.473 7.435 -3.990 1.00 22.57 C
ANISOU 1409 CG PRO A 200 2926 3553 2096 414 -101 -76 C
ATOM 1410 CD PRO A 200 -18.538 6.508 -3.257 1.00 18.75 C
ANISOU 1410 CD PRO A 200 2500 3005 1620 528 -105 -48 C
ATOM 1411 N VAL A 201 -15.683 7.287 -5.761 1.00 16.16 N
ANISOU 1411 N VAL A 201 1959 2948 1232 690 -103 -183 N
ATOM 1412 CA VAL A 201 -14.371 7.646 -6.333 1.00 16.25 C
ANISOU 1412 CA VAL A 201 1871 3096 1208 760 -103 -215 C
ATOM 1413 C VAL A 201 -13.677 6.410 -6.957 1.00 22.45 C
ANISOU 1413 C VAL A 201 2691 3845 1994 883 -84 -286 C
ATOM 1414 O VAL A 201 -13.253 6.476 -8.112 1.00 22.66 O
ANISOU 1414 O VAL A 201 2662 3957 1991 891 -63 -354 O
ATOM 1415 CB VAL A 201 -13.476 8.422 -5.317 1.00 19.26 C
ANISOU 1415 CB VAL A 201 2171 3577 1570 792 -131 -160 C
ATOM 1416 CG1 VAL A 201 -11.994 8.369 -5.682 1.00 18.86 C
ANISOU 1416 CG1 VAL A 201 2024 3659 1483 895 -130 -196 C
ATOM 1417 CG2 VAL A 201 -13.936 9.868 -5.183 1.00 18.79 C
ANISOU 1417 CG2 VAL A 201 2055 3584 1501 667 -141 -125 C
ATOM 1418 N THR A 202 -13.631 5.283 -6.226 1.00 19.34 N
ANISOU 1418 N THR A 202 2399 3318 1633 977 -88 -270 N
ATOM 1419 CA THR A 202 -13.057 4.028 -6.715 1.00 19.04 C
ANISOU 1419 CA THR A 202 2422 3206 1606 1110 -70 -336 C
ATOM 1420 C THR A 202 -13.814 3.563 -7.963 1.00 23.47 C
ANISOU 1420 C THR A 202 3038 3705 2175 1040 -36 -429 C
ATOM 1421 O THR A 202 -13.174 3.249 -8.960 1.00 24.16 O
ANISOU 1421 O THR A 202 3090 3851 2238 1107 -16 -517 O
ATOM 1422 CB THR A 202 -12.992 2.995 -5.584 1.00 26.73 C
ANISOU 1422 CB THR A 202 3516 4025 2615 1213 -83 -278 C
ATOM 1423 OG1 THR A 202 -12.336 3.599 -4.468 1.00 26.98 O
ANISOU 1423 OG1 THR A 202 3474 4155 2622 1263 -119 -195 O
ATOM 1424 CG2 THR A 202 -12.231 1.743 -5.980 1.00 26.06 C
ANISOU 1424 CG2 THR A 202 3500 3856 2546 1385 -68 -341 C
ATOM 1425 N VAL A 203 -15.166 3.597 -7.925 1.00 19.37 N
ANISOU 1425 N VAL A 203 2588 3093 1678 899 -32 -414 N
ATOM 1426 CA VAL A 203 -16.062 3.249 -9.041 1.00 18.63 C
ANISOU 1426 CA VAL A 203 2536 2959 1583 804 -7 -500 C
ATOM 1427 C VAL A 203 -15.791 4.150 -10.270 1.00 22.84 C
ANISOU 1427 C VAL A 203 2944 3677 2057 763 0 -551 C
ATOM 1428 O VAL A 203 -15.662 3.630 -11.378 1.00 23.70 O
ANISOU 1428 O VAL A 203 3059 3802 2143 783 24 -652 O
ATOM 1429 CB VAL A 203 -17.562 3.262 -8.600 1.00 22.02 C
ANISOU 1429 CB VAL A 203 3033 3295 2037 653 -9 -460 C
ATOM 1430 CG1 VAL A 203 -18.519 3.165 -9.786 1.00 21.35 C
ANISOU 1430 CG1 VAL A 203 2952 3225 1934 536 8 -547 C
ATOM 1431 CG2 VAL A 203 -17.856 2.147 -7.598 1.00 21.99 C
ANISOU 1431 CG2 VAL A 203 3174 3096 2084 679 -4 -421 C
ATOM 1432 N MET A 204 -15.669 5.478 -10.070 1.00 17.98 N
ANISOU 1432 N MET A 204 2222 3196 1415 709 -19 -482 N
ATOM 1433 CA MET A 204 -15.455 6.433 -11.161 1.00 16.99 C
ANISOU 1433 CA MET A 204 1989 3237 1231 656 -13 -505 C
ATOM 1434 C MET A 204 -14.058 6.395 -11.775 1.00 23.91 C
ANISOU 1434 C MET A 204 2782 4239 2062 758 4 -555 C
ATOM 1435 O MET A 204 -13.916 6.714 -12.958 1.00 24.06 O
ANISOU 1435 O MET A 204 2743 4373 2026 725 24 -608 O
ATOM 1436 CB MET A 204 -15.814 7.854 -10.728 1.00 18.75 C
ANISOU 1436 CB MET A 204 2146 3533 1444 565 -36 -413 C
ATOM 1437 CG MET A 204 -17.304 8.063 -10.570 1.00 21.80 C
ANISOU 1437 CG MET A 204 2581 3850 1851 454 -47 -386 C
ATOM 1438 SD MET A 204 -17.747 9.756 -10.142 1.00 25.85 S
ANISOU 1438 SD MET A 204 3027 4440 2356 368 -73 -290 S
ATOM 1439 CE MET A 204 -17.210 9.832 -8.424 1.00 21.90 C
ANISOU 1439 CE MET A 204 2542 3883 1897 422 -91 -224 C
ATOM 1440 N CYS A 205 -13.029 6.033 -10.979 1.00 22.26 N
ANISOU 1440 N CYS A 205 2560 4029 1870 882 -3 -537 N
ATOM 1441 CA CYS A 205 -11.639 5.918 -11.429 1.00 22.40 C
ANISOU 1441 CA CYS A 205 2484 4183 1844 995 13 -588 C
ATOM 1442 C CYS A 205 -11.492 4.680 -12.292 1.00 25.83 C
ANISOU 1442 C CYS A 205 2978 4562 2276 1087 44 -706 C
ATOM 1443 O CYS A 205 -10.821 4.729 -13.322 1.00 25.38 O
ANISOU 1443 O CYS A 205 2839 4644 2159 1118 71 -781 O
ATOM 1444 CB CYS A 205 -10.676 5.895 -10.241 1.00 23.14 C
ANISOU 1444 CB CYS A 205 2541 4301 1952 1106 -12 -534 C
ATOM 1445 SG CYS A 205 -10.468 7.505 -9.430 1.00 27.45 S
ANISOU 1445 SG CYS A 205 2979 4971 2478 999 -41 -429 S
ATOM 1446 N THR A 206 -12.149 3.580 -11.875 1.00 22.72 N
ANISOU 1446 N THR A 206 2730 3960 1941 1122 43 -724 N
ATOM 1447 CA THR A 206 -12.186 2.289 -12.565 1.00 22.98 C
ANISOU 1447 CA THR A 206 2860 3881 1988 1200 72 -841 C
ATOM 1448 C THR A 206 -12.955 2.445 -13.878 1.00 27.80 C
ANISOU 1448 C THR A 206 3464 4542 2557 1073 95 -924 C
ATOM 1449 O THR A 206 -12.530 1.910 -14.902 1.00 28.58 O
ANISOU 1449 O THR A 206 3554 4686 2618 1132 126 -1043 O
ATOM 1450 CB THR A 206 -12.778 1.224 -11.629 1.00 29.26 C
ANISOU 1450 CB THR A 206 3827 4428 2863 1235 63 -813 C
ATOM 1451 OG1 THR A 206 -12.036 1.232 -10.401 1.00 26.40 O
ANISOU 1451 OG1 THR A 206 3454 4055 2523 1354 35 -722 O
ATOM 1452 CG2 THR A 206 -12.770 -0.173 -12.239 1.00 25.16 C
ANISOU 1452 CG2 THR A 206 3435 3755 2371 1318 94 -937 C
ATOM 1453 N LEU A 207 -14.058 3.212 -13.849 1.00 23.89 N
ANISOU 1453 N LEU A 207 2964 4055 2059 909 78 -862 N
ATOM 1454 CA LEU A 207 -14.880 3.517 -15.020 1.00 23.61 C
ANISOU 1454 CA LEU A 207 2907 4092 1972 783 89 -918 C
ATOM 1455 C LEU A 207 -14.064 4.322 -16.036 1.00 27.12 C
ANISOU 1455 C LEU A 207 3213 4765 2328 788 105 -941 C
ATOM 1456 O LEU A 207 -14.073 3.980 -17.210 1.00 26.21 O
ANISOU 1456 O LEU A 207 3085 4718 2154 779 130 -1046 O
ATOM 1457 CB LEU A 207 -16.149 4.284 -14.601 1.00 23.46 C
ANISOU 1457 CB LEU A 207 2898 4048 1969 632 61 -829 C
ATOM 1458 CG LEU A 207 -17.491 3.533 -14.625 1.00 27.89 C
ANISOU 1458 CG LEU A 207 3569 4464 2563 536 62 -872 C
ATOM 1459 CD1 LEU A 207 -17.408 2.163 -13.982 1.00 27.55 C
ANISOU 1459 CD1 LEU A 207 3666 4212 2590 611 76 -912 C
ATOM 1460 CD2 LEU A 207 -18.550 4.333 -13.914 1.00 30.89 C
ANISOU 1460 CD2 LEU A 207 3940 4834 2963 422 33 -770 C
ATOM 1461 N TYR A 208 -13.289 5.318 -15.562 1.00 23.50 N
ANISOU 1461 N TYR A 208 2652 4423 1853 804 93 -851 N
ATOM 1462 CA TYR A 208 -12.423 6.163 -16.395 1.00 22.80 C
ANISOU 1462 CA TYR A 208 2428 4555 1678 794 111 -854 C
ATOM 1463 C TYR A 208 -11.264 5.395 -17.077 1.00 28.56 C
ANISOU 1463 C TYR A 208 3111 5378 2363 929 150 -971 C
ATOM 1464 O TYR A 208 -10.960 5.671 -18.233 1.00 27.61 O
ANISOU 1464 O TYR A 208 2914 5421 2155 900 179 -1026 O
ATOM 1465 CB TYR A 208 -11.897 7.374 -15.583 1.00 22.13 C
ANISOU 1465 CB TYR A 208 2260 4552 1598 761 90 -732 C
ATOM 1466 CG TYR A 208 -11.102 8.342 -16.422 1.00 21.71 C
ANISOU 1466 CG TYR A 208 2077 4716 1456 714 112 -719 C
ATOM 1467 CD1 TYR A 208 -11.738 9.263 -17.248 1.00 23.17 C
ANISOU 1467 CD1 TYR A 208 2240 4978 1586 583 113 -678 C
ATOM 1468 CD2 TYR A 208 -9.713 8.272 -16.472 1.00 22.38 C
ANISOU 1468 CD2 TYR A 208 2060 4941 1502 804 135 -752 C
ATOM 1469 CE1 TYR A 208 -11.011 10.104 -18.092 1.00 23.59 C
ANISOU 1469 CE1 TYR A 208 2185 5228 1549 531 139 -659 C
ATOM 1470 CE2 TYR A 208 -8.976 9.112 -17.303 1.00 23.43 C
ANISOU 1470 CE2 TYR A 208 2070 5286 1544 745 163 -744 C
ATOM 1471 CZ TYR A 208 -9.627 10.027 -18.113 1.00 30.20 C
ANISOU 1471 CZ TYR A 208 2921 6204 2349 603 167 -693 C
ATOM 1472 OH TYR A 208 -8.888 10.855 -18.925 1.00 30.23 O
ANISOU 1472 OH TYR A 208 2815 6412 2259 534 199 -672 O
ATOM 1473 N TRP A 209 -10.604 4.471 -16.356 1.00 28.41 N
ANISOU 1473 N TRP A 209 3134 5265 2396 1083 150 -1004 N
ATOM 1474 CA TRP A 209 -9.482 3.677 -16.875 1.00 29.94 C
ANISOU 1474 CA TRP A 209 3284 5535 2556 1244 184 -1119 C
ATOM 1475 C TRP A 209 -9.974 2.748 -18.006 1.00 31.69 C
ANISOU 1475 C TRP A 209 3581 5706 2752 1250 218 -1265 C
ATOM 1476 O TRP A 209 -9.265 2.569 -19.001 1.00 30.88 O
ANISOU 1476 O TRP A 209 3401 5759 2574 1309 256 -1368 O
ATOM 1477 CB TRP A 209 -8.753 2.951 -15.713 1.00 30.12 C
ANISOU 1477 CB TRP A 209 3347 5452 2646 1419 167 -1100 C
ATOM 1478 CG TRP A 209 -7.437 2.235 -15.964 1.00 32.45 C
ANISOU 1478 CG TRP A 209 3577 5842 2912 1623 192 -1194 C
ATOM 1479 CD1 TRP A 209 -6.970 1.168 -15.255 1.00 35.83 C
ANISOU 1479 CD1 TRP A 209 4081 6134 3398 1815 182 -1216 C
ATOM 1480 CD2 TRP A 209 -6.364 2.612 -16.864 1.00 32.58 C
ANISOU 1480 CD2 TRP A 209 3426 6122 2831 1664 229 -1262 C
ATOM 1481 NE1 TRP A 209 -5.705 0.819 -15.687 1.00 35.73 N
ANISOU 1481 NE1 TRP A 209 3959 6283 3333 1988 208 -1305 N
ATOM 1482 CE2 TRP A 209 -5.317 1.677 -16.680 1.00 36.75 C
ANISOU 1482 CE2 TRP A 209 3934 6665 3365 1894 240 -1339 C
ATOM 1483 CE3 TRP A 209 -6.231 3.570 -17.884 1.00 33.92 C
ANISOU 1483 CE3 TRP A 209 3471 6514 2903 1533 257 -1270 C
ATOM 1484 CZ2 TRP A 209 -4.138 1.704 -17.441 1.00 36.16 C
ANISOU 1484 CZ2 TRP A 209 3700 6838 3202 1994 280 -1430 C
ATOM 1485 CZ3 TRP A 209 -5.052 3.609 -18.622 1.00 35.52 C
ANISOU 1485 CZ3 TRP A 209 3522 6957 3015 1615 299 -1350 C
ATOM 1486 CH2 TRP A 209 -4.021 2.686 -18.398 1.00 36.10 C
ANISOU 1486 CH2 TRP A 209 3562 7058 3096 1842 311 -1435 C
ATOM 1487 N ARG A 210 -11.229 2.254 -17.893 1.00 26.68 N
ANISOU 1487 N ARG A 210 3088 4878 2173 1169 204 -1275 N
ATOM 1488 CA ARG A 210 -11.896 1.449 -18.922 1.00 25.74 C
ANISOU 1488 CA ARG A 210 3048 4701 2031 1133 230 -1414 C
ATOM 1489 C ARG A 210 -12.275 2.335 -20.112 1.00 27.06 C
ANISOU 1489 C ARG A 210 3117 5072 2092 993 239 -1426 C
ATOM 1490 O ARG A 210 -12.107 1.904 -21.247 1.00 27.01 O
ANISOU 1490 O ARG A 210 3094 5155 2015 1009 273 -1558 O
ATOM 1491 CB ARG A 210 -13.154 0.757 -18.372 1.00 27.56 C
ANISOU 1491 CB ARG A 210 3443 4681 2346 1058 210 -1409 C
ATOM 1492 CG ARG A 210 -12.863 -0.436 -17.461 1.00 46.44 C
ANISOU 1492 CG ARG A 210 5973 6839 4834 1199 211 -1427 C
ATOM 1493 CD ARG A 210 -14.018 -0.706 -16.505 1.00 61.97 C
ANISOU 1493 CD ARG A 210 8073 8591 6883 1094 186 -1348 C
ATOM 1494 NE ARG A 210 -14.329 -2.132 -16.386 1.00 69.35 N
ANISOU 1494 NE ARG A 210 9189 9273 7886 1147 204 -1434 N
ATOM 1495 CZ ARG A 210 -15.247 -2.634 -15.566 1.00 85.06 C
ANISOU 1495 CZ ARG A 210 11318 11052 9951 1066 192 -1380 C
ATOM 1496 NH1 ARG A 210 -15.950 -1.832 -14.773 1.00 69.26 N
ANISOU 1496 NH1 ARG A 210 9281 9073 7960 940 162 -1246 N
ATOM 1497 NH2 ARG A 210 -15.466 -3.941 -15.526 1.00 76.29 N
ANISOU 1497 NH2 ARG A 210 10383 9703 8901 1109 214 -1460 N
ATOM 1498 N ILE A 211 -12.799 3.557 -19.854 1.00 22.61 N
ANISOU 1498 N ILE A 211 2496 4579 1515 862 209 -1288 N
ATOM 1499 CA ILE A 211 -13.196 4.533 -20.882 1.00 22.41 C
ANISOU 1499 CA ILE A 211 2385 4740 1389 732 210 -1262 C
ATOM 1500 C ILE A 211 -11.961 4.935 -21.714 1.00 27.73 C
ANISOU 1500 C ILE A 211 2924 5649 1961 785 248 -1296 C
ATOM 1501 O ILE A 211 -12.022 4.905 -22.945 1.00 26.97 O
ANISOU 1501 O ILE A 211 2788 5695 1765 747 274 -1377 O
ATOM 1502 CB ILE A 211 -13.986 5.763 -20.307 1.00 24.66 C
ANISOU 1502 CB ILE A 211 2653 5023 1695 605 167 -1099 C
ATOM 1503 CG1 ILE A 211 -15.338 5.334 -19.700 1.00 23.95 C
ANISOU 1503 CG1 ILE A 211 2676 4741 1681 537 136 -1085 C
ATOM 1504 CG2 ILE A 211 -14.243 6.817 -21.390 1.00 25.33 C
ANISOU 1504 CG2 ILE A 211 2650 5304 1670 496 168 -1056 C
ATOM 1505 CD1 ILE A 211 -15.914 6.291 -18.617 1.00 23.44 C
ANISOU 1505 CD1 ILE A 211 2612 4620 1674 469 96 -931 C
ATOM 1506 N TYR A 212 -10.836 5.243 -21.035 1.00 25.47 N
ANISOU 1506 N TYR A 212 2567 5416 1695 871 253 -1242 N
ATOM 1507 CA TYR A 212 -9.575 5.614 -21.683 1.00 25.62 C
ANISOU 1507 CA TYR A 212 2443 5670 1619 918 293 -1270 C
ATOM 1508 C TYR A 212 -8.994 4.485 -22.582 1.00 31.15 C
ANISOU 1508 C TYR A 212 3137 6431 2267 1044 341 -1454 C
ATOM 1509 O TYR A 212 -8.658 4.747 -23.735 1.00 30.93 O
ANISOU 1509 O TYR A 212 3019 6611 2121 1010 379 -1511 O
ATOM 1510 CB TYR A 212 -8.546 6.120 -20.652 1.00 25.85 C
ANISOU 1510 CB TYR A 212 2393 5742 1685 978 283 -1182 C
ATOM 1511 CG TYR A 212 -7.371 6.824 -21.295 1.00 26.19 C
ANISOU 1511 CG TYR A 212 2270 6058 1621 968 322 -1179 C
ATOM 1512 CD1 TYR A 212 -7.370 8.204 -21.467 1.00 27.81 C
ANISOU 1512 CD1 TYR A 212 2402 6387 1776 813 318 -1055 C
ATOM 1513 CD2 TYR A 212 -6.275 6.106 -21.764 1.00 26.57 C
ANISOU 1513 CD2 TYR A 212 2238 6242 1616 1110 366 -1303 C
ATOM 1514 CE1 TYR A 212 -6.303 8.856 -22.085 1.00 27.97 C
ANISOU 1514 CE1 TYR A 212 2275 6662 1693 778 360 -1047 C
ATOM 1515 CE2 TYR A 212 -5.200 6.745 -22.378 1.00 27.67 C
ANISOU 1515 CE2 TYR A 212 2211 6655 1647 1087 408 -1304 C
ATOM 1516 CZ TYR A 212 -5.214 8.123 -22.532 1.00 35.37 C
ANISOU 1516 CZ TYR A 212 3117 7751 2570 911 406 -1172 C
ATOM 1517 OH TYR A 212 -4.144 8.758 -23.126 1.00 37.67 O
ANISOU 1517 OH TYR A 212 3247 8314 2751 868 453 -1167 O
ATOM 1518 N ARG A 213 -8.891 3.248 -22.046 1.00 29.01 N
ANISOU 1518 N ARG A 213 2967 5974 2080 1189 340 -1543 N
ATOM 1519 CA ARG A 213 -8.412 2.034 -22.722 1.00 28.82 C
ANISOU 1519 CA ARG A 213 2971 5945 2032 1334 383 -1729 C
ATOM 1520 C ARG A 213 -9.257 1.720 -23.972 1.00 31.57 C
ANISOU 1520 C ARG A 213 3365 6322 2308 1237 403 -1845 C
ATOM 1521 O ARG A 213 -8.695 1.391 -25.016 1.00 31.26 O
ANISOU 1521 O ARG A 213 3261 6446 2172 1291 450 -1978 O
ATOM 1522 CB ARG A 213 -8.447 0.851 -21.736 1.00 32.09 C
ANISOU 1522 CB ARG A 213 3532 6086 2573 1481 366 -1766 C
ATOM 1523 CG ARG A 213 -7.833 -0.463 -22.249 1.00 54.38 C
ANISOU 1523 CG ARG A 213 6405 8864 5394 1670 408 -1955 C
ATOM 1524 CD ARG A 213 -8.035 -1.618 -21.273 1.00 71.25 C
ANISOU 1524 CD ARG A 213 8720 10691 7662 1799 388 -1970 C
ATOM 1525 NE ARG A 213 -7.121 -1.560 -20.125 1.00 82.90 N
ANISOU 1525 NE ARG A 213 10152 12157 9189 1948 365 -1871 N
ATOM 1526 CZ ARG A 213 -7.436 -1.087 -18.918 1.00 95.64 C
ANISOU 1526 CZ ARG A 213 11793 13674 10871 1894 317 -1706 C
ATOM 1527 NH1 ARG A 213 -8.654 -0.615 -18.677 1.00 79.18 N
ANISOU 1527 NH1 ARG A 213 9778 11491 8817 1698 290 -1619 N
ATOM 1528 NH2 ARG A 213 -6.538 -1.088 -17.945 1.00 83.05 N
ANISOU 1528 NH2 ARG A 213 10150 12097 9307 2040 295 -1631 N
ATOM 1529 N GLU A 214 -10.598 1.822 -23.861 1.00 27.33 N
ANISOU 1529 N GLU A 214 2927 5647 1809 1093 368 -1799 N
ATOM 1530 CA GLU A 214 -11.536 1.588 -24.959 1.00 26.96 C
ANISOU 1530 CA GLU A 214 2919 5634 1692 981 375 -1897 C
ATOM 1531 C GLU A 214 -11.357 2.651 -26.048 1.00 31.58 C
ANISOU 1531 C GLU A 214 3360 6512 2128 882 391 -1860 C
ATOM 1532 O GLU A 214 -11.237 2.291 -27.217 1.00 31.61 O
ANISOU 1532 O GLU A 214 3330 6657 2024 885 427 -1996 O
ATOM 1533 CB GLU A 214 -12.981 1.602 -24.449 1.00 28.18 C
ANISOU 1533 CB GLU A 214 3185 5603 1920 846 328 -1831 C
ATOM 1534 CG GLU A 214 -13.960 0.909 -25.382 1.00 34.44 C
ANISOU 1534 CG GLU A 214 4051 6367 2668 758 334 -1974 C
ATOM 1535 CD GLU A 214 -14.192 -0.569 -25.128 1.00 52.62 C
ANISOU 1535 CD GLU A 214 6512 8424 5057 830 350 -2126 C
ATOM 1536 OE1 GLU A 214 -13.661 -1.106 -24.126 1.00 43.21 O
ANISOU 1536 OE1 GLU A 214 5393 7052 3974 954 350 -2098 O
ATOM 1537 OE2 GLU A 214 -14.927 -1.189 -25.930 1.00 48.49 O
ANISOU 1537 OE2 GLU A 214 6047 7886 4491 756 360 -2270 O
ATOM 1538 N THR A 215 -11.319 3.950 -25.656 1.00 28.28 N
ANISOU 1538 N THR A 215 2864 6182 1700 796 365 -1676 N
ATOM 1539 CA THR A 215 -11.135 5.100 -26.545 1.00 28.04 C
ANISOU 1539 CA THR A 215 2711 6407 1537 693 377 -1599 C
ATOM 1540 C THR A 215 -9.876 4.950 -27.416 1.00 32.81 C
ANISOU 1540 C THR A 215 3196 7244 2026 775 440 -1699 C
ATOM 1541 O THR A 215 -9.985 5.120 -28.626 1.00 32.76 O
ANISOU 1541 O THR A 215 3136 7427 1884 713 466 -1753 O
ATOM 1542 CB THR A 215 -11.184 6.422 -25.753 1.00 32.41 C
ANISOU 1542 CB THR A 215 3227 6960 2129 608 341 -1390 C
ATOM 1543 OG1 THR A 215 -12.453 6.521 -25.087 1.00 30.18 O
ANISOU 1543 OG1 THR A 215 3046 6486 1934 534 288 -1319 O
ATOM 1544 CG2 THR A 215 -10.964 7.655 -26.637 1.00 27.38 C
ANISOU 1544 CG2 THR A 215 2481 6564 1360 496 356 -1292 C
ATOM 1545 N GLU A 216 -8.713 4.591 -26.823 1.00 29.85 N
ANISOU 1545 N GLU A 216 2775 6869 1697 919 464 -1730 N
ATOM 1546 CA GLU A 216 -7.482 4.412 -27.594 1.00 30.39 C
ANISOU 1546 CA GLU A 216 2716 7176 1656 1009 527 -1834 C
ATOM 1547 C GLU A 216 -7.545 3.180 -28.508 1.00 35.14 C
ANISOU 1547 C GLU A 216 3363 7780 2207 1101 565 -2057 C
ATOM 1548 O GLU A 216 -6.999 3.218 -29.619 1.00 34.97 O
ANISOU 1548 O GLU A 216 3240 8004 2043 1104 617 -2147 O
ATOM 1549 CB GLU A 216 -6.210 4.436 -26.720 1.00 32.18 C
ANISOU 1549 CB GLU A 216 2857 7438 1932 1141 539 -1805 C
ATOM 1550 CG GLU A 216 -5.973 3.274 -25.769 1.00 45.68 C
ANISOU 1550 CG GLU A 216 4660 8926 3771 1330 525 -1885 C
ATOM 1551 CD GLU A 216 -4.731 3.448 -24.914 1.00 69.61 C
ANISOU 1551 CD GLU A 216 7583 12033 6831 1453 529 -1838 C
ATOM 1552 OE1 GLU A 216 -4.866 3.483 -23.669 1.00 64.15 O
ANISOU 1552 OE1 GLU A 216 6951 11167 6255 1479 481 -1737 O
ATOM 1553 OE2 GLU A 216 -3.623 3.564 -25.487 1.00 66.68 O
ANISOU 1553 OE2 GLU A 216 7060 11917 6361 1518 579 -1902 O
ATOM 1554 N ASN A 217 -8.261 2.122 -28.065 1.00 31.57 N
ANISOU 1554 N ASN A 217 3072 7058 1867 1160 541 -2145 N
ATOM 1555 CA ASN A 217 -8.457 0.889 -28.832 1.00 31.26 C
ANISOU 1555 CA ASN A 217 3110 6967 1800 1235 573 -2367 C
ATOM 1556 C ASN A 217 -9.310 1.174 -30.071 1.00 33.53 C
ANISOU 1556 C ASN A 217 3385 7399 1957 1076 577 -2414 C
ATOM 1557 O ASN A 217 -8.916 0.802 -31.172 1.00 32.53 O
ANISOU 1557 O ASN A 217 3195 7446 1718 1108 619 -2560 O
ATOM 1558 CB ASN A 217 -9.112 -0.209 -27.966 1.00 33.92 C
ANISOU 1558 CB ASN A 217 3639 6953 2296 1300 544 -2423 C
ATOM 1559 CG ASN A 217 -8.165 -1.061 -27.143 1.00 61.07 C
ANISOU 1559 CG ASN A 217 7116 10252 5834 1523 558 -2475 C
ATOM 1560 OD1 ASN A 217 -7.023 -1.344 -27.525 1.00 57.44 O
ANISOU 1560 OD1 ASN A 217 6561 9947 5316 1676 604 -2571 O
ATOM 1561 ND2 ASN A 217 -8.638 -1.521 -25.993 1.00 53.92 N
ANISOU 1561 ND2 ASN A 217 6354 9058 5077 1552 518 -2412 N
ATOM 1562 N ARG A 218 -10.455 1.862 -29.879 1.00 29.07 N
ANISOU 1562 N ARG A 218 2829 6743 1473 892 486 -2234 N
ATOM 1563 CA ARG A 218 -11.411 2.221 -30.925 1.00 28.65 C
ANISOU 1563 CA ARG A 218 2729 6791 1366 727 444 -2209 C
ATOM 1564 C ARG A 218 -10.859 3.250 -31.910 1.00 34.04 C
ANISOU 1564 C ARG A 218 3325 7863 1746 688 540 -2225 C
ATOM 1565 O ARG A 218 -11.167 3.169 -33.104 1.00 34.96 O
ANISOU 1565 O ARG A 218 3409 8155 1718 627 558 -2318 O
ATOM 1566 CB ARG A 218 -12.743 2.673 -30.319 1.00 26.17 C
ANISOU 1566 CB ARG A 218 2440 6277 1226 580 341 -2019 C
ATOM 1567 CG ARG A 218 -13.525 1.530 -29.689 1.00 26.78 C
ANISOU 1567 CG ARG A 218 2718 6101 1357 610 357 -2157 C
ATOM 1568 CD ARG A 218 -14.810 2.022 -29.075 1.00 33.71 C
ANISOU 1568 CD ARG A 218 3737 6918 2155 501 359 -2124 C
ATOM 1569 NE ARG A 218 -15.609 0.945 -28.487 1.00 38.85 N
ANISOU 1569 NE ARG A 218 4538 7300 2923 490 343 -2213 N
ATOM 1570 CZ ARG A 218 -16.522 0.230 -29.141 1.00 46.07 C
ANISOU 1570 CZ ARG A 218 5517 8185 3802 405 339 -2358 C
ATOM 1571 NH1 ARG A 218 -16.738 0.437 -30.437 1.00 28.56 N
ANISOU 1571 NH1 ARG A 218 3194 6183 1473 331 335 -2408 N
ATOM 1572 NH2 ARG A 218 -17.210 -0.710 -28.510 1.00 27.33 N
ANISOU 1572 NH2 ARG A 218 3258 5542 1585 374 316 -2390 N
ATOM 1573 N ALA A 219 -10.030 4.198 -31.420 1.00 29.94 N
ANISOU 1573 N ALA A 219 2682 7404 1289 684 515 -2035 N
ATOM 1574 CA ALA A 219 -9.373 5.211 -32.244 1.00 29.27 C
ANISOU 1574 CA ALA A 219 2416 7580 1126 602 505 -1916 C
ATOM 1575 C ALA A 219 -8.376 4.531 -33.204 1.00 32.41 C
ANISOU 1575 C ALA A 219 2774 8244 1297 720 637 -2157 C
ATOM 1576 O ALA A 219 -8.311 4.893 -34.382 1.00 32.97 O
ANISOU 1576 O ALA A 219 2739 8543 1245 638 639 -2155 O
ATOM 1577 CB ALA A 219 -8.654 6.216 -31.361 1.00 29.73 C
ANISOU 1577 CB ALA A 219 2453 7698 1143 604 552 -1778 C
ATOM 1578 N ASN A1002 -7.643 3.509 -32.707 1.00 27.11 N
ANISOU 1578 N ASN A1002 3377 5575 1347 394 -784 -2006 N
ATOM 1579 CA ASN A1002 -6.682 2.737 -33.501 1.00 25.46 C
ANISOU 1579 CA ASN A1002 3153 5294 1228 344 -724 -1777 C
ATOM 1580 C ASN A1002 -7.351 1.979 -34.628 1.00 26.57 C
ANISOU 1580 C ASN A1002 3575 5301 1217 227 -647 -1674 C
ATOM 1581 O ASN A1002 -6.834 2.010 -35.738 1.00 26.82 O
ANISOU 1581 O ASN A1002 3659 5194 1338 85 -666 -1642 O
ATOM 1582 CB ASN A1002 -5.818 1.834 -32.627 1.00 23.93 C
ANISOU 1582 CB ASN A1002 2771 5306 1017 556 -654 -1585 C
ATOM 1583 CG ASN A1002 -4.825 2.612 -31.802 1.00 43.03 C
ANISOU 1583 CG ASN A1002 5332 8260 2759 536 -1079 -2154 C
ATOM 1584 OD1 ASN A1002 -4.317 3.656 -32.220 1.00 37.19 O
ANISOU 1584 OD1 ASN A1002 4486 7382 2264 361 -1216 -2372 O
ATOM 1585 ND2 ASN A1002 -4.528 2.129 -30.604 1.00 35.74 N
ANISOU 1585 ND2 ASN A1002 4358 7719 1502 768 -1122 -2153 N
ATOM 1586 N ILE A1003 -8.538 1.383 -34.382 1.00 21.96 N
ANISOU 1586 N ILE A1003 2843 4522 978 320 -420 -1350 N
ATOM 1587 CA ILE A1003 -9.310 0.690 -35.425 1.00 21.60 C
ANISOU 1587 CA ILE A1003 2949 4283 976 214 -309 -1210 C
ATOM 1588 C ILE A1003 -9.817 1.716 -36.459 1.00 25.67 C
ANISOU 1588 C ILE A1003 3717 4740 1297 24 -456 -1530 C
ATOM 1589 O ILE A1003 -9.835 1.412 -37.641 1.00 25.00 O
ANISOU 1589 O ILE A1003 3691 4485 1324 -85 -409 -1418 O
ATOM 1590 CB ILE A1003 -10.450 -0.247 -34.887 1.00 24.04 C
ANISOU 1590 CB ILE A1003 3461 4734 937 283 -185 -1206 C
ATOM 1591 CG1 ILE A1003 -9.987 -1.083 -33.673 1.00 23.84 C
ANISOU 1591 CG1 ILE A1003 3374 4919 764 485 -120 -1054 C
ATOM 1592 CG2 ILE A1003 -10.984 -1.172 -36.016 1.00 24.19 C
ANISOU 1592 CG2 ILE A1003 3637 4573 981 167 -51 -1091 C
ATOM 1593 CD1 ILE A1003 -11.127 -1.677 -32.794 1.00 31.39 C
ANISOU 1593 CD1 ILE A1003 4552 6136 1238 590 56 -1078 C
ATOM 1594 N PHE A1004 -10.190 2.933 -36.007 1.00 24.15 N
ANISOU 1594 N PHE A1004 3359 4474 1343 44 -523 -1626 N
ATOM 1595 CA PHE A1004 -10.678 4.018 -36.864 1.00 24.28 C
ANISOU 1595 CA PHE A1004 3412 4277 1537 -75 -609 -1733 C
ATOM 1596 C PHE A1004 -9.605 4.564 -37.786 1.00 29.30 C
ANISOU 1596 C PHE A1004 4109 4813 2211 -236 -738 -1812 C
ATOM 1597 O PHE A1004 -9.904 4.857 -38.939 1.00 30.07 O
ANISOU 1597 O PHE A1004 4256 4713 2455 -337 -729 -1711 O
ATOM 1598 CB PHE A1004 -11.304 5.154 -36.036 1.00 25.96 C
ANISOU 1598 CB PHE A1004 3602 4523 1739 -22 -724 -2029 C
ATOM 1599 CG PHE A1004 -11.804 6.335 -36.847 1.00 27.54 C
ANISOU 1599 CG PHE A1004 3861 4470 2133 -128 -841 -2171 C
ATOM 1600 CD1 PHE A1004 -12.900 6.207 -37.695 1.00 29.24 C
ANISOU 1600 CD1 PHE A1004 4129 4552 2427 -150 -787 -2047 C
ATOM 1601 CD2 PHE A1004 -11.205 7.586 -36.729 1.00 29.88 C
ANISOU 1601 CD2 PHE A1004 4097 4634 2620 -183 -978 -2363 C
ATOM 1602 CE1 PHE A1004 -13.375 7.302 -38.422 1.00 29.91 C
ANISOU 1602 CE1 PHE A1004 4219 4397 2749 -191 -870 -2075 C
ATOM 1603 CE2 PHE A1004 -11.687 8.683 -37.456 1.00 32.13 C
ANISOU 1603 CE2 PHE A1004 4399 4626 3183 -243 -1037 -2387 C
ATOM 1604 CZ PHE A1004 -12.764 8.530 -38.300 1.00 29.52 C
ANISOU 1604 CZ PHE A1004 4133 4186 2898 -231 -984 -2224 C
ATOM 1605 N GLU A1005 -8.375 4.723 -37.280 1.00 26.09 N
ANISOU 1605 N GLU A1005 3609 4526 1779 -233 -812 -1893 N
ATOM 1606 CA GLU A1005 -7.261 5.234 -38.064 1.00 25.95 C
ANISOU 1606 CA GLU A1005 3527 4393 1939 -374 -862 -1864 C
ATOM 1607 C GLU A1005 -6.741 4.167 -39.032 1.00 29.98 C
ANISOU 1607 C GLU A1005 4086 4907 2396 -403 -736 -1614 C
ATOM 1608 O GLU A1005 -6.284 4.509 -40.127 1.00 29.37 O
ANISOU 1608 O GLU A1005 4010 4683 2467 -531 -716 -1515 O
ATOM 1609 CB GLU A1005 -6.153 5.805 -37.164 1.00 27.16 C
ANISOU 1609 CB GLU A1005 3519 4691 2108 -373 -995 -2076 C
ATOM 1610 CG GLU A1005 -6.568 7.001 -36.312 1.00 40.25 C
ANISOU 1610 CG GLU A1005 5122 6309 3862 -365 -1132 -2386 C
ATOM 1611 CD GLU A1005 -7.082 8.262 -36.991 1.00 67.91 C
ANISOU 1611 CD GLU A1005 8654 9462 7685 -495 -1171 -2447 C
ATOM 1612 OE1 GLU A1005 -6.720 8.511 -38.166 1.00 70.87 O
ANISOU 1612 OE1 GLU A1005 9046 9627 8254 -640 -1127 -2265 O
ATOM 1613 OE2 GLU A1005 -7.838 9.016 -36.333 1.00 57.47 O
ANISOU 1613 OE2 GLU A1005 7336 8083 6416 -435 -1237 -2672 O
ATOM 1614 N MET A1006 -6.854 2.874 -38.643 1.00 25.87 N
ANISOU 1614 N MET A1006 3614 4543 1670 -277 -633 -1507 N
ATOM 1615 CA MET A1006 -6.456 1.721 -39.459 1.00 25.19 C
ANISOU 1615 CA MET A1006 3588 4448 1535 -273 -497 -1305 C
ATOM 1616 C MET A1006 -7.336 1.648 -40.718 1.00 27.32 C
ANISOU 1616 C MET A1006 3975 4524 1883 -371 -428 -1213 C
ATOM 1617 O MET A1006 -6.817 1.582 -41.835 1.00 24.55 O
ANISOU 1617 O MET A1006 3640 4100 1587 -453 -383 -1117 O
ATOM 1618 CB MET A1006 -6.585 0.425 -38.636 1.00 27.51 C
ANISOU 1618 CB MET A1006 3924 4897 1634 -104 -395 -1215 C
ATOM 1619 CG MET A1006 -5.989 -0.786 -39.309 1.00 31.08 C
ANISOU 1619 CG MET A1006 4421 5327 2061 -70 -257 -1040 C
ATOM 1620 SD MET A1006 -6.662 -2.302 -38.619 1.00 35.56 S
ANISOU 1620 SD MET A1006 5096 5927 2489 92 -86 -891 S
ATOM 1621 CE MET A1006 -5.282 -3.394 -38.817 1.00 32.03 C
ANISOU 1621 CE MET A1006 4621 5538 2012 216 3 -742 C
ATOM 1622 N LEU A1007 -8.669 1.686 -40.516 1.00 25.55 N
ANISOU 1622 N LEU A1007 3813 4249 1646 -352 -423 -1252 N
ATOM 1623 CA LEU A1007 -9.677 1.632 -41.582 1.00 26.06 C
ANISOU 1623 CA LEU A1007 3961 4177 1766 -425 -392 -1197 C
ATOM 1624 C LEU A1007 -9.699 2.921 -42.400 1.00 29.47 C
ANISOU 1624 C LEU A1007 4381 4471 2346 -520 -495 -1207 C
ATOM 1625 O LEU A1007 -10.107 2.882 -43.542 1.00 27.61 O
ANISOU 1625 O LEU A1007 4205 4159 2125 -576 -479 -1118 O
ATOM 1626 CB LEU A1007 -11.080 1.304 -41.007 1.00 26.27 C
ANISOU 1626 CB LEU A1007 4009 4218 1754 -371 -357 -1245 C
ATOM 1627 CG LEU A1007 -11.510 -0.182 -40.892 1.00 30.79 C
ANISOU 1627 CG LEU A1007 4636 4821 2241 -336 -199 -1160 C
ATOM 1628 CD1 LEU A1007 -11.816 -0.795 -42.255 1.00 31.30 C
ANISOU 1628 CD1 LEU A1007 4766 4779 2347 -431 -150 -1107 C
ATOM 1629 CD2 LEU A1007 -10.521 -1.032 -40.089 1.00 32.11 C
ANISOU 1629 CD2 LEU A1007 4801 5100 2299 -233 -115 -1083 C
ATOM 1630 N ARG A1008 -9.250 4.059 -41.819 1.00 27.66 N
ANISOU 1630 N ARG A1008 4072 4208 2229 -534 -600 -1316 N
ATOM 1631 CA ARG A1008 -9.165 5.355 -42.501 1.00 27.65 C
ANISOU 1631 CA ARG A1008 4058 4023 2424 -626 -680 -1303 C
ATOM 1632 C ARG A1008 -8.070 5.287 -43.572 1.00 31.96 C
ANISOU 1632 C ARG A1008 4601 4543 2998 -726 -619 -1139 C
ATOM 1633 O ARG A1008 -8.241 5.831 -44.660 1.00 32.40 O
ANISOU 1633 O ARG A1008 4706 4475 3128 -790 -613 -1006 O
ATOM 1634 CB ARG A1008 -8.843 6.458 -41.487 1.00 28.68 C
ANISOU 1634 CB ARG A1008 4092 4107 2697 -627 -791 -1502 C
ATOM 1635 CG ARG A1008 -9.054 7.861 -42.015 1.00 40.46 C
ANISOU 1635 CG ARG A1008 5583 5341 4449 -703 -865 -1504 C
ATOM 1636 CD ARG A1008 -8.517 8.878 -41.038 1.00 49.68 C
ANISOU 1636 CD ARG A1008 6643 6441 5793 -731 -968 -1746 C
ATOM 1637 NE ARG A1008 -8.570 10.221 -41.607 1.00 56.48 N
ANISOU 1637 NE ARG A1008 7505 6990 6966 -820 -1015 -1726 N
ATOM 1638 CZ ARG A1008 -8.246 11.326 -40.951 1.00 71.91 C
ANISOU 1638 CZ ARG A1008 9374 8783 9166 -870 -1107 -1952 C
ATOM 1639 NH1 ARG A1008 -7.831 11.261 -39.690 1.00 61.69 N
ANISOU 1639 NH1 ARG A1008 7976 7664 7798 -834 -1183 -2243 N
ATOM 1640 NH2 ARG A1008 -8.331 12.506 -41.548 1.00 60.00 N
ANISOU 1640 NH2 ARG A1008 7882 6935 7980 -950 -1123 -1891 N
ATOM 1641 N ILE A1009 -6.952 4.612 -43.255 1.00 27.99 N
ANISOU 1641 N ILE A1009 4032 4179 2423 -721 -565 -1137 N
ATOM 1642 CA ILE A1009 -5.815 4.404 -44.153 1.00 27.53 C
ANISOU 1642 CA ILE A1009 3940 4145 2376 -795 -479 -998 C
ATOM 1643 C ILE A1009 -6.187 3.388 -45.259 1.00 31.39 C
ANISOU 1643 C ILE A1009 4552 4667 2709 -771 -362 -859 C
ATOM 1644 O ILE A1009 -6.005 3.677 -46.445 1.00 31.67 O
ANISOU 1644 O ILE A1009 4626 4653 2755 -840 -314 -724 O
ATOM 1645 CB ILE A1009 -4.558 3.978 -43.326 1.00 30.02 C
ANISOU 1645 CB ILE A1009 4115 4629 2663 -760 -474 -1067 C
ATOM 1646 CG1 ILE A1009 -3.962 5.183 -42.552 1.00 29.37 C
ANISOU 1646 CG1 ILE A1009 3878 4514 2768 -833 -605 -1232 C
ATOM 1647 CG2 ILE A1009 -3.494 3.288 -44.200 1.00 30.60 C
ANISOU 1647 CG2 ILE A1009 4151 4780 2695 -783 -343 -923 C
ATOM 1648 CD1 ILE A1009 -3.192 4.814 -41.284 1.00 31.67 C
ANISOU 1648 CD1 ILE A1009 4028 5034 2972 -740 -676 -1384 C
ATOM 1649 N ASP A1010 -6.737 2.227 -44.854 1.00 27.18 N
ANISOU 1649 N ASP A1010 4077 4214 2034 -673 -314 -899 N
ATOM 1650 CA ASP A1010 -7.101 1.095 -45.697 1.00 26.93 C
ANISOU 1650 CA ASP A1010 4149 4207 1877 -648 -206 -840 C
ATOM 1651 C ASP A1010 -8.374 1.267 -46.532 1.00 33.06 C
ANISOU 1651 C ASP A1010 5017 4916 2627 -682 -244 -831 C
ATOM 1652 O ASP A1010 -8.324 1.026 -47.741 1.00 32.82 O
ANISOU 1652 O ASP A1010 5046 4906 2517 -713 -196 -761 O
ATOM 1653 CB ASP A1010 -7.195 -0.171 -44.841 1.00 28.21 C
ANISOU 1653 CB ASP A1010 4328 4431 1958 -542 -131 -882 C
ATOM 1654 CG ASP A1010 -5.860 -0.685 -44.338 1.00 33.66 C
ANISOU 1654 CG ASP A1010 4938 5226 2626 -466 -72 -851 C
ATOM 1655 OD1 ASP A1010 -4.815 -0.359 -44.964 1.00 33.57 O
ANISOU 1655 OD1 ASP A1010 4860 5249 2647 -511 -46 -800 O
ATOM 1656 OD2 ASP A1010 -5.854 -1.419 -43.332 1.00 34.14 O
ANISOU 1656 OD2 ASP A1010 4991 5348 2634 -352 -43 -861 O
ATOM 1657 N GLU A1011 -9.510 1.646 -45.900 1.00 30.21 N
ANISOU 1657 N GLU A1011 4655 4509 2313 -659 -330 -911 N
ATOM 1658 CA GLU A1011 -10.795 1.819 -46.584 1.00 30.11 C
ANISOU 1658 CA GLU A1011 4691 4462 2289 -671 -389 -918 C
ATOM 1659 C GLU A1011 -11.047 3.228 -47.115 1.00 34.78 C
ANISOU 1659 C GLU A1011 5275 4966 2974 -694 -500 -847 C
ATOM 1660 O GLU A1011 -11.704 3.371 -48.151 1.00 34.98 O
ANISOU 1660 O GLU A1011 5346 5002 2940 -696 -541 -781 O
ATOM 1661 CB GLU A1011 -11.970 1.377 -45.699 1.00 31.37 C
ANISOU 1661 CB GLU A1011 4829 4630 2461 -625 -398 -1032 C
ATOM 1662 CG GLU A1011 -12.618 0.063 -46.103 1.00 44.38 C
ANISOU 1662 CG GLU A1011 6516 6308 4037 -642 -314 -1070 C
ATOM 1663 CD GLU A1011 -13.229 -0.021 -47.491 1.00 67.19 C
ANISOU 1663 CD GLU A1011 9442 9220 6866 -689 -364 -1072 C
ATOM 1664 OE1 GLU A1011 -13.101 -1.093 -48.126 1.00 63.16 O
ANISOU 1664 OE1 GLU A1011 8981 8736 6282 -720 -282 -1111 O
ATOM 1665 OE2 GLU A1011 -13.839 0.976 -47.944 1.00 62.17 O
ANISOU 1665 OE2 GLU A1011 8786 8583 6253 -680 -490 -1043 O
ATOM 1666 N GLY A1012 -10.576 4.244 -46.391 1.00 30.73 N
ANISOU 1666 N GLY A1012 4703 4365 2610 -701 -554 -869 N
ATOM 1667 CA GLY A1012 -10.774 5.643 -46.765 1.00 30.45 C
ANISOU 1667 CA GLY A1012 4662 4178 2729 -718 -644 -798 C
ATOM 1668 C GLY A1012 -11.993 6.278 -46.125 1.00 34.38 C
ANISOU 1668 C GLY A1012 5135 4598 3329 -641 -748 -909 C
ATOM 1669 O GLY A1012 -13.025 5.622 -45.955 1.00 33.79 O
ANISOU 1669 O GLY A1012 5061 4609 3167 -585 -756 -979 O
ATOM 1670 N LEU A1013 -11.877 7.571 -45.775 1.00 31.34 N
ANISOU 1670 N LEU A1013 4714 4035 3157 -642 -819 -938 N
ATOM 1671 CA LEU A1013 -12.934 8.340 -45.124 1.00 31.40 C
ANISOU 1671 CA LEU A1013 4688 3942 3299 -549 -912 -1067 C
ATOM 1672 C LEU A1013 -13.504 9.424 -46.030 1.00 36.37 C
ANISOU 1672 C LEU A1013 5354 4387 4076 -508 -985 -910 C
ATOM 1673 O LEU A1013 -12.766 10.277 -46.525 1.00 36.37 O
ANISOU 1673 O LEU A1013 5378 4211 4230 -573 -977 -768 O
ATOM 1674 CB LEU A1013 -12.414 8.934 -43.803 1.00 31.68 C
ANISOU 1674 CB LEU A1013 4651 3912 3474 -550 -942 -1285 C
ATOM 1675 CG LEU A1013 -13.345 9.853 -43.010 1.00 36.94 C
ANISOU 1675 CG LEU A1013 5275 4463 4298 -441 -1025 -1473 C
ATOM 1676 CD1 LEU A1013 -14.460 9.079 -42.382 1.00 37.57 C
ANISOU 1676 CD1 LEU A1013 5325 4738 4213 -333 -1001 -1589 C
ATOM 1677 CD2 LEU A1013 -12.585 10.557 -41.916 1.00 39.26 C
ANISOU 1677 CD2 LEU A1013 5501 4674 4740 -469 -1068 -1702 C
ATOM 1678 N ARG A1014 -14.830 9.389 -46.230 1.00 33.45 N
ANISOU 1678 N ARG A1014 4976 4060 3674 -393 -1050 -922 N
ATOM 1679 CA ARG A1014 -15.557 10.357 -47.047 1.00 33.50 C
ANISOU 1679 CA ARG A1014 5004 3924 3798 -298 -1139 -764 C
ATOM 1680 C ARG A1014 -16.525 11.119 -46.142 1.00 39.49 C
ANISOU 1680 C ARG A1014 5689 4562 4751 -163 -1214 -949 C
ATOM 1681 O ARG A1014 -17.380 10.504 -45.506 1.00 38.82 O
ANISOU 1681 O ARG A1014 5531 4641 4579 -100 -1216 -1122 O
ATOM 1682 CB ARG A1014 -16.316 9.658 -48.198 1.00 32.11 C
ANISOU 1682 CB ARG A1014 4852 3951 3398 -251 -1175 -624 C
ATOM 1683 CG ARG A1014 -15.433 9.018 -49.268 1.00 42.11 C
ANISOU 1683 CG ARG A1014 6201 5339 4459 -350 -1102 -441 C
ATOM 1684 CD ARG A1014 -15.234 7.531 -49.020 1.00 57.70 C
ANISOU 1684 CD ARG A1014 8167 7528 6230 -429 -1019 -586 C
ATOM 1685 NE ARG A1014 -14.712 6.823 -50.191 1.00 69.46 N
ANISOU 1685 NE ARG A1014 9728 9169 7494 -481 -965 -455 N
ATOM 1686 CZ ARG A1014 -14.367 5.538 -50.193 1.00 87.27 C
ANISOU 1686 CZ ARG A1014 11997 11573 9590 -548 -875 -556 C
ATOM 1687 NH1 ARG A1014 -13.905 4.971 -51.299 1.00 80.94 N
ANISOU 1687 NH1 ARG A1014 11261 10907 8585 -577 -825 -464 N
ATOM 1688 NH2 ARG A1014 -14.477 4.812 -49.086 1.00 71.61 N
ANISOU 1688 NH2 ARG A1014 9963 9599 7646 -570 -824 -744 N
ATOM 1689 N LEU A1015 -16.365 12.449 -46.051 1.00 37.78 N
ANISOU 1689 N LEU A1015 5485 4049 4819 -122 -1257 -920 N
ATOM 1690 CA LEU A1015 -17.221 13.292 -45.215 1.00 38.33 C
ANISOU 1690 CA LEU A1015 5489 3969 5105 26 -1321 -1118 C
ATOM 1691 C LEU A1015 -18.525 13.724 -45.915 1.00 44.13 C
ANISOU 1691 C LEU A1015 6200 4684 5885 217 -1414 -985 C
ATOM 1692 O LEU A1015 -19.380 14.346 -45.277 1.00 44.37 O
ANISOU 1692 O LEU A1015 6154 4625 6080 374 -1462 -1153 O
ATOM 1693 CB LEU A1015 -16.449 14.517 -44.679 1.00 38.46 C
ANISOU 1693 CB LEU A1015 5519 3641 5452 -16 -1323 -1217 C
ATOM 1694 CG LEU A1015 -15.349 14.328 -43.599 1.00 43.13 C
ANISOU 1694 CG LEU A1015 6074 4267 6049 -158 -1278 -1475 C
ATOM 1695 CD1 LEU A1015 -15.663 13.197 -42.605 1.00 42.85 C
ANISOU 1695 CD1 LEU A1015 5975 4577 5729 -126 -1246 -1701 C
ATOM 1696 CD2 LEU A1015 -13.981 14.182 -44.225 1.00 46.54 C
ANISOU 1696 CD2 LEU A1015 6546 4662 6476 -355 -1216 -1290 C
ATOM 1697 N LYS A1016 -18.684 13.372 -47.208 1.00 41.14 N
ANISOU 1697 N LYS A1016 5870 4421 5339 223 -1445 -701 N
ATOM 1698 CA LYS A1016 -19.863 13.690 -48.025 1.00 41.26 C
ANISOU 1698 CA LYS A1016 5849 4486 5343 415 -1560 -544 C
ATOM 1699 C LYS A1016 -20.547 12.394 -48.538 1.00 45.19 C
ANISOU 1699 C LYS A1016 6283 5372 5516 399 -1593 -563 C
ATOM 1700 O LYS A1016 -19.857 11.399 -48.786 1.00 44.92 O
ANISOU 1700 O LYS A1016 6301 5503 5265 237 -1519 -553 O
ATOM 1701 CB LYS A1016 -19.457 14.613 -49.198 1.00 43.75 C
ANISOU 1701 CB LYS A1016 6278 4594 5751 464 -1588 -169 C
ATOM 1702 CG LYS A1016 -20.622 15.305 -49.898 1.00 59.62 C
ANISOU 1702 CG LYS A1016 8251 6584 7820 722 -1726 15 C
ATOM 1703 CD LYS A1016 -20.178 15.993 -51.179 1.00 70.51 C
ANISOU 1703 CD LYS A1016 9759 7833 9199 776 -1734 455 C
ATOM 1704 CE LYS A1016 -21.336 16.590 -51.943 1.00 76.38 C
ANISOU 1704 CE LYS A1016 10461 8612 9947 1067 -1889 673 C
ATOM 1705 NZ LYS A1016 -20.896 17.170 -53.240 1.00 82.30 N
ANISOU 1705 NZ LYS A1016 11348 9304 10616 1136 -1887 1152 N
ATOM 1706 N ILE A1017 -21.900 12.417 -48.696 1.00 41.12 N
ANISOU 1706 N ILE A1017 5637 4992 4994 569 -1705 -609 N
ATOM 1707 CA ILE A1017 -22.699 11.280 -49.194 1.00 40.55 C
ANISOU 1707 CA ILE A1017 5463 5272 4673 550 -1758 -667 C
ATOM 1708 C ILE A1017 -22.181 10.801 -50.564 1.00 43.16 C
ANISOU 1708 C ILE A1017 5901 5761 4739 479 -1790 -442 C
ATOM 1709 O ILE A1017 -22.028 11.615 -51.475 1.00 43.44 O
ANISOU 1709 O ILE A1017 6018 5715 4772 587 -1860 -162 O
ATOM 1710 CB ILE A1017 -24.240 11.572 -49.227 1.00 43.64 C
ANISOU 1710 CB ILE A1017 5660 5781 5140 760 -1896 -733 C
ATOM 1711 CG1 ILE A1017 -24.799 11.915 -47.825 1.00 43.97 C
ANISOU 1711 CG1 ILE A1017 5577 5722 5408 835 -1833 -995 C
ATOM 1712 CG2 ILE A1017 -25.011 10.397 -49.835 1.00 44.50 C
ANISOU 1712 CG2 ILE A1017 5640 6253 5014 705 -1966 -811 C
ATOM 1713 CD1 ILE A1017 -26.354 12.140 -47.736 1.00 48.10 C
ANISOU 1713 CD1 ILE A1017 5862 6390 6025 1046 -1941 -1094 C
ATOM 1714 N TYR A1018 -21.906 9.492 -50.688 1.00 37.86 N
ANISOU 1714 N TYR A1018 5232 5306 3848 310 -1724 -560 N
ATOM 1715 CA TYR A1018 -21.431 8.856 -51.920 1.00 37.09 C
ANISOU 1715 CA TYR A1018 5226 5398 3470 239 -1737 -424 C
ATOM 1716 C TYR A1018 -22.160 7.525 -52.174 1.00 41.86 C
ANISOU 1716 C TYR A1018 5719 6299 3887 161 -1774 -639 C
ATOM 1717 O TYR A1018 -22.921 7.075 -51.323 1.00 41.14 O
ANISOU 1717 O TYR A1018 5485 6237 3908 131 -1752 -863 O
ATOM 1718 CB TYR A1018 -19.898 8.658 -51.891 1.00 37.58 C
ANISOU 1718 CB TYR A1018 5447 5343 3490 82 -1573 -341 C
ATOM 1719 CG TYR A1018 -19.412 7.629 -50.892 1.00 38.47 C
ANISOU 1719 CG TYR A1018 5544 5464 3608 -80 -1430 -576 C
ATOM 1720 CD1 TYR A1018 -19.248 7.955 -49.548 1.00 39.84 C
ANISOU 1720 CD1 TYR A1018 5681 5465 3991 -94 -1360 -712 C
ATOM 1721 CD2 TYR A1018 -19.075 6.338 -51.296 1.00 38.85 C
ANISOU 1721 CD2 TYR A1018 5623 5695 3446 -202 -1362 -658 C
ATOM 1722 CE1 TYR A1018 -18.801 7.015 -48.625 1.00 39.98 C
ANISOU 1722 CE1 TYR A1018 5689 5520 3980 -210 -1232 -886 C
ATOM 1723 CE2 TYR A1018 -18.625 5.388 -50.378 1.00 39.33 C
ANISOU 1723 CE2 TYR A1018 5678 5741 3526 -322 -1222 -831 C
ATOM 1724 CZ TYR A1018 -18.475 5.737 -49.047 1.00 45.95 C
ANISOU 1724 CZ TYR A1018 6480 6432 4548 -320 -1158 -921 C
ATOM 1725 OH TYR A1018 -18.027 4.817 -48.130 1.00 49.01 O
ANISOU 1725 OH TYR A1018 6865 6831 4924 -407 -1023 -1050 O
ATOM 1726 N LYS A1019 -21.923 6.902 -53.345 1.00 38.96 N
ANISOU 1726 N LYS A1019 5412 6148 3244 122 -1817 -579 N
ATOM 1727 CA LYS A1019 -22.517 5.620 -53.704 1.00 38.57 C
ANISOU 1727 CA LYS A1019 5265 6356 3035 25 -1856 -814 C
ATOM 1728 C LYS A1019 -21.472 4.522 -53.540 1.00 43.32 C
ANISOU 1728 C LYS A1019 5978 6928 3552 -169 -1670 -919 C
ATOM 1729 O LYS A1019 -20.339 4.691 -53.993 1.00 43.79 O
ANISOU 1729 O LYS A1019 6197 6941 3499 -190 -1586 -752 O
ATOM 1730 CB LYS A1019 -23.038 5.650 -55.155 1.00 40.39 C
ANISOU 1730 CB LYS A1019 5470 6883 2991 136 -2055 -735 C
ATOM 1731 CG LYS A1019 -24.365 6.376 -55.334 1.00 48.79 C
ANISOU 1731 CG LYS A1019 6353 8060 4127 335 -2272 -708 C
ATOM 1732 CD LYS A1019 -24.913 6.135 -56.734 1.00 60.35 C
ANISOU 1732 CD LYS A1019 7754 9903 5272 428 -2488 -707 C
ATOM 1733 CE LYS A1019 -26.315 6.664 -56.943 1.00 67.04 C
ANISOU 1733 CE LYS A1019 8369 10927 6177 629 -2729 -725 C
ATOM 1734 NZ LYS A1019 -26.853 6.295 -58.284 1.00 66.07 N
ANISOU 1734 NZ LYS A1019 8161 11234 5707 713 -2965 -771 N
ATOM 1735 N ASP A1020 -21.838 3.402 -52.892 1.00 39.97 N
ANISOU 1735 N ASP A1020 5464 6522 3201 -303 -1589 -1176 N
ATOM 1736 CA ASP A1020 -20.926 2.264 -52.729 1.00 40.09 C
ANISOU 1736 CA ASP A1020 5578 6493 3161 -462 -1410 -1277 C
ATOM 1737 C ASP A1020 -20.908 1.405 -54.023 1.00 44.61 C
ANISOU 1737 C ASP A1020 6185 7285 3480 -513 -1466 -1379 C
ATOM 1738 O ASP A1020 -21.549 1.794 -55.008 1.00 43.80 O
ANISOU 1738 O ASP A1020 6035 7393 3214 -415 -1654 -1346 O
ATOM 1739 CB ASP A1020 -21.252 1.450 -51.448 1.00 41.92 C
ANISOU 1739 CB ASP A1020 5719 6615 3594 -570 -1270 -1460 C
ATOM 1740 CG ASP A1020 -22.537 0.625 -51.437 1.00 53.72 C
ANISOU 1740 CG ASP A1020 7024 8227 5160 -647 -1318 -1693 C
ATOM 1741 OD1 ASP A1020 -23.373 0.801 -52.353 1.00 55.63 O
ANISOU 1741 OD1 ASP A1020 7163 8665 5309 -600 -1509 -1750 O
ATOM 1742 OD2 ASP A1020 -22.710 -0.191 -50.505 1.00 57.94 O
ANISOU 1742 OD2 ASP A1020 7501 8666 5847 -754 -1163 -1808 O
ATOM 1743 N THR A1021 -20.182 0.256 -54.033 1.00 42.14 N
ANISOU 1743 N THR A1021 5953 6935 3123 -642 -1310 -1508 N
ATOM 1744 CA THR A1021 -20.090 -0.619 -55.226 1.00 42.37 C
ANISOU 1744 CA THR A1021 6023 7158 2917 -689 -1344 -1664 C
ATOM 1745 C THR A1021 -21.461 -1.055 -55.758 1.00 45.49 C
ANISOU 1745 C THR A1021 6240 7757 3285 -717 -1532 -1911 C
ATOM 1746 O THR A1021 -21.629 -1.170 -56.968 1.00 44.80 O
ANISOU 1746 O THR A1021 6159 7931 2934 -671 -1676 -1981 O
ATOM 1747 CB THR A1021 -19.164 -1.831 -54.994 1.00 52.16 C
ANISOU 1747 CB THR A1021 7363 8270 4183 -809 -1129 -1792 C
ATOM 1748 OG1 THR A1021 -19.554 -2.530 -53.810 1.00 53.12 O
ANISOU 1748 OG1 THR A1021 7407 8196 4580 -912 -1009 -1911 O
ATOM 1749 CG2 THR A1021 -17.695 -1.442 -54.922 1.00 51.21 C
ANISOU 1749 CG2 THR A1021 7403 8063 3991 -763 -983 -1567 C
ATOM 1750 N GLU A1022 -22.440 -1.253 -54.851 1.00 42.11 N
ANISOU 1750 N GLU A1022 5638 7239 3122 -785 -1530 -2040 N
ATOM 1751 CA GLU A1022 -23.810 -1.668 -55.165 1.00 41.77 C
ANISOU 1751 CA GLU A1022 5366 7369 3136 -841 -1693 -2293 C
ATOM 1752 C GLU A1022 -24.705 -0.494 -55.597 1.00 44.64 C
ANISOU 1752 C GLU A1022 5596 7942 3423 -657 -1946 -2175 C
ATOM 1753 O GLU A1022 -25.836 -0.718 -56.027 1.00 43.52 O
ANISOU 1753 O GLU A1022 5239 8014 3283 -671 -2128 -2377 O
ATOM 1754 CB GLU A1022 -24.434 -2.405 -53.968 1.00 43.21 C
ANISOU 1754 CB GLU A1022 5404 7362 3654 -994 -1541 -2443 C
ATOM 1755 CG GLU A1022 -23.745 -3.710 -53.608 1.00 53.85 C
ANISOU 1755 CG GLU A1022 6854 8504 5103 -1168 -1305 -2574 C
ATOM 1756 CD GLU A1022 -24.369 -4.440 -52.437 1.00 75.75 C
ANISOU 1756 CD GLU A1022 9490 11088 8201 -1312 -1129 -2666 C
ATOM 1757 OE1 GLU A1022 -24.280 -3.924 -51.300 1.00 78.64 O
ANISOU 1757 OE1 GLU A1022 9866 11331 8685 -1249 -1012 -2478 O
ATOM 1758 OE2 GLU A1022 -24.947 -5.529 -52.654 1.00 69.11 O
ANISOU 1758 OE2 GLU A1022 8530 10228 7501 -1489 -1101 -2929 O
ATOM 1759 N GLY A1023 -24.192 0.733 -55.464 1.00 41.18 N
ANISOU 1759 N GLY A1023 5272 7429 2948 -488 -1953 -1856 N
ATOM 1760 CA GLY A1023 -24.902 1.959 -55.814 1.00 40.46 C
ANISOU 1760 CA GLY A1023 5089 7469 2815 -274 -2166 -1679 C
ATOM 1761 C GLY A1023 -25.779 2.536 -54.716 1.00 43.21 C
ANISOU 1761 C GLY A1023 5260 7694 3464 -214 -2172 -1676 C
ATOM 1762 O GLY A1023 -26.640 3.377 -54.999 1.00 43.07 O
ANISOU 1762 O GLY A1023 5110 7803 3453 -29 -2364 -1590 O
ATOM 1763 N TYR A1024 -25.582 2.087 -53.454 1.00 38.16 N
ANISOU 1763 N TYR A1024 4611 6825 3062 -345 -1957 -1763 N
ATOM 1764 CA TYR A1024 -26.355 2.591 -52.305 1.00 37.00 C
ANISOU 1764 CA TYR A1024 4301 6575 3180 -286 -1919 -1779 C
ATOM 1765 C TYR A1024 -25.649 3.769 -51.631 1.00 37.58 C
ANISOU 1765 C TYR A1024 4521 6420 3338 -149 -1848 -1549 C
ATOM 1766 O TYR A1024 -24.419 3.763 -51.516 1.00 35.73 O
ANISOU 1766 O TYR A1024 4499 6035 3044 -202 -1722 -1436 O
ATOM 1767 CB TYR A1024 -26.592 1.510 -51.238 1.00 37.51 C
ANISOU 1767 CB TYR A1024 4272 6543 3437 -480 -1709 -1977 C
ATOM 1768 CG TYR A1024 -27.278 0.238 -51.675 1.00 38.16 C
ANISOU 1768 CG TYR A1024 4196 6765 3539 -669 -1725 -2241 C
ATOM 1769 CD1 TYR A1024 -28.462 0.277 -52.406 1.00 39.82 C
ANISOU 1769 CD1 TYR A1024 4154 7231 3743 -637 -1949 -2389 C
ATOM 1770 CD2 TYR A1024 -26.824 -1.002 -51.239 1.00 38.59 C
ANISOU 1770 CD2 TYR A1024 4319 6679 3664 -878 -1509 -2356 C
ATOM 1771 CE1 TYR A1024 -29.132 -0.894 -52.761 1.00 40.40 C
ANISOU 1771 CE1 TYR A1024 4047 7420 3882 -841 -1968 -2681 C
ATOM 1772 CE2 TYR A1024 -27.492 -2.176 -51.574 1.00 39.38 C
ANISOU 1772 CE2 TYR A1024 4262 6847 3852 -1075 -1503 -2622 C
ATOM 1773 CZ TYR A1024 -28.642 -2.119 -52.341 1.00 46.52 C
ANISOU 1773 CZ TYR A1024 4911 8008 4757 -1071 -1736 -2802 C
ATOM 1774 OH TYR A1024 -29.285 -3.282 -52.693 1.00 48.07 O
ANISOU 1774 OH TYR A1024 4932 8263 5071 -1293 -1740 -3107 O
ATOM 1775 N TYR A1025 -26.440 4.747 -51.140 1.00 33.11 N
ANISOU 1775 N TYR A1025 3820 5824 2937 20 -1925 -1511 N
ATOM 1776 CA TYR A1025 -25.925 5.922 -50.439 1.00 32.42 C
ANISOU 1776 CA TYR A1025 3841 5496 2983 153 -1870 -1353 C
ATOM 1777 C TYR A1025 -25.233 5.547 -49.149 1.00 34.09 C
ANISOU 1777 C TYR A1025 4127 5531 3295 32 -1640 -1435 C
ATOM 1778 O TYR A1025 -25.768 4.795 -48.330 1.00 33.13 O
ANISOU 1778 O TYR A1025 3874 5457 3254 -57 -1525 -1608 O
ATOM 1779 CB TYR A1025 -26.993 6.996 -50.240 1.00 34.15 C
ANISOU 1779 CB TYR A1025 3889 5718 3368 383 -2004 -1329 C
ATOM 1780 CG TYR A1025 -27.419 7.646 -51.537 1.00 37.05 C
ANISOU 1780 CG TYR A1025 4235 6228 3614 565 -2243 -1153 C
ATOM 1781 CD1 TYR A1025 -26.536 8.435 -52.267 1.00 39.19 C
ANISOU 1781 CD1 TYR A1025 4725 6378 3786 651 -2281 -869 C
ATOM 1782 CD2 TYR A1025 -28.702 7.458 -52.046 1.00 38.10 C
ANISOU 1782 CD2 TYR A1025 4114 6638 3725 654 -2427 -1255 C
ATOM 1783 CE1 TYR A1025 -26.913 9.014 -53.476 1.00 40.74 C
ANISOU 1783 CE1 TYR A1025 4917 6731 3832 841 -2488 -658 C
ATOM 1784 CE2 TYR A1025 -29.091 8.035 -53.255 1.00 39.00 C
ANISOU 1784 CE2 TYR A1025 4203 6933 3682 852 -2667 -1078 C
ATOM 1785 CZ TYR A1025 -28.194 8.818 -53.964 1.00 46.64 C
ANISOU 1785 CZ TYR A1025 5419 7779 4522 956 -2692 -761 C
ATOM 1786 OH TYR A1025 -28.565 9.408 -55.147 1.00 47.66 O
ANISOU 1786 OH TYR A1025 5539 8102 4468 1178 -2914 -535 O
ATOM 1787 N THR A1026 -23.991 6.021 -49.035 1.00 29.60 N
ANISOU 1787 N THR A1026 3764 4777 2704 24 -1570 -1296 N
ATOM 1788 CA THR A1026 -23.035 5.758 -47.969 1.00 28.54 C
ANISOU 1788 CA THR A1026 3732 4499 2612 -71 -1385 -1337 C
ATOM 1789 C THR A1026 -22.397 7.095 -47.497 1.00 31.66 C
ANISOU 1789 C THR A1026 4219 4669 3142 35 -1394 -1240 C
ATOM 1790 O THR A1026 -22.597 8.137 -48.125 1.00 30.85 O
ANISOU 1790 O THR A1026 4135 4486 3102 165 -1520 -1098 O
ATOM 1791 CB THR A1026 -22.004 4.727 -48.506 1.00 31.90 C
ANISOU 1791 CB THR A1026 4298 4959 2863 -233 -1296 -1301 C
ATOM 1792 OG1 THR A1026 -22.684 3.661 -49.168 1.00 31.58 O
ANISOU 1792 OG1 THR A1026 4173 5099 2726 -319 -1327 -1409 O
ATOM 1793 CG2 THR A1026 -21.156 4.132 -47.434 1.00 28.79 C
ANISOU 1793 CG2 THR A1026 3972 4482 2487 -327 -1110 -1358 C
ATOM 1794 N ILE A1027 -21.665 7.051 -46.366 1.00 28.12 N
ANISOU 1794 N ILE A1027 3819 4119 2746 -15 -1261 -1324 N
ATOM 1795 CA ILE A1027 -20.929 8.157 -45.743 1.00 28.06 C
ANISOU 1795 CA ILE A1027 3884 3897 2881 40 -1255 -1312 C
ATOM 1796 C ILE A1027 -19.865 7.568 -44.799 1.00 32.22 C
ANISOU 1796 C ILE A1027 4475 4424 3344 -72 -1115 -1395 C
ATOM 1797 O ILE A1027 -20.006 6.420 -44.374 1.00 30.43 O
ANISOU 1797 O ILE A1027 4217 4345 3001 -142 -1012 -1466 O
ATOM 1798 CB ILE A1027 -21.884 9.195 -45.065 1.00 31.16 C
ANISOU 1798 CB ILE A1027 4164 4202 3475 219 -1314 -1428 C
ATOM 1799 CG1 ILE A1027 -21.205 10.577 -44.922 1.00 31.29 C
ANISOU 1799 CG1 ILE A1027 4266 3931 3693 286 -1358 -1386 C
ATOM 1800 CG2 ILE A1027 -22.488 8.693 -43.741 1.00 31.44 C
ANISOU 1800 CG2 ILE A1027 4077 4364 3504 239 -1202 -1656 C
ATOM 1801 CD1 ILE A1027 -22.127 11.752 -45.146 1.00 35.53 C
ANISOU 1801 CD1 ILE A1027 4738 4321 4441 490 -1472 -1360 C
ATOM 1802 N GLY A1028 -18.813 8.344 -44.518 1.00 30.89 N
ANISOU 1802 N GLY A1028 4385 4086 3265 -88 -1116 -1373 N
ATOM 1803 CA GLY A1028 -17.713 7.967 -43.627 1.00 30.94 C
ANISOU 1803 CA GLY A1028 4430 4108 3218 -169 -1023 -1455 C
ATOM 1804 C GLY A1028 -16.898 6.794 -44.124 1.00 34.57 C
ANISOU 1804 C GLY A1028 4956 4680 3497 -293 -937 -1351 C
ATOM 1805 O GLY A1028 -16.517 6.756 -45.298 1.00 35.00 O
ANISOU 1805 O GLY A1028 5076 4713 3508 -347 -959 -1187 O
ATOM 1806 N ILE A1029 -16.637 5.822 -43.230 1.00 30.12 N
ANISOU 1806 N ILE A1029 4379 4246 2821 -317 -829 -1438 N
ATOM 1807 CA ILE A1029 -15.907 4.595 -43.566 1.00 29.32 C
ANISOU 1807 CA ILE A1029 4335 4233 2570 -405 -728 -1357 C
ATOM 1808 C ILE A1029 -16.944 3.497 -43.854 1.00 34.21 C
ANISOU 1808 C ILE A1029 4924 4954 3122 -426 -669 -1369 C
ATOM 1809 O ILE A1029 -17.181 2.618 -43.019 1.00 34.32 O
ANISOU 1809 O ILE A1029 4907 5047 3087 -423 -554 -1422 O
ATOM 1810 CB ILE A1029 -14.802 4.171 -42.528 1.00 31.59 C
ANISOU 1810 CB ILE A1029 4632 4582 2787 -407 -646 -1399 C
ATOM 1811 CG1 ILE A1029 -13.847 5.344 -42.173 1.00 30.60 C
ANISOU 1811 CG1 ILE A1029 4493 4364 2771 -407 -728 -1450 C
ATOM 1812 CG2 ILE A1029 -14.013 2.954 -43.046 1.00 32.77 C
ANISOU 1812 CG2 ILE A1029 4844 4787 2818 -474 -544 -1291 C
ATOM 1813 CD1 ILE A1029 -12.756 5.033 -41.207 1.00 28.94 C
ANISOU 1813 CD1 ILE A1029 4258 4257 2482 -398 -691 -1514 C
ATOM 1814 N GLY A1030 -17.580 3.607 -45.022 1.00 30.79 N
ANISOU 1814 N GLY A1030 4487 4519 2692 -444 -752 -1318 N
ATOM 1815 CA GLY A1030 -18.573 2.663 -45.522 1.00 29.85 C
ANISOU 1815 CA GLY A1030 4314 4496 2533 -488 -735 -1364 C
ATOM 1816 C GLY A1030 -19.857 2.501 -44.730 1.00 33.25 C
ANISOU 1816 C GLY A1030 4602 4986 3043 -453 -705 -1481 C
ATOM 1817 O GLY A1030 -20.414 1.397 -44.704 1.00 32.92 O
ANISOU 1817 O GLY A1030 4508 5006 2996 -531 -613 -1535 O
ATOM 1818 N HIS A1031 -20.365 3.593 -44.113 1.00 29.38 N
ANISOU 1818 N HIS A1031 4041 4471 2652 -338 -769 -1531 N
ATOM 1819 CA HIS A1031 -21.628 3.546 -43.367 1.00 28.81 C
ANISOU 1819 CA HIS A1031 3808 4481 2656 -282 -728 -1646 C
ATOM 1820 C HIS A1031 -22.851 3.696 -44.304 1.00 32.04 C
ANISOU 1820 C HIS A1031 4084 4957 3131 -262 -857 -1671 C
ATOM 1821 O HIS A1031 -23.139 4.797 -44.773 1.00 30.52 O
ANISOU 1821 O HIS A1031 3871 4720 3007 -146 -1008 -1641 O
ATOM 1822 CB HIS A1031 -21.670 4.564 -42.203 1.00 29.16 C
ANISOU 1822 CB HIS A1031 3819 4497 2766 -146 -722 -1735 C
ATOM 1823 CG HIS A1031 -22.932 4.470 -41.396 1.00 32.31 C
ANISOU 1823 CG HIS A1031 4043 5013 3222 -75 -648 -1852 C
ATOM 1824 ND1 HIS A1031 -23.084 3.514 -40.405 1.00 33.75 N
ANISOU 1824 ND1 HIS A1031 4182 5312 3331 -112 -450 -1878 N
ATOM 1825 CD2 HIS A1031 -24.082 5.177 -41.501 1.00 33.76 C
ANISOU 1825 CD2 HIS A1031 4074 5221 3531 36 -732 -1927 C
ATOM 1826 CE1 HIS A1031 -24.311 3.676 -39.934 1.00 33.09 C
ANISOU 1826 CE1 HIS A1031 3917 5330 3328 -41 -406 -1972 C
ATOM 1827 NE2 HIS A1031 -24.951 4.662 -40.564 1.00 33.43 N
ANISOU 1827 NE2 HIS A1031 3879 5326 3496 54 -577 -2019 N
ATOM 1828 N LEU A1032 -23.565 2.578 -44.567 1.00 29.18 N
ANISOU 1828 N LEU A1032 3623 4698 2766 -373 -799 -1728 N
ATOM 1829 CA LEU A1032 -24.764 2.558 -45.406 1.00 28.52 C
ANISOU 1829 CA LEU A1032 3370 4730 2738 -372 -930 -1792 C
ATOM 1830 C LEU A1032 -25.856 3.390 -44.749 1.00 33.60 C
ANISOU 1830 C LEU A1032 3824 5427 3517 -225 -964 -1867 C
ATOM 1831 O LEU A1032 -26.181 3.185 -43.570 1.00 33.10 O
ANISOU 1831 O LEU A1032 3678 5388 3509 -215 -800 -1935 O
ATOM 1832 CB LEU A1032 -25.254 1.121 -45.640 1.00 28.12 C
ANISOU 1832 CB LEU A1032 3228 4754 2702 -555 -835 -1887 C
ATOM 1833 CG LEU A1032 -26.358 0.939 -46.688 1.00 32.05 C
ANISOU 1833 CG LEU A1032 3539 5402 3235 -589 -1003 -1995 C
ATOM 1834 CD1 LEU A1032 -25.788 0.893 -48.062 1.00 31.52 C
ANISOU 1834 CD1 LEU A1032 3601 5371 3003 -610 -1160 -1956 C
ATOM 1835 CD2 LEU A1032 -27.130 -0.337 -46.449 1.00 34.22 C
ANISOU 1835 CD2 LEU A1032 3642 5726 3635 -775 -868 -2141 C
ATOM 1836 N LEU A1033 -26.372 4.371 -45.498 1.00 30.83 N
ANISOU 1836 N LEU A1033 3410 5097 3205 -86 -1169 -1837 N
ATOM 1837 CA LEU A1033 -27.421 5.253 -45.000 1.00 30.95 C
ANISOU 1837 CA LEU A1033 3236 5153 3370 94 -1221 -1908 C
ATOM 1838 C LEU A1033 -28.784 4.669 -45.319 1.00 35.54 C
ANISOU 1838 C LEU A1033 3537 5942 4024 57 -1262 -2023 C
ATOM 1839 O LEU A1033 -29.634 4.587 -44.428 1.00 35.39 O
ANISOU 1839 O LEU A1033 3319 6004 4124 89 -1146 -2135 O
ATOM 1840 CB LEU A1033 -27.284 6.684 -45.563 1.00 30.72 C
ANISOU 1840 CB LEU A1033 3278 5003 3391 297 -1409 -1794 C
ATOM 1841 CG LEU A1033 -26.047 7.469 -45.124 1.00 34.93 C
ANISOU 1841 CG LEU A1033 4036 5303 3934 333 -1365 -1717 C
ATOM 1842 CD1 LEU A1033 -25.737 8.587 -46.096 1.00 34.62 C
ANISOU 1842 CD1 LEU A1033 4101 5116 3937 461 -1537 -1536 C
ATOM 1843 CD2 LEU A1033 -26.200 7.998 -43.706 1.00 37.18 C
ANISOU 1843 CD2 LEU A1033 4266 5526 4334 434 -1248 -1869 C
ATOM 1844 N THR A1034 -28.982 4.242 -46.588 1.00 31.67 N
ANISOU 1844 N THR A1034 3016 5563 3454 -16 -1422 -2011 N
ATOM 1845 CA THR A1034 -30.237 3.693 -47.090 1.00 31.58 C
ANISOU 1845 CA THR A1034 2715 5773 3510 -70 -1512 -2151 C
ATOM 1846 C THR A1034 -30.035 2.893 -48.371 1.00 37.50 C
ANISOU 1846 C THR A1034 3509 6627 4111 -218 -1641 -2181 C
ATOM 1847 O THR A1034 -29.119 3.169 -49.146 1.00 36.70 O
ANISOU 1847 O THR A1034 3640 6472 3834 -186 -1729 -2048 O
ATOM 1848 CB THR A1034 -31.295 4.822 -47.261 1.00 39.20 C
ANISOU 1848 CB THR A1034 3460 6848 4587 185 -1697 -2155 C
ATOM 1849 OG1 THR A1034 -32.576 4.263 -47.543 1.00 38.06 O
ANISOU 1849 OG1 THR A1034 2974 6946 4543 126 -1762 -2323 O
ATOM 1850 CG2 THR A1034 -30.914 5.854 -48.321 1.00 38.10 C
ANISOU 1850 CG2 THR A1034 3460 6680 4337 381 -1942 -1971 C
ATOM 1851 N LYS A1035 -30.912 1.904 -48.587 1.00 36.24 N
ANISOU 1851 N LYS A1035 3113 6626 4032 -384 -1640 -2374 N
ATOM 1852 CA LYS A1035 -30.959 1.070 -49.782 1.00 36.24 C
ANISOU 1852 CA LYS A1035 3092 6764 3914 -531 -1780 -2494 C
ATOM 1853 C LYS A1035 -31.884 1.746 -50.813 1.00 41.17 C
ANISOU 1853 C LYS A1035 3509 7661 4472 -355 -2105 -2525 C
ATOM 1854 O LYS A1035 -31.879 1.365 -51.982 1.00 40.69 O
ANISOU 1854 O LYS A1035 3458 7774 4229 -394 -2294 -2597 O
ATOM 1855 CB LYS A1035 -31.460 -0.336 -49.431 1.00 38.55 C
ANISOU 1855 CB LYS A1035 3212 7058 4379 -815 -1611 -2716 C
ATOM 1856 CG LYS A1035 -30.366 -1.268 -48.924 1.00 54.02 C
ANISOU 1856 CG LYS A1035 5422 8772 6331 -994 -1344 -2674 C
ATOM 1857 CD LYS A1035 -30.922 -2.671 -48.714 1.00 63.89 C
ANISOU 1857 CD LYS A1035 6496 9988 7793 -1277 -1182 -2880 C
ATOM 1858 CE LYS A1035 -29.896 -3.677 -48.257 1.00 72.16 C
ANISOU 1858 CE LYS A1035 7778 10774 8864 -1435 -910 -2824 C
ATOM 1859 NZ LYS A1035 -30.541 -4.970 -47.901 1.00 77.91 N
ANISOU 1859 NZ LYS A1035 8316 11415 9871 -1701 -710 -2984 N
ATOM 1860 N SER A1036 -32.644 2.778 -50.373 1.00 38.67 N
ANISOU 1860 N SER A1036 3012 7395 4286 -134 -2172 -2467 N
ATOM 1861 CA SER A1036 -33.575 3.566 -51.185 1.00 38.88 C
ANISOU 1861 CA SER A1036 2820 7673 4281 97 -2474 -2455 C
ATOM 1862 C SER A1036 -32.831 4.397 -52.253 1.00 42.58 C
ANISOU 1862 C SER A1036 3544 8149 4485 300 -2676 -2209 C
ATOM 1863 O SER A1036 -31.819 5.014 -51.922 1.00 40.65 O
ANISOU 1863 O SER A1036 3589 7647 4209 371 -2563 -1998 O
ATOM 1864 CB SER A1036 -34.423 4.471 -50.293 1.00 42.67 C
ANISOU 1864 CB SER A1036 3081 8139 4993 306 -2440 -2437 C
ATOM 1865 OG SER A1036 -35.660 4.793 -50.906 1.00 53.66 O
ANISOU 1865 OG SER A1036 4122 9834 6434 459 -2695 -2524 O
ATOM 1866 N PRO A1037 -33.312 4.431 -53.528 1.00 41.04 N
ANISOU 1866 N PRO A1037 3238 8261 4097 395 -2969 -2228 N
ATOM 1867 CA PRO A1037 -32.599 5.190 -54.573 1.00 41.32 C
ANISOU 1867 CA PRO A1037 3531 8313 3856 599 -3109 -1945 C
ATOM 1868 C PRO A1037 -32.942 6.687 -54.618 1.00 46.07 C
ANISOU 1868 C PRO A1037 4109 8883 4513 961 -3271 -1671 C
ATOM 1869 O PRO A1037 -33.191 7.243 -55.694 1.00 46.10 O
ANISOU 1869 O PRO A1037 4090 9111 4313 1188 -3529 -1508 O
ATOM 1870 CB PRO A1037 -33.003 4.455 -55.858 1.00 43.02 C
ANISOU 1870 CB PRO A1037 3660 8831 3856 566 -3216 -2088 C
ATOM 1871 CG PRO A1037 -34.359 3.946 -55.580 1.00 46.73 C
ANISOU 1871 CG PRO A1037 3675 9590 4490 470 -3419 -2417 C
ATOM 1872 CD PRO A1037 -34.496 3.748 -54.093 1.00 42.65 C
ANISOU 1872 CD PRO A1037 3119 8744 4340 347 -3045 -2480 C
ATOM 1873 N SER A1038 -32.942 7.337 -53.443 1.00 42.74 N
ANISOU 1873 N SER A1038 3703 8166 4369 1032 -3092 -1618 N
ATOM 1874 CA SER A1038 -33.230 8.761 -53.260 1.00 42.30 C
ANISOU 1874 CA SER A1038 3644 7964 4462 1369 -3166 -1393 C
ATOM 1875 C SER A1038 -32.146 9.392 -52.403 1.00 46.28 C
ANISOU 1875 C SER A1038 4444 8039 5101 1354 -2932 -1253 C
ATOM 1876 O SER A1038 -31.792 8.840 -51.353 1.00 45.61 O
ANISOU 1876 O SER A1038 4390 7808 5130 1150 -2697 -1424 O
ATOM 1877 CB SER A1038 -34.587 8.944 -52.591 1.00 45.50 C
ANISOU 1877 CB SER A1038 3668 8492 5128 1499 -3208 -1577 C
ATOM 1878 OG SER A1038 -34.818 10.291 -52.215 1.00 55.46 O
ANISOU 1878 OG SER A1038 4938 9544 6591 1822 -3227 -1402 O
ATOM 1879 N LEU A1039 -31.604 10.539 -52.859 1.00 43.09 N
ANISOU 1879 N LEU A1039 4250 7436 4684 1570 -2995 -936 N
ATOM 1880 CA LEU A1039 -30.563 11.276 -52.136 1.00 42.84 C
ANISOU 1880 CA LEU A1039 4481 6982 4813 1562 -2804 -809 C
ATOM 1881 C LEU A1039 -31.159 11.977 -50.901 1.00 47.29 C
ANISOU 1881 C LEU A1039 4906 7348 5714 1707 -2716 -949 C
ATOM 1882 O LEU A1039 -30.492 12.057 -49.863 1.00 46.85 O
ANISOU 1882 O LEU A1039 4975 7036 5791 1597 -2511 -1046 O
ATOM 1883 CB LEU A1039 -29.823 12.259 -53.068 1.00 42.78 C
ANISOU 1883 CB LEU A1039 4723 6810 4723 1722 -2882 -418 C
ATOM 1884 CG LEU A1039 -28.724 13.140 -52.444 1.00 47.58 C
ANISOU 1884 CG LEU A1039 5584 6954 5541 1705 -2703 -277 C
ATOM 1885 CD1 LEU A1039 -27.544 12.315 -51.944 1.00 47.48 C
ANISOU 1885 CD1 LEU A1039 5743 6859 5440 1379 -2495 -396 C
ATOM 1886 CD2 LEU A1039 -28.265 14.203 -53.414 1.00 49.90 C
ANISOU 1886 CD2 LEU A1039 6061 7078 5821 1902 -2785 142 C
ATOM 1887 N ASN A1040 -32.431 12.437 -51.004 1.00 43.89 N
ANISOU 1887 N ASN A1040 4198 7073 5406 1964 -2873 -984 N
ATOM 1888 CA ASN A1040 -33.151 13.072 -49.898 1.00 43.87 C
ANISOU 1888 CA ASN A1040 4020 6937 5712 2137 -2792 -1146 C
ATOM 1889 C ASN A1040 -33.467 12.067 -48.789 1.00 47.76 C
ANISOU 1889 C ASN A1040 4343 7560 6243 1908 -2593 -1482 C
ATOM 1890 O ASN A1040 -33.418 12.438 -47.613 1.00 48.03 O
ANISOU 1890 O ASN A1040 4377 7410 6464 1944 -2416 -1626 O
ATOM 1891 CB ASN A1040 -34.399 13.797 -50.383 1.00 46.33 C
ANISOU 1891 CB ASN A1040 4066 7400 6138 2494 -3014 -1075 C
ATOM 1892 CG ASN A1040 -34.095 14.981 -51.275 1.00 75.34 C
ANISOU 1892 CG ASN A1040 7926 10870 9832 2780 -3170 -696 C
ATOM 1893 OD1 ASN A1040 -33.284 15.859 -50.950 1.00 69.95 O
ANISOU 1893 OD1 ASN A1040 7497 9764 9317 2833 -3060 -555 O
ATOM 1894 ND2 ASN A1040 -34.749 15.037 -52.421 1.00 69.51 N
ANISOU 1894 ND2 ASN A1040 7053 10429 8927 2971 -3431 -518 N
ATOM 1895 N ALA A1041 -33.721 10.782 -49.158 1.00 43.33 N
ANISOU 1895 N ALA A1041 3656 7305 5504 1665 -2607 -1605 N
ATOM 1896 CA ALA A1041 -33.944 9.678 -48.214 1.00 42.55 C
ANISOU 1896 CA ALA A1041 3418 7313 5435 1407 -2392 -1869 C
ATOM 1897 C ALA A1041 -32.639 9.396 -47.447 1.00 45.74 C
ANISOU 1897 C ALA A1041 4132 7461 5785 1206 -2155 -1863 C
ATOM 1898 O ALA A1041 -32.678 9.105 -46.249 1.00 45.65 O
ANISOU 1898 O ALA A1041 4075 7408 5862 1130 -1935 -2022 O
ATOM 1899 CB ALA A1041 -34.395 8.430 -48.955 1.00 43.11 C
ANISOU 1899 CB ALA A1041 3318 7701 5360 1187 -2477 -1979 C
ATOM 1900 N ALA A1042 -31.486 9.524 -48.136 1.00 41.31 N
ANISOU 1900 N ALA A1042 3873 6753 5069 1142 -2201 -1670 N
ATOM 1901 CA ALA A1042 -30.160 9.351 -47.552 1.00 40.59 C
ANISOU 1901 CA ALA A1042 4066 6433 4925 974 -2016 -1641 C
ATOM 1902 C ALA A1042 -29.840 10.504 -46.593 1.00 44.73 C
ANISOU 1902 C ALA A1042 4679 6672 5644 1138 -1933 -1651 C
ATOM 1903 O ALA A1042 -29.362 10.247 -45.489 1.00 44.31 O
ANISOU 1903 O ALA A1042 4688 6538 5609 1034 -1742 -1785 O
ATOM 1904 CB ALA A1042 -29.118 9.263 -48.648 1.00 41.10 C
ANISOU 1904 CB ALA A1042 4379 6446 4791 891 -2097 -1428 C
ATOM 1905 N LYS A1043 -30.141 11.764 -46.999 1.00 41.62 N
ANISOU 1905 N LYS A1043 4283 6133 5399 1406 -2080 -1520 N
ATOM 1906 CA LYS A1043 -29.934 12.969 -46.187 1.00 41.62 C
ANISOU 1906 CA LYS A1043 4353 5821 5638 1585 -2023 -1560 C
ATOM 1907 C LYS A1043 -30.792 12.929 -44.912 1.00 46.62 C
ANISOU 1907 C LYS A1043 4765 6546 6402 1667 -1892 -1851 C
ATOM 1908 O LYS A1043 -30.299 13.278 -43.840 1.00 45.62 O
ANISOU 1908 O LYS A1043 4726 6250 6356 1665 -1749 -2004 O
ATOM 1909 CB LYS A1043 -30.237 14.245 -46.997 1.00 43.51 C
ANISOU 1909 CB LYS A1043 4614 5877 6041 1876 -2206 -1334 C
ATOM 1910 CG LYS A1043 -29.117 14.662 -47.943 1.00 48.99 C
ANISOU 1910 CG LYS A1043 5589 6355 6672 1824 -2261 -1024 C
ATOM 1911 CD LYS A1043 -29.493 15.880 -48.772 1.00 54.12 C
ANISOU 1911 CD LYS A1043 6253 6831 7479 2131 -2426 -746 C
ATOM 1912 CE LYS A1043 -28.360 16.307 -49.674 1.00 60.17 C
ANISOU 1912 CE LYS A1043 7295 7379 8188 2071 -2439 -400 C
ATOM 1913 NZ LYS A1043 -28.766 17.405 -50.589 1.00 65.15 N
ANISOU 1913 NZ LYS A1043 7946 7865 8942 2384 -2592 -61 N
ATOM 1914 N SER A1044 -32.062 12.472 -45.030 1.00 44.59 N
ANISOU 1914 N SER A1044 4207 6585 6152 1732 -1937 -1939 N
ATOM 1915 CA SER A1044 -33.002 12.349 -43.911 1.00 44.87 C
ANISOU 1915 CA SER A1044 3985 6766 6298 1808 -1791 -2195 C
ATOM 1916 C SER A1044 -32.544 11.286 -42.915 1.00 50.21 C
ANISOU 1916 C SER A1044 4706 7540 6832 1545 -1544 -2339 C
ATOM 1917 O SER A1044 -32.635 11.509 -41.708 1.00 50.27 O
ANISOU 1917 O SER A1044 4677 7532 6893 1611 -1370 -2521 O
ATOM 1918 CB SER A1044 -34.405 12.041 -44.417 1.00 47.80 C
ANISOU 1918 CB SER A1044 3997 7449 6715 1902 -1904 -2231 C
ATOM 1919 OG SER A1044 -34.850 13.075 -45.281 1.00 56.18 O
ANISOU 1919 OG SER A1044 5009 8440 7896 2195 -2141 -2075 O
ATOM 1920 N GLU A1045 -32.022 10.147 -43.421 1.00 47.16 N
ANISOU 1920 N GLU A1045 4411 7254 6256 1269 -1526 -2254 N
ATOM 1921 CA GLU A1045 -31.505 9.057 -42.592 1.00 46.89 C
ANISOU 1921 CA GLU A1045 4442 7287 6086 1026 -1295 -2332 C
ATOM 1922 C GLU A1045 -30.208 9.473 -41.886 1.00 50.02 C
ANISOU 1922 C GLU A1045 5123 7459 6425 1008 -1204 -2331 C
ATOM 1923 O GLU A1045 -29.923 8.970 -40.801 1.00 49.40 O
ANISOU 1923 O GLU A1045 5067 7441 6261 929 -1001 -2435 O
ATOM 1924 CB GLU A1045 -31.301 7.778 -43.419 1.00 48.20 C
ANISOU 1924 CB GLU A1045 4632 7575 6107 761 -1314 -2250 C
ATOM 1925 CG GLU A1045 -31.401 6.503 -42.592 1.00 59.84 C
ANISOU 1925 CG GLU A1045 6032 9180 7526 544 -1064 -2340 C
ATOM 1926 CD GLU A1045 -32.792 6.086 -42.148 1.00 79.17 C
ANISOU 1926 CD GLU A1045 8123 11855 10105 553 -962 -2476 C
ATOM 1927 OE1 GLU A1045 -33.672 5.903 -43.021 1.00 69.89 O
ANISOU 1927 OE1 GLU A1045 6722 10829 9006 536 -1112 -2503 O
ATOM 1928 OE2 GLU A1045 -32.997 5.924 -40.924 1.00 73.17 O
ANISOU 1928 OE2 GLU A1045 7294 11148 9360 578 -728 -2560 O
ATOM 1929 N LEU A1046 -29.443 10.404 -42.498 1.00 46.16 N
ANISOU 1929 N LEU A1046 4834 6721 5983 1086 -1351 -2208 N
ATOM 1930 CA LEU A1046 -28.199 10.942 -41.951 1.00 45.62 C
ANISOU 1930 CA LEU A1046 5005 6419 5909 1062 -1301 -2224 C
ATOM 1931 C LEU A1046 -28.507 11.869 -40.769 1.00 49.94 C
ANISOU 1931 C LEU A1046 5491 6882 6602 1263 -1229 -2451 C
ATOM 1932 O LEU A1046 -27.930 11.679 -39.703 1.00 49.49 O
ANISOU 1932 O LEU A1046 5505 6846 6453 1208 -1090 -2597 O
ATOM 1933 CB LEU A1046 -27.378 11.660 -43.048 1.00 45.44 C
ANISOU 1933 CB LEU A1046 5180 6149 5934 1066 -1462 -2004 C
ATOM 1934 CG LEU A1046 -26.006 12.264 -42.664 1.00 49.86 C
ANISOU 1934 CG LEU A1046 5966 6442 6535 1004 -1427 -2006 C
ATOM 1935 CD1 LEU A1046 -25.029 11.203 -42.141 1.00 50.20 C
ANISOU 1935 CD1 LEU A1046 6111 6599 6362 775 -1291 -2041 C
ATOM 1936 CD2 LEU A1046 -25.388 12.972 -43.839 1.00 51.11 C
ANISOU 1936 CD2 LEU A1046 6277 6368 6774 1012 -1560 -1749 C
ATOM 1937 N ASP A1047 -29.443 12.833 -40.948 1.00 47.28 N
ANISOU 1937 N ASP A1047 5011 6474 6479 1514 -1326 -2494 N
ATOM 1938 CA ASP A1047 -29.896 13.790 -39.924 1.00 47.41 C
ANISOU 1938 CA ASP A1047 4944 6402 6669 1750 -1266 -2741 C
ATOM 1939 C ASP A1047 -30.505 13.077 -38.708 1.00 51.43 C
ANISOU 1939 C ASP A1047 5276 7217 7046 1745 -1050 -2963 C
ATOM 1940 O ASP A1047 -30.358 13.560 -37.584 1.00 51.05 O
ANISOU 1940 O ASP A1047 5243 7145 7007 1855 -942 -3203 O
ATOM 1941 CB ASP A1047 -30.921 14.784 -40.510 1.00 49.57 C
ANISOU 1941 CB ASP A1047 5067 6569 7200 2038 -1413 -2702 C
ATOM 1942 CG ASP A1047 -30.455 15.606 -41.706 1.00 62.16 C
ANISOU 1942 CG ASP A1047 6826 7853 8939 2101 -1610 -2438 C
ATOM 1943 OD1 ASP A1047 -29.271 15.483 -42.092 1.00 62.21 O
ANISOU 1943 OD1 ASP A1047 7067 7709 8859 1905 -1625 -2295 O
ATOM 1944 OD2 ASP A1047 -31.282 16.366 -42.264 1.00 69.15 O
ANISOU 1944 OD2 ASP A1047 7595 8658 10020 2358 -1740 -2353 O
ATOM 1945 N LYS A1048 -31.182 11.932 -38.943 1.00 47.83 N
ANISOU 1945 N LYS A1048 4650 7052 6470 1613 -980 -2885 N
ATOM 1946 CA LYS A1048 -31.803 11.077 -37.927 1.00 47.86 C
ANISOU 1946 CA LYS A1048 4473 7360 6353 1565 -742 -3016 C
ATOM 1947 C LYS A1048 -30.706 10.386 -37.087 1.00 51.84 C
ANISOU 1947 C LYS A1048 5178 7903 6615 1389 -579 -3029 C
ATOM 1948 O LYS A1048 -30.891 10.187 -35.886 1.00 51.70 O
ANISOU 1948 O LYS A1048 5097 8066 6481 1443 -375 -3180 O
ATOM 1949 CB LYS A1048 -32.709 10.040 -38.621 1.00 50.80 C
ANISOU 1949 CB LYS A1048 4617 7960 6722 1425 -737 -2902 C
ATOM 1950 CG LYS A1048 -33.557 9.157 -37.707 1.00 67.19 C
ANISOU 1950 CG LYS A1048 6452 10338 8741 1360 -472 -2995 C
ATOM 1951 CD LYS A1048 -34.308 8.119 -38.541 1.00 77.95 C
ANISOU 1951 CD LYS A1048 7604 11866 10148 1163 -495 -2893 C
ATOM 1952 CE LYS A1048 -34.996 7.060 -37.716 1.00 90.41 C
ANISOU 1952 CE LYS A1048 8957 13696 11697 1028 -200 -2936 C
ATOM 1953 NZ LYS A1048 -35.643 6.030 -38.577 1.00 98.31 N
ANISOU 1953 NZ LYS A1048 9753 14813 12789 796 -234 -2871 N
ATOM 1954 N ALA A1049 -29.566 10.042 -37.723 1.00 48.13 N
ANISOU 1954 N ALA A1049 4943 7287 6056 1203 -668 -2864 N
ATOM 1955 CA ALA A1049 -28.420 9.387 -37.086 1.00 47.79 C
ANISOU 1955 CA ALA A1049 5091 7272 5793 1049 -553 -2843 C
ATOM 1956 C ALA A1049 -27.492 10.382 -36.373 1.00 52.59 C
ANISOU 1956 C ALA A1049 5865 7717 6399 1152 -597 -3006 C
ATOM 1957 O ALA A1049 -26.933 10.050 -35.324 1.00 52.40 O
ANISOU 1957 O ALA A1049 5907 7826 6178 1132 -469 -3101 O
ATOM 1958 CB ALA A1049 -27.631 8.597 -38.118 1.00 48.15 C
ANISOU 1958 CB ALA A1049 5284 7247 5766 820 -625 -2614 C
ATOM 1959 N ILE A1050 -27.304 11.580 -36.957 1.00 48.69 N
ANISOU 1959 N ILE A1050 5434 6937 6127 1257 -780 -3030 N
ATOM 1960 CA ILE A1050 -26.415 12.597 -36.410 1.00 48.41 C
ANISOU 1960 CA ILE A1050 5542 6686 6165 1324 -840 -3208 C
ATOM 1961 C ILE A1050 -27.125 13.432 -35.338 1.00 53.02 C
ANISOU 1961 C ILE A1050 6005 7309 6831 1571 -775 -3533 C
ATOM 1962 O ILE A1050 -26.583 13.611 -34.249 1.00 52.85 O
ANISOU 1962 O ILE A1050 6038 7360 6683 1605 -708 -3770 O
ATOM 1963 CB ILE A1050 -25.754 13.458 -37.535 1.00 51.33 C
ANISOU 1963 CB ILE A1050 6056 6684 6765 1290 -1033 -3055 C
ATOM 1964 CG1 ILE A1050 -24.993 12.603 -38.587 1.00 51.37 C
ANISOU 1964 CG1 ILE A1050 6179 6693 6646 1056 -1077 -2750 C
ATOM 1965 CG2 ILE A1050 -24.858 14.568 -36.970 1.00 52.57 C
ANISOU 1965 CG2 ILE A1050 6333 6571 7071 1331 -1088 -3268 C
ATOM 1966 CD1 ILE A1050 -23.822 11.690 -38.104 1.00 58.60 C
ANISOU 1966 CD1 ILE A1050 7214 7737 7316 858 -987 -2732 C
ATOM 1967 N GLY A1051 -28.318 13.920 -35.656 1.00 49.84 N
ANISOU 1967 N GLY A1051 5431 6883 6622 1756 -801 -3555 N
ATOM 1968 CA GLY A1051 -29.109 14.748 -34.758 1.00 49.73 C
ANISOU 1968 CA GLY A1051 5278 6899 6719 2025 -734 -3865 C
ATOM 1969 C GLY A1051 -29.083 16.215 -35.130 1.00 55.25 C
ANISOU 1969 C GLY A1051 6030 7187 7777 2213 -893 -3967 C
ATOM 1970 O GLY A1051 -29.397 17.063 -34.291 1.00 55.69 O
ANISOU 1970 O GLY A1051 6030 7180 7948 2432 -850 -4292 O
ATOM 1971 N ARG A1052 -28.709 16.526 -36.394 1.00 52.52 N
ANISOU 1971 N ARG A1052 5794 6551 7611 2139 -1065 -3686 N
ATOM 1972 CA ARG A1052 -28.626 17.889 -36.949 1.00 52.71 C
ANISOU 1972 CA ARG A1052 5892 6125 8010 2300 -1211 -3678 C
ATOM 1973 C ARG A1052 -28.850 17.910 -38.475 1.00 59.25 C
ANISOU 1973 C ARG A1052 6737 6826 8951 2288 -1363 -3272 C
ATOM 1974 O ARG A1052 -28.713 16.870 -39.130 1.00 59.00 O
ANISOU 1974 O ARG A1052 6711 7017 8691 2092 -1373 -3030 O
ATOM 1975 CB ARG A1052 -27.279 18.563 -36.588 1.00 50.15 C
ANISOU 1975 CB ARG A1052 5785 5480 7790 2185 -1249 -3822 C
ATOM 1976 CG ARG A1052 -26.057 17.939 -37.251 1.00 53.40 C
ANISOU 1976 CG ARG A1052 6371 5866 8054 1877 -1294 -3555 C
ATOM 1977 CD ARG A1052 -24.814 18.796 -37.126 1.00 57.83 C
ANISOU 1977 CD ARG A1052 7101 6053 8817 1772 -1353 -3665 C
ATOM 1978 NE ARG A1052 -23.753 18.346 -38.031 1.00 61.75 N
ANISOU 1978 NE ARG A1052 7740 6477 9246 1512 -1402 -3340 N
ATOM 1979 CZ ARG A1052 -23.591 18.781 -39.278 1.00 72.73 C
ANISOU 1979 CZ ARG A1052 9213 7585 10836 1489 -1488 -3000 C
ATOM 1980 NH1 ARG A1052 -24.418 19.687 -39.787 1.00 62.84 N
ANISOU 1980 NH1 ARG A1052 7924 6077 9875 1720 -1552 -2916 N
ATOM 1981 NH2 ARG A1052 -22.597 18.319 -40.024 1.00 53.16 N
ANISOU 1981 NH2 ARG A1052 6852 5090 8255 1256 -1503 -2730 N
ATOM 1982 N ASN A1053 -29.155 19.099 -39.042 1.00 57.37 N
ANISOU 1982 N ASN A1053 6515 6224 9059 2506 -1480 -3197 N
ATOM 1983 CA ASN A1053 -29.347 19.261 -40.488 1.00 57.60 C
ANISOU 1983 CA ASN A1053 6574 6135 9178 2543 -1635 -2789 C
ATOM 1984 C ASN A1053 -27.975 19.322 -41.187 1.00 61.15 C
ANISOU 1984 C ASN A1053 7282 6336 9617 2299 -1683 -2543 C
ATOM 1985 O ASN A1053 -27.419 20.398 -41.433 1.00 60.63 O
ANISOU 1985 O ASN A1053 7358 5826 9851 2350 -1729 -2478 O
ATOM 1986 CB ASN A1053 -30.253 20.462 -40.805 1.00 59.73 C
ANISOU 1986 CB ASN A1053 6750 6135 9808 2907 -1728 -2758 C
ATOM 1987 CG ASN A1053 -31.693 20.279 -40.363 1.00 91.26 C
ANISOU 1987 CG ASN A1053 10439 10443 13792 3151 -1694 -2930 C
ATOM 1988 OD1 ASN A1053 -32.350 19.268 -40.664 1.00 87.62 O
ANISOU 1988 OD1 ASN A1053 9802 10398 13094 3081 -1698 -2836 O
ATOM 1989 ND2 ASN A1053 -32.224 21.266 -39.649 1.00 84.09 N
ANISOU 1989 ND2 ASN A1053 9447 9335 13167 3443 -1652 -3203 N
ATOM 1990 N THR A1054 -27.423 18.129 -41.449 1.00 57.51 N
ANISOU 1990 N THR A1054 6869 6158 8825 2026 -1650 -2421 N
ATOM 1991 CA THR A1054 -26.100 17.887 -42.039 1.00 57.24 C
ANISOU 1991 CA THR A1054 7043 6004 8701 1766 -1661 -2208 C
ATOM 1992 C THR A1054 -25.955 18.337 -43.493 1.00 60.08 C
ANISOU 1992 C THR A1054 7503 6173 9152 1801 -1782 -1792 C
ATOM 1993 O THR A1054 -24.857 18.742 -43.890 1.00 59.64 O
ANISOU 1993 O THR A1054 7626 5848 9188 1663 -1778 -1631 O
ATOM 1994 CB THR A1054 -25.721 16.400 -41.908 1.00 64.94 C
ANISOU 1994 CB THR A1054 8015 7364 9297 1514 -1581 -2204 C
ATOM 1995 OG1 THR A1054 -26.670 15.622 -42.630 1.00 65.38 O
ANISOU 1995 OG1 THR A1054 7935 7716 9190 1546 -1629 -2049 O
ATOM 1996 CG2 THR A1054 -25.651 15.925 -40.460 1.00 62.94 C
ANISOU 1996 CG2 THR A1054 7698 7304 8911 1468 -1441 -2553 C
ATOM 1997 N ASN A1055 -27.046 18.211 -44.293 1.00 55.42 N
ANISOU 1997 N ASN A1055 6782 5764 8511 1981 -1887 -1609 N
ATOM 1998 CA ASN A1055 -27.124 18.522 -45.731 1.00 54.36 C
ANISOU 1998 CA ASN A1055 6712 5567 8374 2067 -2022 -1191 C
ATOM 1999 C ASN A1055 -26.132 17.664 -46.549 1.00 54.33 C
ANISOU 1999 C ASN A1055 6854 5719 8070 1787 -2008 -963 C
ATOM 2000 O ASN A1055 -25.527 18.133 -47.518 1.00 53.61 O
ANISOU 2000 O ASN A1055 6915 5454 8001 1776 -2050 -627 O
ATOM 2001 CB ASN A1055 -26.987 20.044 -46.006 1.00 57.53 C
ANISOU 2001 CB ASN A1055 7226 5461 9173 2273 -2064 -1021 C
ATOM 2002 CG ASN A1055 -27.453 20.509 -47.374 1.00 86.01 C
ANISOU 2002 CG ASN A1055 10849 9035 12795 2488 -2211 -581 C
ATOM 2003 OD1 ASN A1055 -27.885 19.726 -48.237 1.00 77.28 O
ANISOU 2003 OD1 ASN A1055 9679 8313 11372 2479 -2309 -393 O
ATOM 2004 ND2 ASN A1055 -27.372 21.812 -47.603 1.00 81.63 N
ANISOU 2004 ND2 ASN A1055 10382 8017 12616 2699 -2231 -409 N
ATOM 2005 N GLY A1056 -25.980 16.410 -46.126 1.00 48.58 N
ANISOU 2005 N GLY A1056 6076 5313 7070 1575 -1929 -1145 N
ATOM 2006 CA GLY A1056 -25.111 15.436 -46.772 1.00 47.52 C
ANISOU 2006 CA GLY A1056 6054 5354 6646 1321 -1897 -999 C
ATOM 2007 C GLY A1056 -23.638 15.480 -46.421 1.00 49.94 C
ANISOU 2007 C GLY A1056 6542 5456 6977 1102 -1785 -1000 C
ATOM 2008 O GLY A1056 -22.876 14.648 -46.919 1.00 49.40 O
ANISOU 2008 O GLY A1056 6564 5527 6680 908 -1746 -876 O
ATOM 2009 N VAL A1057 -23.213 16.458 -45.595 1.00 45.77 N
ANISOU 2009 N VAL A1057 6056 4600 6735 1135 -1737 -1158 N
ATOM 2010 CA VAL A1057 -21.815 16.613 -45.156 1.00 44.85 C
ANISOU 2010 CA VAL A1057 6068 4283 6689 926 -1648 -1213 C
ATOM 2011 C VAL A1057 -21.718 16.459 -43.644 1.00 46.20 C
ANISOU 2011 C VAL A1057 6172 4500 6883 891 -1573 -1624 C
ATOM 2012 O VAL A1057 -22.586 16.966 -42.933 1.00 46.39 O
ANISOU 2012 O VAL A1057 6097 4475 7056 1079 -1587 -1849 O
ATOM 2013 CB VAL A1057 -21.090 17.890 -45.678 1.00 48.70 C
ANISOU 2013 CB VAL A1057 6684 4318 7502 933 -1659 -995 C
ATOM 2014 CG1 VAL A1057 -20.909 17.845 -47.191 1.00 48.33 C
ANISOU 2014 CG1 VAL A1057 6729 4302 7330 930 -1696 -540 C
ATOM 2015 CG2 VAL A1057 -21.805 19.170 -45.254 1.00 48.69 C
ANISOU 2015 CG2 VAL A1057 6642 3973 7885 1175 -1707 -1107 C
ATOM 2016 N ILE A1058 -20.700 15.720 -43.158 1.00 40.11 N
ANISOU 2016 N ILE A1058 5444 3861 5933 677 -1494 -1721 N
ATOM 2017 CA ILE A1058 -20.488 15.449 -41.725 1.00 38.70 C
ANISOU 2017 CA ILE A1058 5211 3803 5692 647 -1426 -2084 C
ATOM 2018 C ILE A1058 -19.025 15.663 -41.318 1.00 41.96 C
ANISOU 2018 C ILE A1058 5700 4079 6166 460 -1401 -2172 C
ATOM 2019 O ILE A1058 -18.152 15.689 -42.182 1.00 42.03 O
ANISOU 2019 O ILE A1058 5794 3963 6211 316 -1402 -1926 O
ATOM 2020 CB ILE A1058 -21.006 14.033 -41.296 1.00 41.13 C
ANISOU 2020 CB ILE A1058 5435 4535 5656 618 -1349 -2148 C
ATOM 2021 CG1 ILE A1058 -20.299 12.891 -42.079 1.00 41.09 C
ANISOU 2021 CG1 ILE A1058 5504 4699 5408 424 -1314 -1912 C
ATOM 2022 CG2 ILE A1058 -22.535 13.927 -41.370 1.00 40.72 C
ANISOU 2022 CG2 ILE A1058 5243 4628 5599 803 -1366 -2170 C
ATOM 2023 CD1 ILE A1058 -20.392 11.511 -41.446 1.00 44.85 C
ANISOU 2023 CD1 ILE A1058 5934 5504 5603 351 -1206 -1998 C
ATOM 2024 N THR A1059 -18.757 15.795 -40.008 1.00 37.43 N
ANISOU 2024 N THR A1059 5077 3562 5581 468 -1377 -2529 N
ATOM 2025 CA THR A1059 -17.393 15.954 -39.479 1.00 36.53 C
ANISOU 2025 CA THR A1059 4991 3382 5507 298 -1378 -2677 C
ATOM 2026 C THR A1059 -16.748 14.570 -39.305 1.00 39.17 C
ANISOU 2026 C THR A1059 5326 4082 5474 168 -1313 -2610 C
ATOM 2027 O THR A1059 -17.440 13.552 -39.429 1.00 38.55 O
ANISOU 2027 O THR A1059 5231 4272 5143 214 -1256 -2500 O
ATOM 2028 CB THR A1059 -17.405 16.729 -38.150 1.00 41.11 C
ANISOU 2028 CB THR A1059 5509 3889 6221 388 -1409 -3127 C
ATOM 2029 OG1 THR A1059 -18.213 16.029 -37.204 1.00 41.80 O
ANISOU 2029 OG1 THR A1059 5522 4341 6021 530 -1353 -3321 O
ATOM 2030 CG2 THR A1059 -17.896 18.160 -38.301 1.00 37.07 C
ANISOU 2030 CG2 THR A1059 5005 2940 6139 512 -1465 -3219 C
ATOM 2031 N LYS A1060 -15.428 14.537 -39.012 1.00 34.75 N
ANISOU 2031 N LYS A1060 4772 3519 4913 9 -1321 -2681 N
ATOM 2032 CA LYS A1060 -14.649 13.310 -38.781 1.00 33.91 C
ANISOU 2032 CA LYS A1060 4660 3730 4493 -91 -1266 -2625 C
ATOM 2033 C LYS A1060 -15.144 12.588 -37.510 1.00 37.55 C
ANISOU 2033 C LYS A1060 5064 4536 4667 36 -1222 -2850 C
ATOM 2034 O LYS A1060 -15.212 11.357 -37.497 1.00 36.42 O
ANISOU 2034 O LYS A1060 4932 4660 4245 31 -1137 -2707 O
ATOM 2035 CB LYS A1060 -13.153 13.648 -38.676 1.00 35.85 C
ANISOU 2035 CB LYS A1060 4882 3885 4856 -264 -1305 -2690 C
ATOM 2036 CG LYS A1060 -12.217 12.448 -38.758 1.00 45.61 C
ANISOU 2036 CG LYS A1060 6111 5399 5821 -363 -1249 -2554 C
ATOM 2037 CD LYS A1060 -10.758 12.865 -38.844 1.00 54.24 C
ANISOU 2037 CD LYS A1060 7145 6390 7075 -540 -1288 -2587 C
ATOM 2038 CE LYS A1060 -10.100 13.095 -37.499 1.00 70.11 C
ANISOU 2038 CE LYS A1060 9040 8547 9051 -534 -1376 -2964 C
ATOM 2039 NZ LYS A1060 -9.805 11.817 -36.796 1.00 80.65 N
ANISOU 2039 NZ LYS A1060 10346 10304 9993 -463 -1344 -2966 N
ATOM 2040 N ASP A1061 -15.521 13.367 -36.467 1.00 34.68 N
ANISOU 2040 N ASP A1061 4644 4154 4378 159 -1265 -3194 N
ATOM 2041 CA ASP A1061 -16.048 12.886 -35.187 1.00 34.99 C
ANISOU 2041 CA ASP A1061 4626 4531 4140 310 -1210 -3424 C
ATOM 2042 C ASP A1061 -17.441 12.260 -35.321 1.00 38.74 C
ANISOU 2042 C ASP A1061 5080 5150 4488 432 -1101 -3287 C
ATOM 2043 O ASP A1061 -17.723 11.252 -34.663 1.00 39.21 O
ANISOU 2043 O ASP A1061 5115 5536 4246 481 -991 -3262 O
ATOM 2044 CB ASP A1061 -16.038 14.009 -34.142 1.00 37.30 C
ANISOU 2044 CB ASP A1061 4861 4750 4562 413 -1289 -3861 C
ATOM 2045 CG ASP A1061 -14.646 14.440 -33.718 1.00 53.92 C
ANISOU 2045 CG ASP A1061 6939 6816 6734 287 -1399 -4079 C
ATOM 2046 OD1 ASP A1061 -13.717 13.599 -33.772 1.00 54.38 O
ANISOU 2046 OD1 ASP A1061 6997 7060 6604 173 -1394 -3927 O
ATOM 2047 OD2 ASP A1061 -14.488 15.612 -33.307 1.00 65.50 O
ANISOU 2047 OD2 ASP A1061 8368 8065 8454 306 -1493 -4424 O
ATOM 2048 N GLU A1062 -18.305 12.839 -36.184 1.00 33.34 N
ANISOU 2048 N GLU A1062 4396 4229 4044 480 -1129 -3183 N
ATOM 2049 CA GLU A1062 -19.624 12.279 -36.479 1.00 32.02 C
ANISOU 2049 CA GLU A1062 4173 4191 3803 574 -1050 -3052 C
ATOM 2050 C GLU A1062 -19.427 10.995 -37.298 1.00 33.14 C
ANISOU 2050 C GLU A1062 4358 4465 3767 431 -990 -2736 C
ATOM 2051 O GLU A1062 -20.177 10.041 -37.114 1.00 33.83 O
ANISOU 2051 O GLU A1062 4390 4783 3681 454 -880 -2673 O
ATOM 2052 CB GLU A1062 -20.494 13.278 -37.253 1.00 33.21 C
ANISOU 2052 CB GLU A1062 4298 4062 4258 678 -1129 -3010 C
ATOM 2053 CG GLU A1062 -21.067 14.387 -36.390 1.00 36.68 C
ANISOU 2053 CG GLU A1062 4670 4387 4879 872 -1153 -3343 C
ATOM 2054 CD GLU A1062 -21.465 15.664 -37.108 1.00 57.54 C
ANISOU 2054 CD GLU A1062 7325 6630 7907 971 -1255 -3311 C
ATOM 2055 OE1 GLU A1062 -22.119 16.516 -36.463 1.00 71.21 O
ANISOU 2055 OE1 GLU A1062 8989 8258 9809 1163 -1262 -3582 O
ATOM 2056 OE2 GLU A1062 -21.123 15.823 -38.303 1.00 46.98 O
ANISOU 2056 OE2 GLU A1062 6066 5085 6700 874 -1319 -3009 O
ATOM 2057 N ALA A1063 -18.396 10.962 -38.166 1.00 27.05 N
ANISOU 2057 N ALA A1063 3679 3547 3051 279 -1046 -2553 N
ATOM 2058 CA ALA A1063 -18.040 9.794 -38.987 1.00 26.20 C
ANISOU 2058 CA ALA A1063 3626 3545 2784 147 -991 -2289 C
ATOM 2059 C ALA A1063 -17.394 8.682 -38.135 1.00 29.24 C
ANISOU 2059 C ALA A1063 4018 4185 2906 107 -887 -2314 C
ATOM 2060 O ALA A1063 -17.465 7.510 -38.503 1.00 28.15 O
ANISOU 2060 O ALA A1063 3902 4172 2621 45 -797 -2145 O
ATOM 2061 CB ALA A1063 -17.105 10.211 -40.111 1.00 26.62 C
ANISOU 2061 CB ALA A1063 3765 3383 2968 22 -1062 -2105 C
ATOM 2062 N GLU A1064 -16.760 9.062 -37.004 1.00 26.22 N
ANISOU 2062 N GLU A1064 3581 3877 2504 167 -888 -2478 N
ATOM 2063 CA GLU A1064 -16.126 8.152 -36.046 1.00 25.62 C
ANISOU 2063 CA GLU A1064 3435 4060 2239 202 -778 -2406 C
ATOM 2064 C GLU A1064 -17.191 7.507 -35.154 1.00 29.92 C
ANISOU 2064 C GLU A1064 4027 4862 2478 296 -689 -2597 C
ATOM 2065 O GLU A1064 -17.109 6.309 -34.876 1.00 29.39 O
ANISOU 2065 O GLU A1064 3979 4982 2206 288 -560 -2444 O
ATOM 2066 CB GLU A1064 -15.096 8.899 -35.202 1.00 26.56 C
ANISOU 2066 CB GLU A1064 3505 4206 2380 228 -867 -2616 C
ATOM 2067 CG GLU A1064 -14.093 7.984 -34.529 1.00 33.32 C
ANISOU 2067 CG GLU A1064 4485 5343 2831 187 -893 -2763 C
ATOM 2068 CD GLU A1064 -12.955 8.665 -33.795 1.00 48.91 C
ANISOU 2068 CD GLU A1064 6402 7379 4804 182 -1029 -3013 C
ATOM 2069 OE1 GLU A1064 -12.972 9.911 -33.658 1.00 40.79 O
ANISOU 2069 OE1 GLU A1064 5334 6163 3999 171 -1143 -3269 O
ATOM 2070 OE2 GLU A1064 -12.039 7.941 -33.348 1.00 40.71 O
ANISOU 2070 OE2 GLU A1064 5346 6570 3552 195 -1024 -2962 O
ATOM 2071 N LYS A1065 -18.197 8.301 -34.725 1.00 27.01 N
ANISOU 2071 N LYS A1065 3516 4468 2279 432 -678 -2688 N
ATOM 2072 CA LYS A1065 -19.335 7.834 -33.934 1.00 27.43 C
ANISOU 2072 CA LYS A1065 3500 4750 2172 548 -538 -2753 C
ATOM 2073 C LYS A1065 -20.137 6.783 -34.740 1.00 31.27 C
ANISOU 2073 C LYS A1065 4022 5251 2607 455 -432 -2570 C
ATOM 2074 O LYS A1065 -20.523 5.758 -34.176 1.00 31.34 O
ANISOU 2074 O LYS A1065 4002 5467 2439 468 -255 -2473 O
ATOM 2075 CB LYS A1065 -20.232 9.020 -33.546 1.00 30.66 C
ANISOU 2075 CB LYS A1065 3879 5107 2665 695 -590 -3096 C
ATOM 2076 CG LYS A1065 -20.209 9.353 -32.060 1.00 53.29 C
ANISOU 2076 CG LYS A1065 6701 8218 5327 860 -545 -3388 C
ATOM 2077 CD LYS A1065 -20.690 10.784 -31.759 1.00 64.58 C
ANISOU 2077 CD LYS A1065 8073 9498 6967 1003 -639 -3726 C
ATOM 2078 CE LYS A1065 -19.546 11.766 -31.615 1.00 71.75 C
ANISOU 2078 CE LYS A1065 9037 10229 7994 968 -817 -3969 C
ATOM 2079 NZ LYS A1065 -20.028 13.138 -31.310 1.00 79.91 N
ANISOU 2079 NZ LYS A1065 10023 11062 9278 1107 -895 -4316 N
ATOM 2080 N LEU A1066 -20.337 7.018 -36.062 1.00 27.32 N
ANISOU 2080 N LEU A1066 3538 4528 2316 363 -531 -2454 N
ATOM 2081 CA LEU A1066 -21.040 6.099 -36.967 1.00 27.28 C
ANISOU 2081 CA LEU A1066 3502 4524 2338 264 -468 -2261 C
ATOM 2082 C LEU A1066 -20.233 4.819 -37.189 1.00 30.43 C
ANISOU 2082 C LEU A1066 3994 4973 2593 134 -377 -2075 C
ATOM 2083 O LEU A1066 -20.813 3.735 -37.334 1.00 30.17 O
ANISOU 2083 O LEU A1066 3924 5012 2526 67 -246 -1964 O
ATOM 2084 CB LEU A1066 -21.331 6.762 -38.328 1.00 27.67 C
ANISOU 2084 CB LEU A1066 3556 4364 2594 227 -627 -2193 C
ATOM 2085 CG LEU A1066 -22.396 7.870 -38.381 1.00 33.03 C
ANISOU 2085 CG LEU A1066 4125 4965 3461 373 -714 -2318 C
ATOM 2086 CD1 LEU A1066 -22.408 8.535 -39.749 1.00 33.39 C
ANISOU 2086 CD1 LEU A1066 4209 4808 3671 353 -879 -2185 C
ATOM 2087 CD2 LEU A1066 -23.796 7.351 -38.016 1.00 34.23 C
ANISOU 2087 CD2 LEU A1066 4098 5306 3601 438 -597 -2371 C
ATOM 2088 N PHE A1067 -18.893 4.958 -37.227 1.00 25.65 N
ANISOU 2088 N PHE A1067 3494 4313 1937 98 -445 -2052 N
ATOM 2089 CA PHE A1067 -17.948 3.863 -37.408 1.00 24.59 C
ANISOU 2089 CA PHE A1067 3447 4215 1679 10 -373 -1890 C
ATOM 2090 C PHE A1067 -17.899 2.967 -36.171 1.00 27.23 C
ANISOU 2090 C PHE A1067 3774 4767 1805 86 -204 -1857 C
ATOM 2091 O PHE A1067 -17.750 1.753 -36.311 1.00 26.86 O
ANISOU 2091 O PHE A1067 3771 4741 1695 29 -73 -1685 O
ATOM 2092 CB PHE A1067 -16.552 4.412 -37.742 1.00 26.12 C
ANISOU 2092 CB PHE A1067 3714 4312 1900 -34 -497 -1891 C
ATOM 2093 CG PHE A1067 -15.472 3.366 -37.878 1.00 26.69 C
ANISOU 2093 CG PHE A1067 3856 4435 1851 -91 -428 -1741 C
ATOM 2094 CD1 PHE A1067 -15.379 2.586 -39.024 1.00 28.17 C
ANISOU 2094 CD1 PHE A1067 4101 4532 2073 -198 -387 -1582 C
ATOM 2095 CD2 PHE A1067 -14.554 3.155 -36.853 1.00 28.00 C
ANISOU 2095 CD2 PHE A1067 4021 4759 1860 -15 -410 -1773 C
ATOM 2096 CE1 PHE A1067 -14.393 1.607 -39.142 1.00 29.13 C
ANISOU 2096 CE1 PHE A1067 4281 4685 2101 -225 -309 -1458 C
ATOM 2097 CE2 PHE A1067 -13.570 2.175 -36.971 1.00 30.83 C
ANISOU 2097 CE2 PHE A1067 4428 5167 2118 -34 -346 -1621 C
ATOM 2098 CZ PHE A1067 -13.496 1.405 -38.116 1.00 28.76 C
ANISOU 2098 CZ PHE A1067 4227 4779 1921 -137 -286 -1464 C
ATOM 2099 N ASN A1068 -18.023 3.556 -34.972 1.00 23.31 N
ANISOU 2099 N ASN A1068 3092 4370 1395 231 -188 -1860 N
ATOM 2100 CA ASN A1068 -17.999 2.788 -33.732 1.00 23.60 C
ANISOU 2100 CA ASN A1068 3100 4636 1231 327 -47 -1789 C
ATOM 2101 C ASN A1068 -19.256 1.945 -33.530 1.00 29.15 C
ANISOU 2101 C ASN A1068 3896 5493 1688 326 184 -1847 C
ATOM 2102 O ASN A1068 -19.163 0.869 -32.928 1.00 30.04 O
ANISOU 2102 O ASN A1068 4037 5730 1647 352 370 -1665 O
ATOM 2103 CB ASN A1068 -17.684 3.651 -32.533 1.00 22.62 C
ANISOU 2103 CB ASN A1068 2771 4622 1200 481 -128 -1827 C
ATOM 2104 CG ASN A1068 -16.194 3.764 -32.342 1.00 32.75 C
ANISOU 2104 CG ASN A1068 4440 6121 1884 499 -228 -2219 C
ATOM 2105 OD1 ASN A1068 -15.489 2.765 -32.214 1.00 27.82 O
ANISOU 2105 OD1 ASN A1068 3832 5558 1180 499 -157 -1981 O
ATOM 2106 ND2 ASN A1068 -15.675 4.974 -32.344 1.00 23.65 N
ANISOU 2106 ND2 ASN A1068 2890 4718 1377 521 -371 -2039 N
ATOM 2107 N GLN A1069 -20.404 2.377 -34.093 1.00 24.98 N
ANISOU 2107 N GLN A1069 3270 4870 1353 284 164 -1926 N
ATOM 2108 CA GLN A1069 -21.627 1.572 -34.073 1.00 24.40 C
ANISOU 2108 CA GLN A1069 3090 4841 1340 234 358 -1829 C
ATOM 2109 C GLN A1069 -21.380 0.353 -34.994 1.00 28.95 C
ANISOU 2109 C GLN A1069 3732 5263 2004 56 420 -1625 C
ATOM 2110 O GLN A1069 -21.682 -0.781 -34.607 1.00 29.46 O
ANISOU 2110 O GLN A1069 3785 5370 2039 12 642 -1464 O
ATOM 2111 CB GLN A1069 -22.818 2.383 -34.574 1.00 25.33 C
ANISOU 2111 CB GLN A1069 3062 4901 1662 239 275 -1980 C
ATOM 2112 CG GLN A1069 -23.244 3.509 -33.644 1.00 37.21 C
ANISOU 2112 CG GLN A1069 4478 6547 3114 429 262 -2201 C
ATOM 2113 CD GLN A1069 -24.279 4.409 -34.273 1.00 59.81 C
ANISOU 2113 CD GLN A1069 7208 9307 6211 464 141 -2342 C
ATOM 2114 OE1 GLN A1069 -24.362 5.602 -33.959 1.00 55.53 O
ANISOU 2114 OE1 GLN A1069 6644 8740 5715 609 29 -2548 O
ATOM 2115 NE2 GLN A1069 -25.093 3.867 -35.179 1.00 53.83 N
ANISOU 2115 NE2 GLN A1069 6350 8485 5617 343 152 -2246 N
ATOM 2116 N ASP A1070 -20.757 0.596 -36.176 1.00 24.31 N
ANISOU 2116 N ASP A1070 3223 4492 1523 -37 239 -1632 N
ATOM 2117 CA ASP A1070 -20.381 -0.412 -37.171 1.00 23.71 C
ANISOU 2117 CA ASP A1070 3223 4268 1517 -189 264 -1497 C
ATOM 2118 C ASP A1070 -19.390 -1.450 -36.638 1.00 25.80 C
ANISOU 2118 C ASP A1070 3604 4553 1647 -170 405 -1327 C
ATOM 2119 O ASP A1070 -19.551 -2.629 -36.944 1.00 25.28 O
ANISOU 2119 O ASP A1070 3562 4392 1650 -269 551 -1202 O
ATOM 2120 CB ASP A1070 -19.855 0.250 -38.457 1.00 26.07 C
ANISOU 2120 CB ASP A1070 3581 4423 1902 -251 44 -1545 C
ATOM 2121 CG ASP A1070 -20.899 1.014 -39.260 1.00 40.76 C
ANISOU 2121 CG ASP A1070 5333 6241 3911 -271 -90 -1648 C
ATOM 2122 OD1 ASP A1070 -22.114 0.755 -39.066 1.00 43.68 O
ANISOU 2122 OD1 ASP A1070 5560 6679 4357 -283 -8 -1691 O
ATOM 2123 OD2 ASP A1070 -20.505 1.859 -40.095 1.00 44.00 O
ANISOU 2123 OD2 ASP A1070 5790 6560 4368 -270 -269 -1669 O
ATOM 2124 N VAL A1071 -18.389 -1.027 -35.833 1.00 21.92 N
ANISOU 2124 N VAL A1071 3116 4141 1073 -44 338 -1278 N
ATOM 2125 CA VAL A1071 -17.425 -1.933 -35.187 1.00 21.73 C
ANISOU 2125 CA VAL A1071 3150 4155 951 24 430 -1083 C
ATOM 2126 C VAL A1071 -18.208 -2.881 -34.249 1.00 28.31 C
ANISOU 2126 C VAL A1071 4040 5161 1557 84 739 -1002 C
ATOM 2127 O VAL A1071 -17.984 -4.090 -34.282 1.00 27.67 O
ANISOU 2127 O VAL A1071 4025 4990 1499 53 907 -795 O
ATOM 2128 CB VAL A1071 -16.288 -1.163 -34.454 1.00 24.69 C
ANISOU 2128 CB VAL A1071 3636 4765 980 180 331 -1244 C
ATOM 2129 CG1 VAL A1071 -15.502 -2.070 -33.504 1.00 24.30 C
ANISOU 2129 CG1 VAL A1071 3581 4827 824 312 424 -1015 C
ATOM 2130 CG2 VAL A1071 -15.350 -0.501 -35.449 1.00 24.06 C
ANISOU 2130 CG2 VAL A1071 3574 4534 1035 98 126 -1311 C
ATOM 2131 N ASP A1072 -19.170 -2.330 -33.474 1.00 26.74 N
ANISOU 2131 N ASP A1072 3732 5124 1302 153 796 -1094 N
ATOM 2132 CA ASP A1072 -20.052 -3.088 -32.582 1.00 27.00 C
ANISOU 2132 CA ASP A1072 3705 5276 1276 190 1076 -940 C
ATOM 2133 C ASP A1072 -20.912 -4.091 -33.348 1.00 30.00 C
ANISOU 2133 C ASP A1072 4038 5433 1926 -14 1236 -831 C
ATOM 2134 O ASP A1072 -21.059 -5.223 -32.885 1.00 28.76 O
ANISOU 2134 O ASP A1072 3908 5245 1775 -30 1492 -595 O
ATOM 2135 CB ASP A1072 -20.942 -2.146 -31.770 1.00 29.33 C
ANISOU 2135 CB ASP A1072 3869 5793 1482 300 1089 -1112 C
ATOM 2136 CG ASP A1072 -20.339 -1.682 -30.473 1.00 47.86 C
ANISOU 2136 CG ASP A1072 6248 8449 3488 532 1088 -1149 C
ATOM 2137 OD1 ASP A1072 -19.133 -1.356 -30.462 1.00 49.53 O
ANISOU 2137 OD1 ASP A1072 6553 8692 3574 602 911 -1198 O
ATOM 2138 OD2 ASP A1072 -21.077 -1.630 -29.463 1.00 60.03 O
ANISOU 2138 OD2 ASP A1072 7705 10226 4878 646 1264 -1146 O
ATOM 2139 N ALA A1073 -21.471 -3.683 -34.516 1.00 26.78 N
ANISOU 2139 N ALA A1073 3557 4872 1747 -166 1085 -1002 N
ATOM 2140 CA ALA A1073 -22.279 -4.557 -35.379 1.00 27.26 C
ANISOU 2140 CA ALA A1073 3546 4737 2075 -379 1179 -978 C
ATOM 2141 C ALA A1073 -21.424 -5.732 -35.902 1.00 33.80 C
ANISOU 2141 C ALA A1073 4526 5351 2966 -462 1251 -827 C
ATOM 2142 O ALA A1073 -21.876 -6.882 -35.867 1.00 34.54 O
ANISOU 2142 O ALA A1073 4601 5306 3218 -577 1478 -696 O
ATOM 2143 CB ALA A1073 -22.851 -3.765 -36.548 1.00 27.71 C
ANISOU 2143 CB ALA A1073 3506 4732 2290 -474 942 -1203 C
ATOM 2144 N ALA A1074 -20.174 -5.437 -36.337 1.00 30.26 N
ANISOU 2144 N ALA A1074 4217 4868 2413 -399 1075 -845 N
ATOM 2145 CA ALA A1074 -19.213 -6.421 -36.844 1.00 30.30 C
ANISOU 2145 CA ALA A1074 4364 4691 2459 -433 1124 -727 C
ATOM 2146 C ALA A1074 -18.768 -7.399 -35.747 1.00 35.50 C
ANISOU 2146 C ALA A1074 5101 5365 3022 -313 1371 -453 C
ATOM 2147 O ALA A1074 -18.762 -8.614 -35.979 1.00 36.34 O
ANISOU 2147 O ALA A1074 5263 5252 3291 -393 1555 -316 O
ATOM 2148 CB ALA A1074 -18.008 -5.722 -37.467 1.00 30.77 C
ANISOU 2148 CB ALA A1074 4513 4764 2412 -373 891 -808 C
ATOM 2149 N VAL A1075 -18.424 -6.871 -34.553 1.00 31.25 N
ANISOU 2149 N VAL A1075 4565 5087 2222 -112 1377 -379 N
ATOM 2150 CA VAL A1075 -17.999 -7.654 -33.386 1.00 30.98 C
ANISOU 2150 CA VAL A1075 4601 5154 2016 59 1591 -92 C
ATOM 2151 C VAL A1075 -19.153 -8.573 -32.905 1.00 37.88 C
ANISOU 2151 C VAL A1075 5415 5947 3032 -26 1913 94 C
ATOM 2152 O VAL A1075 -18.894 -9.701 -32.473 1.00 38.60 O
ANISOU 2152 O VAL A1075 5592 5927 3148 25 2149 385 O
ATOM 2153 CB VAL A1075 -17.391 -6.744 -32.274 1.00 33.11 C
ANISOU 2153 CB VAL A1075 4868 5780 1930 299 1475 -119 C
ATOM 2154 CG1 VAL A1075 -17.335 -7.442 -30.913 1.00 32.19 C
ANISOU 2154 CG1 VAL A1075 4790 5864 1578 498 1715 182 C
ATOM 2155 CG2 VAL A1075 -16.005 -6.251 -32.683 1.00 32.32 C
ANISOU 2155 CG2 VAL A1075 4833 5706 1741 370 1224 -216 C
ATOM 2156 N ARG A1076 -20.417 -8.121 -33.052 1.00 35.27 N
ANISOU 2156 N ARG A1076 4925 5647 2831 -160 1931 -65 N
ATOM 2157 CA ARG A1076 -21.592 -8.931 -32.718 1.00 35.68 C
ANISOU 2157 CA ARG A1076 4869 5613 3073 -288 2237 78 C
ATOM 2158 C ARG A1076 -21.637 -10.150 -33.659 1.00 40.49 C
ANISOU 2158 C ARG A1076 5522 5827 4035 -506 2349 133 C
ATOM 2159 O ARG A1076 -21.845 -11.272 -33.192 1.00 40.77 O
ANISOU 2159 O ARG A1076 5587 5702 4201 -542 2655 403 O
ATOM 2160 CB ARG A1076 -22.887 -8.108 -32.838 1.00 36.57 C
ANISOU 2160 CB ARG A1076 4766 5851 3279 -387 2188 -155 C
ATOM 2161 CG ARG A1076 -23.595 -7.858 -31.511 1.00 48.65 C
ANISOU 2161 CG ARG A1076 6189 7675 4620 -253 2404 -41 C
ATOM 2162 CD ARG A1076 -24.907 -7.110 -31.699 1.00 67.90 C
ANISOU 2162 CD ARG A1076 8386 10219 7194 -345 2370 -278 C
ATOM 2163 NE ARG A1076 -25.963 -7.968 -32.249 1.00 85.00 N
ANISOU 2163 NE ARG A1076 10390 12167 9738 -615 2551 -254 N
ATOM 2164 CZ ARG A1076 -26.912 -7.556 -33.087 1.00100.62 C
ANISOU 2164 CZ ARG A1076 12164 14110 11957 -776 2418 -511 C
ATOM 2165 NH1 ARG A1076 -26.947 -6.292 -33.494 1.00 88.28 N
ANISOU 2165 NH1 ARG A1076 10553 12686 10303 -679 2117 -776 N
ATOM 2166 NH2 ARG A1076 -27.826 -8.408 -33.533 1.00 86.08 N
ANISOU 2166 NH2 ARG A1076 10155 12087 10464 -1034 2581 -506 N
ATOM 2167 N GLY A1077 -21.373 -9.914 -34.949 1.00 36.66 N
ANISOU 2167 N GLY A1077 5052 5190 3686 -632 2105 -116 N
ATOM 2168 CA GLY A1077 -21.355 -10.938 -35.987 1.00 36.63 C
ANISOU 2168 CA GLY A1077 5090 4837 3991 -831 2154 -163 C
ATOM 2169 C GLY A1077 -20.290 -11.991 -35.764 1.00 40.40 C
ANISOU 2169 C GLY A1077 5761 5116 4474 -728 2309 89 C
ATOM 2170 O GLY A1077 -20.574 -13.191 -35.839 1.00 39.43 O
ANISOU 2170 O GLY A1077 5660 4691 4629 -851 2554 216 O
ATOM 2171 N ILE A1078 -19.059 -11.539 -35.474 1.00 37.26 N
ANISOU 2171 N ILE A1078 5488 4879 3790 -497 2167 158 N
ATOM 2172 CA ILE A1078 -17.901 -12.391 -35.201 1.00 37.35 C
ANISOU 2172 CA ILE A1078 5669 4769 3755 -331 2272 403 C
ATOM 2173 C ILE A1078 -18.197 -13.361 -34.045 1.00 45.11 C
ANISOU 2173 C ILE A1078 6688 5689 4765 -242 2623 787 C
ATOM 2174 O ILE A1078 -18.025 -14.569 -34.201 1.00 44.98 O
ANISOU 2174 O ILE A1078 6763 5338 4988 -274 2834 965 O
ATOM 2175 CB ILE A1078 -16.634 -11.520 -34.965 1.00 39.57 C
ANISOU 2175 CB ILE A1078 6012 5321 3702 -99 2029 379 C
ATOM 2176 CG1 ILE A1078 -16.176 -10.845 -36.290 1.00 39.73 C
ANISOU 2176 CG1 ILE A1078 6029 5298 3768 -204 1747 69 C
ATOM 2177 CG2 ILE A1078 -15.507 -12.340 -34.342 1.00 38.63 C
ANISOU 2177 CG2 ILE A1078 6025 5175 3477 137 2150 684 C
ATOM 2178 CD1 ILE A1078 -15.430 -9.504 -36.150 1.00 42.76 C
ANISOU 2178 CD1 ILE A1078 6388 5975 3883 -77 1472 -58 C
ATOM 2179 N LEU A1079 -18.700 -12.836 -32.918 1.00 44.66 N
ANISOU 2179 N LEU A1079 6555 5937 4478 -134 2703 911 N
ATOM 2180 CA LEU A1079 -19.023 -13.640 -31.734 1.00 45.91 C
ANISOU 2180 CA LEU A1079 6740 6104 4598 -26 3055 1316 C
ATOM 2181 C LEU A1079 -20.239 -14.574 -31.930 1.00 50.31 C
ANISOU 2181 C LEU A1079 7208 6335 5573 -301 3363 1392 C
ATOM 2182 O LEU A1079 -20.397 -15.529 -31.166 1.00 49.67 O
ANISOU 2182 O LEU A1079 7177 6128 5567 -250 3706 1776 O
ATOM 2183 CB LEU A1079 -19.185 -12.748 -30.484 1.00 46.37 C
ANISOU 2183 CB LEU A1079 6742 6646 4231 193 3044 1398 C
ATOM 2184 CG LEU A1079 -17.959 -11.886 -30.107 1.00 51.64 C
ANISOU 2184 CG LEU A1079 7478 7649 4492 466 2754 1323 C
ATOM 2185 CD1 LEU A1079 -18.353 -10.750 -29.180 1.00 51.84 C
ANISOU 2185 CD1 LEU A1079 7401 8126 4170 594 2662 1194 C
ATOM 2186 CD2 LEU A1079 -16.816 -12.729 -29.515 1.00 54.52 C
ANISOU 2186 CD2 LEU A1079 7999 8022 4696 733 2855 1691 C
ATOM 2187 N ARG A1080 -21.066 -14.321 -32.971 1.00 47.52 N
ANISOU 2187 N ARG A1080 6715 5841 5499 -591 3243 1037 N
ATOM 2188 CA ARG A1080 -22.239 -15.141 -33.315 1.00 47.47 C
ANISOU 2188 CA ARG A1080 6575 5527 5933 -897 3484 1017 C
ATOM 2189 C ARG A1080 -21.898 -16.246 -34.346 1.00 50.54 C
ANISOU 2189 C ARG A1080 7062 5426 6713 -1068 3529 946 C
ATOM 2190 O ARG A1080 -22.636 -17.228 -34.458 1.00 49.56 O
ANISOU 2190 O ARG A1080 6879 4961 6992 -1290 3805 1023 O
ATOM 2191 CB ARG A1080 -23.411 -14.255 -33.780 1.00 48.19 C
ANISOU 2191 CB ARG A1080 6421 5791 6097 -1095 3325 666 C
ATOM 2192 CG ARG A1080 -24.160 -13.623 -32.611 1.00 64.76 C
ANISOU 2192 CG ARG A1080 8381 8255 7972 -988 3465 801 C
ATOM 2193 CD ARG A1080 -24.928 -12.371 -32.996 1.00 82.11 C
ANISOU 2193 CD ARG A1080 10375 10722 10103 -1044 3208 440 C
ATOM 2194 NE ARG A1080 -25.201 -11.517 -31.834 1.00 95.04 N
ANISOU 2194 NE ARG A1080 11946 12770 11396 -827 3263 528 N
ATOM 2195 CZ ARG A1080 -26.286 -11.605 -31.068 1.00112.23 C
ANISOU 2195 CZ ARG A1080 13935 15088 13619 -871 3542 646 C
ATOM 2196 NH1 ARG A1080 -27.223 -12.510 -31.331 1.00 96.63 N
ANISOU 2196 NH1 ARG A1080 11802 12858 12056 -1151 3797 704 N
ATOM 2197 NH2 ARG A1080 -26.443 -10.788 -30.035 1.00102.84 N
ANISOU 2197 NH2 ARG A1080 12702 14300 12074 -643 3576 686 N
ATOM 2198 N ASN A1081 -20.754 -16.084 -35.056 1.00 46.48 N
ANISOU 2198 N ASN A1081 6695 4881 6084 -955 3277 798 N
ATOM 2199 CA ASN A1081 -20.195 -16.977 -36.077 1.00 45.92 C
ANISOU 2199 CA ASN A1081 6741 4412 6295 -1047 3269 677 C
ATOM 2200 C ASN A1081 -19.263 -17.997 -35.408 1.00 49.72 C
ANISOU 2200 C ASN A1081 7421 4673 6796 -823 3515 1085 C
ATOM 2201 O ASN A1081 -18.228 -17.617 -34.854 1.00 48.92 O
ANISOU 2201 O ASN A1081 7428 4818 6342 -519 3419 1266 O
ATOM 2202 CB ASN A1081 -19.413 -16.139 -37.102 1.00 46.62 C
ANISOU 2202 CB ASN A1081 6871 4660 6182 -994 2888 347 C
ATOM 2203 CG ASN A1081 -19.091 -16.849 -38.383 1.00 66.22 C
ANISOU 2203 CG ASN A1081 9422 6806 8931 -1132 2835 95 C
ATOM 2204 OD1 ASN A1081 -18.228 -17.732 -38.441 1.00 59.20 O
ANISOU 2204 OD1 ASN A1081 8693 5664 8134 -1013 2954 233 O
ATOM 2205 ND2 ASN A1081 -19.772 -16.457 -39.445 1.00 58.07 N
ANISOU 2205 ND2 ASN A1081 8265 5790 8009 -1364 2647 -291 N
ATOM 2206 N ALA A1082 -19.628 -19.294 -35.473 1.00 46.90 N
ANISOU 2206 N ALA A1082 7102 3845 6875 -971 3825 1222 N
ATOM 2207 CA ALA A1082 -18.888 -20.403 -34.855 1.00 46.75 C
ANISOU 2207 CA ALA A1082 7270 3534 6959 -764 4108 1651 C
ATOM 2208 C ALA A1082 -17.456 -20.613 -35.375 1.00 50.77 C
ANISOU 2208 C ALA A1082 7956 3957 7377 -532 3953 1611 C
ATOM 2209 O ALA A1082 -16.650 -21.227 -34.676 1.00 51.19 O
ANISOU 2209 O ALA A1082 8156 3926 7369 -249 4115 2005 O
ATOM 2210 CB ALA A1082 -19.681 -21.695 -34.969 1.00 47.40 C
ANISOU 2210 CB ALA A1082 7336 3064 7609 -1022 4473 1751 C
ATOM 2211 N LYS A1083 -17.141 -20.108 -36.577 1.00 46.71 N
ANISOU 2211 N LYS A1083 7419 3486 6843 -632 3651 1160 N
ATOM 2212 CA LYS A1083 -15.820 -20.240 -37.204 1.00 46.26 C
ANISOU 2212 CA LYS A1083 7495 3374 6706 -438 3503 1069 C
ATOM 2213 C LYS A1083 -14.846 -19.092 -36.852 1.00 48.98 C
ANISOU 2213 C LYS A1083 7841 4227 6541 -165 3225 1107 C
ATOM 2214 O LYS A1083 -13.629 -19.296 -36.877 1.00 48.08 O
ANISOU 2214 O LYS A1083 7827 4123 6320 83 3173 1199 O
ATOM 2215 CB LYS A1083 -15.977 -20.373 -38.723 1.00 48.61 C
ANISOU 2215 CB LYS A1083 7766 3462 7241 -689 3354 568 C
ATOM 2216 CG LYS A1083 -15.048 -21.394 -39.354 1.00 57.74 C
ANISOU 2216 CG LYS A1083 9076 4243 8622 -584 3439 517 C
ATOM 2217 CD LYS A1083 -15.458 -21.635 -40.791 1.00 63.48 C
ANISOU 2217 CD LYS A1083 9762 4748 9608 -869 3341 1 C
ATOM 2218 CE LYS A1083 -14.449 -22.437 -41.564 1.00 68.00 C
ANISOU 2218 CE LYS A1083 10477 5031 10328 -743 3375 -142 C
ATOM 2219 NZ LYS A1083 -14.684 -22.335 -43.033 1.00 72.04 N
ANISOU 2219 NZ LYS A1083 10943 5524 10907 -967 3186 -698 N
ATOM 2220 N LEU A1084 -15.386 -17.899 -36.509 1.00 44.59 N
ANISOU 2220 N LEU A1084 7159 4081 5704 -210 3053 1025 N
ATOM 2221 CA LEU A1084 -14.621 -16.692 -36.153 1.00 43.21 C
ANISOU 2221 CA LEU A1084 6955 4377 5086 -4 2780 1003 C
ATOM 2222 C LEU A1084 -14.556 -16.419 -34.645 1.00 47.17 C
ANISOU 2222 C LEU A1084 7451 5195 5277 235 2865 1358 C
ATOM 2223 O LEU A1084 -13.631 -15.731 -34.202 1.00 45.90 O
ANISOU 2223 O LEU A1084 7291 5375 4772 466 2675 1394 O
ATOM 2224 CB LEU A1084 -15.199 -15.457 -36.866 1.00 42.57 C
ANISOU 2224 CB LEU A1084 6744 4523 4909 -202 2502 618 C
ATOM 2225 CG LEU A1084 -15.358 -15.532 -38.380 1.00 46.19 C
ANISOU 2225 CG LEU A1084 7190 4778 5584 -429 2376 244 C
ATOM 2226 CD1 LEU A1084 -16.298 -14.458 -38.869 1.00 45.90 C
ANISOU 2226 CD1 LEU A1084 7008 4944 5489 -623 2169 -44 C
ATOM 2227 CD2 LEU A1084 -14.006 -15.489 -39.093 1.00 47.16 C
ANISOU 2227 CD2 LEU A1084 7402 4912 5605 -286 2230 156 C
ATOM 2228 N LYS A1085 -15.557 -16.918 -33.867 1.00 44.21 N
ANISOU 2228 N LYS A1085 7051 4732 5014 170 3147 1600 N
ATOM 2229 CA LYS A1085 -15.638 -16.717 -32.418 1.00 44.31 C
ANISOU 2229 CA LYS A1085 7058 5070 4708 397 3268 1949 C
ATOM 2230 C LYS A1085 -14.421 -17.272 -31.643 1.00 49.46 C
ANISOU 2230 C LYS A1085 7845 5799 5150 771 3332 2331 C
ATOM 2231 O LYS A1085 -13.922 -16.537 -30.783 1.00 48.76 O
ANISOU 2231 O LYS A1085 7730 6167 4628 1015 3189 2414 O
ATOM 2232 CB LYS A1085 -16.959 -17.251 -31.834 1.00 46.80 C
ANISOU 2232 CB LYS A1085 7312 5249 5222 235 3606 2153 C
ATOM 2233 CG LYS A1085 -17.245 -16.761 -30.417 1.00 58.57 C
ANISOU 2233 CG LYS A1085 8762 7177 6316 441 3706 2429 C
ATOM 2234 CD LYS A1085 -18.006 -17.798 -29.598 1.00 68.12 C
ANISOU 2234 CD LYS A1085 9993 8188 7702 423 4157 2877 C
ATOM 2235 CE LYS A1085 -17.965 -17.515 -28.111 1.00 76.17 C
ANISOU 2235 CE LYS A1085 11023 9671 8249 726 4284 3244 C
ATOM 2236 NZ LYS A1085 -18.752 -16.305 -27.736 1.00 82.72 N
ANISOU 2236 NZ LYS A1085 11684 10944 8802 673 4153 2982 N
ATOM 2237 N PRO A1086 -13.908 -18.515 -31.893 1.00 47.32 N
ANISOU 2237 N PRO A1086 7704 5114 5162 845 3528 2554 N
ATOM 2238 CA PRO A1086 -12.752 -18.984 -31.108 1.00 47.56 C
ANISOU 2238 CA PRO A1086 7842 5262 4969 1247 3571 2942 C
ATOM 2239 C PRO A1086 -11.466 -18.219 -31.414 1.00 52.42 C
ANISOU 2239 C PRO A1086 8427 6190 5300 1438 3213 2733 C
ATOM 2240 O PRO A1086 -10.729 -17.894 -30.479 1.00 53.08 O
ANISOU 2240 O PRO A1086 8503 6668 4996 1759 3119 2945 O
ATOM 2241 CB PRO A1086 -12.638 -20.473 -31.469 1.00 49.19 C
ANISOU 2241 CB PRO A1086 8185 4871 5634 1245 3875 3179 C
ATOM 2242 CG PRO A1086 -13.881 -20.807 -32.219 1.00 53.49 C
ANISOU 2242 CG PRO A1086 8683 5014 6627 823 4025 2940 C
ATOM 2243 CD PRO A1086 -14.326 -19.546 -32.864 1.00 49.00 C
ANISOU 2243 CD PRO A1086 7966 4742 5910 593 3712 2452 C
ATOM 2244 N VAL A1087 -11.218 -17.888 -32.701 1.00 47.97 N
ANISOU 2244 N VAL A1087 7829 5487 4913 1239 3013 2313 N
ATOM 2245 CA VAL A1087 -10.016 -17.153 -33.095 1.00 47.50 C
ANISOU 2245 CA VAL A1087 7717 5695 4634 1376 2701 2105 C
ATOM 2246 C VAL A1087 -10.044 -15.721 -32.491 1.00 51.42 C
ANISOU 2246 C VAL A1087 8088 6727 4724 1401 2434 1947 C
ATOM 2247 O VAL A1087 -9.083 -15.369 -31.808 1.00 51.68 O
ANISOU 2247 O VAL A1087 8082 7111 4442 1675 2286 2050 O
ATOM 2248 CB VAL A1087 -9.686 -17.212 -34.618 1.00 50.78 C
ANISOU 2248 CB VAL A1087 8138 5834 5323 1185 2596 1744 C
ATOM 2249 CG1 VAL A1087 -10.842 -16.741 -35.488 1.00 50.53 C
ANISOU 2249 CG1 VAL A1087 8054 5672 5472 804 2551 1392 C
ATOM 2250 CG2 VAL A1087 -8.400 -16.465 -34.950 1.00 50.47 C
ANISOU 2250 CG2 VAL A1087 8026 6091 5061 1330 2312 1578 C
ATOM 2251 N TYR A1088 -11.162 -14.965 -32.631 1.00 46.99 N
ANISOU 2251 N TYR A1088 7453 6228 4174 1143 2389 1717 N
ATOM 2252 CA TYR A1088 -11.322 -13.615 -32.055 1.00 46.46 C
ANISOU 2252 CA TYR A1088 7273 6609 3771 1161 2165 1542 C
ATOM 2253 C TYR A1088 -11.072 -13.573 -30.536 1.00 49.91 C
ANISOU 2253 C TYR A1088 7706 7435 3821 1470 2211 1840 C
ATOM 2254 O TYR A1088 -10.440 -12.625 -30.056 1.00 48.22 O
ANISOU 2254 O TYR A1088 7412 7624 3286 1610 1962 1705 O
ATOM 2255 CB TYR A1088 -12.713 -13.043 -32.371 1.00 47.46 C
ANISOU 2255 CB TYR A1088 7326 6685 4021 869 2178 1312 C
ATOM 2256 CG TYR A1088 -12.928 -11.618 -31.898 1.00 49.38 C
ANISOU 2256 CG TYR A1088 7456 7330 3975 884 1954 1091 C
ATOM 2257 CD1 TYR A1088 -12.553 -10.536 -32.689 1.00 51.21 C
ANISOU 2257 CD1 TYR A1088 7621 7639 4198 780 1659 743 C
ATOM 2258 CD2 TYR A1088 -13.553 -11.351 -30.681 1.00 50.39 C
ANISOU 2258 CD2 TYR A1088 7547 7745 3855 1001 2056 1227 C
ATOM 2259 CE1 TYR A1088 -12.760 -9.222 -32.267 1.00 51.61 C
ANISOU 2259 CE1 TYR A1088 7574 7999 4036 792 1462 527 C
ATOM 2260 CE2 TYR A1088 -13.753 -10.041 -30.241 1.00 51.35 C
ANISOU 2260 CE2 TYR A1088 7566 8218 3725 1029 1854 981 C
ATOM 2261 CZ TYR A1088 -13.357 -8.979 -31.040 1.00 57.94 C
ANISOU 2261 CZ TYR A1088 8340 9077 4599 920 1554 623 C
ATOM 2262 OH TYR A1088 -13.552 -7.683 -30.625 1.00 58.83 O
ANISOU 2262 OH TYR A1088 8358 9476 4518 943 1362 366 O
ATOM 2263 N ASP A1089 -11.593 -14.578 -29.787 1.00 47.54 N
ANISOU 2263 N ASP A1089 7488 7020 3553 1569 2533 2237 N
ATOM 2264 CA ASP A1089 -11.429 -14.663 -28.333 1.00 48.22 C
ANISOU 2264 CA ASP A1089 7590 7492 3241 1886 2620 2579 C
ATOM 2265 C ASP A1089 -9.955 -14.883 -27.961 1.00 53.57 C
ANISOU 2265 C ASP A1089 8289 8382 3683 2237 2474 2748 C
ATOM 2266 O ASP A1089 -9.509 -14.394 -26.920 1.00 53.46 O
ANISOU 2266 O ASP A1089 8225 8860 3227 2502 2348 2827 O
ATOM 2267 CB ASP A1089 -12.304 -15.786 -27.729 1.00 50.45 C
ANISOU 2267 CB ASP A1089 7962 7547 3658 1899 3042 3020 C
ATOM 2268 CG ASP A1089 -13.807 -15.524 -27.622 1.00 62.35 C
ANISOU 2268 CG ASP A1089 9400 9011 5280 1630 3217 2932 C
ATOM 2269 OD1 ASP A1089 -14.217 -14.336 -27.656 1.00 62.83 O
ANISOU 2269 OD1 ASP A1089 9341 9347 5184 1519 3005 2570 O
ATOM 2270 OD2 ASP A1089 -14.570 -16.507 -27.484 1.00 68.03 O
ANISOU 2270 OD2 ASP A1089 10171 9413 6266 1534 3576 3231 O
ATOM 2271 N SER A1090 -9.204 -15.608 -28.822 1.00 50.37 N
ANISOU 2271 N SER A1090 7941 7629 3569 2245 2483 2775 N
ATOM 2272 CA SER A1090 -7.786 -15.921 -28.629 1.00 50.14 C
ANISOU 2272 CA SER A1090 7908 7749 3392 2574 2358 2929 C
ATOM 2273 C SER A1090 -6.881 -14.718 -28.840 1.00 52.66 C
ANISOU 2273 C SER A1090 8071 8447 3491 2590 1963 2551 C
ATOM 2274 O SER A1090 -5.917 -14.540 -28.090 1.00 51.89 O
ANISOU 2274 O SER A1090 7900 8750 3067 2898 1800 2654 O
ATOM 2275 CB SER A1090 -7.356 -17.044 -29.567 1.00 54.83 C
ANISOU 2275 CB SER A1090 8602 7821 4409 2562 2517 3034 C
ATOM 2276 OG SER A1090 -7.840 -18.297 -29.115 1.00 69.12 O
ANISOU 2276 OG SER A1090 10557 9290 6416 2636 2889 3467 O
ATOM 2277 N LEU A1091 -7.175 -13.917 -29.885 1.00 48.40 N
ANISOU 2277 N LEU A1091 7470 7772 3146 2261 1814 2124 N
ATOM 2278 CA LEU A1091 -6.401 -12.748 -30.316 1.00 47.19 C
ANISOU 2278 CA LEU A1091 7171 7869 2891 2198 1474 1748 C
ATOM 2279 C LEU A1091 -6.400 -11.597 -29.314 1.00 50.63 C
ANISOU 2279 C LEU A1091 7488 8811 2936 2278 1256 1594 C
ATOM 2280 O LEU A1091 -7.335 -11.455 -28.518 1.00 49.91 O
ANISOU 2280 O LEU A1091 7429 8853 2682 2283 1362 1668 O
ATOM 2281 CB LEU A1091 -6.887 -12.239 -31.695 1.00 46.67 C
ANISOU 2281 CB LEU A1091 7096 7499 3137 1827 1417 1391 C
ATOM 2282 CG LEU A1091 -6.903 -13.228 -32.871 1.00 50.84 C
ANISOU 2282 CG LEU A1091 7726 7543 4049 1703 1593 1417 C
ATOM 2283 CD1 LEU A1091 -7.852 -12.761 -33.959 1.00 50.79 C
ANISOU 2283 CD1 LEU A1091 7726 7301 4272 1342 1575 1110 C
ATOM 2284 CD2 LEU A1091 -5.506 -13.478 -33.435 1.00 52.94 C
ANISOU 2284 CD2 LEU A1091 7947 7804 4364 1847 1497 1397 C
ATOM 2285 N ASP A1092 -5.328 -10.775 -29.378 1.00 46.67 N
ANISOU 2285 N ASP A1092 6837 8589 2305 2334 958 1357 N
ATOM 2286 CA ASP A1092 -5.103 -9.547 -28.603 1.00 45.58 C
ANISOU 2286 CA ASP A1092 6555 8911 1853 2378 688 1096 C
ATOM 2287 C ASP A1092 -5.751 -8.372 -29.366 1.00 46.55 C
ANISOU 2287 C ASP A1092 6636 8895 2158 2031 570 692 C
ATOM 2288 O ASP A1092 -6.075 -8.526 -30.544 1.00 45.80 O
ANISOU 2288 O ASP A1092 6598 8411 2392 1794 651 627 O
ATOM 2289 CB ASP A1092 -3.592 -9.299 -28.426 1.00 47.30 C
ANISOU 2289 CB ASP A1092 6604 9436 1931 2567 432 1018 C
ATOM 2290 CG ASP A1092 -2.797 -9.325 -29.728 1.00 54.73 C
ANISOU 2290 CG ASP A1092 7488 10103 3203 2414 376 890 C
ATOM 2291 OD1 ASP A1092 -2.719 -10.408 -30.355 1.00 54.17 O
ANISOU 2291 OD1 ASP A1092 7526 9702 3353 2449 582 1121 O
ATOM 2292 OD2 ASP A1092 -2.243 -8.264 -30.110 1.00 58.81 O
ANISOU 2292 OD2 ASP A1092 7847 10734 3764 2263 138 557 O
ATOM 2293 N ALA A1093 -5.903 -7.206 -28.704 1.00 41.46 N
ANISOU 2293 N ALA A1093 5888 8569 1295 2021 372 417 N
ATOM 2294 CA ALA A1093 -6.536 -5.982 -29.220 1.00 40.66 C
ANISOU 2294 CA ALA A1093 5741 8368 1340 1745 249 45 C
ATOM 2295 C ALA A1093 -6.105 -5.547 -30.630 1.00 43.36 C
ANISOU 2295 C ALA A1093 6043 8410 2020 1494 146 -146 C
ATOM 2296 O ALA A1093 -6.955 -5.108 -31.403 1.00 43.58 O
ANISOU 2296 O ALA A1093 6113 8185 2263 1257 175 -288 O
ATOM 2297 CB ALA A1093 -6.338 -4.833 -28.240 1.00 41.35 C
ANISOU 2297 CB ALA A1093 5700 8867 1144 1832 16 -243 C
ATOM 2298 N VAL A1094 -4.807 -5.671 -30.963 1.00 38.55 N
ANISOU 2298 N VAL A1094 5343 7856 1447 1559 35 -136 N
ATOM 2299 CA VAL A1094 -4.231 -5.285 -32.262 1.00 36.99 C
ANISOU 2299 CA VAL A1094 5091 7429 1533 1348 -42 -284 C
ATOM 2300 C VAL A1094 -4.641 -6.270 -33.364 1.00 38.54 C
ANISOU 2300 C VAL A1094 5435 7236 1974 1247 184 -109 C
ATOM 2301 O VAL A1094 -5.045 -5.843 -34.446 1.00 37.39 O
ANISOU 2301 O VAL A1094 5319 6847 2042 1008 183 -249 O
ATOM 2302 CB VAL A1094 -2.685 -5.093 -32.172 1.00 40.50 C
ANISOU 2302 CB VAL A1094 5349 8108 1930 1459 -224 -342 C
ATOM 2303 CG1 VAL A1094 -2.077 -4.740 -33.528 1.00 40.10 C
ANISOU 2303 CG1 VAL A1094 5237 7832 2168 1242 -256 -458 C
ATOM 2304 CG2 VAL A1094 -2.319 -4.033 -31.133 1.00 40.00 C
ANISOU 2304 CG2 VAL A1094 5119 8428 1649 1522 -476 -594 C
ATOM 2305 N ARG A1095 -4.545 -7.581 -33.085 1.00 34.03 N
ANISOU 2305 N ARG A1095 4956 6604 1369 1436 375 191 N
ATOM 2306 CA ARG A1095 -4.909 -8.629 -34.044 1.00 32.84 C
ANISOU 2306 CA ARG A1095 4945 6068 1466 1355 598 330 C
ATOM 2307 C ARG A1095 -6.424 -8.759 -34.227 1.00 35.80 C
ANISOU 2307 C ARG A1095 5439 6213 1950 1175 749 323 C
ATOM 2308 O ARG A1095 -6.878 -9.213 -35.279 1.00 35.99 O
ANISOU 2308 O ARG A1095 5545 5919 2212 1007 864 294 O
ATOM 2309 CB ARG A1095 -4.252 -9.961 -33.680 1.00 31.42 C
ANISOU 2309 CB ARG A1095 4817 5855 1266 1625 755 645 C
ATOM 2310 CG ARG A1095 -2.741 -9.879 -33.696 1.00 34.03 C
ANISOU 2310 CG ARG A1095 4997 6398 1535 1795 606 633 C
ATOM 2311 CD ARG A1095 -2.114 -11.233 -33.566 1.00 33.27 C
ANISOU 2311 CD ARG A1095 4958 6201 1483 2066 774 939 C
ATOM 2312 NE ARG A1095 -0.666 -11.167 -33.757 1.00 33.66 N
ANISOU 2312 NE ARG A1095 4834 6440 1516 2218 639 905 N
ATOM 2313 CZ ARG A1095 0.217 -11.085 -32.771 1.00 46.29 C
ANISOU 2313 CZ ARG A1095 6284 8427 2875 2497 492 1005 C
ATOM 2314 NH1 ARG A1095 -0.190 -11.035 -31.510 1.00 34.06 N
ANISOU 2314 NH1 ARG A1095 4760 7140 1043 2666 459 1144 N
ATOM 2315 NH2 ARG A1095 1.515 -11.051 -33.038 1.00 32.82 N
ANISOU 2315 NH2 ARG A1095 4389 6885 1196 2618 375 958 N
ATOM 2316 N ARG A1096 -7.201 -8.325 -33.214 1.00 31.35 N
ANISOU 2316 N ARG A1096 4865 5842 1207 1210 740 321 N
ATOM 2317 CA ARG A1096 -8.668 -8.285 -33.239 1.00 30.42 C
ANISOU 2317 CA ARG A1096 4806 5577 1175 1048 867 292 C
ATOM 2318 C ARG A1096 -9.107 -7.255 -34.281 1.00 32.15 C
ANISOU 2318 C ARG A1096 4982 5673 1560 785 720 -13 C
ATOM 2319 O ARG A1096 -10.041 -7.508 -35.042 1.00 32.18 O
ANISOU 2319 O ARG A1096 5037 5427 1763 603 819 -51 O
ATOM 2320 CB ARG A1096 -9.235 -7.914 -31.848 1.00 29.13 C
ANISOU 2320 CB ARG A1096 4612 5721 734 1186 880 340 C
ATOM 2321 CG ARG A1096 -9.299 -9.109 -30.919 1.00 38.50 C
ANISOU 2321 CG ARG A1096 5882 6953 1796 1407 1119 718 C
ATOM 2322 CD ARG A1096 -9.978 -8.829 -29.603 1.00 49.63 C
ANISOU 2322 CD ARG A1096 7272 8680 2907 1544 1182 794 C
ATOM 2323 NE ARG A1096 -9.842 -9.988 -28.721 1.00 59.84 N
ANISOU 2323 NE ARG A1096 8649 10037 4051 1793 1412 1219 N
ATOM 2324 CZ ARG A1096 -10.490 -10.152 -27.574 1.00 70.03 C
ANISOU 2324 CZ ARG A1096 9958 11566 5085 1941 1575 1419 C
ATOM 2325 NH1 ARG A1096 -11.344 -9.228 -27.146 1.00 51.76 N
ANISOU 2325 NH1 ARG A1096 7575 9457 2635 1867 1531 1197 N
ATOM 2326 NH2 ARG A1096 -10.299 -11.246 -26.850 1.00 56.35 N
ANISOU 2326 NH2 ARG A1096 8315 9864 3233 2179 1799 1859 N
ATOM 2327 N ALA A1097 -8.400 -6.108 -34.321 1.00 26.39 N
ANISOU 2327 N ALA A1097 4150 5119 759 772 483 -221 N
ATOM 2328 CA ALA A1097 -8.633 -5.007 -35.247 1.00 25.55 C
ANISOU 2328 CA ALA A1097 3999 4910 797 559 332 -470 C
ATOM 2329 C ALA A1097 -8.323 -5.424 -36.689 1.00 29.03 C
ANISOU 2329 C ALA A1097 4490 5095 1446 420 372 -466 C
ATOM 2330 O ALA A1097 -9.031 -4.997 -37.605 1.00 29.21 O
ANISOU 2330 O ALA A1097 4534 4960 1607 239 347 -583 O
ATOM 2331 CB ALA A1097 -7.774 -3.826 -34.856 1.00 25.91 C
ANISOU 2331 CB ALA A1097 3921 5177 748 591 101 -656 C
ATOM 2332 N ALA A1098 -7.272 -6.257 -36.887 1.00 24.24 N
ANISOU 2332 N ALA A1098 3894 4472 844 528 432 -336 N
ATOM 2333 CA ALA A1098 -6.881 -6.771 -38.197 1.00 23.61 C
ANISOU 2333 CA ALA A1098 3862 4182 928 437 495 -341 C
ATOM 2334 C ALA A1098 -7.972 -7.712 -38.734 1.00 27.27 C
ANISOU 2334 C ALA A1098 4448 4378 1536 339 677 -300 C
ATOM 2335 O ALA A1098 -8.262 -7.678 -39.924 1.00 26.30 O
ANISOU 2335 O ALA A1098 4360 4100 1534 180 675 -416 O
ATOM 2336 CB ALA A1098 -5.539 -7.479 -38.115 1.00 24.04 C
ANISOU 2336 CB ALA A1098 3883 4300 952 617 534 -215 C
ATOM 2337 N LEU A1099 -8.631 -8.483 -37.836 1.00 24.57 N
ANISOU 2337 N LEU A1099 4159 4003 1175 424 830 -142 N
ATOM 2338 CA LEU A1099 -9.742 -9.382 -38.177 1.00 23.70 C
ANISOU 2338 CA LEU A1099 4134 3631 1241 310 1018 -106 C
ATOM 2339 C LEU A1099 -11.000 -8.571 -38.524 1.00 26.77 C
ANISOU 2339 C LEU A1099 4480 4012 1680 108 939 -288 C
ATOM 2340 O LEU A1099 -11.678 -8.889 -39.502 1.00 26.54 O
ANISOU 2340 O LEU A1099 4477 3790 1816 -62 975 -400 O
ATOM 2341 CB LEU A1099 -10.010 -10.383 -37.039 1.00 23.33 C
ANISOU 2341 CB LEU A1099 4138 3557 1168 465 1228 163 C
ATOM 2342 CG LEU A1099 -10.767 -11.660 -37.415 1.00 27.08 C
ANISOU 2342 CG LEU A1099 4705 3686 1899 370 1476 250 C
ATOM 2343 CD1 LEU A1099 -9.961 -12.526 -38.387 1.00 26.62 C
ANISOU 2343 CD1 LEU A1099 4721 3386 2009 385 1540 225 C
ATOM 2344 CD2 LEU A1099 -11.115 -12.464 -36.167 1.00 28.52 C
ANISOU 2344 CD2 LEU A1099 4930 3860 2046 521 1699 565 C
ATOM 2345 N ILE A1100 -11.275 -7.503 -37.744 1.00 23.09 N
ANISOU 2345 N ILE A1100 3936 3769 1067 142 816 -342 N
ATOM 2346 CA ILE A1100 -12.375 -6.548 -37.953 1.00 22.95 C
ANISOU 2346 CA ILE A1100 3856 3779 1085 3 717 -515 C
ATOM 2347 C ILE A1100 -12.179 -5.876 -39.334 1.00 27.35 C
ANISOU 2347 C ILE A1100 4406 4257 1728 -138 557 -686 C
ATOM 2348 O ILE A1100 -13.136 -5.822 -40.125 1.00 26.35 O
ANISOU 2348 O ILE A1100 4271 4024 1718 -284 544 -789 O
ATOM 2349 CB ILE A1100 -12.453 -5.525 -36.779 1.00 25.53 C
ANISOU 2349 CB ILE A1100 4107 4366 1227 115 616 -557 C
ATOM 2350 CG1 ILE A1100 -13.080 -6.160 -35.516 1.00 25.26 C
ANISOU 2350 CG1 ILE A1100 4077 4431 1091 230 806 -391 C
ATOM 2351 CG2 ILE A1100 -13.202 -4.259 -37.176 1.00 25.59 C
ANISOU 2351 CG2 ILE A1100 4043 4391 1287 5 454 -772 C
ATOM 2352 CD1 ILE A1100 -12.667 -5.497 -34.226 1.00 26.17 C
ANISOU 2352 CD1 ILE A1100 4143 4861 939 422 730 -393 C
ATOM 2353 N ASN A1101 -10.918 -5.432 -39.638 1.00 24.10 N
ANISOU 2353 N ASN A1101 3987 3914 1256 -88 448 -698 N
ATOM 2354 CA ASN A1101 -10.533 -4.862 -40.940 1.00 23.69 C
ANISOU 2354 CA ASN A1101 3936 3806 1261 -200 336 -800 C
ATOM 2355 C ASN A1101 -10.953 -5.825 -42.054 1.00 27.72 C
ANISOU 2355 C ASN A1101 4521 4137 1875 -300 439 -824 C
ATOM 2356 O ASN A1101 -11.698 -5.414 -42.943 1.00 28.07 O
ANISOU 2356 O ASN A1101 4560 4139 1964 -425 363 -935 O
ATOM 2357 CB ASN A1101 -9.023 -4.581 -41.016 1.00 21.87 C
ANISOU 2357 CB ASN A1101 3648 3650 1010 -127 271 -751 C
ATOM 2358 CG ASN A1101 -8.596 -3.713 -42.187 1.00 32.12 C
ANISOU 2358 CG ASN A1101 4947 4947 2311 -239 168 -842 C
ATOM 2359 OD1 ASN A1101 -8.923 -3.966 -43.358 1.00 27.98 O
ANISOU 2359 OD1 ASN A1101 4481 4324 1828 -331 199 -872 O
ATOM 2360 ND2 ASN A1101 -7.840 -2.668 -41.898 1.00 14.34 N
ANISOU 2360 ND2 ASN A1101 2238 2517 693 -230 53 -578 N
ATOM 2361 N MET A1102 -10.557 -7.112 -41.956 1.00 24.91 N
ANISOU 2361 N MET A1102 4228 3675 1561 -233 607 -731 N
ATOM 2362 CA MET A1102 -10.910 -8.161 -42.929 1.00 25.69 C
ANISOU 2362 CA MET A1102 4400 3577 1786 -322 721 -796 C
ATOM 2363 C MET A1102 -12.432 -8.326 -43.104 1.00 30.70 C
ANISOU 2363 C MET A1102 5016 4118 2533 -475 740 -898 C
ATOM 2364 O MET A1102 -12.897 -8.505 -44.232 1.00 29.90 O
ANISOU 2364 O MET A1102 4927 3945 2490 -601 705 -1055 O
ATOM 2365 CB MET A1102 -10.289 -9.514 -42.542 1.00 27.83 C
ANISOU 2365 CB MET A1102 4740 3705 2127 -198 920 -662 C
ATOM 2366 CG MET A1102 -8.808 -9.600 -42.761 1.00 31.16 C
ANISOU 2366 CG MET A1102 5165 4196 2480 -56 915 -604 C
ATOM 2367 SD MET A1102 -8.234 -11.280 -42.438 1.00 35.02 S
ANISOU 2367 SD MET A1102 5744 4463 3099 111 1160 -452 S
ATOM 2368 CE MET A1102 -8.758 -12.116 -43.974 1.00 31.46 C
ANISOU 2368 CE MET A1102 5380 3751 2823 -58 1246 -693 C
ATOM 2369 N VAL A1103 -13.189 -8.310 -41.978 1.00 28.50 N
ANISOU 2369 N VAL A1103 4691 3866 2271 -454 801 -814 N
ATOM 2370 CA VAL A1103 -14.655 -8.430 -41.941 1.00 28.19 C
ANISOU 2370 CA VAL A1103 4588 3770 2355 -591 838 -893 C
ATOM 2371 C VAL A1103 -15.292 -7.236 -42.665 1.00 32.46 C
ANISOU 2371 C VAL A1103 5050 4428 2854 -680 622 -1060 C
ATOM 2372 O VAL A1103 -16.185 -7.432 -43.488 1.00 31.87 O
ANISOU 2372 O VAL A1103 4933 4295 2879 -818 587 -1206 O
ATOM 2373 CB VAL A1103 -15.185 -8.621 -40.491 1.00 31.57 C
ANISOU 2373 CB VAL A1103 4975 4248 2774 -517 979 -732 C
ATOM 2374 CG1 VAL A1103 -16.697 -8.415 -40.406 1.00 31.21 C
ANISOU 2374 CG1 VAL A1103 4811 4208 2838 -652 994 -826 C
ATOM 2375 CG2 VAL A1103 -14.798 -9.993 -39.941 1.00 31.20 C
ANISOU 2375 CG2 VAL A1103 5013 4031 2810 -441 1224 -531 C
ATOM 2376 N PHE A1104 -14.791 -6.011 -42.396 1.00 29.36 N
ANISOU 2376 N PHE A1104 4634 4195 2328 -594 472 -1044 N
ATOM 2377 CA PHE A1104 -15.265 -4.787 -43.039 1.00 29.11 C
ANISOU 2377 CA PHE A1104 4544 4244 2273 -643 274 -1156 C
ATOM 2378 C PHE A1104 -15.070 -4.833 -44.550 1.00 33.62 C
ANISOU 2378 C PHE A1104 5159 4780 2836 -725 192 -1240 C
ATOM 2379 O PHE A1104 -15.916 -4.324 -45.279 1.00 34.60 O
ANISOU 2379 O PHE A1104 5230 4940 2976 -793 70 -1337 O
ATOM 2380 CB PHE A1104 -14.580 -3.536 -42.449 1.00 30.78 C
ANISOU 2380 CB PHE A1104 4736 4572 2387 -541 154 -1123 C
ATOM 2381 CG PHE A1104 -15.172 -2.966 -41.178 1.00 32.38 C
ANISOU 2381 CG PHE A1104 4863 4872 2570 -465 153 -1133 C
ATOM 2382 CD1 PHE A1104 -16.537 -2.731 -41.068 1.00 35.93 C
ANISOU 2382 CD1 PHE A1104 5224 5333 3093 -506 143 -1212 C
ATOM 2383 CD2 PHE A1104 -14.355 -2.578 -40.125 1.00 35.00 C
ANISOU 2383 CD2 PHE A1104 5193 5313 2794 -342 147 -1091 C
ATOM 2384 CE1 PHE A1104 -17.077 -2.164 -39.907 1.00 36.83 C
ANISOU 2384 CE1 PHE A1104 5261 5559 3173 -418 158 -1240 C
ATOM 2385 CE2 PHE A1104 -14.898 -2.007 -38.967 1.00 37.34 C
ANISOU 2385 CE2 PHE A1104 5421 5732 3033 -256 142 -1138 C
ATOM 2386 CZ PHE A1104 -16.254 -1.811 -38.864 1.00 35.30 C
ANISOU 2386 CZ PHE A1104 5089 5476 2849 -290 161 -1209 C
ATOM 2387 N GLN A1105 -13.984 -5.475 -45.021 1.00 29.23 N
ANISOU 2387 N GLN A1105 4691 4176 2240 -701 262 -1203 N
ATOM 2388 CA GLN A1105 -13.676 -5.584 -46.446 1.00 28.12 C
ANISOU 2388 CA GLN A1105 4600 4038 2047 -756 211 -1286 C
ATOM 2389 C GLN A1105 -14.418 -6.699 -47.177 1.00 32.96 C
ANISOU 2389 C GLN A1105 5228 4553 2742 -861 276 -1442 C
ATOM 2390 O GLN A1105 -15.028 -6.413 -48.209 1.00 32.94 O
ANISOU 2390 O GLN A1105 5201 4625 2691 -934 152 -1570 O
ATOM 2391 CB GLN A1105 -12.162 -5.704 -46.696 1.00 28.77 C
ANISOU 2391 CB GLN A1105 4747 4136 2049 -676 267 -1204 C
ATOM 2392 CG GLN A1105 -11.804 -5.550 -48.184 1.00 36.53 C
ANISOU 2392 CG GLN A1105 5772 5182 2925 -715 214 -1272 C
ATOM 2393 CD GLN A1105 -10.341 -5.703 -48.517 1.00 51.37 C
ANISOU 2393 CD GLN A1105 7688 7098 4733 -639 293 -1200 C
ATOM 2394 OE1 GLN A1105 -9.468 -5.772 -47.641 1.00 46.62 O
ANISOU 2394 OE1 GLN A1105 7062 6491 4162 -551 355 -1092 O
ATOM 2395 NE2 GLN A1105 -10.044 -5.748 -49.810 1.00 41.15 N
ANISOU 2395 NE2 GLN A1105 6437 5874 3324 -661 292 -1262 N
ATOM 2396 N MET A1106 -14.319 -7.960 -46.693 1.00 30.22 N
ANISOU 2396 N MET A1106 4921 4040 2521 -863 464 -1434 N
ATOM 2397 CA MET A1106 -14.866 -9.157 -47.359 1.00 30.93 C
ANISOU 2397 CA MET A1106 5031 3975 2747 -977 553 -1611 C
ATOM 2398 C MET A1106 -16.207 -9.665 -46.862 1.00 36.66 C
ANISOU 2398 C MET A1106 5661 4596 3671 -1105 613 -1680 C
ATOM 2399 O MET A1106 -16.822 -10.490 -47.542 1.00 36.64 O
ANISOU 2399 O MET A1106 5636 4485 3800 -1242 639 -1886 O
ATOM 2400 CB MET A1106 -13.879 -10.335 -47.280 1.00 33.71 C
ANISOU 2400 CB MET A1106 5491 4141 3177 -904 751 -1569 C
ATOM 2401 CG MET A1106 -12.414 -9.958 -47.304 1.00 38.27 C
ANISOU 2401 CG MET A1106 6126 4815 3599 -746 749 -1439 C
ATOM 2402 SD MET A1106 -11.421 -11.377 -46.802 1.00 43.17 S
ANISOU 2402 SD MET A1106 6839 5205 4357 -609 998 -1336 S
ATOM 2403 CE MET A1106 -11.447 -12.324 -48.365 1.00 40.41 C
ANISOU 2403 CE MET A1106 6562 4725 4066 -696 1046 -1645 C
ATOM 2404 N GLY A1107 -16.598 -9.266 -45.654 1.00 34.35 N
ANISOU 2404 N GLY A1107 5306 4334 3410 -1063 658 -1521 N
ATOM 2405 CA GLY A1107 -17.818 -9.741 -45.017 1.00 34.48 C
ANISOU 2405 CA GLY A1107 5214 4266 3621 -1174 764 -1537 C
ATOM 2406 C GLY A1107 -17.536 -10.868 -44.045 1.00 40.02 C
ANISOU 2406 C GLY A1107 5979 4755 4472 -1140 1036 -1360 C
ATOM 2407 O GLY A1107 -16.396 -11.312 -43.925 1.00 38.56 O
ANISOU 2407 O GLY A1107 5920 4490 4239 -1015 1121 -1243 O
ATOM 2408 N GLU A1108 -18.579 -11.343 -43.358 1.00 39.87 N
ANISOU 2408 N GLU A1108 5861 4647 4641 -1242 1184 -1322 N
ATOM 2409 CA GLU A1108 -18.518 -12.423 -42.372 1.00 41.57 C
ANISOU 2409 CA GLU A1108 6125 4647 5021 -1218 1476 -1103 C
ATOM 2410 C GLU A1108 -18.060 -13.778 -42.960 1.00 47.63 C
ANISOU 2410 C GLU A1108 7006 5083 6009 -1276 1631 -1159 C
ATOM 2411 O GLU A1108 -17.087 -14.353 -42.465 1.00 46.99 O
ANISOU 2411 O GLU A1108 7058 4881 5914 -1114 1776 -947 O
ATOM 2412 CB GLU A1108 -19.888 -12.588 -41.689 1.00 43.39 C
ANISOU 2412 CB GLU A1108 6192 4862 5433 -1356 1612 -1071 C
ATOM 2413 CG GLU A1108 -20.224 -11.518 -40.672 1.00 55.71 C
ANISOU 2413 CG GLU A1108 7666 6708 6793 -1235 1567 -939 C
ATOM 2414 CD GLU A1108 -19.857 -11.889 -39.252 1.00 82.15 C
ANISOU 2414 CD GLU A1108 11082 10068 10065 -1071 1803 -605 C
ATOM 2415 OE1 GLU A1108 -20.207 -13.011 -38.814 1.00 65.30 O
ANISOU 2415 OE1 GLU A1108 8954 7705 8151 -1143 2081 -447 O
ATOM 2416 OE2 GLU A1108 -19.221 -11.050 -38.574 1.00 85.38 O
ANISOU 2416 OE2 GLU A1108 11531 10717 10192 -868 1709 -500 O
ATOM 2417 N THR A1109 -18.776 -14.294 -43.988 1.00 45.99 N
ANISOU 2417 N THR A1109 6733 4731 6009 -1496 1597 -1458 N
ATOM 2418 CA THR A1109 -18.469 -15.587 -44.623 1.00 46.57 C
ANISOU 2418 CA THR A1109 6901 4460 6333 -1577 1740 -1593 C
ATOM 2419 C THR A1109 -17.113 -15.605 -45.341 1.00 48.99 C
ANISOU 2419 C THR A1109 7368 4785 6460 -1410 1661 -1646 C
ATOM 2420 O THR A1109 -16.451 -16.647 -45.339 1.00 48.63 O
ANISOU 2420 O THR A1109 7445 4451 6582 -1350 1846 -1606 O
ATOM 2421 CB THR A1109 -19.604 -16.064 -45.549 1.00 61.31 C
ANISOU 2421 CB THR A1109 8630 6212 8454 -1864 1690 -1963 C
ATOM 2422 OG1 THR A1109 -19.975 -15.012 -46.445 1.00 64.17 O
ANISOU 2422 OG1 THR A1109 8887 6912 8581 -1901 1379 -2194 O
ATOM 2423 CG2 THR A1109 -20.820 -16.579 -44.774 1.00 61.10 C
ANISOU 2423 CG2 THR A1109 8449 6011 8755 -2056 1895 -1888 C
ATOM 2424 N GLY A1110 -16.726 -14.467 -45.932 1.00 43.85 N
ANISOU 2424 N GLY A1110 6707 4457 5495 -1333 1411 -1719 N
ATOM 2425 CA GLY A1110 -15.456 -14.300 -46.634 1.00 42.97 C
ANISOU 2425 CA GLY A1110 6714 4428 5185 -1181 1336 -1752 C
ATOM 2426 C GLY A1110 -14.262 -14.618 -45.755 1.00 45.31 C
ANISOU 2426 C GLY A1110 7117 4652 5448 -953 1490 -1452 C
ATOM 2427 O GLY A1110 -13.435 -15.462 -46.114 1.00 45.91 O
ANISOU 2427 O GLY A1110 7296 4543 5604 -863 1608 -1478 O
ATOM 2428 N VAL A1111 -14.197 -13.974 -44.576 1.00 39.20 N
ANISOU 2428 N VAL A1111 6306 4032 4556 -842 1488 -1179 N
ATOM 2429 CA VAL A1111 -13.154 -14.173 -43.559 1.00 38.50 C
ANISOU 2429 CA VAL A1111 6286 3949 4394 -605 1601 -874 C
ATOM 2430 C VAL A1111 -13.241 -15.600 -42.992 1.00 43.27 C
ANISOU 2430 C VAL A1111 6967 4198 5277 -575 1889 -717 C
ATOM 2431 O VAL A1111 -12.207 -16.212 -42.710 1.00 42.41 O
ANISOU 2431 O VAL A1111 6949 3986 5180 -371 2004 -545 O
ATOM 2432 CB VAL A1111 -13.254 -13.109 -42.435 1.00 41.50 C
ANISOU 2432 CB VAL A1111 6591 4612 4565 -514 1511 -681 C
ATOM 2433 CG1 VAL A1111 -12.113 -13.243 -41.431 1.00 40.93 C
ANISOU 2433 CG1 VAL A1111 6569 4619 4365 -253 1581 -398 C
ATOM 2434 CG2 VAL A1111 -13.279 -11.707 -43.023 1.00 41.11 C
ANISOU 2434 CG2 VAL A1111 6469 4838 4313 -563 1245 -840 C
ATOM 2435 N ALA A1112 -14.480 -16.128 -42.845 1.00 41.00 N
ANISOU 2435 N ALA A1112 6628 3712 5238 -777 2010 -770 N
ATOM 2436 CA ALA A1112 -14.745 -17.482 -42.354 1.00 41.16 C
ANISOU 2436 CA ALA A1112 6711 3335 5593 -802 2310 -620 C
ATOM 2437 C ALA A1112 -14.232 -18.531 -43.340 1.00 45.87 C
ANISOU 2437 C ALA A1112 7412 3596 6422 -820 2398 -826 C
ATOM 2438 O ALA A1112 -13.965 -19.653 -42.931 1.00 46.95 O
ANISOU 2438 O ALA A1112 7644 3377 6818 -744 2651 -651 O
ATOM 2439 CB ALA A1112 -16.231 -17.674 -42.102 1.00 42.02 C
ANISOU 2439 CB ALA A1112 6697 3337 5930 -1059 2404 -674 C
ATOM 2440 N GLY A1113 -14.062 -18.143 -44.609 1.00 40.98 N
ANISOU 2440 N GLY A1113 6780 3097 5693 -895 2198 -1179 N
ATOM 2441 CA GLY A1113 -13.529 -18.995 -45.665 1.00 39.93 C
ANISOU 2441 CA GLY A1113 6739 2720 5711 -895 2252 -1442 C
ATOM 2442 C GLY A1113 -12.071 -19.364 -45.465 1.00 42.72 C
ANISOU 2442 C GLY A1113 7213 3021 6000 -592 2350 -1245 C
ATOM 2443 O GLY A1113 -11.633 -20.403 -45.958 1.00 42.84 O
ANISOU 2443 O GLY A1113 7322 2707 6247 -542 2505 -1363 O
ATOM 2444 N PHE A1114 -11.309 -18.531 -44.732 1.00 38.63 N
ANISOU 2444 N PHE A1114 6673 2820 5183 -381 2258 -964 N
ATOM 2445 CA PHE A1114 -9.889 -18.743 -44.431 1.00 38.83 C
ANISOU 2445 CA PHE A1114 6761 2879 5113 -73 2316 -755 C
ATOM 2446 C PHE A1114 -9.699 -19.695 -43.226 1.00 44.75 C
ANISOU 2446 C PHE A1114 7584 3363 6057 113 2566 -370 C
ATOM 2447 O PHE A1114 -9.067 -19.317 -42.235 1.00 44.29 O
ANISOU 2447 O PHE A1114 7506 3527 5797 342 2543 -48 O
ATOM 2448 CB PHE A1114 -9.208 -17.393 -44.136 1.00 40.43 C
ANISOU 2448 CB PHE A1114 6877 3551 4934 46 2094 -642 C
ATOM 2449 CG PHE A1114 -8.992 -16.478 -45.313 1.00 41.59 C
ANISOU 2449 CG PHE A1114 6972 3956 4875 -55 1882 -927 C
ATOM 2450 CD1 PHE A1114 -9.931 -15.507 -45.639 1.00 44.18 C
ANISOU 2450 CD1 PHE A1114 7226 4473 5089 -267 1702 -1075 C
ATOM 2451 CD2 PHE A1114 -7.823 -16.548 -46.064 1.00 42.93 C
ANISOU 2451 CD2 PHE A1114 7157 4202 4954 85 1872 -1014 C
ATOM 2452 CE1 PHE A1114 -9.713 -14.635 -46.707 1.00 44.37 C
ANISOU 2452 CE1 PHE A1114 7212 4739 4907 -334 1517 -1278 C
ATOM 2453 CE2 PHE A1114 -7.608 -15.672 -47.131 1.00 45.11 C
ANISOU 2453 CE2 PHE A1114 7386 4738 5016 -1 1703 -1225 C
ATOM 2454 CZ PHE A1114 -8.552 -14.716 -47.438 1.00 42.90 C
ANISOU 2454 CZ PHE A1114 7051 4628 4619 -206 1526 -1338 C
ATOM 2455 N THR A1115 -10.218 -20.935 -43.336 1.00 42.53 N
ANISOU 2455 N THR A1115 7385 2605 6170 22 2802 -408 N
ATOM 2456 CA THR A1115 -10.205 -21.991 -42.307 1.00 42.89 C
ANISOU 2456 CA THR A1115 7519 2298 6480 166 3089 -31 C
ATOM 2457 C THR A1115 -8.823 -22.257 -41.655 1.00 48.37 C
ANISOU 2457 C THR A1115 8273 3055 7053 577 3150 317 C
ATOM 2458 O THR A1115 -8.730 -22.246 -40.426 1.00 48.41 O
ANISOU 2458 O THR A1115 8280 3164 6948 758 3223 736 O
ATOM 2459 CB THR A1115 -10.799 -23.303 -42.875 1.00 48.86 C
ANISOU 2459 CB THR A1115 8356 2468 7740 -13 3323 -232 C
ATOM 2460 OG1 THR A1115 -11.896 -23.012 -43.747 1.00 49.68 O
ANISOU 2460 OG1 THR A1115 8372 2586 7920 -380 3203 -654 O
ATOM 2461 CG2 THR A1115 -11.220 -24.289 -41.782 1.00 43.15 C
ANISOU 2461 CG2 THR A1115 7706 1340 7348 33 3646 177 C
ATOM 2462 N ASN A1116 -7.777 -22.528 -42.468 1.00 45.17 N
ANISOU 2462 N ASN A1116 7901 2606 6657 737 3126 142 N
ATOM 2463 CA ASN A1116 -6.434 -22.859 -41.978 1.00 45.00 C
ANISOU 2463 CA ASN A1116 7904 2637 6557 1138 3179 432 C
ATOM 2464 C ASN A1116 -5.667 -21.672 -41.396 1.00 48.58 C
ANISOU 2464 C ASN A1116 8229 3670 6559 1308 2938 593 C
ATOM 2465 O ASN A1116 -4.928 -21.860 -40.422 1.00 48.33 O
ANISOU 2465 O ASN A1116 8188 3750 6426 1624 2977 964 O
ATOM 2466 CB ASN A1116 -5.625 -23.569 -43.043 1.00 46.31 C
ANISOU 2466 CB ASN A1116 8126 2561 6908 1252 3256 171 C
ATOM 2467 CG ASN A1116 -6.152 -24.954 -43.301 1.00 75.75 C
ANISOU 2467 CG ASN A1116 11995 5647 11137 1179 3538 94 C
ATOM 2468 OD1 ASN A1116 -5.733 -25.927 -42.667 1.00 67.22 O
ANISOU 2468 OD1 ASN A1116 11009 4228 10304 1434 3766 418 O
ATOM 2469 ND2 ASN A1116 -7.108 -25.066 -44.215 1.00 72.17 N
ANISOU 2469 ND2 ASN A1116 11552 5010 10858 830 3525 -333 N
ATOM 2470 N SER A1117 -5.848 -20.461 -41.966 1.00 44.51 N
ANISOU 2470 N SER A1117 7608 3517 5786 1104 2689 321 N
ATOM 2471 CA SER A1117 -5.225 -19.233 -41.462 1.00 43.77 C
ANISOU 2471 CA SER A1117 7380 3940 5311 1202 2452 416 C
ATOM 2472 C SER A1117 -5.813 -18.925 -40.086 1.00 47.24 C
ANISOU 2472 C SER A1117 7801 4530 5618 1239 2449 730 C
ATOM 2473 O SER A1117 -5.057 -18.637 -39.157 1.00 46.85 O
ANISOU 2473 O SER A1117 7688 4766 5347 1496 2378 985 O
ATOM 2474 CB SER A1117 -5.482 -18.065 -42.407 1.00 47.24 C
ANISOU 2474 CB SER A1117 7735 4638 5575 945 2228 74 C
ATOM 2475 OG SER A1117 -5.082 -18.369 -43.731 1.00 56.94 O
ANISOU 2475 OG SER A1117 8986 5763 6884 903 2244 -222 O
ATOM 2476 N LEU A1118 -7.157 -19.052 -39.944 1.00 43.60 N
ANISOU 2476 N LEU A1118 7384 3888 5294 996 2539 706 N
ATOM 2477 CA LEU A1118 -7.873 -18.820 -38.686 1.00 43.26 C
ANISOU 2477 CA LEU A1118 7325 3976 5136 1009 2582 989 C
ATOM 2478 C LEU A1118 -7.384 -19.767 -37.583 1.00 49.06 C
ANISOU 2478 C LEU A1118 8138 4594 5909 1333 2792 1445 C
ATOM 2479 O LEU A1118 -7.226 -19.335 -36.439 1.00 49.44 O
ANISOU 2479 O LEU A1118 8142 4967 5674 1513 2742 1719 O
ATOM 2480 CB LEU A1118 -9.404 -18.919 -38.867 1.00 42.94 C
ANISOU 2480 CB LEU A1118 7292 3727 5297 676 2676 859 C
ATOM 2481 CG LEU A1118 -10.100 -17.855 -39.746 1.00 47.21 C
ANISOU 2481 CG LEU A1118 7737 4449 5752 380 2450 466 C
ATOM 2482 CD1 LEU A1118 -11.515 -18.269 -40.086 1.00 47.30 C
ANISOU 2482 CD1 LEU A1118 7741 4186 6046 73 2568 313 C
ATOM 2483 CD2 LEU A1118 -10.077 -16.472 -39.122 1.00 48.32 C
ANISOU 2483 CD2 LEU A1118 7768 5060 5533 415 2223 491 C
ATOM 2484 N ARG A1119 -7.100 -21.037 -37.938 1.00 46.25 N
ANISOU 2484 N ARG A1119 7898 3786 5889 1428 3019 1522 N
ATOM 2485 CA ARG A1119 -6.594 -22.044 -37.009 1.00 46.90 C
ANISOU 2485 CA ARG A1119 8073 3690 6059 1764 3241 1984 C
ATOM 2486 C ARG A1119 -5.186 -21.703 -36.513 1.00 53.18 C
ANISOU 2486 C ARG A1119 8791 4879 6537 2152 3078 2165 C
ATOM 2487 O ARG A1119 -4.915 -21.834 -35.319 1.00 53.27 O
ANISOU 2487 O ARG A1119 8806 5078 6356 2433 3121 2577 O
ATOM 2488 CB ARG A1119 -6.626 -23.437 -37.642 1.00 48.38 C
ANISOU 2488 CB ARG A1119 8400 3245 6739 1758 3518 1964 C
ATOM 2489 CG ARG A1119 -7.592 -24.396 -36.952 1.00 62.41 C
ANISOU 2489 CG ARG A1119 10289 4597 8827 1693 3846 2290 C
ATOM 2490 CD ARG A1119 -7.615 -25.769 -37.604 1.00 76.25 C
ANISOU 2490 CD ARG A1119 12179 5665 11127 1667 4123 2232 C
ATOM 2491 NE ARG A1119 -8.131 -25.728 -38.975 1.00 90.44 N
ANISOU 2491 NE ARG A1119 13955 7256 13153 1304 4053 1652 N
ATOM 2492 CZ ARG A1119 -8.132 -26.762 -39.810 1.00109.43 C
ANISOU 2492 CZ ARG A1119 16456 9112 16011 1233 4228 1422 C
ATOM 2493 NH1 ARG A1119 -7.643 -27.936 -39.427 1.00 99.21 N
ANISOU 2493 NH1 ARG A1119 15295 7362 15039 1500 4503 1738 N
ATOM 2494 NH2 ARG A1119 -8.616 -26.630 -41.038 1.00 98.48 N
ANISOU 2494 NH2 ARG A1119 15034 7632 14754 911 4127 867 N
ATOM 2495 N MET A1120 -4.304 -21.247 -37.422 1.00 51.32 N
ANISOU 2495 N MET A1120 8468 4798 6233 2167 2891 1859 N
ATOM 2496 CA MET A1120 -2.924 -20.873 -37.103 1.00 51.76 C
ANISOU 2496 CA MET A1120 8400 5239 6027 2496 2720 1964 C
ATOM 2497 C MET A1120 -2.844 -19.616 -36.248 1.00 53.96 C
ANISOU 2497 C MET A1120 8533 6092 5878 2514 2461 2006 C
ATOM 2498 O MET A1120 -1.955 -19.520 -35.402 1.00 53.70 O
ANISOU 2498 O MET A1120 8412 6382 5610 2839 2368 2249 O
ATOM 2499 CB MET A1120 -2.082 -20.731 -38.374 1.00 54.68 C
ANISOU 2499 CB MET A1120 8699 5602 6473 2471 2631 1616 C
ATOM 2500 CG MET A1120 -1.585 -22.050 -38.895 1.00 59.52 C
ANISOU 2500 CG MET A1120 9421 5757 7436 2658 2869 1655 C
ATOM 2501 SD MET A1120 -1.116 -21.955 -40.635 1.00 65.22 S
ANISOU 2501 SD MET A1120 10106 6391 8284 2499 2830 1137 S
ATOM 2502 CE MET A1120 -1.944 -23.400 -41.249 1.00 62.24 C
ANISOU 2502 CE MET A1120 9952 5289 8406 2379 3148 1022 C
ATOM 2503 N LEU A1121 -3.773 -18.662 -36.461 1.00 49.00 N
ANISOU 2503 N LEU A1121 7872 5593 5155 2178 2337 1756 N
ATOM 2504 CA LEU A1121 -3.843 -17.415 -35.692 1.00 48.23 C
ANISOU 2504 CA LEU A1121 7646 5989 4690 2158 2100 1733 C
ATOM 2505 C LEU A1121 -4.196 -17.669 -34.210 1.00 53.61 C
ANISOU 2505 C LEU A1121 8364 6831 5173 2368 2188 2124 C
ATOM 2506 O LEU A1121 -3.639 -16.996 -33.340 1.00 53.34 O
ANISOU 2506 O LEU A1121 8214 7257 4794 2558 1999 2203 O
ATOM 2507 CB LEU A1121 -4.826 -16.405 -36.322 1.00 47.47 C
ANISOU 2507 CB LEU A1121 7519 5928 4588 1770 1978 1385 C
ATOM 2508 CG LEU A1121 -4.409 -15.700 -37.621 1.00 50.02 C
ANISOU 2508 CG LEU A1121 7767 6280 4958 1578 1815 1011 C
ATOM 2509 CD1 LEU A1121 -5.595 -15.015 -38.254 1.00 49.60 C
ANISOU 2509 CD1 LEU A1121 7728 6156 4960 1225 1760 744 C
ATOM 2510 CD2 LEU A1121 -3.282 -14.700 -37.394 1.00 49.69 C
ANISOU 2510 CD2 LEU A1121 7549 6667 4663 1696 1564 944 C
ATOM 2511 N GLN A1122 -5.099 -18.642 -33.924 1.00 50.83 N
ANISOU 2511 N GLN A1122 8165 6111 5037 2335 2481 2366 N
ATOM 2512 CA GLN A1122 -5.472 -18.981 -32.544 1.00 51.23 C
ANISOU 2512 CA GLN A1122 8268 6295 4902 2543 2623 2794 C
ATOM 2513 C GLN A1122 -4.436 -19.917 -31.887 1.00 54.00 C
ANISOU 2513 C GLN A1122 8663 6642 5211 2993 2725 3220 C
ATOM 2514 O GLN A1122 -4.445 -20.084 -30.666 1.00 52.85 O
ANISOU 2514 O GLN A1122 8539 6739 4803 3256 2787 3609 O
ATOM 2515 CB GLN A1122 -6.918 -19.514 -32.434 1.00 52.92 C
ANISOU 2515 CB GLN A1122 8594 6156 5357 2298 2905 2898 C
ATOM 2516 CG GLN A1122 -7.093 -21.013 -32.625 1.00 63.99 C
ANISOU 2516 CG GLN A1122 10157 6965 7192 2340 3254 3161 C
ATOM 2517 CD GLN A1122 -8.541 -21.382 -32.490 1.00 81.94 C
ANISOU 2517 CD GLN A1122 12489 8938 9707 2047 3510 3221 C
ATOM 2518 OE1 GLN A1122 -9.317 -21.288 -33.443 1.00 80.36 O
ANISOU 2518 OE1 GLN A1122 12268 8488 9776 1680 3508 2855 O
ATOM 2519 NE2 GLN A1122 -8.939 -21.796 -31.300 1.00 73.13 N
ANISOU 2519 NE2 GLN A1122 11430 7871 8486 2208 3735 3686 N
ATOM 2520 N GLN A1123 -3.541 -20.500 -32.713 1.00 49.79 N
ANISOU 2520 N GLN A1123 8138 5862 4918 3099 2738 3144 N
ATOM 2521 CA GLN A1123 -2.435 -21.362 -32.297 1.00 48.98 C
ANISOU 2521 CA GLN A1123 8051 5737 4822 3544 2809 3495 C
ATOM 2522 C GLN A1123 -1.162 -20.523 -32.069 1.00 52.57 C
ANISOU 2522 C GLN A1123 8288 6767 4918 3775 2472 3390 C
ATOM 2523 O GLN A1123 -0.118 -21.079 -31.704 1.00 52.45 O
ANISOU 2523 O GLN A1123 8228 6851 4851 4176 2464 3650 O
ATOM 2524 CB GLN A1123 -2.167 -22.437 -33.360 1.00 49.92 C
ANISOU 2524 CB GLN A1123 8275 5268 5423 3536 3014 3417 C
ATOM 2525 CG GLN A1123 -3.040 -23.677 -33.227 1.00 56.81 C
ANISOU 2525 CG GLN A1123 9362 5537 6687 3497 3397 3704 C
ATOM 2526 CD GLN A1123 -2.619 -24.770 -34.181 1.00 72.95 C
ANISOU 2526 CD GLN A1123 11505 7010 9204 3552 3587 3615 C
ATOM 2527 OE1 GLN A1123 -1.996 -24.524 -35.223 1.00 67.56 O
ANISOU 2527 OE1 GLN A1123 10743 6341 8586 3489 3450 3223 O
ATOM 2528 NE2 GLN A1123 -2.955 -26.009 -33.849 1.00 62.68 N
ANISOU 2528 NE2 GLN A1123 10379 5183 8252 3675 3926 3976 N
ATOM 2529 N LYS A1124 -1.258 -19.189 -32.309 1.00 48.06 N
ANISOU 2529 N LYS A1124 7571 6556 4133 3517 2197 3002 N
ATOM 2530 CA LYS A1124 -0.200 -18.177 -32.170 1.00 47.54 C
ANISOU 2530 CA LYS A1124 7269 7026 3768 3619 1859 2806 C
ATOM 2531 C LYS A1124 0.966 -18.409 -33.152 1.00 51.21 C
ANISOU 2531 C LYS A1124 7626 7404 4429 3704 1809 2640 C
ATOM 2532 O LYS A1124 2.084 -17.947 -32.921 1.00 51.15 O
ANISOU 2532 O LYS A1124 7402 7802 4228 3897 1585 2593 O
ATOM 2533 CB LYS A1124 0.271 -18.024 -30.702 1.00 50.12 C
ANISOU 2533 CB LYS A1124 7504 7870 3668 3991 1727 3116 C
ATOM 2534 CG LYS A1124 -0.876 -17.705 -29.746 1.00 62.47 C
ANISOU 2534 CG LYS A1124 9161 9582 4994 3907 1784 3245 C
ATOM 2535 CD LYS A1124 -0.595 -16.512 -28.851 1.00 72.52 C
ANISOU 2535 CD LYS A1124 10250 11506 5799 3972 1465 3094 C
ATOM 2536 CE LYS A1124 -1.814 -15.638 -28.647 1.00 81.46 C
ANISOU 2536 CE LYS A1124 11419 12709 6824 3653 1446 2874 C
ATOM 2537 NZ LYS A1124 -2.858 -16.309 -27.825 1.00 89.46 N
ANISOU 2537 NZ LYS A1124 12610 13619 7763 3724 1729 3248 N
ATOM 2538 N ARG A1125 0.670 -19.081 -34.278 1.00 47.57 N
ANISOU 2538 N ARG A1125 7296 6429 4350 3538 2015 2512 N
ATOM 2539 CA ARG A1125 1.601 -19.385 -35.366 1.00 47.22 C
ANISOU 2539 CA ARG A1125 7180 6240 4521 3585 2029 2318 C
ATOM 2540 C ARG A1125 1.312 -18.352 -36.460 1.00 50.55 C
ANISOU 2540 C ARG A1125 7536 6711 4961 3171 1893 1857 C
ATOM 2541 O ARG A1125 0.659 -18.658 -37.461 1.00 50.04 O
ANISOU 2541 O ARG A1125 7602 6268 5143 2919 2034 1651 O
ATOM 2542 CB ARG A1125 1.366 -20.821 -35.880 1.00 46.94 C
ANISOU 2542 CB ARG A1125 7352 5597 4887 3669 2357 2446 C
ATOM 2543 CG ARG A1125 1.587 -21.923 -34.838 1.00 50.55 C
ANISOU 2543 CG ARG A1125 7906 5919 5381 4087 2536 2960 C
ATOM 2544 CD ARG A1125 1.123 -23.279 -35.337 1.00 52.45 C
ANISOU 2544 CD ARG A1125 8377 5469 6082 4088 2884 3057 C
ATOM 2545 NE ARG A1125 1.829 -23.703 -36.550 1.00 56.37 N
ANISOU 2545 NE ARG A1125 8848 5716 6853 4120 2944 2776 N
ATOM 2546 CZ ARG A1125 1.488 -24.754 -37.290 1.00 67.90 C
ANISOU 2546 CZ ARG A1125 10487 6568 8744 4066 3215 2695 C
ATOM 2547 NH1 ARG A1125 0.447 -25.505 -36.949 1.00 52.95 N
ANISOU 2547 NH1 ARG A1125 8800 4221 7099 3954 3456 2885 N
ATOM 2548 NH2 ARG A1125 2.182 -25.061 -38.377 1.00 54.08 N
ANISOU 2548 NH2 ARG A1125 8699 4660 7190 4120 3256 2406 N
ATOM 2549 N TRP A1126 1.761 -17.111 -36.229 1.00 47.05 N
ANISOU 2549 N TRP A1126 6886 6738 4252 3103 1615 1698 N
ATOM 2550 CA TRP A1126 1.490 -15.967 -37.090 1.00 47.26 C
ANISOU 2550 CA TRP A1126 6840 6857 4261 2732 1469 1322 C
ATOM 2551 C TRP A1126 2.253 -15.956 -38.399 1.00 51.44 C
ANISOU 2551 C TRP A1126 7289 7307 4950 2663 1491 1086 C
ATOM 2552 O TRP A1126 1.674 -15.539 -39.403 1.00 51.08 O
ANISOU 2552 O TRP A1126 7303 7119 4986 2351 1503 827 O
ATOM 2553 CB TRP A1126 1.698 -14.659 -36.336 1.00 46.51 C
ANISOU 2553 CB TRP A1126 6558 7243 3871 2682 1184 1240 C
ATOM 2554 CG TRP A1126 0.861 -14.556 -35.093 1.00 48.09 C
ANISOU 2554 CG TRP A1126 6839 7565 3868 2731 1164 1423 C
ATOM 2555 CD1 TRP A1126 -0.501 -14.461 -35.016 1.00 51.02 C
ANISOU 2555 CD1 TRP A1126 7375 7741 4271 2505 1259 1403 C
ATOM 2556 CD2 TRP A1126 1.339 -14.577 -33.746 1.00 48.20 C
ANISOU 2556 CD2 TRP A1126 6761 7953 3600 3049 1056 1661 C
ATOM 2557 NE1 TRP A1126 -0.898 -14.404 -33.701 1.00 50.45 N
ANISOU 2557 NE1 TRP A1126 7320 7896 3951 2657 1237 1617 N
ATOM 2558 CE2 TRP A1126 0.212 -14.463 -32.899 1.00 52.12 C
ANISOU 2558 CE2 TRP A1126 7385 8471 3946 2995 1106 1777 C
ATOM 2559 CE3 TRP A1126 2.616 -14.662 -33.170 1.00 49.65 C
ANISOU 2559 CE3 TRP A1126 6745 8495 3624 3383 911 1778 C
ATOM 2560 CZ2 TRP A1126 0.326 -14.402 -31.513 1.00 51.90 C
ANISOU 2560 CZ2 TRP A1126 7312 8828 3581 3266 1020 2000 C
ATOM 2561 CZ3 TRP A1126 2.728 -14.630 -31.794 1.00 51.84 C
ANISOU 2561 CZ3 TRP A1126 6973 9153 3573 3658 802 1999 C
ATOM 2562 CH2 TRP A1126 1.594 -14.510 -30.977 1.00 52.79 C
ANISOU 2562 CH2 TRP A1126 7244 9298 3515 3604 863 2113 C
ATOM 2563 N ASP A1127 3.530 -16.400 -38.407 1.00 47.99 N
ANISOU 2563 N ASP A1127 6707 6986 4541 2964 1501 1176 N
ATOM 2564 CA ASP A1127 4.344 -16.476 -39.628 1.00 47.81 C
ANISOU 2564 CA ASP A1127 6589 6914 4661 2940 1560 968 C
ATOM 2565 C ASP A1127 3.677 -17.410 -40.640 1.00 50.28 C
ANISOU 2565 C ASP A1127 7141 6732 5233 2837 1814 858 C
ATOM 2566 O ASP A1127 3.604 -17.077 -41.824 1.00 49.91 O
ANISOU 2566 O ASP A1127 7100 6627 5239 2607 1838 577 O
ATOM 2567 CB ASP A1127 5.778 -16.961 -39.327 1.00 50.29 C
ANISOU 2567 CB ASP A1127 6694 7434 4981 3334 1550 1117 C
ATOM 2568 CG ASP A1127 6.734 -15.928 -38.738 1.00 66.19 C
ANISOU 2568 CG ASP A1127 8385 9986 6779 3386 1276 1091 C
ATOM 2569 OD1 ASP A1127 6.527 -14.707 -38.985 1.00 66.37 O
ANISOU 2569 OD1 ASP A1127 8316 10194 6706 3065 1115 870 O
ATOM 2570 OD2 ASP A1127 7.706 -16.341 -38.045 1.00 73.47 O
ANISOU 2570 OD2 ASP A1127 9132 11139 7646 3753 1219 1285 O
ATOM 2571 N GLU A1128 3.153 -18.552 -40.153 1.00 45.84 N
ANISOU 2571 N GLU A1128 6774 5819 4826 2997 2002 1078 N
ATOM 2572 CA GLU A1128 2.460 -19.567 -40.946 1.00 45.50 C
ANISOU 2572 CA GLU A1128 6957 5255 5075 2907 2250 972 C
ATOM 2573 C GLU A1128 1.103 -19.053 -41.452 1.00 47.09 C
ANISOU 2573 C GLU A1128 7286 5326 5282 2482 2225 742 C
ATOM 2574 O GLU A1128 0.783 -19.257 -42.621 1.00 47.24 O
ANISOU 2574 O GLU A1128 7382 5131 5434 2294 2307 451 O
ATOM 2575 CB GLU A1128 2.286 -20.869 -40.137 1.00 47.20 C
ANISOU 2575 CB GLU A1128 7328 5120 5485 3193 2461 1318 C
ATOM 2576 CG GLU A1128 3.572 -21.631 -39.857 1.00 60.99 C
ANISOU 2576 CG GLU A1128 8980 6892 7303 3651 2531 1534 C
ATOM 2577 CD GLU A1128 3.997 -22.567 -40.970 1.00 92.50 C
ANISOU 2577 CD GLU A1128 13035 10509 11600 3742 2744 1333 C
ATOM 2578 OE1 GLU A1128 3.756 -23.790 -40.842 1.00 84.86 O
ANISOU 2578 OE1 GLU A1128 12248 9062 10933 3917 2985 1490 O
ATOM 2579 OE2 GLU A1128 4.563 -22.077 -41.975 1.00 94.61 O
ANISOU 2579 OE2 GLU A1128 13176 10956 11815 3640 2684 1017 O
ATOM 2580 N ALA A1129 0.321 -18.378 -40.585 1.00 41.21 N
ANISOU 2580 N ALA A1129 6547 4739 4373 2350 2105 856 N
ATOM 2581 CA ALA A1129 -0.989 -17.803 -40.921 1.00 40.21 C
ANISOU 2581 CA ALA A1129 6504 4538 4238 1976 2060 664 C
ATOM 2582 C ALA A1129 -0.891 -16.742 -42.049 1.00 42.72 C
ANISOU 2582 C ALA A1129 6728 5058 4446 1724 1901 329 C
ATOM 2583 O ALA A1129 -1.778 -16.658 -42.904 1.00 42.19 O
ANISOU 2583 O ALA A1129 6750 4828 4452 1455 1920 97 O
ATOM 2584 CB ALA A1129 -1.610 -17.189 -39.681 1.00 40.64 C
ANISOU 2584 CB ALA A1129 6536 4804 4100 1952 1954 860 C
ATOM 2585 N ALA A1130 0.208 -15.960 -42.037 1.00 37.32 N
ANISOU 2585 N ALA A1130 5852 4734 3594 1821 1749 321 N
ATOM 2586 CA ALA A1130 0.567 -14.913 -42.986 1.00 35.92 C
ANISOU 2586 CA ALA A1130 5557 4780 3312 1630 1619 83 C
ATOM 2587 C ALA A1130 0.779 -15.450 -44.405 1.00 38.96 C
ANISOU 2587 C ALA A1130 6004 4983 3817 1584 1764 -139 C
ATOM 2588 O ALA A1130 0.496 -14.742 -45.379 1.00 38.44 O
ANISOU 2588 O ALA A1130 5932 4999 3677 1353 1703 -350 O
ATOM 2589 CB ALA A1130 1.832 -14.226 -42.514 1.00 36.44 C
ANISOU 2589 CB ALA A1130 5382 5226 3237 1783 1472 164 C
ATOM 2590 N VAL A1131 1.307 -16.686 -44.515 1.00 34.67 N
ANISOU 2590 N VAL A1131 5518 4208 3447 1827 1958 -89 N
ATOM 2591 CA VAL A1131 1.594 -17.364 -45.783 1.00 34.04 C
ANISOU 2591 CA VAL A1131 5501 3945 3489 1840 2122 -323 C
ATOM 2592 C VAL A1131 0.287 -17.663 -46.527 1.00 38.57 C
ANISOU 2592 C VAL A1131 6269 4232 4155 1571 2179 -561 C
ATOM 2593 O VAL A1131 0.173 -17.351 -47.716 1.00 38.96 O
ANISOU 2593 O VAL A1131 6331 4344 4130 1412 2172 -832 O
ATOM 2594 CB VAL A1131 2.441 -18.653 -45.566 1.00 37.40 C
ANISOU 2594 CB VAL A1131 5941 4155 4115 2202 2320 -205 C
ATOM 2595 CG1 VAL A1131 2.736 -19.359 -46.889 1.00 37.06 C
ANISOU 2595 CG1 VAL A1131 5960 3929 4192 2229 2498 -499 C
ATOM 2596 CG2 VAL A1131 3.738 -18.345 -44.830 1.00 37.16 C
ANISOU 2596 CG2 VAL A1131 5681 4458 3982 2485 2236 24 C
ATOM 2597 N ASN A1132 -0.689 -18.260 -45.818 1.00 34.30 N
ANISOU 2597 N ASN A1132 5862 3403 3768 1525 2238 -453 N
ATOM 2598 CA ASN A1132 -1.989 -18.668 -46.355 1.00 33.64 C
ANISOU 2598 CA ASN A1132 5932 3022 3828 1269 2296 -670 C
ATOM 2599 C ASN A1132 -2.893 -17.508 -46.709 1.00 35.72 C
ANISOU 2599 C ASN A1132 6163 3507 3903 959 2099 -813 C
ATOM 2600 O ASN A1132 -3.633 -17.611 -47.686 1.00 35.41 O
ANISOU 2600 O ASN A1132 6193 3366 3895 754 2099 -1101 O
ATOM 2601 CB ASN A1132 -2.690 -19.644 -45.406 1.00 34.34 C
ANISOU 2601 CB ASN A1132 6141 2733 4175 1315 2448 -468 C
ATOM 2602 CG ASN A1132 -2.090 -21.026 -45.402 1.00 54.09 C
ANISOU 2602 CG ASN A1132 8733 4858 6962 1575 2690 -410 C
ATOM 2603 OD1 ASN A1132 -2.789 -22.032 -45.293 1.00 51.54 O
ANISOU 2603 OD1 ASN A1132 8548 4091 6945 1527 2869 -420 O
ATOM 2604 ND2 ASN A1132 -0.784 -21.114 -45.536 1.00 43.45 N
ANISOU 2604 ND2 ASN A1132 7297 3659 5553 1857 2711 -353 N
ATOM 2605 N LEU A1133 -2.832 -16.409 -45.925 1.00 30.98 N
ANISOU 2605 N LEU A1133 5453 3212 3108 937 1925 -629 N
ATOM 2606 CA LEU A1133 -3.620 -15.195 -46.157 1.00 29.93 C
ANISOU 2606 CA LEU A1133 5278 3289 2807 681 1732 -730 C
ATOM 2607 C LEU A1133 -3.168 -14.463 -47.435 1.00 34.33 C
ANISOU 2607 C LEU A1133 5781 4061 3203 587 1651 -937 C
ATOM 2608 O LEU A1133 -4.020 -13.955 -48.162 1.00 34.12 O
ANISOU 2608 O LEU A1133 5787 4070 3107 371 1561 -1113 O
ATOM 2609 CB LEU A1133 -3.539 -14.242 -44.959 1.00 29.33 C
ANISOU 2609 CB LEU A1133 5095 3464 2586 715 1580 -506 C
ATOM 2610 CG LEU A1133 -4.256 -14.598 -43.657 1.00 32.68 C
ANISOU 2610 CG LEU A1133 5564 3781 3072 762 1625 -292 C
ATOM 2611 CD1 LEU A1133 -3.753 -13.715 -42.537 1.00 32.27 C
ANISOU 2611 CD1 LEU A1133 5386 4048 2826 876 1476 -105 C
ATOM 2612 CD2 LEU A1133 -5.776 -14.474 -43.779 1.00 31.26 C
ANISOU 2612 CD2 LEU A1133 5450 3468 2960 507 1611 -405 C
ATOM 2613 N ALA A1134 -1.834 -14.421 -47.707 1.00 30.55 N
ANISOU 2613 N ALA A1134 5206 3741 2661 760 1691 -900 N
ATOM 2614 CA ALA A1134 -1.248 -13.769 -48.888 1.00 29.93 C
ANISOU 2614 CA ALA A1134 5061 3887 2423 698 1662 -1045 C
ATOM 2615 C ALA A1134 -1.600 -14.482 -50.192 1.00 34.63 C
ANISOU 2615 C ALA A1134 5778 4345 3034 641 1777 -1331 C
ATOM 2616 O ALA A1134 -1.693 -13.841 -51.235 1.00 34.55 O
ANISOU 2616 O ALA A1134 5761 4521 2845 517 1722 -1472 O
ATOM 2617 CB ALA A1134 0.259 -13.663 -48.738 1.00 30.39 C
ANISOU 2617 CB ALA A1134 4955 4144 2448 904 1706 -923 C
ATOM 2618 N LYS A1135 -1.804 -15.806 -50.134 1.00 31.12 N
ANISOU 2618 N LYS A1135 5448 3574 2803 739 1937 -1420 N
ATOM 2619 CA LYS A1135 -2.146 -16.610 -51.302 1.00 30.12 C
ANISOU 2619 CA LYS A1135 5437 3283 2723 692 2047 -1751 C
ATOM 2620 C LYS A1135 -3.675 -16.671 -51.476 1.00 32.62 C
ANISOU 2620 C LYS A1135 5852 3443 3100 436 1961 -1923 C
ATOM 2621 O LYS A1135 -4.283 -17.739 -51.392 1.00 31.87 O
ANISOU 2621 O LYS A1135 5857 2996 3256 410 2071 -2053 O
ATOM 2622 CB LYS A1135 -1.466 -17.994 -51.226 1.00 32.44 C
ANISOU 2622 CB LYS A1135 5787 3279 3258 939 2276 -1792 C
ATOM 2623 CG LYS A1135 0.054 -17.890 -51.075 1.00 41.24 C
ANISOU 2623 CG LYS A1135 6762 4598 4310 1208 2347 -1627 C
ATOM 2624 CD LYS A1135 0.751 -19.226 -51.143 1.00 48.35 C
ANISOU 2624 CD LYS A1135 7711 5214 5446 1485 2575 -1685 C
ATOM 2625 CE LYS A1135 2.251 -19.065 -51.229 1.00 57.91 C
ANISOU 2625 CE LYS A1135 8748 6686 6570 1743 2643 -1583 C
ATOM 2626 NZ LYS A1135 2.928 -20.344 -51.577 1.00 68.66 N
ANISOU 2626 NZ LYS A1135 10156 7788 8143 2022 2881 -1722 N
ATOM 2627 N SER A1136 -4.291 -15.488 -51.712 1.00 28.95 N
ANISOU 2627 N SER A1136 5328 3236 2434 240 1754 -1897 N
ATOM 2628 CA SER A1136 -5.741 -15.315 -51.875 1.00 28.51 C
ANISOU 2628 CA SER A1136 5291 3124 2417 -8 1615 -2004 C
ATOM 2629 C SER A1136 -6.099 -14.249 -52.928 1.00 31.36 C
ANISOU 2629 C SER A1136 5653 3811 2451 -129 1465 -2181 C
ATOM 2630 O SER A1136 -5.273 -13.393 -53.243 1.00 29.83 O
ANISOU 2630 O SER A1136 5391 3887 2056 -69 1425 -2050 O
ATOM 2631 CB SER A1136 -6.361 -14.913 -50.538 1.00 30.54 C
ANISOU 2631 CB SER A1136 5538 3327 2740 -44 1565 -1797 C
ATOM 2632 OG SER A1136 -5.888 -13.642 -50.124 1.00 35.35 O
ANISOU 2632 OG SER A1136 6046 4230 3156 -22 1428 -1583 O
ATOM 2633 N ARG A1137 -7.364 -14.261 -53.401 1.00 29.03 N
ANISOU 2633 N ARG A1137 5281 3486 2262 -351 1305 -2237 N
ATOM 2634 CA ARG A1137 -7.928 -13.281 -54.340 1.00 29.24 C
ANISOU 2634 CA ARG A1137 5237 3800 2072 -470 1111 -2279 C
ATOM 2635 C ARG A1137 -7.939 -11.887 -53.684 1.00 32.02 C
ANISOU 2635 C ARG A1137 5653 4355 2156 -457 1023 -2178 C
ATOM 2636 O ARG A1137 -7.821 -10.874 -54.382 1.00 33.26 O
ANISOU 2636 O ARG A1137 5784 4784 2070 -473 915 -2122 O
ATOM 2637 CB ARG A1137 -9.356 -13.693 -54.740 1.00 31.89 C
ANISOU 2637 CB ARG A1137 5647 4067 2403 -632 1043 -2654 C
ATOM 2638 CG ARG A1137 -9.818 -13.141 -56.084 1.00 50.71 C
ANISOU 2638 CG ARG A1137 8113 6769 4386 -684 899 -2991 C
ATOM 2639 CD ARG A1137 -11.319 -13.296 -56.277 1.00 69.50 C
ANISOU 2639 CD ARG A1137 10445 9120 6841 -872 740 -3229 C
ATOM 2640 NE ARG A1137 -11.707 -14.672 -56.605 1.00 80.14 N
ANISOU 2640 NE ARG A1137 11832 10211 8408 -948 835 -3610 N
ATOM 2641 CZ ARG A1137 -12.880 -15.218 -56.294 1.00 95.58 C
ANISOU 2641 CZ ARG A1137 13725 11962 10628 -1130 792 -3793 C
ATOM 2642 NH1 ARG A1137 -13.794 -14.517 -55.633 1.00 77.83 N
ANISOU 2642 NH1 ARG A1137 11370 9764 8437 -1235 659 -3625 N
ATOM 2643 NH2 ARG A1137 -13.143 -16.473 -56.631 1.00 88.71 N
ANISOU 2643 NH2 ARG A1137 12887 10823 9994 -1211 895 -4157 N
ATOM 2644 N TRP A1138 -8.052 -11.853 -52.333 1.00 25.72 N
ANISOU 2644 N TRP A1138 4702 3374 1696 -471 991 -1813 N
ATOM 2645 CA TRP A1138 -8.022 -10.661 -51.483 1.00 23.68 C
ANISOU 2645 CA TRP A1138 4335 3216 1445 -478 864 -1527 C
ATOM 2646 C TRP A1138 -6.696 -9.912 -51.650 1.00 26.42 C
ANISOU 2646 C TRP A1138 4772 3815 1450 -345 931 -1551 C
ATOM 2647 O TRP A1138 -6.716 -8.708 -51.924 1.00 25.87 O
ANISOU 2647 O TRP A1138 4632 3917 1282 -406 795 -1434 O
ATOM 2648 CB TRP A1138 -8.256 -11.060 -50.017 1.00 21.77 C
ANISOU 2648 CB TRP A1138 4070 2786 1415 -447 912 -1358 C
ATOM 2649 CG TRP A1138 -7.952 -9.995 -48.999 1.00 22.54 C
ANISOU 2649 CG TRP A1138 4185 3042 1339 -379 862 -1265 C
ATOM 2650 CD1 TRP A1138 -8.420 -8.713 -48.981 1.00 25.28 C
ANISOU 2650 CD1 TRP A1138 4522 3566 1518 -454 713 -1281 C
ATOM 2651 CD2 TRP A1138 -7.141 -10.144 -47.820 1.00 22.17 C
ANISOU 2651 CD2 TRP A1138 4137 2997 1291 -222 944 -1114 C
ATOM 2652 NE1 TRP A1138 -7.923 -8.042 -47.888 1.00 24.60 N
ANISOU 2652 NE1 TRP A1138 4364 3548 1435 -384 670 -1105 N
ATOM 2653 CE2 TRP A1138 -7.157 -8.903 -47.142 1.00 26.28 C
ANISOU 2653 CE2 TRP A1138 4581 3686 1719 -240 803 -1010 C
ATOM 2654 CE3 TRP A1138 -6.385 -11.203 -47.281 1.00 23.28 C
ANISOU 2654 CE3 TRP A1138 4312 3016 1517 -50 1113 -1038 C
ATOM 2655 CZ2 TRP A1138 -6.474 -8.697 -45.936 1.00 25.82 C
ANISOU 2655 CZ2 TRP A1138 4453 3700 1658 -112 796 -844 C
ATOM 2656 CZ3 TRP A1138 -5.712 -11.000 -46.085 1.00 24.99 C
ANISOU 2656 CZ3 TRP A1138 4458 3316 1719 96 1105 -828 C
ATOM 2657 CH2 TRP A1138 -5.753 -9.758 -45.429 1.00 25.81 C
ANISOU 2657 CH2 TRP A1138 4468 3618 1720 59 940 -750 C
ATOM 2658 N TYR A1139 -5.552 -10.621 -51.496 1.00 22.60 N
ANISOU 2658 N TYR A1139 4119 3185 1284 -241 984 -1305 N
ATOM 2659 CA TYR A1139 -4.223 -10.029 -51.664 1.00 22.76 C
ANISOU 2659 CA TYR A1139 4062 3381 1204 -144 1010 -1198 C
ATOM 2660 C TYR A1139 -4.025 -9.543 -53.096 1.00 28.22 C
ANISOU 2660 C TYR A1139 4919 4395 1409 -145 1127 -1464 C
ATOM 2661 O TYR A1139 -3.490 -8.455 -53.283 1.00 27.72 O
ANISOU 2661 O TYR A1139 4773 4519 1242 -174 1078 -1309 O
ATOM 2662 CB TYR A1139 -3.113 -11.015 -51.271 1.00 23.84 C
ANISOU 2662 CB TYR A1139 4243 3476 1340 67 1218 -1231 C
ATOM 2663 CG TYR A1139 -1.726 -10.406 -51.177 1.00 25.13 C
ANISOU 2663 CG TYR A1139 4319 3896 1334 193 1308 -1157 C
ATOM 2664 CD1 TYR A1139 -0.910 -10.299 -52.300 1.00 26.48 C
ANISOU 2664 CD1 TYR A1139 4460 4248 1353 229 1418 -1226 C
ATOM 2665 CD2 TYR A1139 -1.217 -9.969 -49.956 1.00 26.32 C
ANISOU 2665 CD2 TYR A1139 4367 4111 1522 265 1264 -989 C
ATOM 2666 CE1 TYR A1139 0.353 -9.714 -52.224 1.00 27.12 C
ANISOU 2666 CE1 TYR A1139 4377 4538 1391 298 1470 -1091 C
ATOM 2667 CE2 TYR A1139 0.055 -9.404 -49.863 1.00 27.39 C
ANISOU 2667 CE2 TYR A1139 4325 4449 1633 333 1274 -875 C
ATOM 2668 CZ TYR A1139 0.847 -9.302 -50.995 1.00 36.33 C
ANISOU 2668 CZ TYR A1139 5403 5730 2670 343 1387 -921 C
ATOM 2669 OH TYR A1139 2.111 -8.772 -50.899 1.00 39.66 O
ANISOU 2669 OH TYR A1139 5615 6350 3101 393 1417 -809 O
ATOM 2670 N ASN A1140 -4.458 -10.336 -54.098 1.00 26.32 N
ANISOU 2670 N ASN A1140 4630 4027 1345 -197 1083 -1536 N
ATOM 2671 CA ASN A1140 -4.338 -9.979 -55.513 1.00 26.97 C
ANISOU 2671 CA ASN A1140 4680 4305 1263 -228 1053 -1578 C
ATOM 2672 C ASN A1140 -5.057 -8.669 -55.885 1.00 29.83 C
ANISOU 2672 C ASN A1140 5179 4951 1205 -314 970 -1637 C
ATOM 2673 O ASN A1140 -4.535 -7.908 -56.699 1.00 29.12 O
ANISOU 2673 O ASN A1140 4995 5032 1037 -317 949 -1470 O
ATOM 2674 CB ASN A1140 -4.803 -11.121 -56.409 1.00 30.16 C
ANISOU 2674 CB ASN A1140 5233 4696 1531 -208 1152 -1953 C
ATOM 2675 CG ASN A1140 -4.451 -10.911 -57.857 1.00 45.97 C
ANISOU 2675 CG ASN A1140 7435 7099 2933 -126 1299 -2277 C
ATOM 2676 OD1 ASN A1140 -3.282 -10.765 -58.225 1.00 40.77 O
ANISOU 2676 OD1 ASN A1140 6724 6600 2167 -15 1445 -2173 O
ATOM 2677 ND2 ASN A1140 -5.461 -10.872 -58.706 1.00 38.94 N
ANISOU 2677 ND2 ASN A1140 6612 6324 1860 -211 1175 -2492 N
ATOM 2678 N GLN A1141 -6.232 -8.413 -55.292 1.00 26.36 N
ANISOU 2678 N GLN A1141 4609 4306 1101 -437 762 -1500 N
ATOM 2679 CA GLN A1141 -7.026 -7.210 -55.543 1.00 27.01 C
ANISOU 2679 CA GLN A1141 4709 4538 1016 -518 608 -1442 C
ATOM 2680 C GLN A1141 -6.506 -5.963 -54.793 1.00 29.55 C
ANISOU 2680 C GLN A1141 5107 4992 1131 -515 605 -1302 C
ATOM 2681 O GLN A1141 -6.366 -4.892 -55.405 1.00 28.92 O
ANISOU 2681 O GLN A1141 5010 5066 914 -542 551 -1147 O
ATOM 2682 CB GLN A1141 -8.499 -7.470 -55.191 1.00 29.38 C
ANISOU 2682 CB GLN A1141 5152 4810 1200 -600 507 -1707 C
ATOM 2683 CG GLN A1141 -9.462 -6.425 -55.757 1.00 58.95 C
ANISOU 2683 CG GLN A1141 8918 8742 4737 -661 311 -1696 C
ATOM 2684 CD GLN A1141 -10.891 -6.780 -55.450 1.00 83.96 C
ANISOU 2684 CD GLN A1141 12062 11815 8026 -751 183 -1871 C
ATOM 2685 OE1 GLN A1141 -11.488 -7.662 -56.083 1.00 83.21 O
ANISOU 2685 OE1 GLN A1141 11991 11734 7891 -794 166 -2148 O
ATOM 2686 NE2 GLN A1141 -11.467 -6.099 -54.471 1.00 72.32 N
ANISOU 2686 NE2 GLN A1141 10521 10246 6710 -786 96 -1736 N
ATOM 2687 N THR A1142 -6.259 -6.093 -53.462 1.00 24.28 N
ANISOU 2687 N THR A1142 4232 4045 950 -510 573 -1104 N
ATOM 2688 CA THR A1142 -5.773 -4.993 -52.616 1.00 22.60 C
ANISOU 2688 CA THR A1142 3902 3814 869 -525 507 -898 C
ATOM 2689 C THR A1142 -4.400 -5.356 -51.985 1.00 24.00 C
ANISOU 2689 C THR A1142 4113 4090 917 -421 668 -916 C
ATOM 2690 O THR A1142 -4.346 -5.540 -50.768 1.00 23.72 O
ANISOU 2690 O THR A1142 4062 3989 960 -376 658 -907 O
ATOM 2691 CB THR A1142 -6.866 -4.580 -51.593 1.00 28.40 C
ANISOU 2691 CB THR A1142 4791 4573 1428 -566 412 -1018 C
ATOM 2692 OG1 THR A1142 -7.149 -5.669 -50.712 1.00 30.45 O
ANISOU 2692 OG1 THR A1142 5070 4688 1811 -522 474 -1105 O
ATOM 2693 CG2 THR A1142 -8.154 -4.102 -52.256 1.00 22.58 C
ANISOU 2693 CG2 THR A1142 3979 3780 820 -644 265 -977 C
ATOM 2694 N PRO A1143 -3.285 -5.458 -52.775 1.00 19.48 N
ANISOU 2694 N PRO A1143 3247 3398 755 -403 642 -714 N
ATOM 2695 CA PRO A1143 -1.991 -5.873 -52.183 1.00 19.15 C
ANISOU 2695 CA PRO A1143 3114 3380 781 -296 722 -675 C
ATOM 2696 C PRO A1143 -1.460 -5.005 -51.040 1.00 24.94 C
ANISOU 2696 C PRO A1143 3964 4412 1101 -275 844 -719 C
ATOM 2697 O PRO A1143 -0.982 -5.550 -50.045 1.00 26.21 O
ANISOU 2697 O PRO A1143 4057 4539 1361 -165 857 -712 O
ATOM 2698 CB PRO A1143 -1.022 -5.894 -53.381 1.00 20.68 C
ANISOU 2698 CB PRO A1143 3307 3771 781 -257 875 -693 C
ATOM 2699 CG PRO A1143 -1.858 -5.886 -54.576 1.00 24.19 C
ANISOU 2699 CG PRO A1143 3980 4389 820 -293 971 -843 C
ATOM 2700 CD PRO A1143 -3.166 -5.266 -54.240 1.00 19.99 C
ANISOU 2700 CD PRO A1143 3325 3585 685 -424 679 -719 C
ATOM 2701 N ASN A1144 -1.566 -3.673 -51.160 1.00 21.11 N
ANISOU 2701 N ASN A1144 3343 3877 802 -416 682 -578 N
ATOM 2702 CA ASN A1144 -1.109 -2.725 -50.139 1.00 20.22 C
ANISOU 2702 CA ASN A1144 3113 3801 769 -463 600 -521 C
ATOM 2703 C ASN A1144 -1.861 -2.875 -48.839 1.00 23.95 C
ANISOU 2703 C ASN A1144 3664 4229 1208 -421 505 -607 C
ATOM 2704 O ASN A1144 -1.232 -2.882 -47.776 1.00 24.15 O
ANISOU 2704 O ASN A1144 3567 4299 1311 -356 464 -603 O
ATOM 2705 CB ASN A1144 -1.210 -1.284 -50.639 1.00 18.28 C
ANISOU 2705 CB ASN A1144 2799 3512 636 -620 512 -407 C
ATOM 2706 CG ASN A1144 -0.356 -0.996 -51.833 1.00 35.05 C
ANISOU 2706 CG ASN A1144 4957 5853 2507 -658 719 -313 C
ATOM 2707 OD1 ASN A1144 0.484 -1.799 -52.227 1.00 23.62 O
ANISOU 2707 OD1 ASN A1144 3462 4521 992 -568 876 -331 O
ATOM 2708 ND2 ASN A1144 -0.556 0.165 -52.434 1.00 35.77 N
ANISOU 2708 ND2 ASN A1144 5054 5920 2618 -784 692 -173 N
ATOM 2709 N ARG A1145 -3.206 -2.974 -48.919 1.00 19.23 N
ANISOU 2709 N ARG A1145 3101 3427 778 -465 400 -605 N
ATOM 2710 CA ARG A1145 -4.071 -3.146 -47.757 1.00 18.15 C
ANISOU 2710 CA ARG A1145 2940 3166 788 -436 307 -614 C
ATOM 2711 C ARG A1145 -3.881 -4.536 -47.154 1.00 23.67 C
ANISOU 2711 C ARG A1145 3832 3974 1187 -281 457 -741 C
ATOM 2712 O ARG A1145 -3.741 -4.629 -45.933 1.00 23.94 O
ANISOU 2712 O ARG A1145 3810 4030 1257 -198 418 -712 O
ATOM 2713 CB ARG A1145 -5.547 -2.894 -48.112 1.00 15.42 C
ANISOU 2713 CB ARG A1145 2521 2593 743 -519 222 -529 C
ATOM 2714 CG ARG A1145 -6.495 -3.107 -46.939 1.00 21.74 C
ANISOU 2714 CG ARG A1145 3684 3608 967 -477 211 -827 C
ATOM 2715 CD ARG A1145 -7.922 -2.891 -47.330 1.00 25.34 C
ANISOU 2715 CD ARG A1145 4207 4004 1418 -553 137 -892 C
ATOM 2716 NE ARG A1145 -8.822 -2.977 -46.180 1.00 30.71 N
ANISOU 2716 NE ARG A1145 4874 4639 2155 -530 101 -931 N
ATOM 2717 CZ ARG A1145 -10.121 -2.706 -46.242 1.00 45.12 C
ANISOU 2717 CZ ARG A1145 6713 6428 4005 -584 30 -993 C
ATOM 2718 NH1 ARG A1145 -10.676 -2.344 -47.394 1.00 38.16 N
ANISOU 2718 NH1 ARG A1145 5860 5554 3085 -652 -36 -1023 N
ATOM 2719 NH2 ARG A1145 -10.877 -2.806 -45.158 1.00 26.97 N
ANISOU 2719 NH2 ARG A1145 4384 4110 1753 -555 29 -1020 N
ATOM 2720 N ALA A1146 -3.864 -5.610 -47.996 1.00 21.56 N
ANISOU 2720 N ALA A1146 3620 3621 949 -243 577 -766 N
ATOM 2721 CA ALA A1146 -3.691 -6.987 -47.510 1.00 22.10 C
ANISOU 2721 CA ALA A1146 3767 3622 1007 -95 722 -797 C
ATOM 2722 C ALA A1146 -2.364 -7.195 -46.775 1.00 27.82 C
ANISOU 2722 C ALA A1146 4366 4452 1754 67 764 -698 C
ATOM 2723 O ALA A1146 -2.377 -7.750 -45.678 1.00 27.83 O
ANISOU 2723 O ALA A1146 4363 4419 1792 193 773 -629 O
ATOM 2724 CB ALA A1146 -3.850 -7.991 -48.635 1.00 22.64 C
ANISOU 2724 CB ALA A1146 3935 3589 1078 -89 848 -906 C
ATOM 2725 N LYS A1147 -1.244 -6.682 -47.330 1.00 24.55 N
ANISOU 2725 N LYS A1147 3827 4186 1316 65 781 -672 N
ATOM 2726 CA LYS A1147 0.073 -6.772 -46.702 1.00 24.75 C
ANISOU 2726 CA LYS A1147 3675 4352 1377 207 797 -594 C
ATOM 2727 C LYS A1147 0.037 -6.131 -45.309 1.00 29.78 C
ANISOU 2727 C LYS A1147 4213 5073 2028 225 630 -550 C
ATOM 2728 O LYS A1147 0.417 -6.794 -44.341 1.00 31.50 O
ANISOU 2728 O LYS A1147 4391 5333 2243 411 638 -484 O
ATOM 2729 CB LYS A1147 1.151 -6.134 -47.595 1.00 27.91 C
ANISOU 2729 CB LYS A1147 3926 4906 1770 145 843 -581 C
ATOM 2730 CG LYS A1147 2.573 -6.570 -47.260 1.00 50.84 C
ANISOU 2730 CG LYS A1147 6633 7962 4723 319 913 -529 C
ATOM 2731 CD LYS A1147 3.584 -5.938 -48.213 1.00 63.43 C
ANISOU 2731 CD LYS A1147 8060 9713 6327 231 991 -510 C
ATOM 2732 CE LYS A1147 5.013 -6.112 -47.749 1.00 68.63 C
ANISOU 2732 CE LYS A1147 8448 10565 7063 374 1017 -466 C
ATOM 2733 NZ LYS A1147 5.961 -5.340 -48.597 1.00 71.01 N
ANISOU 2733 NZ LYS A1147 8550 11025 7405 247 1103 -435 N
ATOM 2734 N ARG A1148 -0.498 -4.890 -45.195 1.00 24.29 N
ANISOU 2734 N ARG A1148 3495 4394 1339 51 484 -589 N
ATOM 2735 CA ARG A1148 -0.626 -4.164 -43.927 1.00 23.36 C
ANISOU 2735 CA ARG A1148 3289 4361 1225 54 316 -608 C
ATOM 2736 C ARG A1148 -1.425 -4.948 -42.867 1.00 27.64 C
ANISOU 2736 C ARG A1148 3938 4859 1704 189 320 -576 C
ATOM 2737 O ARG A1148 -1.016 -4.978 -41.703 1.00 27.76 O
ANISOU 2737 O ARG A1148 3858 5024 1665 323 245 -547 O
ATOM 2738 CB ARG A1148 -1.237 -2.771 -44.138 1.00 20.87 C
ANISOU 2738 CB ARG A1148 2971 4000 959 -150 188 -676 C
ATOM 2739 CG ARG A1148 -0.240 -1.708 -44.570 1.00 19.71 C
ANISOU 2739 CG ARG A1148 2649 3926 912 -275 146 -681 C
ATOM 2740 CD ARG A1148 -0.798 -0.282 -44.454 1.00 21.31 C
ANISOU 2740 CD ARG A1148 2840 4045 1211 -448 7 -743 C
ATOM 2741 NE ARG A1148 -1.982 -0.038 -45.289 1.00 15.96 N
ANISOU 2741 NE ARG A1148 2268 3146 651 -531 38 -661 N
ATOM 2742 CZ ARG A1148 -1.951 0.297 -46.574 1.00 26.08 C
ANISOU 2742 CZ ARG A1148 3673 4438 1800 -634 102 -632 C
ATOM 2743 NH1 ARG A1148 -0.792 0.439 -47.204 1.00 24.02 N
ANISOU 2743 NH1 ARG A1148 3294 4255 1579 -677 196 -557 N
ATOM 2744 NH2 ARG A1148 -3.079 0.482 -47.243 1.00 7.76 N
ANISOU 2744 NH2 ARG A1148 920 1443 586 -580 124 -191 N
ATOM 2745 N VAL A1149 -2.544 -5.588 -43.269 1.00 24.03 N
ANISOU 2745 N VAL A1149 3664 4219 1249 153 411 -579 N
ATOM 2746 CA VAL A1149 -3.372 -6.401 -42.363 1.00 24.34 C
ANISOU 2746 CA VAL A1149 3803 4182 1262 254 464 -521 C
ATOM 2747 C VAL A1149 -2.595 -7.664 -41.927 1.00 30.07 C
ANISOU 2747 C VAL A1149 4530 4909 1987 484 595 -387 C
ATOM 2748 O VAL A1149 -2.553 -7.973 -40.733 1.00 30.19 O
ANISOU 2748 O VAL A1149 4524 5015 1932 643 582 -278 O
ATOM 2749 CB VAL A1149 -4.768 -6.750 -42.962 1.00 27.82 C
ANISOU 2749 CB VAL A1149 4400 4417 1752 125 531 -578 C
ATOM 2750 CG1 VAL A1149 -5.589 -7.615 -42.002 1.00 27.11 C
ANISOU 2750 CG1 VAL A1149 4391 4238 1671 210 622 -494 C
ATOM 2751 CG2 VAL A1149 -5.543 -5.491 -43.347 1.00 27.46 C
ANISOU 2751 CG2 VAL A1149 4344 4384 1705 -57 391 -683 C
ATOM 2752 N ILE A1150 -1.976 -8.374 -42.895 1.00 27.20 N
ANISOU 2752 N ILE A1150 4190 4456 1689 522 725 -392 N
ATOM 2753 CA ILE A1150 -1.198 -9.591 -42.663 1.00 27.14 C
ANISOU 2753 CA ILE A1150 4185 4406 1721 759 866 -274 C
ATOM 2754 C ILE A1150 0.005 -9.314 -41.723 1.00 33.42 C
ANISOU 2754 C ILE A1150 4785 5475 2440 948 764 -176 C
ATOM 2755 O ILE A1150 0.277 -10.131 -40.838 1.00 33.04 O
ANISOU 2755 O ILE A1150 4741 5448 2365 1184 815 -14 O
ATOM 2756 CB ILE A1150 -0.821 -10.253 -44.019 1.00 29.64 C
ANISOU 2756 CB ILE A1150 4554 4585 2121 747 1018 -362 C
ATOM 2757 CG1 ILE A1150 -2.077 -10.890 -44.682 1.00 29.66 C
ANISOU 2757 CG1 ILE A1150 4755 4312 2201 614 1120 -469 C
ATOM 2758 CG2 ILE A1150 0.312 -11.280 -43.880 1.00 29.47 C
ANISOU 2758 CG2 ILE A1150 4479 4560 2157 1019 1149 -260 C
ATOM 2759 CD1 ILE A1150 -2.001 -11.130 -46.252 1.00 30.82 C
ANISOU 2759 CD1 ILE A1150 4960 4387 2363 520 1209 -652 C
ATOM 2760 N THR A1151 0.680 -8.143 -41.886 1.00 31.11 N
ANISOU 2760 N THR A1151 4312 5391 2117 841 617 -268 N
ATOM 2761 CA THR A1151 1.820 -7.717 -41.058 1.00 30.86 C
ANISOU 2761 CA THR A1151 4045 5651 2030 972 482 -239 C
ATOM 2762 C THR A1151 1.353 -7.477 -39.624 1.00 34.84 C
ANISOU 2762 C THR A1151 4545 6294 2399 1059 346 -198 C
ATOM 2763 O THR A1151 2.073 -7.822 -38.690 1.00 34.84 O
ANISOU 2763 O THR A1151 4427 6506 2303 1294 288 -99 O
ATOM 2764 CB THR A1151 2.516 -6.485 -41.666 1.00 39.07 C
ANISOU 2764 CB THR A1151 4895 6822 3127 777 379 -369 C
ATOM 2765 OG1 THR A1151 2.826 -6.760 -43.025 1.00 38.02 O
ANISOU 2765 OG1 THR A1151 4794 6579 3074 709 538 -385 O
ATOM 2766 CG2 THR A1151 3.808 -6.114 -40.940 1.00 40.40 C
ANISOU 2766 CG2 THR A1151 4773 7296 3282 891 244 -378 C
ATOM 2767 N THR A1152 0.143 -6.902 -39.454 1.00 31.19 N
ANISOU 2767 N THR A1152 4202 5738 1909 892 296 -272 N
ATOM 2768 CA THR A1152 -0.474 -6.643 -38.146 1.00 30.85 C
ANISOU 2768 CA THR A1152 4175 5830 1718 966 196 -254 C
ATOM 2769 C THR A1152 -0.652 -7.991 -37.417 1.00 34.35 C
ANISOU 2769 C THR A1152 4730 6239 2083 1226 344 -17 C
ATOM 2770 O THR A1152 -0.308 -8.094 -36.240 1.00 33.87 O
ANISOU 2770 O THR A1152 4596 6426 1846 1436 267 79 O
ATOM 2771 CB THR A1152 -1.777 -5.822 -38.317 1.00 35.16 C
ANISOU 2771 CB THR A1152 4824 6248 2288 738 152 -385 C
ATOM 2772 OG1 THR A1152 -1.494 -4.603 -39.014 1.00 31.25 O
ANISOU 2772 OG1 THR A1152 4227 5756 1891 528 32 -556 O
ATOM 2773 CG2 THR A1152 -2.445 -5.500 -37.001 1.00 32.69 C
ANISOU 2773 CG2 THR A1152 4515 6095 1810 815 65 -398 C
ATOM 2774 N PHE A1153 -1.119 -9.032 -38.150 1.00 30.37 N
ANISOU 2774 N PHE A1153 4394 5430 1714 1219 557 76 N
ATOM 2775 CA PHE A1153 -1.281 -10.398 -37.642 1.00 29.60 C
ANISOU 2775 CA PHE A1153 4421 5201 1627 1444 744 319 C
ATOM 2776 C PHE A1153 0.082 -11.017 -37.303 1.00 36.25 C
ANISOU 2776 C PHE A1153 5141 6202 2431 1744 745 471 C
ATOM 2777 O PHE A1153 0.186 -11.758 -36.335 1.00 36.11 O
ANISOU 2777 O PHE A1153 5155 6249 2317 2007 803 711 O
ATOM 2778 CB PHE A1153 -2.014 -11.287 -38.663 1.00 30.13 C
ANISOU 2778 CB PHE A1153 4672 4870 1907 1326 959 309 C
ATOM 2779 CG PHE A1153 -3.514 -11.142 -38.751 1.00 30.66 C
ANISOU 2779 CG PHE A1153 4868 4761 2022 1106 1005 241 C
ATOM 2780 CD1 PHE A1153 -4.301 -11.141 -37.602 1.00 33.58 C
ANISOU 2780 CD1 PHE A1153 5274 5200 2284 1158 1023 371 C
ATOM 2781 CD2 PHE A1153 -4.151 -11.098 -39.983 1.00 31.49 C
ANISOU 2781 CD2 PHE A1153 5046 4649 2271 868 1045 54 C
ATOM 2782 CE1 PHE A1153 -5.695 -11.054 -37.688 1.00 34.13 C
ANISOU 2782 CE1 PHE A1153 5430 5116 2422 959 1084 308 C
ATOM 2783 CE2 PHE A1153 -5.542 -11.016 -40.069 1.00 34.06 C
ANISOU 2783 CE2 PHE A1153 5455 4831 2654 677 1077 -15 C
ATOM 2784 CZ PHE A1153 -6.305 -10.991 -38.923 1.00 32.67 C
ANISOU 2784 CZ PHE A1153 5295 4714 2404 718 1101 110 C
ATOM 2785 N ARG A1154 1.120 -10.702 -38.091 1.00 34.61 N
ANISOU 2785 N ARG A1154 4784 6071 2296 1719 690 350 N
ATOM 2786 CA ARG A1154 2.478 -11.205 -37.899 1.00 35.27 C
ANISOU 2786 CA ARG A1154 4702 6329 2369 1998 682 460 C
ATOM 2787 C ARG A1154 3.169 -10.603 -36.661 1.00 40.58 C
ANISOU 2787 C ARG A1154 5161 7435 2824 2163 450 490 C
ATOM 2788 O ARG A1154 3.578 -11.348 -35.780 1.00 40.75 O
ANISOU 2788 O ARG A1154 5158 7593 2734 2485 461 715 O
ATOM 2789 CB ARG A1154 3.319 -10.926 -39.153 1.00 36.22 C
ANISOU 2789 CB ARG A1154 4696 6437 2630 1886 703 297 C
ATOM 2790 CG ARG A1154 3.608 -12.143 -40.009 1.00 49.19 C
ANISOU 2790 CG ARG A1154 6441 7808 4441 2014 942 358 C
ATOM 2791 CD ARG A1154 4.346 -11.743 -41.274 1.00 64.59 C
ANISOU 2791 CD ARG A1154 8268 9791 6482 1880 973 179 C
ATOM 2792 NE ARG A1154 5.759 -11.463 -41.022 1.00 82.85 N
ANISOU 2792 NE ARG A1154 10278 12428 8772 2042 877 196 N
ATOM 2793 CZ ARG A1154 6.736 -12.353 -41.166 1.00107.22 C
ANISOU 2793 CZ ARG A1154 13266 15538 11936 2325 992 288 C
ATOM 2794 NH1 ARG A1154 6.464 -13.590 -41.568 1.00 98.09 N
ANISOU 2794 NH1 ARG A1154 12312 14061 10896 2480 1216 362 N
ATOM 2795 NH2 ARG A1154 7.992 -12.014 -40.909 1.00 99.35 N
ANISOU 2795 NH2 ARG A1154 11951 14875 10922 2457 884 289 N
ATOM 2796 N THR A1155 3.281 -9.261 -36.598 1.00 38.05 N
ANISOU 2796 N THR A1155 4685 7324 2448 1949 239 259 N
ATOM 2797 CA THR A1155 3.977 -8.502 -35.550 1.00 38.16 C
ANISOU 2797 CA THR A1155 4460 7761 2279 2046 -17 181 C
ATOM 2798 C THR A1155 3.184 -8.271 -34.249 1.00 43.02 C
ANISOU 2798 C THR A1155 5157 8547 2644 2127 -113 219 C
ATOM 2799 O THR A1155 3.799 -8.186 -33.182 1.00 41.72 O
ANISOU 2799 O THR A1155 4835 8759 2258 2359 -279 255 O
ATOM 2800 CB THR A1155 4.481 -7.152 -36.101 1.00 45.64 C
ANISOU 2800 CB THR A1155 5195 8811 3334 1759 -183 -109 C
ATOM 2801 OG1 THR A1155 3.374 -6.267 -36.314 1.00 48.01 O
ANISOU 2801 OG1 THR A1155 5634 8940 3668 1471 -208 -264 O
ATOM 2802 CG2 THR A1155 5.325 -7.298 -37.377 1.00 40.85 C
ANISOU 2802 CG2 THR A1155 4481 8095 2945 1680 -71 -135 C
ATOM 2803 N GLY A1156 1.861 -8.108 -34.354 1.00 41.38 N
ANISOU 2803 N GLY A1156 5163 8103 2454 1941 -23 189 N
ATOM 2804 CA GLY A1156 0.986 -7.834 -33.210 1.00 41.72 C
ANISOU 2804 CA GLY A1156 5285 8298 2267 1993 -78 206 C
ATOM 2805 C GLY A1156 1.061 -6.402 -32.728 1.00 47.05 C
ANISOU 2805 C GLY A1156 5794 9244 2839 1855 -341 -104 C
ATOM 2806 O GLY A1156 0.599 -6.080 -31.630 1.00 46.84 O
ANISOU 2806 O GLY A1156 5773 9458 2565 1953 -432 -138 O
ATOM 2807 N THR A1157 1.649 -5.537 -33.569 1.00 44.74 N
ANISOU 2807 N THR A1157 5351 8901 2747 1624 -448 -336 N
ATOM 2808 CA THR A1157 1.865 -4.109 -33.345 1.00 44.59 C
ANISOU 2808 CA THR A1157 5154 9045 2745 1438 -685 -662 C
ATOM 2809 C THR A1157 1.180 -3.340 -34.470 1.00 47.91 C
ANISOU 2809 C THR A1157 5667 9114 3421 1099 -626 -800 C
ATOM 2810 O THR A1157 0.608 -3.951 -35.371 1.00 47.30 O
ANISOU 2810 O THR A1157 5772 8737 3464 1030 -427 -657 O
ATOM 2811 CB THR A1157 3.385 -3.799 -33.330 1.00 53.64 C
ANISOU 2811 CB THR A1157 5985 10457 3937 1481 -858 -772 C
ATOM 2812 OG1 THR A1157 3.941 -4.093 -34.618 1.00 56.67 O
ANISOU 2812 OG1 THR A1157 6340 10617 4576 1371 -717 -698 O
ATOM 2813 CG2 THR A1157 4.147 -4.552 -32.230 1.00 47.94 C
ANISOU 2813 CG2 THR A1157 5137 10135 2943 1855 -950 -630 C
ATOM 2814 N TRP A1158 1.266 -2.006 -34.427 1.00 45.25 N
ANISOU 2814 N TRP A1158 5200 8816 3177 897 -804 -1080 N
ATOM 2815 CA TRP A1158 0.710 -1.102 -35.429 1.00 45.61 C
ANISOU 2815 CA TRP A1158 5309 8552 3467 595 -776 -1200 C
ATOM 2816 C TRP A1158 1.809 -0.572 -36.386 1.00 51.13 C
ANISOU 2816 C TRP A1158 5821 9197 4409 419 -799 -1258 C
ATOM 2817 O TRP A1158 1.592 0.434 -37.060 1.00 51.02 O
ANISOU 2817 O TRP A1158 5799 8984 4602 170 -820 -1374 O
ATOM 2818 CB TRP A1158 0.004 0.067 -34.730 1.00 44.30 C
ANISOU 2818 CB TRP A1158 5137 8412 3283 495 -932 -1459 C
ATOM 2819 CG TRP A1158 -1.190 -0.324 -33.916 1.00 45.42 C
ANISOU 2819 CG TRP A1158 5457 8596 3205 636 -876 -1408 C
ATOM 2820 CD1 TRP A1158 -1.331 -0.216 -32.565 1.00 48.38 C
ANISOU 2820 CD1 TRP A1158 5788 9279 3317 813 -990 -1517 C
ATOM 2821 CD2 TRP A1158 -2.435 -0.838 -34.411 1.00 45.42 C
ANISOU 2821 CD2 TRP A1158 5687 8342 3228 602 -685 -1249 C
ATOM 2822 NE1 TRP A1158 -2.588 -0.627 -32.185 1.00 47.87 N
ANISOU 2822 NE1 TRP A1158 5915 9161 3114 891 -856 -1410 N
ATOM 2823 CE2 TRP A1158 -3.287 -1.016 -33.299 1.00 49.22 C
ANISOU 2823 CE2 TRP A1158 6243 8979 3478 753 -672 -1251 C
ATOM 2824 CE3 TRP A1158 -2.912 -1.180 -35.691 1.00 46.64 C
ANISOU 2824 CE3 TRP A1158 5975 8179 3565 461 -526 -1118 C
ATOM 2825 CZ2 TRP A1158 -4.583 -1.524 -33.423 1.00 48.42 C
ANISOU 2825 CZ2 TRP A1158 6326 8706 3365 746 -494 -1118 C
ATOM 2826 CZ3 TRP A1158 -4.208 -1.652 -35.814 1.00 48.00 C
ANISOU 2826 CZ3 TRP A1158 6329 8191 3719 454 -384 -1022 C
ATOM 2827 CH2 TRP A1158 -5.024 -1.825 -34.689 1.00 48.54 C
ANISOU 2827 CH2 TRP A1158 6449 8398 3596 587 -363 -1017 C
ATOM 2828 N ASP A1159 2.973 -1.267 -36.453 1.00 48.01 N
ANISOU 2828 N ASP A1159 5270 8976 3996 561 -775 -1152 N
ATOM 2829 CA ASP A1159 4.147 -0.901 -37.254 1.00 47.69 C
ANISOU 2829 CA ASP A1159 5004 8950 4166 430 -771 -1186 C
ATOM 2830 C ASP A1159 3.878 -0.723 -38.758 1.00 51.08 C
ANISOU 2830 C ASP A1159 5553 9060 4794 211 -585 -1098 C
ATOM 2831 O ASP A1159 4.543 0.116 -39.369 1.00 50.42 O
ANISOU 2831 O ASP A1159 5298 8944 4917 8 -599 -1172 O
ATOM 2832 CB ASP A1159 5.307 -1.888 -37.018 1.00 49.69 C
ANISOU 2832 CB ASP A1159 5084 9462 4336 685 -753 -1059 C
ATOM 2833 CG ASP A1159 5.869 -1.887 -35.597 1.00 62.15 C
ANISOU 2833 CG ASP A1159 6460 11440 5716 898 -982 -1162 C
ATOM 2834 OD1 ASP A1159 5.738 -0.851 -34.900 1.00 62.88 O
ANISOU 2834 OD1 ASP A1159 6450 11643 5797 780 -1187 -1420 O
ATOM 2835 OD2 ASP A1159 6.439 -2.925 -35.181 1.00 68.16 O
ANISOU 2835 OD2 ASP A1159 7163 12408 6326 1199 -961 -992 O
ATOM 2836 N ALA A1160 2.900 -1.470 -39.342 1.00 47.54 N
ANISOU 2836 N ALA A1160 5387 8391 4284 244 -414 -949 N
ATOM 2837 CA ALA A1160 2.505 -1.381 -40.766 1.00 46.83 C
ANISOU 2837 CA ALA A1160 5434 8043 4317 69 -253 -875 C
ATOM 2838 C ALA A1160 1.841 -0.028 -41.095 1.00 50.75 C
ANISOU 2838 C ALA A1160 5967 8367 4949 -185 -332 -986 C
ATOM 2839 O ALA A1160 1.837 0.404 -42.250 1.00 50.13 O
ANISOU 2839 O ALA A1160 5921 8136 4989 -351 -238 -928 O
ATOM 2840 CB ALA A1160 1.572 -2.527 -41.129 1.00 47.31 C
ANISOU 2840 CB ALA A1160 5759 7943 4273 176 -90 -743 C
ATOM 2841 N TYR A1161 1.278 0.620 -40.065 1.00 47.59 N
ANISOU 2841 N TYR A1161 5565 8000 4518 -192 -496 -1137 N
ATOM 2842 CA TYR A1161 0.648 1.939 -40.090 1.00 47.80 C
ANISOU 2842 CA TYR A1161 5610 7861 4691 -387 -597 -1276 C
ATOM 2843 C TYR A1161 1.568 2.838 -39.223 1.00 57.67 C
ANISOU 2843 C TYR A1161 6595 9273 6046 -444 -787 -1497 C
ATOM 2844 O TYR A1161 2.590 2.357 -38.717 1.00 58.01 O
ANISOU 2844 O TYR A1161 6451 9571 6021 -328 -834 -1515 O
ATOM 2845 CB TYR A1161 -0.788 1.855 -39.490 1.00 47.34 C
ANISOU 2845 CB TYR A1161 5751 7731 4506 -314 -626 -1318 C
ATOM 2846 CG TYR A1161 -1.643 0.747 -40.081 1.00 46.49 C
ANISOU 2846 CG TYR A1161 5861 7520 4283 -233 -458 -1138 C
ATOM 2847 CD1 TYR A1161 -1.612 -0.542 -39.554 1.00 47.77 C
ANISOU 2847 CD1 TYR A1161 6075 7805 4272 -28 -378 -1032 C
ATOM 2848 CD2 TYR A1161 -2.456 0.981 -41.186 1.00 46.39 C
ANISOU 2848 CD2 TYR A1161 5992 7284 4349 -360 -381 -1073 C
ATOM 2849 CE1 TYR A1161 -2.344 -1.577 -40.132 1.00 46.83 C
ANISOU 2849 CE1 TYR A1161 6139 7549 4104 17 -214 -894 C
ATOM 2850 CE2 TYR A1161 -3.202 -0.045 -41.765 1.00 46.66 C
ANISOU 2850 CE2 TYR A1161 6198 7236 4295 -306 -244 -957 C
ATOM 2851 CZ TYR A1161 -3.128 -1.327 -41.246 1.00 51.83 C
ANISOU 2851 CZ TYR A1161 6895 7977 4822 -133 -155 -882 C
ATOM 2852 OH TYR A1161 -3.854 -2.345 -41.815 1.00 49.42 O
ANISOU 2852 OH TYR A1161 6747 7549 4479 -105 -14 -798 O
ATOM 2853 N THR A 354 1.247 4.128 -39.076 1.00 57.72 N
ANISOU 2853 N THR A 354 4643 14014 3274 1247 1338 -2975 N
ATOM 2854 CA THR A 354 2.015 5.037 -38.208 1.00 58.60 C
ANISOU 2854 CA THR A 354 4645 14182 3440 1189 1333 -2784 C
ATOM 2855 C THR A 354 0.974 5.785 -37.401 1.00 63.44 C
ANISOU 2855 C THR A 354 5413 14496 4195 1034 1239 -2555 C
ATOM 2856 O THR A 354 0.406 6.766 -37.885 1.00 64.22 O
ANISOU 2856 O THR A 354 5529 14663 4207 820 1228 -2387 O
ATOM 2857 CB THR A 354 2.970 5.946 -39.004 1.00 72.16 C
ANISOU 2857 CB THR A 354 6144 16330 4943 1054 1419 -2716 C
ATOM 2858 OG1 THR A 354 2.266 6.495 -40.117 1.00 76.98 O
ANISOU 2858 OG1 THR A 354 6783 17078 5387 867 1433 -2656 O
ATOM 2859 CG2 THR A 354 4.227 5.219 -39.481 1.00 70.51 C
ANISOU 2859 CG2 THR A 354 5746 16419 4626 1242 1512 -2937 C
ATOM 2860 N PHE A 355 0.649 5.269 -36.209 1.00 58.81 N
ANISOU 2860 N PHE A 355 4951 13571 3821 1153 1172 -2555 N
ATOM 2861 CA PHE A 355 -0.407 5.864 -35.405 1.00 57.98 C
ANISOU 2861 CA PHE A 355 5000 13172 3857 1027 1083 -2363 C
ATOM 2862 C PHE A 355 0.040 6.906 -34.431 1.00 62.00 C
ANISOU 2862 C PHE A 355 5453 13663 4441 934 1058 -2153 C
ATOM 2863 O PHE A 355 1.067 6.768 -33.754 1.00 62.08 O
ANISOU 2863 O PHE A 355 5358 13732 4498 1046 1075 -2178 O
ATOM 2864 CB PHE A 355 -1.239 4.803 -34.668 1.00 59.30 C
ANISOU 2864 CB PHE A 355 5359 12965 4209 1165 1020 -2457 C
ATOM 2865 CG PHE A 355 -2.172 4.001 -35.540 1.00 60.15 C
ANISOU 2865 CG PHE A 355 5583 13004 4269 1174 1018 -2614 C
ATOM 2866 CD1 PHE A 355 -2.524 4.447 -36.809 1.00 62.63 C
ANISOU 2866 CD1 PHE A 355 5853 13549 4395 1029 1048 -2614 C
ATOM 2867 CD2 PHE A 355 -2.709 2.807 -35.090 1.00 61.63 C
ANISOU 2867 CD2 PHE A 355 5926 12898 4593 1317 986 -2760 C
ATOM 2868 CE1 PHE A 355 -3.362 3.693 -37.621 1.00 63.38 C
ANISOU 2868 CE1 PHE A 355 6044 13604 4435 1033 1044 -2774 C
ATOM 2869 CE2 PHE A 355 -3.569 2.069 -35.895 1.00 64.28 C
ANISOU 2869 CE2 PHE A 355 6368 13172 4882 1306 986 -2917 C
ATOM 2870 CZ PHE A 355 -3.881 2.512 -37.157 1.00 62.37 C
ANISOU 2870 CZ PHE A 355 6067 13182 4449 1166 1014 -2930 C
ATOM 2871 N SER A 356 -0.792 7.946 -34.334 1.00 57.65 N
ANISOU 2871 N SER A 356 4980 13020 3903 733 1011 -1950 N
ATOM 2872 CA SER A 356 -0.633 9.036 -33.393 1.00 56.53 C
ANISOU 2872 CA SER A 356 4827 12807 3844 614 976 -1739 C
ATOM 2873 C SER A 356 -1.160 8.553 -32.045 1.00 58.92 C
ANISOU 2873 C SER A 356 5267 12758 4364 719 898 -1727 C
ATOM 2874 O SER A 356 -1.862 7.534 -31.971 1.00 58.71 O
ANISOU 2874 O SER A 356 5366 12529 4413 836 868 -1847 O
ATOM 2875 CB SER A 356 -1.402 10.272 -33.871 1.00 59.30 C
ANISOU 2875 CB SER A 356 5231 13175 4126 379 956 -1537 C
ATOM 2876 OG SER A 356 -2.754 10.323 -33.444 1.00 65.77 O
ANISOU 2876 OG SER A 356 6229 13699 5060 345 875 -1463 O
ATOM 2877 N LEU A 357 -0.836 9.292 -30.983 1.00 53.74 N
ANISOU 2877 N LEU A 357 4589 12028 3801 665 867 -1583 N
ATOM 2878 CA LEU A 357 -1.315 9.004 -29.640 1.00 52.27 C
ANISOU 2878 CA LEU A 357 4524 11530 3808 741 794 -1543 C
ATOM 2879 C LEU A 357 -2.810 9.328 -29.627 1.00 55.51 C
ANISOU 2879 C LEU A 357 5108 11709 4276 627 733 -1444 C
ATOM 2880 O LEU A 357 -3.279 10.061 -30.502 1.00 54.25 O
ANISOU 2880 O LEU A 357 4951 11654 4008 476 744 -1365 O
ATOM 2881 CB LEU A 357 -0.534 9.844 -28.604 1.00 51.81 C
ANISOU 2881 CB LEU A 357 4379 11502 3805 687 781 -1415 C
ATOM 2882 CG LEU A 357 1.010 9.850 -28.743 1.00 55.35 C
ANISOU 2882 CG LEU A 357 4612 12261 4158 739 847 -1480 C
ATOM 2883 CD1 LEU A 357 1.630 10.985 -27.963 1.00 54.92 C
ANISOU 2883 CD1 LEU A 357 4471 12272 4124 600 837 -1328 C
ATOM 2884 CD2 LEU A 357 1.624 8.524 -28.333 1.00 56.93 C
ANISOU 2884 CD2 LEU A 357 4774 12445 4410 1007 852 -1658 C
ATOM 2885 N VAL A 358 -3.570 8.732 -28.696 1.00 53.14 N
ANISOU 2885 N VAL A 358 4948 11110 4132 707 671 -1453 N
ATOM 2886 CA VAL A 358 -5.017 8.954 -28.610 1.00 52.83 C
ANISOU 2886 CA VAL A 358 5062 10859 4151 612 613 -1373 C
ATOM 2887 C VAL A 358 -5.346 10.448 -28.375 1.00 55.52 C
ANISOU 2887 C VAL A 358 5404 11202 4488 425 586 -1157 C
ATOM 2888 O VAL A 358 -4.897 11.052 -27.390 1.00 54.95 O
ANISOU 2888 O VAL A 358 5306 11081 4492 400 569 -1058 O
ATOM 2889 CB VAL A 358 -5.738 8.001 -27.596 1.00 57.04 C
ANISOU 2889 CB VAL A 358 5742 11080 4852 725 558 -1425 C
ATOM 2890 CG1 VAL A 358 -5.159 8.099 -26.182 1.00 56.52 C
ANISOU 2890 CG1 VAL A 358 5666 10899 4910 795 530 -1359 C
ATOM 2891 CG2 VAL A 358 -7.259 8.211 -27.590 1.00 56.93 C
ANISOU 2891 CG2 VAL A 358 5866 10883 4883 619 503 -1355 C
ATOM 2892 N LYS A 359 -6.102 11.032 -29.325 1.00 50.74 N
ANISOU 2892 N LYS A 359 4829 10662 3787 298 583 -1092 N
ATOM 2893 CA LYS A 359 -6.599 12.405 -29.270 1.00 49.56 C
ANISOU 2893 CA LYS A 359 4711 10492 3627 131 555 -890 C
ATOM 2894 C LYS A 359 -7.699 12.417 -28.192 1.00 50.54 C
ANISOU 2894 C LYS A 359 4971 10318 3913 142 479 -827 C
ATOM 2895 O LYS A 359 -8.755 11.805 -28.377 1.00 50.92 O
ANISOU 2895 O LYS A 359 5111 10250 3986 172 445 -885 O
ATOM 2896 CB LYS A 359 -7.119 12.839 -30.668 1.00 52.01 C
ANISOU 2896 CB LYS A 359 5018 10967 3777 28 571 -853 C
ATOM 2897 CG LYS A 359 -8.012 14.087 -30.716 1.00 70.18 C
ANISOU 2897 CG LYS A 359 7392 13201 6072 -116 527 -649 C
ATOM 2898 CD LYS A 359 -7.269 15.394 -30.420 1.00 82.21 C
ANISOU 2898 CD LYS A 359 8864 14797 7575 -239 552 -483 C
ATOM 2899 CE LYS A 359 -8.181 16.599 -30.442 1.00 91.85 C
ANISOU 2899 CE LYS A 359 10178 15917 8803 -361 507 -284 C
ATOM 2900 NZ LYS A 359 -9.125 16.618 -29.292 1.00 97.76 N
ANISOU 2900 NZ LYS A 359 11036 16382 9725 -323 436 -241 N
ATOM 2901 N GLU A 360 -7.412 13.033 -27.037 1.00 44.36 N
ANISOU 2901 N GLU A 360 4195 9424 3236 121 455 -727 N
ATOM 2902 CA GLU A 360 -8.360 13.085 -25.921 1.00 42.88 C
ANISOU 2902 CA GLU A 360 4125 8972 3196 132 389 -668 C
ATOM 2903 C GLU A 360 -9.441 14.132 -26.187 1.00 43.98 C
ANISOU 2903 C GLU A 360 4336 9054 3319 7 351 -520 C
ATOM 2904 O GLU A 360 -9.169 15.336 -26.149 1.00 44.54 O
ANISOU 2904 O GLU A 360 4388 9167 3368 -101 356 -381 O
ATOM 2905 CB GLU A 360 -7.635 13.321 -24.581 1.00 44.19 C
ANISOU 2905 CB GLU A 360 4266 9055 3469 164 377 -629 C
ATOM 2906 CG GLU A 360 -6.786 12.140 -24.137 1.00 55.55 C
ANISOU 2906 CG GLU A 360 5654 10510 4942 325 397 -772 C
ATOM 2907 CD GLU A 360 -5.696 12.442 -23.124 1.00 71.84 C
ANISOU 2907 CD GLU A 360 7635 12608 7052 352 400 -743 C
ATOM 2908 OE1 GLU A 360 -6.028 12.862 -21.991 1.00 52.16 O
ANISOU 2908 OE1 GLU A 360 5201 9954 4665 331 354 -662 O
ATOM 2909 OE2 GLU A 360 -4.507 12.238 -23.461 1.00 66.98 O
ANISOU 2909 OE2 GLU A 360 6889 12198 6363 397 448 -810 O
ATOM 2910 N LYS A 361 -10.655 13.673 -26.507 1.00 37.34 N
ANISOU 2910 N LYS A 361 3576 8128 2483 21 316 -554 N
ATOM 2911 CA LYS A 361 -11.760 14.580 -26.804 1.00 35.97 C
ANISOU 2911 CA LYS A 361 3465 7914 2289 -72 274 -423 C
ATOM 2912 C LYS A 361 -12.289 15.253 -25.547 1.00 36.54 C
ANISOU 2912 C LYS A 361 3609 7780 2496 -91 225 -311 C
ATOM 2913 O LYS A 361 -12.158 14.703 -24.454 1.00 35.45 O
ANISOU 2913 O LYS A 361 3493 7502 2473 -23 212 -361 O
ATOM 2914 CB LYS A 361 -12.885 13.872 -27.585 1.00 38.49 C
ANISOU 2914 CB LYS A 361 3828 8239 2558 -54 250 -505 C
ATOM 2915 CG LYS A 361 -12.683 13.871 -29.107 1.00 49.77 C
ANISOU 2915 CG LYS A 361 5194 9910 3805 -94 286 -537 C
ATOM 2916 CD LYS A 361 -11.831 12.700 -29.598 1.00 58.18 C
ANISOU 2916 CD LYS A 361 6196 11093 4816 -14 342 -726 C
ATOM 2917 CE LYS A 361 -11.941 12.476 -31.087 1.00 66.85 C
ANISOU 2917 CE LYS A 361 7248 12415 5735 -45 369 -792 C
ATOM 2918 NZ LYS A 361 -13.175 11.727 -31.444 1.00 72.53 N
ANISOU 2918 NZ LYS A 361 8033 13075 6449 -31 328 -889 N
ATOM 2919 N ALA A 362 -12.884 16.451 -25.721 1.00 31.12 N
ANISOU 2919 N ALA A 362 2961 7077 1787 -178 198 -159 N
ATOM 2920 CA ALA A 362 -13.463 17.313 -24.689 1.00 29.98 C
ANISOU 2920 CA ALA A 362 2887 6752 1752 -205 154 -42 C
ATOM 2921 C ALA A 362 -14.272 16.563 -23.630 1.00 33.64 C
ANISOU 2921 C ALA A 362 3411 7028 2344 -129 112 -108 C
ATOM 2922 O ALA A 362 -14.207 16.930 -22.464 1.00 33.29 O
ANISOU 2922 O ALA A 362 3397 6847 2404 -124 93 -63 O
ATOM 2923 CB ALA A 362 -14.320 18.395 -25.337 1.00 30.32 C
ANISOU 2923 CB ALA A 362 2976 6809 1735 -273 125 100 C
ATOM 2924 N ALA A 363 -15.007 15.507 -24.032 1.00 30.22 N
ANISOU 2924 N ALA A 363 2994 6593 1894 -79 100 -218 N
ATOM 2925 CA ALA A 363 -15.849 14.680 -23.162 1.00 29.75 C
ANISOU 2925 CA ALA A 363 2995 6368 1941 -25 67 -286 C
ATOM 2926 C ALA A 363 -15.019 13.909 -22.148 1.00 33.49 C
ANISOU 2926 C ALA A 363 3468 6751 2506 47 85 -360 C
ATOM 2927 O ALA A 363 -15.341 13.929 -20.959 1.00 33.66 O
ANISOU 2927 O ALA A 363 3536 6619 2634 67 59 -332 O
ATOM 2928 CB ALA A 363 -16.678 13.721 -23.999 1.00 30.49 C
ANISOU 2928 CB ALA A 363 3101 6507 1979 -12 59 -396 C
ATOM 2929 N LEU A 364 -13.942 13.249 -22.620 1.00 29.35 N
ANISOU 2929 N LEU A 364 2885 6334 1932 94 131 -454 N
ATOM 2930 CA LEU A 364 -13.000 12.469 -21.817 1.00 28.82 C
ANISOU 2930 CA LEU A 364 2803 6217 1930 186 151 -530 C
ATOM 2931 C LEU A 364 -12.274 13.401 -20.844 1.00 31.57 C
ANISOU 2931 C LEU A 364 3119 6546 2329 162 146 -429 C
ATOM 2932 O LEU A 364 -12.226 13.126 -19.642 1.00 32.48 O
ANISOU 2932 O LEU A 364 3267 6533 2542 214 126 -429 O
ATOM 2933 CB LEU A 364 -11.998 11.774 -22.769 1.00 29.22 C
ANISOU 2933 CB LEU A 364 2780 6433 1889 240 203 -647 C
ATOM 2934 CG LEU A 364 -11.134 10.652 -22.206 1.00 34.29 C
ANISOU 2934 CG LEU A 364 3410 7035 2582 373 224 -758 C
ATOM 2935 CD1 LEU A 364 -11.954 9.432 -21.910 1.00 34.68 C
ANISOU 2935 CD1 LEU A 364 3564 6906 2706 441 205 -853 C
ATOM 2936 CD2 LEU A 364 -10.033 10.282 -23.179 1.00 36.32 C
ANISOU 2936 CD2 LEU A 364 3568 7496 2734 422 281 -856 C
ATOM 2937 N ARG A 365 -11.759 14.526 -21.362 1.00 26.24 N
ANISOU 2937 N ARG A 365 2387 6000 1583 74 165 -340 N
ATOM 2938 CA ARG A 365 -11.049 15.539 -20.588 1.00 25.35 C
ANISOU 2938 CA ARG A 365 2242 5886 1503 20 165 -248 C
ATOM 2939 C ARG A 365 -11.938 16.161 -19.506 1.00 27.41 C
ANISOU 2939 C ARG A 365 2588 5960 1867 -7 116 -163 C
ATOM 2940 O ARG A 365 -11.464 16.309 -18.386 1.00 26.43 O
ANISOU 2940 O ARG A 365 2457 5773 1813 9 106 -152 O
ATOM 2941 CB ARG A 365 -10.439 16.612 -21.502 1.00 25.19 C
ANISOU 2941 CB ARG A 365 2162 6031 1379 -93 200 -167 C
ATOM 2942 CG ARG A 365 -9.210 16.138 -22.259 1.00 35.68 C
ANISOU 2942 CG ARG A 365 3376 7572 2608 -72 258 -248 C
ATOM 2943 CD ARG A 365 -8.431 17.299 -22.856 1.00 46.15 C
ANISOU 2943 CD ARG A 365 4635 9055 3845 -204 297 -153 C
ATOM 2944 NE ARG A 365 -7.205 17.594 -22.097 1.00 50.55 N
ANISOU 2944 NE ARG A 365 5107 9673 4428 -225 317 -155 N
ATOM 2945 CZ ARG A 365 -6.919 18.772 -21.542 1.00 46.39 C
ANISOU 2945 CZ ARG A 365 4587 9110 3929 -343 312 -48 C
ATOM 2946 NH1 ARG A 365 -7.765 19.790 -21.651 1.00 27.11 N
ANISOU 2946 NH1 ARG A 365 2244 6555 1501 -439 289 76 N
ATOM 2947 NH2 ARG A 365 -5.780 18.943 -20.891 1.00 19.12 N
ANISOU 2947 NH2 ARG A 365 1026 5707 531 -364 294 -71 N
ATOM 2948 N THR A 366 -13.225 16.485 -19.826 1.00 23.60 N
ANISOU 2948 N THR A 366 2175 5403 1386 -39 84 -112 N
ATOM 2949 CA THR A 366 -14.200 17.062 -18.876 1.00 22.91 C
ANISOU 2949 CA THR A 366 2165 5153 1389 -53 39 -41 C
ATOM 2950 C THR A 366 -14.455 16.103 -17.723 1.00 25.79 C
ANISOU 2950 C THR A 366 2563 5388 1847 28 21 -111 C
ATOM 2951 O THR A 366 -14.419 16.533 -16.569 1.00 26.21 O
ANISOU 2951 O THR A 366 2639 5344 1974 26 1 -71 O
ATOM 2952 CB THR A 366 -15.509 17.479 -19.573 1.00 25.41 C
ANISOU 2952 CB THR A 366 2530 5454 1672 -83 11 13 C
ATOM 2953 OG1 THR A 366 -15.210 18.454 -20.567 1.00 25.59 O
ANISOU 2953 OG1 THR A 366 2531 5586 1604 -156 27 102 O
ATOM 2954 CG2 THR A 366 -16.529 18.060 -18.612 1.00 19.62 C
ANISOU 2954 CG2 THR A 366 1863 4567 1026 -81 -33 75 C
ATOM 2955 N LEU A 367 -14.685 14.808 -18.048 1.00 20.93 N
ANISOU 2955 N LEU A 367 1958 4771 1224 93 28 -216 N
ATOM 2956 CA LEU A 367 -14.921 13.713 -17.106 1.00 19.92 C
ANISOU 2956 CA LEU A 367 1877 4516 1177 169 16 -283 C
ATOM 2957 C LEU A 367 -13.751 13.583 -16.131 1.00 23.26 C
ANISOU 2957 C LEU A 367 2266 4932 1641 224 25 -289 C
ATOM 2958 O LEU A 367 -13.976 13.541 -14.928 1.00 23.40 O
ANISOU 2958 O LEU A 367 2323 4836 1733 245 1 -263 O
ATOM 2959 CB LEU A 367 -15.164 12.389 -17.867 1.00 19.66 C
ANISOU 2959 CB LEU A 367 1863 4493 1114 219 33 -402 C
ATOM 2960 CG LEU A 367 -15.311 11.107 -17.030 1.00 23.82 C
ANISOU 2960 CG LEU A 367 2455 4879 1718 299 29 -477 C
ATOM 2961 CD1 LEU A 367 -16.537 11.155 -16.120 1.00 23.96 C
ANISOU 2961 CD1 LEU A 367 2545 4752 1808 264 -5 -431 C
ATOM 2962 CD2 LEU A 367 -15.353 9.888 -17.910 1.00 24.88 C
ANISOU 2962 CD2 LEU A 367 2610 5026 1816 342 54 -604 C
ATOM 2963 N SER A 368 -12.511 13.568 -16.650 1.00 19.58 N
ANISOU 2963 N SER A 368 1716 4607 1116 244 59 -321 N
ATOM 2964 CA SER A 368 -11.289 13.488 -15.853 1.00 18.98 C
ANISOU 2964 CA SER A 368 1580 4572 1059 297 67 -332 C
ATOM 2965 C SER A 368 -11.158 14.721 -14.937 1.00 20.88 C
ANISOU 2965 C SER A 368 1813 4787 1336 220 45 -235 C
ATOM 2966 O SER A 368 -10.917 14.551 -13.748 1.00 20.89 O
ANISOU 2966 O SER A 368 1823 4721 1395 265 24 -231 O
ATOM 2967 CB SER A 368 -10.076 13.349 -16.768 1.00 23.29 C
ANISOU 2967 CB SER A 368 2020 5311 1517 317 111 -386 C
ATOM 2968 OG SER A 368 -8.864 13.281 -16.036 1.00 33.62 O
ANISOU 2968 OG SER A 368 3249 6692 2834 370 117 -399 O
ATOM 2969 N ALA A 369 -11.386 15.939 -15.477 1.00 15.65 N
ANISOU 2969 N ALA A 369 1145 4164 638 105 49 -157 N
ATOM 2970 CA ALA A 369 -11.323 17.207 -14.746 1.00 15.17 C
ANISOU 2970 CA ALA A 369 1092 4062 610 18 32 -70 C
ATOM 2971 C ALA A 369 -12.327 17.272 -13.573 1.00 21.02 C
ANISOU 2971 C ALA A 369 1919 4630 1439 38 -9 -44 C
ATOM 2972 O ALA A 369 -11.907 17.553 -12.451 1.00 20.98 O
ANISOU 2972 O ALA A 369 1904 4591 1476 39 -24 -34 O
ATOM 2973 CB ALA A 369 -11.534 18.380 -15.700 1.00 15.50 C
ANISOU 2973 CB ALA A 369 1142 4152 598 -96 45 12 C
ATOM 2974 N ILE A 370 -13.631 16.984 -13.819 1.00 18.79 N
ANISOU 2974 N ILE A 370 1708 4257 1176 52 -27 -39 N
ATOM 2975 CA ILE A 370 -14.674 17.010 -12.771 1.00 18.62 C
ANISOU 2975 CA ILE A 370 1757 4090 1228 68 -61 -19 C
ATOM 2976 C ILE A 370 -14.439 15.907 -11.719 1.00 22.84 C
ANISOU 2976 C ILE A 370 2302 4568 1809 154 -69 -74 C
ATOM 2977 O ILE A 370 -14.790 16.102 -10.553 1.00 22.43 O
ANISOU 2977 O ILE A 370 2284 4430 1809 158 -91 -50 O
ATOM 2978 CB ILE A 370 -16.147 17.028 -13.304 1.00 21.15 C
ANISOU 2978 CB ILE A 370 2133 4354 1547 56 -78 -1 C
ATOM 2979 CG1 ILE A 370 -16.503 15.748 -14.105 1.00 21.60 C
ANISOU 2979 CG1 ILE A 370 2195 4436 1575 100 -67 -80 C
ATOM 2980 CG2 ILE A 370 -16.432 18.306 -14.090 1.00 20.71 C
ANISOU 2980 CG2 ILE A 370 2082 4336 1453 -15 -81 79 C
ATOM 2981 CD1 ILE A 370 -17.951 15.641 -14.643 1.00 25.83 C
ANISOU 2981 CD1 ILE A 370 2769 4946 2100 80 -86 -78 C
ATOM 2982 N LEU A 371 -13.833 14.767 -12.127 1.00 19.43 N
ANISOU 2982 N LEU A 371 1845 4185 1354 226 -49 -145 N
ATOM 2983 CA LEU A 371 -13.514 13.677 -11.206 1.00 19.11 C
ANISOU 2983 CA LEU A 371 1823 4086 1352 323 -56 -187 C
ATOM 2984 C LEU A 371 -12.376 14.121 -10.294 1.00 22.55 C
ANISOU 2984 C LEU A 371 2196 4582 1790 339 -63 -167 C
ATOM 2985 O LEU A 371 -12.465 13.918 -9.090 1.00 23.37 O
ANISOU 2985 O LEU A 371 2327 4617 1934 376 -86 -152 O
ATOM 2986 CB LEU A 371 -13.187 12.357 -11.942 1.00 19.08 C
ANISOU 2986 CB LEU A 371 1823 4101 1325 409 -33 -273 C
ATOM 2987 CG LEU A 371 -12.675 11.150 -11.100 1.00 23.76 C
ANISOU 2987 CG LEU A 371 2443 4631 1954 534 -37 -314 C
ATOM 2988 CD1 LEU A 371 -13.588 10.841 -9.880 1.00 23.65 C
ANISOU 2988 CD1 LEU A 371 2519 4462 2004 537 -64 -274 C
ATOM 2989 CD2 LEU A 371 -12.521 9.913 -11.971 1.00 26.10 C
ANISOU 2989 CD2 LEU A 371 2764 4920 2233 613 -11 -407 C
ATOM 2990 N LEU A 372 -11.341 14.767 -10.858 1.00 17.59 N
ANISOU 2990 N LEU A 372 1479 4096 1110 298 -44 -166 N
ATOM 2991 CA LEU A 372 -10.211 15.288 -10.097 1.00 16.17 C
ANISOU 2991 CA LEU A 372 1220 4004 920 288 -50 -155 C
ATOM 2992 C LEU A 372 -10.625 16.468 -9.224 1.00 20.84 C
ANISOU 2992 C LEU A 372 1842 4530 1547 195 -74 -93 C
ATOM 2993 O LEU A 372 -10.029 16.662 -8.165 1.00 22.13 O
ANISOU 2993 O LEU A 372 1970 4718 1720 204 -92 -92 O
ATOM 2994 CB LEU A 372 -9.047 15.678 -11.009 1.00 15.29 C
ANISOU 2994 CB LEU A 372 999 4074 737 248 -16 -173 C
ATOM 2995 CG LEU A 372 -8.265 14.536 -11.640 1.00 18.37 C
ANISOU 2995 CG LEU A 372 1328 4567 1085 363 10 -252 C
ATOM 2996 CD1 LEU A 372 -7.301 15.068 -12.692 1.00 17.63 C
ANISOU 2996 CD1 LEU A 372 1123 4668 908 298 51 -266 C
ATOM 2997 CD2 LEU A 372 -7.531 13.696 -10.585 1.00 18.81 C
ANISOU 2997 CD2 LEU A 372 1351 4634 1161 496 -12 -287 C
ATOM 2998 N ALA A 373 -11.649 17.236 -9.651 1.00 16.06 N
ANISOU 2998 N ALA A 373 1300 3846 956 116 -75 -47 N
ATOM 2999 CA ALA A 373 -12.193 18.383 -8.912 1.00 15.15 C
ANISOU 2999 CA ALA A 373 1231 3648 879 40 -95 4 C
ATOM 3000 C ALA A 373 -12.891 17.879 -7.662 1.00 18.18 C
ANISOU 3000 C ALA A 373 1669 3926 1314 101 -124 -3 C
ATOM 3001 O ALA A 373 -12.736 18.480 -6.590 1.00 17.40 O
ANISOU 3001 O ALA A 373 1571 3805 1236 73 -142 8 O
ATOM 3002 CB ALA A 373 -13.170 19.166 -9.784 1.00 15.68 C
ANISOU 3002 CB ALA A 373 1353 3660 944 -26 -91 54 C
ATOM 3003 N PHE A 374 -13.623 16.744 -7.790 1.00 13.52 N
ANISOU 3003 N PHE A 374 1124 3276 739 176 -125 -26 N
ATOM 3004 CA PHE A 374 -14.297 16.110 -6.649 1.00 12.34 C
ANISOU 3004 CA PHE A 374 1029 3030 629 228 -145 -27 C
ATOM 3005 C PHE A 374 -13.268 15.504 -5.673 1.00 16.13 C
ANISOU 3005 C PHE A 374 1472 3554 1103 300 -157 -44 C
ATOM 3006 O PHE A 374 -13.377 15.729 -4.468 1.00 15.36 O
ANISOU 3006 O PHE A 374 1389 3427 1021 301 -178 -26 O
ATOM 3007 CB PHE A 374 -15.345 15.073 -7.105 1.00 12.70 C
ANISOU 3007 CB PHE A 374 1138 2999 690 264 -139 -46 C
ATOM 3008 CG PHE A 374 -16.029 14.302 -5.997 1.00 12.80 C
ANISOU 3008 CG PHE A 374 1211 2915 736 305 -152 -41 C
ATOM 3009 CD1 PHE A 374 -16.699 14.965 -4.974 1.00 15.10 C
ANISOU 3009 CD1 PHE A 374 1527 3160 1051 269 -168 -8 C
ATOM 3010 CD2 PHE A 374 -16.048 12.912 -6.005 1.00 14.18 C
ANISOU 3010 CD2 PHE A 374 1429 3041 919 374 -144 -71 C
ATOM 3011 CE1 PHE A 374 -17.335 14.251 -3.956 1.00 15.80 C
ANISOU 3011 CE1 PHE A 374 1668 3176 1159 296 -174 1 C
ATOM 3012 CE2 PHE A 374 -16.723 12.198 -5.010 1.00 16.88 C
ANISOU 3012 CE2 PHE A 374 1838 3288 1288 396 -150 -55 C
ATOM 3013 CZ PHE A 374 -17.343 12.871 -3.979 1.00 14.89 C
ANISOU 3013 CZ PHE A 374 1597 3012 1049 354 -165 -15 C
ATOM 3014 N ILE A 375 -12.267 14.764 -6.193 1.00 13.28 N
ANISOU 3014 N ILE A 375 1058 3276 711 368 -144 -80 N
ATOM 3015 CA ILE A 375 -11.213 14.172 -5.363 1.00 14.06 C
ANISOU 3015 CA ILE A 375 1109 3439 796 459 -158 -95 C
ATOM 3016 C ILE A 375 -10.418 15.269 -4.618 1.00 19.88 C
ANISOU 3016 C ILE A 375 1769 4272 1511 394 -175 -81 C
ATOM 3017 O ILE A 375 -10.221 15.158 -3.419 1.00 20.34 O
ANISOU 3017 O ILE A 375 1826 4331 1570 429 -203 -69 O
ATOM 3018 CB ILE A 375 -10.293 13.195 -6.150 1.00 16.74 C
ANISOU 3018 CB ILE A 375 1399 3858 1104 561 -139 -145 C
ATOM 3019 CG1 ILE A 375 -11.100 11.989 -6.731 1.00 17.07 C
ANISOU 3019 CG1 ILE A 375 1534 3780 1170 624 -124 -173 C
ATOM 3020 CG2 ILE A 375 -9.138 12.708 -5.266 1.00 16.02 C
ANISOU 3020 CG2 ILE A 375 1244 3852 991 670 -161 -154 C
ATOM 3021 CD1 ILE A 375 -10.329 11.105 -7.852 1.00 17.50 C
ANISOU 3021 CD1 ILE A 375 1549 3906 1192 715 -95 -245 C
ATOM 3022 N LEU A 376 -10.023 16.337 -5.308 1.00 16.14 N
ANISOU 3022 N LEU A 376 1241 3877 1016 290 -158 -81 N
ATOM 3023 CA LEU A 376 -9.243 17.407 -4.702 1.00 16.09 C
ANISOU 3023 CA LEU A 376 1166 3958 988 203 -169 -78 C
ATOM 3024 C LEU A 376 -9.930 18.129 -3.535 1.00 20.48 C
ANISOU 3024 C LEU A 376 1781 4423 1578 151 -195 -56 C
ATOM 3025 O LEU A 376 -9.307 18.362 -2.508 1.00 20.86 O
ANISOU 3025 O LEU A 376 1784 4535 1609 150 -219 -69 O
ATOM 3026 CB LEU A 376 -8.826 18.418 -5.797 1.00 15.86 C
ANISOU 3026 CB LEU A 376 1094 4000 933 81 -138 -71 C
ATOM 3027 CG LEU A 376 -8.042 19.657 -5.369 1.00 19.43 C
ANISOU 3027 CG LEU A 376 1489 4527 1367 -49 -140 -69 C
ATOM 3028 CD1 LEU A 376 -6.627 19.303 -5.013 1.00 19.08 C
ANISOU 3028 CD1 LEU A 376 1311 4671 1270 -19 -146 -112 C
ATOM 3029 CD2 LEU A 376 -8.059 20.697 -6.470 1.00 21.28 C
ANISOU 3029 CD2 LEU A 376 1734 4762 1589 -182 -107 -37 C
ATOM 3030 N THR A 377 -11.179 18.529 -3.723 1.00 16.65 N
ANISOU 3030 N THR A 377 1388 3806 1133 109 -191 -29 N
ATOM 3031 CA THR A 377 -11.916 19.350 -2.772 1.00 15.69 C
ANISOU 3031 CA THR A 377 1323 3598 1042 58 -208 -16 C
ATOM 3032 C THR A 377 -12.549 18.582 -1.635 1.00 19.52 C
ANISOU 3032 C THR A 377 1851 4024 1540 138 -229 -14 C
ATOM 3033 O THR A 377 -12.775 19.175 -0.586 1.00 19.10 O
ANISOU 3033 O THR A 377 1813 3951 1491 108 -246 -19 O
ATOM 3034 CB THR A 377 -12.946 20.200 -3.507 1.00 18.72 C
ANISOU 3034 CB THR A 377 1776 3881 1458 -8 -194 13 C
ATOM 3035 OG1 THR A 377 -13.812 19.346 -4.250 1.00 17.04 O
ANISOU 3035 OG1 THR A 377 1604 3616 1255 52 -185 25 O
ATOM 3036 CG2 THR A 377 -12.300 21.275 -4.396 1.00 14.17 C
ANISOU 3036 CG2 THR A 377 1172 3349 865 -113 -174 27 C
ATOM 3037 N TRP A 378 -12.826 17.282 -1.821 1.00 16.19 N
ANISOU 3037 N TRP A 378 1455 3574 1121 233 -226 -8 N
ATOM 3038 CA TRP A 378 -13.443 16.442 -0.793 1.00 15.70 C
ANISOU 3038 CA TRP A 378 1447 3450 1067 301 -240 7 C
ATOM 3039 C TRP A 378 -12.459 15.591 -0.022 1.00 17.39 C
ANISOU 3039 C TRP A 378 1622 3740 1247 394 -261 6 C
ATOM 3040 O TRP A 378 -12.857 15.003 0.981 1.00 17.01 O
ANISOU 3040 O TRP A 378 1618 3650 1195 444 -275 31 O
ATOM 3041 CB TRP A 378 -14.566 15.578 -1.384 1.00 14.94 C
ANISOU 3041 CB TRP A 378 1427 3249 1000 330 -223 18 C
ATOM 3042 CG TRP A 378 -15.863 16.305 -1.561 1.00 16.11 C
ANISOU 3042 CG TRP A 378 1622 3322 1177 261 -215 28 C
ATOM 3043 CD1 TRP A 378 -16.098 17.392 -2.351 1.00 18.94 C
ANISOU 3043 CD1 TRP A 378 1970 3680 1544 192 -208 29 C
ATOM 3044 CD2 TRP A 378 -17.109 15.984 -0.937 1.00 16.46 C
ANISOU 3044 CD2 TRP A 378 1726 3289 1238 261 -214 43 C
ATOM 3045 NE1 TRP A 378 -17.405 17.782 -2.240 1.00 18.48 N
ANISOU 3045 NE1 TRP A 378 1959 3551 1510 167 -207 41 N
ATOM 3046 CE2 TRP A 378 -18.051 16.940 -1.370 1.00 20.21 C
ANISOU 3046 CE2 TRP A 378 2214 3732 1734 203 -209 44 C
ATOM 3047 CE3 TRP A 378 -17.514 15.000 -0.012 1.00 18.16 C
ANISOU 3047 CE3 TRP A 378 1985 3465 1450 303 -216 60 C
ATOM 3048 CZ2 TRP A 378 -19.380 16.933 -0.928 1.00 19.86 C
ANISOU 3048 CZ2 TRP A 378 2207 3635 1703 191 -205 51 C
ATOM 3049 CZ3 TRP A 378 -18.831 14.992 0.424 1.00 19.95 C
ANISOU 3049 CZ3 TRP A 378 2255 3636 1689 272 -208 71 C
ATOM 3050 CH2 TRP A 378 -19.749 15.950 -0.032 1.00 20.63 C
ANISOU 3050 CH2 TRP A 378 2336 3709 1793 219 -203 61 C
ATOM 3051 N THR A 379 -11.179 15.527 -0.459 1.00 13.49 N
ANISOU 3051 N THR A 379 1040 3366 721 422 -262 -17 N
ATOM 3052 CA THR A 379 -10.142 14.756 0.245 1.00 13.71 C
ANISOU 3052 CA THR A 379 1012 3489 708 531 -287 -18 C
ATOM 3053 C THR A 379 -9.873 15.342 1.650 1.00 19.84 C
ANISOU 3053 C THR A 379 1757 4331 1451 504 -322 -11 C
ATOM 3054 O THR A 379 -9.991 14.558 2.588 1.00 21.67 O
ANISOU 3054 O THR A 379 2023 4544 1666 592 -344 21 O
ATOM 3055 CB THR A 379 -8.876 14.553 -0.613 1.00 14.95 C
ANISOU 3055 CB THR A 379 1067 3782 834 574 -278 -53 C
ATOM 3056 OG1 THR A 379 -9.191 13.575 -1.601 1.00 12.68 O
ANISOU 3056 OG1 THR A 379 831 3414 574 647 -244 -62 O
ATOM 3057 CG2 THR A 379 -7.673 14.056 0.194 1.00 10.77 C
ANISOU 3057 CG2 THR A 379 527 3173 393 622 -24 -108 C
ATOM 3058 N PRO A 380 -9.560 16.659 1.861 1.00 16.39 N
ANISOU 3058 N PRO A 380 1267 3959 1002 383 -326 -40 N
ATOM 3059 CA PRO A 380 -9.313 17.147 3.240 1.00 15.99 C
ANISOU 3059 CA PRO A 380 1188 3977 912 359 -360 -49 C
ATOM 3060 C PRO A 380 -10.345 16.730 4.286 1.00 18.29 C
ANISOU 3060 C PRO A 380 1569 4173 1207 399 -372 -14 C
ATOM 3061 O PRO A 380 -9.934 16.183 5.310 1.00 17.51 O
ANISOU 3061 O PRO A 380 1449 4147 1057 475 -404 6 O
ATOM 3062 CB PRO A 380 -9.249 18.663 3.071 1.00 17.80 C
ANISOU 3062 CB PRO A 380 1394 4218 1152 202 -350 -91 C
ATOM 3063 CG PRO A 380 -8.722 18.833 1.700 1.00 22.43 C
ANISOU 3063 CG PRO A 380 1937 4835 1750 164 -321 -100 C
ATOM 3064 CD PRO A 380 -9.354 17.750 0.882 1.00 17.79 C
ANISOU 3064 CD PRO A 380 1412 4155 1194 261 -301 -67 C
ATOM 3065 N TYR A 381 -11.667 16.909 4.006 1.00 14.10 N
ANISOU 3065 N TYR A 381 1133 3497 728 355 -346 0 N
ATOM 3066 CA TYR A 381 -12.752 16.522 4.925 1.00 13.49 C
ANISOU 3066 CA TYR A 381 1136 3338 651 378 -347 32 C
ATOM 3067 C TYR A 381 -12.757 15.000 5.230 1.00 19.05 C
ANISOU 3067 C TYR A 381 1882 4018 1338 500 -354 88 C
ATOM 3068 O TYR A 381 -12.913 14.626 6.396 1.00 18.67 O
ANISOU 3068 O TYR A 381 1857 3990 1248 537 -373 122 O
ATOM 3069 CB TYR A 381 -14.131 17.030 4.442 1.00 13.99 C
ANISOU 3069 CB TYR A 381 1271 3275 769 311 -317 29 C
ATOM 3070 CG TYR A 381 -15.319 16.341 5.088 1.00 15.49 C
ANISOU 3070 CG TYR A 381 1538 3386 961 339 -307 66 C
ATOM 3071 CD1 TYR A 381 -15.836 16.787 6.304 1.00 17.29 C
ANISOU 3071 CD1 TYR A 381 1777 3633 1158 314 -314 60 C
ATOM 3072 CD2 TYR A 381 -15.925 15.240 4.487 1.00 16.24 C
ANISOU 3072 CD2 TYR A 381 1691 3395 1083 380 -287 101 C
ATOM 3073 CE1 TYR A 381 -16.908 16.136 6.917 1.00 16.65 C
ANISOU 3073 CE1 TYR A 381 1757 3500 1067 329 -299 98 C
ATOM 3074 CE2 TYR A 381 -16.977 14.564 5.105 1.00 16.85 C
ANISOU 3074 CE2 TYR A 381 1836 3408 1157 387 -274 138 C
ATOM 3075 CZ TYR A 381 -17.475 15.025 6.311 1.00 22.27 C
ANISOU 3075 CZ TYR A 381 2526 4126 1808 359 -279 140 C
ATOM 3076 OH TYR A 381 -18.525 14.364 6.896 1.00 23.30 O
ANISOU 3076 OH TYR A 381 2716 4209 1927 353 -259 178 O
ATOM 3077 N ASN A 382 -12.555 14.137 4.193 1.00 15.55 N
ANISOU 3077 N ASN A 382 1454 3530 923 562 -339 98 N
ATOM 3078 CA ASN A 382 -12.541 12.678 4.348 1.00 14.92 C
ANISOU 3078 CA ASN A 382 1435 3395 839 680 -341 147 C
ATOM 3079 C ASN A 382 -11.313 12.181 5.070 1.00 20.16 C
ANISOU 3079 C ASN A 382 2040 4177 1444 792 -379 167 C
ATOM 3080 O ASN A 382 -11.400 11.161 5.763 1.00 21.05 O
ANISOU 3080 O ASN A 382 2216 4247 1536 886 -392 227 O
ATOM 3081 CB ASN A 382 -12.765 11.960 3.030 1.00 15.23 C
ANISOU 3081 CB ASN A 382 1517 3344 927 708 -311 134 C
ATOM 3082 CG ASN A 382 -14.213 12.044 2.616 1.00 24.65 C
ANISOU 3082 CG ASN A 382 2789 4410 2165 622 -280 135 C
ATOM 3083 OD1 ASN A 382 -15.062 11.308 3.107 1.00 20.41 O
ANISOU 3083 OD1 ASN A 382 2339 3781 1637 629 -271 174 O
ATOM 3084 ND2 ASN A 382 -14.545 12.973 1.749 1.00 10.00 N
ANISOU 3084 ND2 ASN A 382 860 2467 474 518 -148 61 N
ATOM 3085 N ILE A 383 -10.193 12.924 4.989 1.00 16.34 N
ANISOU 3085 N ILE A 383 1435 3849 926 776 -399 122 N
ATOM 3086 CA ILE A 383 -8.997 12.575 5.756 1.00 16.37 C
ANISOU 3086 CA ILE A 383 1356 4005 859 878 -443 134 C
ATOM 3087 C ILE A 383 -9.262 12.923 7.213 1.00 21.10 C
ANISOU 3087 C ILE A 383 1963 4651 1403 850 -473 161 C
ATOM 3088 O ILE A 383 -8.901 12.143 8.092 1.00 21.28 O
ANISOU 3088 O ILE A 383 1992 4722 1370 963 -507 217 O
ATOM 3089 CB ILE A 383 -7.693 13.216 5.197 1.00 19.64 C
ANISOU 3089 CB ILE A 383 1621 4597 1245 861 -453 71 C
ATOM 3090 CG1 ILE A 383 -7.327 12.641 3.792 1.00 20.13 C
ANISOU 3090 CG1 ILE A 383 1670 4636 1343 922 -422 48 C
ATOM 3091 CG2 ILE A 383 -6.503 13.127 6.198 1.00 18.78 C
ANISOU 3091 CG2 ILE A 383 1399 4689 1046 942 -507 75 C
ATOM 3092 CD1 ILE A 383 -7.250 11.050 3.662 1.00 27.05 C
ANISOU 3092 CD1 ILE A 383 2617 5433 2229 1111 -425 91 C
ATOM 3093 N MET A 384 -9.947 14.074 7.463 1.00 17.70 N
ANISOU 3093 N MET A 384 1540 4199 985 707 -460 124 N
ATOM 3094 CA MET A 384 -10.341 14.534 8.806 1.00 16.05 C
ANISOU 3094 CA MET A 384 1342 4032 723 665 -480 131 C
ATOM 3095 C MET A 384 -11.273 13.513 9.451 1.00 21.29 C
ANISOU 3095 C MET A 384 2120 4590 1380 729 -473 213 C
ATOM 3096 O MET A 384 -11.076 13.198 10.612 1.00 21.79 O
ANISOU 3096 O MET A 384 2180 4731 1368 778 -504 255 O
ATOM 3097 CB MET A 384 -11.002 15.916 8.758 1.00 17.17 C
ANISOU 3097 CB MET A 384 1487 4142 896 513 -459 65 C
ATOM 3098 CG MET A 384 -10.028 17.021 8.540 1.00 18.77 C
ANISOU 3098 CG MET A 384 1585 4464 1084 429 -472 -11 C
ATOM 3099 SD MET A 384 -10.867 18.593 8.391 1.00 20.45 S
ANISOU 3099 SD MET A 384 1834 4588 1347 266 -443 -81 S
ATOM 3100 CE MET A 384 -9.852 19.374 7.175 1.00 16.32 C
ANISOU 3100 CE MET A 384 1231 4117 852 182 -433 -130 C
ATOM 3101 N VAL A 385 -12.230 12.950 8.678 1.00 18.72 N
ANISOU 3101 N VAL A 385 1890 4097 1124 725 -432 239 N
ATOM 3102 CA VAL A 385 -13.154 11.893 9.125 1.00 18.76 C
ANISOU 3102 CA VAL A 385 2012 3985 1131 764 -416 318 C
ATOM 3103 C VAL A 385 -12.341 10.621 9.507 1.00 26.25 C
ANISOU 3103 C VAL A 385 2985 4950 2037 919 -445 395 C
ATOM 3104 O VAL A 385 -12.542 10.061 10.580 1.00 26.87 O
ANISOU 3104 O VAL A 385 3116 5036 2058 961 -460 470 O
ATOM 3105 CB VAL A 385 -14.256 11.605 8.056 1.00 20.26 C
ANISOU 3105 CB VAL A 385 2284 4009 1405 711 -367 311 C
ATOM 3106 CG1 VAL A 385 -15.005 10.309 8.352 1.00 19.24 C
ANISOU 3106 CG1 VAL A 385 2276 3754 1280 751 -348 392 C
ATOM 3107 CG2 VAL A 385 -15.235 12.770 7.940 1.00 19.57 C
ANISOU 3107 CG2 VAL A 385 2185 3905 1346 582 -343 257 C
ATOM 3108 N LEU A 386 -11.412 10.210 8.634 1.00 24.78 N
ANISOU 3108 N LEU A 386 2761 4779 1876 1008 -453 376 N
ATOM 3109 CA LEU A 386 -10.522 9.063 8.796 1.00 25.28 C
ANISOU 3109 CA LEU A 386 2836 4860 1908 1181 -482 434 C
ATOM 3110 C LEU A 386 -9.744 9.169 10.103 1.00 28.96 C
ANISOU 3110 C LEU A 386 3234 5500 2271 1249 -538 474 C
ATOM 3111 O LEU A 386 -9.738 8.216 10.883 1.00 28.85 O
ANISOU 3111 O LEU A 386 3295 5455 2213 1357 -559 570 O
ATOM 3112 CB LEU A 386 -9.545 9.031 7.600 1.00 25.85 C
ANISOU 3112 CB LEU A 386 2826 4984 2014 1240 -481 368 C
ATOM 3113 CG LEU A 386 -8.869 7.715 7.220 1.00 31.48 C
ANISOU 3113 CG LEU A 386 3577 5650 2736 1426 -489 401 C
ATOM 3114 CD1 LEU A 386 -8.606 7.666 5.714 1.00 31.71 C
ANISOU 3114 CD1 LEU A 386 3576 5647 2826 1426 -455 321 C
ATOM 3115 CD2 LEU A 386 -7.551 7.536 7.959 1.00 34.90 C
ANISOU 3115 CD2 LEU A 386 3905 6271 3083 1572 -548 426 C
ATOM 3116 N VAL A 387 -9.112 10.329 10.359 1.00 25.64 N
ANISOU 3116 N VAL A 387 2676 5260 1806 1179 -564 403 N
ATOM 3117 CA VAL A 387 -8.288 10.521 11.560 1.00 25.60 C
ANISOU 3117 CA VAL A 387 2581 5454 1691 1230 -622 421 C
ATOM 3118 C VAL A 387 -9.162 10.634 12.856 1.00 27.82 C
ANISOU 3118 C VAL A 387 2932 5726 1913 1175 -626 475 C
ATOM 3119 O VAL A 387 -8.735 10.166 13.906 1.00 27.13 O
ANISOU 3119 O VAL A 387 2837 5741 1731 1270 -670 545 O
ATOM 3120 CB VAL A 387 -7.221 11.654 11.421 1.00 29.86 C
ANISOU 3120 CB VAL A 387 2947 6204 2196 1164 -649 319 C
ATOM 3121 CG1 VAL A 387 -6.365 11.453 10.176 1.00 29.32 C
ANISOU 3121 CG1 VAL A 387 2804 6164 2170 1223 -640 275 C
ATOM 3122 CG2 VAL A 387 -7.839 13.032 11.397 1.00 30.21 C
ANISOU 3122 CG2 VAL A 387 2977 6234 2268 967 -621 235 C
ATOM 3123 N SER A 388 -10.395 11.169 12.758 1.00 23.29 N
ANISOU 3123 N SER A 388 2427 5034 1389 1036 -579 448 N
ATOM 3124 CA SER A 388 -11.314 11.278 13.885 1.00 22.61 C
ANISOU 3124 CA SER A 388 2401 4940 1248 977 -571 488 C
ATOM 3125 C SER A 388 -11.781 9.899 14.423 1.00 30.48 C
ANISOU 3125 C SER A 388 3528 5835 2218 1073 -566 624 C
ATOM 3126 O SER A 388 -12.149 9.799 15.597 1.00 29.76 O
ANISOU 3126 O SER A 388 3466 5801 2039 1065 -576 683 O
ATOM 3127 CB SER A 388 -12.486 12.186 13.544 1.00 22.42 C
ANISOU 3127 CB SER A 388 2408 4824 1288 822 -520 419 C
ATOM 3128 OG SER A 388 -13.513 11.466 12.889 1.00 30.80 O
ANISOU 3128 OG SER A 388 3582 5695 2425 812 -472 464 O
ATOM 3129 N THR A 389 -11.732 8.841 13.580 1.00 29.95 N
ANISOU 3129 N THR A 389 3541 5619 2219 1161 -549 673 N
ATOM 3130 CA THR A 389 -12.096 7.475 13.987 1.00 30.97 C
ANISOU 3130 CA THR A 389 3813 5620 2335 1252 -542 804 C
ATOM 3131 C THR A 389 -11.001 6.846 14.867 1.00 39.43 C
ANISOU 3131 C THR A 389 4860 6817 3305 1422 -606 892 C
ATOM 3132 O THR A 389 -11.314 6.039 15.738 1.00 39.34 O
ANISOU 3132 O THR A 389 4948 6768 3230 1471 -613 1014 O
ATOM 3133 CB THR A 389 -12.446 6.580 12.787 1.00 34.98 C
ANISOU 3133 CB THR A 389 4426 5912 2952 1281 -501 812 C
ATOM 3134 OG1 THR A 389 -11.259 6.263 12.060 1.00 39.03 O
ANISOU 3134 OG1 THR A 389 4881 6460 3488 1419 -530 783 O
ATOM 3135 CG2 THR A 389 -13.507 7.188 11.875 1.00 30.60 C
ANISOU 3135 CG2 THR A 389 3884 5257 2487 1122 -445 727 C
ATOM 3136 N PHE A 390 -9.728 7.208 14.619 1.00 39.31 N
ANISOU 3136 N PHE A 390 4708 6959 3267 1509 -653 834 N
ATOM 3137 CA PHE A 390 -8.549 6.735 15.346 1.00 40.52 C
ANISOU 3137 CA PHE A 390 4801 7275 3320 1683 -723 900 C
ATOM 3138 C PHE A 390 -8.199 7.636 16.527 1.00 46.84 C
ANISOU 3138 C PHE A 390 5483 8319 3993 1630 -770 877 C
ATOM 3139 O PHE A 390 -7.419 7.228 17.390 1.00 46.91 O
ANISOU 3139 O PHE A 390 5457 8476 3892 1762 -831 954 O
ATOM 3140 CB PHE A 390 -7.336 6.644 14.406 1.00 42.84 C
ANISOU 3140 CB PHE A 390 4986 7645 3647 1802 -748 836 C
ATOM 3141 CG PHE A 390 -7.441 5.578 13.344 1.00 45.48 C
ANISOU 3141 CG PHE A 390 5433 7764 4082 1905 -714 861 C
ATOM 3142 CD1 PHE A 390 -7.123 4.252 13.631 1.00 49.38 C
ANISOU 3142 CD1 PHE A 390 6035 8169 4558 2104 -737 980 C
ATOM 3143 CD2 PHE A 390 -7.824 5.900 12.048 1.00 48.36 C
ANISOU 3143 CD2 PHE A 390 5801 8016 4557 1808 -660 764 C
ATOM 3144 CE1 PHE A 390 -7.212 3.264 12.643 1.00 50.67 C
ANISOU 3144 CE1 PHE A 390 6313 8120 4818 2198 -703 988 C
ATOM 3145 CE2 PHE A 390 -7.909 4.913 11.060 1.00 51.71 C
ANISOU 3145 CE2 PHE A 390 6329 8252 5069 1899 -628 772 C
ATOM 3146 CZ PHE A 390 -7.598 3.602 11.362 1.00 49.94 C
ANISOU 3146 CZ PHE A 390 6214 7929 4831 2091 -648 877 C
ATOM 3147 N CYS A 391 -8.742 8.862 16.559 1.00 45.19 N
ANISOU 3147 N CYS A 391 5214 8158 3797 1444 -745 769 N
ATOM 3148 CA CYS A 391 -8.452 9.813 17.624 1.00 46.16 C
ANISOU 3148 CA CYS A 391 5228 8504 3806 1374 -783 719 C
ATOM 3149 C CYS A 391 -9.652 10.685 17.971 1.00 49.81 C
ANISOU 3149 C CYS A 391 5730 8917 4279 1192 -736 663 C
ATOM 3150 O CYS A 391 -10.102 11.469 17.135 1.00 48.72 O
ANISOU 3150 O CYS A 391 5580 8696 4236 1070 -694 562 O
ATOM 3151 CB CYS A 391 -7.229 10.650 17.269 1.00 47.51 C
ANISOU 3151 CB CYS A 391 5219 8872 3960 1364 -824 603 C
ATOM 3152 SG CYS A 391 -6.736 11.823 18.560 1.00 52.18 S
ANISOU 3152 SG CYS A 391 5668 9751 4406 1267 -876 520 S
ATOM 3153 N LYS A 392 -10.153 10.562 19.218 1.00 47.43 N
ANISOU 3153 N LYS A 392 5471 8681 3870 1181 -744 729 N
ATOM 3154 CA LYS A 392 -11.320 11.324 19.684 1.00 47.65 C
ANISOU 3154 CA LYS A 392 5531 8683 3890 1026 -698 676 C
ATOM 3155 C LYS A 392 -11.023 12.807 19.934 1.00 50.53 C
ANISOU 3155 C LYS A 392 5770 9202 4226 907 -713 518 C
ATOM 3156 O LYS A 392 -10.212 13.142 20.811 1.00 50.35 O
ANISOU 3156 O LYS A 392 5650 9397 4085 929 -770 492 O
ATOM 3157 CB LYS A 392 -11.988 10.676 20.921 1.00 49.98 C
ANISOU 3157 CB LYS A 392 5912 9007 4071 1047 -694 798 C
ATOM 3158 CG LYS A 392 -12.668 9.332 20.647 1.00 60.49 C
ANISOU 3158 CG LYS A 392 7404 10128 5451 1105 -656 946 C
ATOM 3159 CD LYS A 392 -13.835 9.407 19.644 1.00 61.52 C
ANISOU 3159 CD LYS A 392 7611 10042 5721 993 -579 901 C
ATOM 3160 CE LYS A 392 -13.959 8.131 18.847 1.00 63.52 C
ANISOU 3160 CE LYS A 392 7991 10083 6062 1070 -556 1001 C
ATOM 3161 NZ LYS A 392 -12.819 7.943 17.905 1.00 67.89 N
ANISOU 3161 NZ LYS A 392 8494 10621 6681 1184 -592 969 N
ATOM 3162 N ASP A 393 -11.694 13.685 19.145 1.00 44.55 N
ANISOU 3162 N ASP A 393 5021 8328 3577 782 -661 412 N
ATOM 3163 CA ASP A 393 -11.607 15.152 19.193 1.00 43.81 C
ANISOU 3163 CA ASP A 393 4844 8311 3489 654 -660 256 C
ATOM 3164 C ASP A 393 -10.212 15.694 18.814 1.00 46.34 C
ANISOU 3164 C ASP A 393 5036 8765 3805 655 -708 177 C
ATOM 3165 O ASP A 393 -9.865 16.829 19.157 1.00 45.11 O
ANISOU 3165 O ASP A 393 4801 8724 3616 554 -723 55 O
ATOM 3166 CB ASP A 393 -12.099 15.716 20.552 1.00 45.99 C
ANISOU 3166 CB ASP A 393 5109 8716 3648 590 -663 214 C
ATOM 3167 CG ASP A 393 -13.458 15.207 21.001 1.00 54.95 C
ANISOU 3167 CG ASP A 393 6352 9754 4771 575 -610 285 C
ATOM 3168 OD1 ASP A 393 -14.405 15.217 20.173 1.00 52.62 O
ANISOU 3168 OD1 ASP A 393 6125 9277 4590 531 -553 279 O
ATOM 3169 OD2 ASP A 393 -13.580 14.810 22.182 1.00 65.32 O
ANISOU 3169 OD2 ASP A 393 7675 11190 5953 602 -625 346 O
ATOM 3170 N CYS A 394 -9.441 14.891 18.058 1.00 43.66 N
ANISOU 3170 N CYS A 394 4678 8408 3504 763 -727 238 N
ATOM 3171 CA CYS A 394 -8.124 15.235 17.529 1.00 43.84 C
ANISOU 3171 CA CYS A 394 4571 8559 3527 773 -765 174 C
ATOM 3172 C CYS A 394 -8.251 16.443 16.628 1.00 40.66 C
ANISOU 3172 C CYS A 394 4143 8082 3222 622 -727 50 C
ATOM 3173 O CYS A 394 -7.558 17.437 16.841 1.00 41.15 O
ANISOU 3173 O CYS A 394 4103 8284 3247 527 -750 -56 O
ATOM 3174 CB CYS A 394 -7.544 14.057 16.755 1.00 46.47 C
ANISOU 3174 CB CYS A 394 4912 8847 3898 929 -776 265 C
ATOM 3175 SG CYS A 394 -6.027 13.383 17.469 1.00 52.06 S
ANISOU 3175 SG CYS A 394 5492 9819 4468 1098 -864 317 S
ATOM 3176 N VAL A 395 -9.155 16.340 15.619 1.00 30.11 N
ANISOU 3176 N VAL A 395 2905 6526 2007 595 -669 66 N
ATOM 3177 CA VAL A 395 -9.431 17.331 14.588 1.00 26.25 C
ANISOU 3177 CA VAL A 395 2421 5930 1623 473 -628 -21 C
ATOM 3178 C VAL A 395 -9.967 18.612 15.205 1.00 25.91 C
ANISOU 3178 C VAL A 395 2385 5893 1567 336 -615 -122 C
ATOM 3179 O VAL A 395 -11.012 18.579 15.843 1.00 25.98 O
ANISOU 3179 O VAL A 395 2469 5841 1563 330 -593 -106 O
ATOM 3180 CB VAL A 395 -10.348 16.791 13.446 1.00 28.43 C
ANISOU 3180 CB VAL A 395 2801 5987 2013 495 -575 32 C
ATOM 3181 CG1 VAL A 395 -10.408 17.768 12.273 1.00 27.97 C
ANISOU 3181 CG1 VAL A 395 2733 5845 2050 387 -542 -44 C
ATOM 3182 CG2 VAL A 395 -9.896 15.421 12.963 1.00 27.61 C
ANISOU 3182 CG2 VAL A 395 2711 5862 1917 640 -586 126 C
ATOM 3183 N PRO A 396 -9.270 19.753 15.020 1.00 20.72 N
ANISOU 3183 N PRO A 396 1651 5307 914 223 -625 -231 N
ATOM 3184 CA PRO A 396 -9.766 21.018 15.588 1.00 20.26 C
ANISOU 3184 CA PRO A 396 1614 5231 852 95 -610 -341 C
ATOM 3185 C PRO A 396 -11.004 21.526 14.859 1.00 25.50 C
ANISOU 3185 C PRO A 396 2386 5673 1630 47 -552 -353 C
ATOM 3186 O PRO A 396 -11.209 21.194 13.694 1.00 25.41 O
ANISOU 3186 O PRO A 396 2409 5540 1706 72 -526 -301 O
ATOM 3187 CB PRO A 396 -8.585 21.981 15.388 1.00 21.58 C
ANISOU 3187 CB PRO A 396 1680 5514 1007 -18 -633 -443 C
ATOM 3188 CG PRO A 396 -7.403 21.115 15.044 1.00 25.50 C
ANISOU 3188 CG PRO A 396 2073 6154 1463 70 -670 -385 C
ATOM 3189 CD PRO A 396 -7.987 19.960 14.318 1.00 21.52 C
ANISOU 3189 CD PRO A 396 1644 5511 1020 200 -645 -265 C
ATOM 3190 N GLU A 397 -11.827 22.333 15.550 1.00 23.57 N
ANISOU 3190 N GLU A 397 2190 5388 1378 -15 -533 -426 N
ATOM 3191 CA GLU A 397 -13.042 22.962 15.016 1.00 23.83 C
ANISOU 3191 CA GLU A 397 2316 5232 1506 -51 -483 -452 C
ATOM 3192 C GLU A 397 -12.705 23.790 13.763 1.00 26.71 C
ANISOU 3192 C GLU A 397 2689 5488 1971 -130 -465 -488 C
ATOM 3193 O GLU A 397 -13.439 23.712 12.774 1.00 27.52 O
ANISOU 3193 O GLU A 397 2854 5441 2163 -111 -432 -444 O
ATOM 3194 CB GLU A 397 -13.710 23.849 16.089 1.00 25.72 C
ANISOU 3194 CB GLU A 397 2584 5484 1704 -101 -472 -553 C
ATOM 3195 CG GLU A 397 -14.487 23.075 17.146 1.00 43.14 C
ANISOU 3195 CG GLU A 397 4809 7756 3827 -27 -468 -504 C
ATOM 3196 CD GLU A 397 -14.881 23.891 18.366 1.00 82.18 C
ANISOU 3196 CD GLU A 397 9753 12778 8694 -74 -466 -616 C
ATOM 3197 OE1 GLU A 397 -15.826 24.707 18.257 1.00 87.34 O
ANISOU 3197 OE1 GLU A 397 10464 13318 9403 -102 -426 -689 O
ATOM 3198 OE2 GLU A 397 -14.245 23.715 19.432 1.00 80.96 O
ANISOU 3198 OE2 GLU A 397 9537 12806 8418 -74 -504 -636 O
ATOM 3199 N THR A 398 -11.562 24.530 13.791 1.00 21.04 N
ANISOU 3199 N THR A 398 1904 4861 1230 -224 -489 -563 N
ATOM 3200 CA THR A 398 -11.061 25.341 12.669 1.00 20.14 C
ANISOU 3200 CA THR A 398 1791 4667 1194 -321 -472 -593 C
ATOM 3201 C THR A 398 -10.849 24.470 11.430 1.00 21.89 C
ANISOU 3201 C THR A 398 1998 4854 1463 -256 -462 -491 C
ATOM 3202 O THR A 398 -11.191 24.900 10.334 1.00 21.81 O
ANISOU 3202 O THR A 398 2041 4707 1538 -293 -430 -476 O
ATOM 3203 CB THR A 398 -9.782 26.122 13.063 1.00 24.34 C
ANISOU 3203 CB THR A 398 2236 5339 1672 -446 -501 -690 C
ATOM 3204 OG1 THR A 398 -10.056 26.893 14.225 1.00 26.41 O
ANISOU 3204 OG1 THR A 398 2518 5629 1885 -502 -510 -796 O
ATOM 3205 CG2 THR A 398 -9.298 27.065 11.965 1.00 21.53 C
ANISOU 3205 CG2 THR A 398 1895 4892 1393 -574 -476 -722 C
ATOM 3206 N LEU A 399 -10.321 23.247 11.609 1.00 17.12 N
ANISOU 3206 N LEU A 399 1332 4372 803 -152 -489 -422 N
ATOM 3207 CA LEU A 399 -10.069 22.338 10.501 1.00 16.67 C
ANISOU 3207 CA LEU A 399 1260 4290 783 -78 -479 -339 C
ATOM 3208 C LEU A 399 -11.349 21.767 9.912 1.00 18.94 C
ANISOU 3208 C LEU A 399 1650 4408 1139 -9 -444 -271 C
ATOM 3209 O LEU A 399 -11.492 21.772 8.684 1.00 17.23 O
ANISOU 3209 O LEU A 399 1458 4100 991 -19 -418 -244 O
ATOM 3210 CB LEU A 399 -9.044 21.274 10.860 1.00 16.88 C
ANISOU 3210 CB LEU A 399 1191 4482 740 23 -508 -295 C
ATOM 3211 CG LEU A 399 -7.675 21.745 10.364 1.00 20.72 C
ANISOU 3211 CG LEU A 399 1562 5114 1197 -50 -534 -345 C
ATOM 3212 CD1 LEU A 399 -6.777 22.193 11.481 1.00 19.78 C
ANISOU 3212 CD1 LEU A 399 1342 5195 979 -102 -579 -416 C
ATOM 3213 CD2 LEU A 399 -7.088 20.827 9.328 1.00 21.88 C
ANISOU 3213 CD2 LEU A 399 1663 5289 1361 42 -528 -284 C
ATOM 3214 N TRP A 400 -12.332 21.418 10.763 1.00 15.73 N
ANISOU 3214 N TRP A 400 1301 3965 711 40 -441 -250 N
ATOM 3215 CA TRP A 400 -13.643 20.986 10.266 1.00 14.62 C
ANISOU 3215 CA TRP A 400 1246 3672 638 83 -400 -198 C
ATOM 3216 C TRP A 400 -14.215 22.089 9.402 1.00 16.60 C
ANISOU 3216 C TRP A 400 1545 3799 963 6 -375 -239 C
ATOM 3217 O TRP A 400 -14.584 21.817 8.273 1.00 17.86 O
ANISOU 3217 O TRP A 400 1735 3869 1182 24 -354 -196 O
ATOM 3218 CB TRP A 400 -14.600 20.645 11.423 1.00 13.43 C
ANISOU 3218 CB TRP A 400 1097 3447 560 123 -307 -176 C
ATOM 3219 CG TRP A 400 -14.291 19.347 12.107 1.00 13.87 C
ANISOU 3219 CG TRP A 400 1140 3588 543 211 -330 -107 C
ATOM 3220 CD1 TRP A 400 -13.958 19.169 13.417 1.00 16.88 C
ANISOU 3220 CD1 TRP A 400 1531 4184 696 233 -454 -108 C
ATOM 3221 CD2 TRP A 400 -14.282 18.044 11.508 1.00 13.30 C
ANISOU 3221 CD2 TRP A 400 1083 3444 527 293 -298 -25 C
ATOM 3222 NE1 TRP A 400 -13.725 17.837 13.671 1.00 16.41 N
ANISOU 3222 NE1 TRP A 400 1481 4154 601 334 -464 -9 N
ATOM 3223 CE2 TRP A 400 -13.918 17.122 12.518 1.00 17.31 C
ANISOU 3223 CE2 TRP A 400 1639 4154 785 375 -448 46 C
ATOM 3224 CE3 TRP A 400 -14.555 17.562 10.214 1.00 13.90 C
ANISOU 3224 CE3 TRP A 400 1230 3476 577 315 -350 14 C
ATOM 3225 CZ2 TRP A 400 -13.786 15.750 12.267 1.00 16.14 C
ANISOU 3225 CZ2 TRP A 400 1529 3968 637 476 -450 141 C
ATOM 3226 CZ3 TRP A 400 -14.446 16.202 9.972 1.00 15.29 C
ANISOU 3226 CZ3 TRP A 400 1457 3660 692 409 -395 99 C
ATOM 3227 CH2 TRP A 400 -14.057 15.312 10.985 1.00 16.00 C
ANISOU 3227 CH2 TRP A 400 1550 3823 705 490 -423 160 C
ATOM 3228 N GLU A 401 -14.165 23.350 9.884 1.00 13.47 N
ANISOU 3228 N GLU A 401 1140 3370 609 -75 -341 -316 N
ATOM 3229 CA GLU A 401 -14.639 24.560 9.188 1.00 13.44 C
ANISOU 3229 CA GLU A 401 1206 3263 639 -150 -350 -366 C
ATOM 3230 C GLU A 401 -14.034 24.771 7.809 1.00 17.67 C
ANISOU 3230 C GLU A 401 1732 3758 1223 -194 -341 -336 C
ATOM 3231 O GLU A 401 -14.762 25.123 6.884 1.00 17.68 O
ANISOU 3231 O GLU A 401 1792 3635 1289 -195 -317 -309 O
ATOM 3232 CB GLU A 401 -14.410 25.819 10.023 1.00 14.89 C
ANISOU 3232 CB GLU A 401 1399 3454 805 -239 -357 -472 C
ATOM 3233 CG GLU A 401 -15.373 25.989 11.178 1.00 29.43 C
ANISOU 3233 CG GLU A 401 3276 5292 2615 -203 -351 -519 C
ATOM 3234 CD GLU A 401 -15.216 27.278 11.964 1.00 56.37 C
ANISOU 3234 CD GLU A 401 6708 8697 6012 -287 -354 -643 C
ATOM 3235 OE1 GLU A 401 -15.458 27.246 13.193 1.00 46.26 O
ANISOU 3235 OE1 GLU A 401 5414 7501 4661 -268 -362 -696 O
ATOM 3236 OE2 GLU A 401 -14.861 28.318 11.360 1.00 52.78 O
ANISOU 3236 OE2 GLU A 401 6288 8151 5614 -375 -346 -687 O
ATOM 3237 N LEU A 402 -12.705 24.581 7.683 1.00 13.96 N
ANISOU 3237 N LEU A 402 1180 3409 715 -230 -360 -341 N
ATOM 3238 CA LEU A 402 -11.971 24.752 6.438 1.00 13.59 C
ANISOU 3238 CA LEU A 402 1105 3362 697 -281 -348 -317 C
ATOM 3239 C LEU A 402 -12.206 23.606 5.450 1.00 16.88 C
ANISOU 3239 C LEU A 402 1520 3762 1133 -186 -336 -235 C
ATOM 3240 O LEU A 402 -12.328 23.866 4.254 1.00 16.82 O
ANISOU 3240 O LEU A 402 1537 3685 1169 -215 -313 -206 O
ATOM 3241 CB LEU A 402 -10.472 24.984 6.698 1.00 13.72 C
ANISOU 3241 CB LEU A 402 1013 3519 681 -351 -338 -353 C
ATOM 3242 CG LEU A 402 -10.078 26.217 7.542 1.00 17.36 C
ANISOU 3242 CG LEU A 402 1474 4024 1097 -485 -380 -459 C
ATOM 3243 CD1 LEU A 402 -8.595 26.197 7.867 1.00 16.55 C
ANISOU 3243 CD1 LEU A 402 1241 4123 922 -552 -407 -503 C
ATOM 3244 CD2 LEU A 402 -10.463 27.537 6.848 1.00 17.72 C
ANISOU 3244 CD2 LEU A 402 1614 3902 1219 -598 -347 -482 C
ATOM 3245 N GLY A 403 -12.296 22.372 5.952 1.00 12.51 N
ANISOU 3245 N GLY A 403 935 3220 598 -73 -294 -191 N
ATOM 3246 CA GLY A 403 -12.576 21.191 5.140 1.00 12.01 C
ANISOU 3246 CA GLY A 403 880 3108 576 18 -260 -129 C
ATOM 3247 C GLY A 403 -13.970 21.231 4.539 1.00 18.36 C
ANISOU 3247 C GLY A 403 1788 3828 1359 25 -313 -107 C
ATOM 3248 O GLY A 403 -14.172 20.738 3.425 1.00 20.29 O
ANISOU 3248 O GLY A 403 2046 4031 1632 51 -296 -72 O
ATOM 3249 N TYR A 404 -14.948 21.822 5.277 1.00 14.00 N
ANISOU 3249 N TYR A 404 1289 3214 819 8 -309 -130 N
ATOM 3250 CA TYR A 404 -16.337 22.039 4.849 1.00 12.93 C
ANISOU 3250 CA TYR A 404 1221 2961 731 18 -287 -116 C
ATOM 3251 C TYR A 404 -16.359 23.051 3.703 1.00 18.68 C
ANISOU 3251 C TYR A 404 1973 3617 1508 -41 -273 -117 C
ATOM 3252 O TYR A 404 -17.144 22.892 2.775 1.00 18.54 O
ANISOU 3252 O TYR A 404 1988 3534 1524 -17 -258 -81 O
ATOM 3253 CB TYR A 404 -17.189 22.628 6.001 1.00 13.05 C
ANISOU 3253 CB TYR A 404 1268 2953 737 14 -286 -158 C
ATOM 3254 CG TYR A 404 -17.654 21.673 7.081 1.00 13.50 C
ANISOU 3254 CG TYR A 404 1324 3060 745 71 -289 -141 C
ATOM 3255 CD1 TYR A 404 -17.357 20.313 7.018 1.00 15.05 C
ANISOU 3255 CD1 TYR A 404 1507 3294 916 128 -295 -82 C
ATOM 3256 CD2 TYR A 404 -18.369 22.134 8.182 1.00 13.91 C
ANISOU 3256 CD2 TYR A 404 1393 3121 772 68 -285 -183 C
ATOM 3257 CE1 TYR A 404 -17.774 19.436 8.014 1.00 15.55 C
ANISOU 3257 CE1 TYR A 404 1585 3393 932 172 -296 -51 C
ATOM 3258 CE2 TYR A 404 -18.798 21.266 9.180 1.00 14.65 C
ANISOU 3258 CE2 TYR A 404 1485 3271 809 109 -284 -158 C
ATOM 3259 CZ TYR A 404 -18.499 19.918 9.091 1.00 24.23 C
ANISOU 3259 CZ TYR A 404 2695 4512 1999 157 -289 -85 C
ATOM 3260 OH TYR A 404 -18.935 19.059 10.063 1.00 28.54 O
ANISOU 3260 OH TYR A 404 3255 5101 2488 190 -286 -46 O
ATOM 3261 N TRP A 405 -15.537 24.114 3.803 1.00 17.32 N
ANISOU 3261 N TRP A 405 1788 3457 1335 -124 -278 -157 N
ATOM 3262 CA TRP A 405 -15.413 25.169 2.798 1.00 18.82 C
ANISOU 3262 CA TRP A 405 2012 3574 1566 -197 -263 -150 C
ATOM 3263 C TRP A 405 -14.830 24.625 1.520 1.00 21.83 C
ANISOU 3263 C TRP A 405 2357 3995 1943 -199 -253 -99 C
ATOM 3264 O TRP A 405 -15.266 25.013 0.442 1.00 22.52 O
ANISOU 3264 O TRP A 405 2484 4012 2060 -212 -238 -60 O
ATOM 3265 CB TRP A 405 -14.549 26.334 3.304 1.00 18.68 C
ANISOU 3265 CB TRP A 405 1991 3565 1543 -306 -268 -209 C
ATOM 3266 CG TRP A 405 -15.289 27.384 4.088 1.00 20.27 C
ANISOU 3266 CG TRP A 405 2265 3664 1771 -324 -266 -265 C
ATOM 3267 CD1 TRP A 405 -14.994 27.816 5.348 1.00 23.42 C
ANISOU 3267 CD1 TRP A 405 2655 4102 2143 -361 -280 -346 C
ATOM 3268 CD2 TRP A 405 -16.387 28.196 3.631 1.00 20.28 C
ANISOU 3268 CD2 TRP A 405 2360 3516 1832 -303 -252 -251 C
ATOM 3269 NE1 TRP A 405 -15.858 28.821 5.720 1.00 23.47 N
ANISOU 3269 NE1 TRP A 405 2746 3982 2188 -362 -270 -392 N
ATOM 3270 CE2 TRP A 405 -16.718 29.081 4.680 1.00 24.92 C
ANISOU 3270 CE2 TRP A 405 2994 4046 2428 -320 -254 -332 C
ATOM 3271 CE3 TRP A 405 -17.135 28.251 2.440 1.00 21.56 C
ANISOU 3271 CE3 TRP A 405 2565 3594 2031 -262 -239 -181 C
ATOM 3272 CZ2 TRP A 405 -17.764 30.013 4.574 1.00 24.05 C
ANISOU 3272 CZ2 TRP A 405 2976 3790 2371 -284 -242 -345 C
ATOM 3273 CZ3 TRP A 405 -18.172 29.167 2.339 1.00 22.81 C
ANISOU 3273 CZ3 TRP A 405 2809 3621 2238 -227 -233 -184 C
ATOM 3274 CH2 TRP A 405 -18.472 30.039 3.392 1.00 23.46 C
ANISOU 3274 CH2 TRP A 405 2940 3639 2336 -233 -233 -265 C
ATOM 3275 N LEU A 406 -13.852 23.724 1.633 1.00 17.63 N
ANISOU 3275 N LEU A 406 1747 3585 1367 -177 -262 -100 N
ATOM 3276 CA LEU A 406 -13.232 23.067 0.487 1.00 17.14 C
ANISOU 3276 CA LEU A 406 1639 3582 1292 -162 -250 -67 C
ATOM 3277 C LEU A 406 -14.227 22.173 -0.254 1.00 20.63 C
ANISOU 3277 C LEU A 406 2120 3965 1753 -80 -240 -26 C
ATOM 3278 O LEU A 406 -14.184 22.122 -1.477 1.00 19.49 O
ANISOU 3278 O LEU A 406 1975 3818 1612 -91 -223 2 O
ATOM 3279 CB LEU A 406 -11.971 22.298 0.897 1.00 17.14 C
ANISOU 3279 CB LEU A 406 1542 3732 1239 -133 -265 -87 C
ATOM 3280 CG LEU A 406 -10.771 23.176 1.199 1.00 22.57 C
ANISOU 3280 CG LEU A 406 2164 4517 1897 -239 -271 -130 C
ATOM 3281 CD1 LEU A 406 -9.741 22.428 1.998 1.00 23.48 C
ANISOU 3281 CD1 LEU A 406 2181 4790 1953 -188 -299 -157 C
ATOM 3282 CD2 LEU A 406 -10.166 23.755 -0.075 1.00 26.10 C
ANISOU 3282 CD2 LEU A 406 2584 4988 2344 -331 -244 -114 C
ATOM 3283 N CYS A 407 -15.162 21.516 0.478 1.00 17.53 N
ANISOU 3283 N CYS A 407 1762 3529 1367 -11 -248 -24 N
ATOM 3284 CA CYS A 407 -16.219 20.688 -0.128 1.00 16.90 C
ANISOU 3284 CA CYS A 407 1722 3394 1306 47 -237 6 C
ATOM 3285 C CYS A 407 -17.091 21.561 -1.021 1.00 19.48 C
ANISOU 3285 C CYS A 407 2093 3645 1665 13 -226 25 C
ATOM 3286 O CYS A 407 -17.459 21.147 -2.117 1.00 20.15 O
ANISOU 3286 O CYS A 407 2183 3722 1751 28 -216 49 O
ATOM 3287 CB CYS A 407 -17.050 19.988 0.944 1.00 16.61 C
ANISOU 3287 CB CYS A 407 1714 3333 1266 100 -243 5 C
ATOM 3288 SG CYS A 407 -16.211 18.596 1.733 1.00 20.22 S
ANISOU 3288 SG CYS A 407 2141 3860 1682 172 -256 13 S
ATOM 3289 N TYR A 408 -17.387 22.783 -0.544 1.00 14.38 N
ANISOU 3289 N TYR A 408 1478 2945 1039 -29 -229 11 N
ATOM 3290 CA TYR A 408 -18.171 23.807 -1.224 1.00 13.33 C
ANISOU 3290 CA TYR A 408 1398 2729 938 -48 -224 33 C
ATOM 3291 C TYR A 408 -17.470 24.342 -2.455 1.00 16.07 C
ANISOU 3291 C TYR A 408 1742 3083 1280 -106 -214 69 C
ATOM 3292 O TYR A 408 -18.151 24.635 -3.439 1.00 16.10 O
ANISOU 3292 O TYR A 408 1778 3046 1293 -96 -210 111 O
ATOM 3293 CB TYR A 408 -18.527 24.950 -0.258 1.00 13.79 C
ANISOU 3293 CB TYR A 408 1499 2718 1020 -68 -229 -2 C
ATOM 3294 CG TYR A 408 -19.640 24.630 0.721 1.00 15.11 C
ANISOU 3294 CG TYR A 408 1677 2872 1190 -4 -233 -29 C
ATOM 3295 CD1 TYR A 408 -20.569 23.626 0.454 1.00 16.41 C
ANISOU 3295 CD1 TYR A 408 1830 3056 1349 53 -229 -7 C
ATOM 3296 CD2 TYR A 408 -19.771 25.339 1.914 1.00 16.07 C
ANISOU 3296 CD2 TYR A 408 1820 2971 1317 -12 -237 -84 C
ATOM 3297 CE1 TYR A 408 -21.597 23.335 1.348 1.00 17.85 C
ANISOU 3297 CE1 TYR A 408 2014 3241 1525 96 -226 -29 C
ATOM 3298 CE2 TYR A 408 -20.789 25.047 2.823 1.00 16.73 C
ANISOU 3298 CE2 TYR A 408 1904 3063 1391 43 -234 -111 C
ATOM 3299 CZ TYR A 408 -21.708 24.056 2.526 1.00 24.46 C
ANISOU 3299 CZ TYR A 408 2865 4067 2361 94 -228 -79 C
ATOM 3300 OH TYR A 408 -22.756 23.829 3.376 1.00 26.43 O
ANISOU 3300 OH TYR A 408 3111 4336 2597 134 -219 -103 O
ATOM 3301 N VAL A 409 -16.117 24.449 -2.416 1.00 11.59 N
ANISOU 3301 N VAL A 409 1129 2587 689 -169 -209 55 N
ATOM 3302 CA VAL A 409 -15.268 24.913 -3.535 1.00 11.73 C
ANISOU 3302 CA VAL A 409 1129 2640 688 -243 -192 87 C
ATOM 3303 C VAL A 409 -15.459 24.013 -4.805 1.00 16.71 C
ANISOU 3303 C VAL A 409 1736 3321 1292 -198 -181 122 C
ATOM 3304 O VAL A 409 -15.330 24.516 -5.918 1.00 16.45 O
ANISOU 3304 O VAL A 409 1714 3292 1244 -244 -166 167 O
ATOM 3305 CB VAL A 409 -13.777 25.089 -3.092 1.00 15.23 C
ANISOU 3305 CB VAL A 409 1503 3182 1102 -321 -189 51 C
ATOM 3306 CG1 VAL A 409 -12.804 25.120 -4.267 1.00 14.32 C
ANISOU 3306 CG1 VAL A 409 1337 3155 948 -385 -165 79 C
ATOM 3307 CG2 VAL A 409 -13.608 26.343 -2.219 1.00 15.14 C
ANISOU 3307 CG2 VAL A 409 1533 3105 1114 -405 -195 18 C
ATOM 3308 N ASN A 410 -15.840 22.723 -4.635 1.00 13.49 N
ANISOU 3308 N ASN A 410 1306 2943 878 -112 -187 103 N
ATOM 3309 CA ASN A 410 -16.125 21.821 -5.752 1.00 13.98 C
ANISOU 3309 CA ASN A 410 1354 3040 917 -70 -177 116 C
ATOM 3310 C ASN A 410 -17.212 22.413 -6.668 1.00 19.50 C
ANISOU 3310 C ASN A 410 2104 3682 1623 -76 -177 162 C
ATOM 3311 O ASN A 410 -17.117 22.303 -7.891 1.00 18.92 O
ANISOU 3311 O ASN A 410 2018 3655 1515 -88 -166 188 O
ATOM 3312 CB ASN A 410 -16.568 20.445 -5.238 1.00 14.65 C
ANISOU 3312 CB ASN A 410 1435 3125 1006 12 -183 85 C
ATOM 3313 CG ASN A 410 -16.732 19.395 -6.316 1.00 32.73 C
ANISOU 3313 CG ASN A 410 3715 5449 3273 50 -171 78 C
ATOM 3314 OD1 ASN A 410 -16.104 19.432 -7.372 1.00 20.00 O
ANISOU 3314 OD1 ASN A 410 2069 3903 1626 29 -155 82 O
ATOM 3315 ND2 ASN A 410 -17.571 18.413 -6.063 1.00 35.27 N
ANISOU 3315 ND2 ASN A 410 4065 5729 3607 99 -175 62 N
ATOM 3316 N ALA A 411 -18.230 23.067 -6.058 1.00 17.49 N
ANISOU 3316 N ALA A 411 1900 3338 1405 -59 -192 170 N
ATOM 3317 CA ALA A 411 -19.347 23.718 -6.747 1.00 17.31 C
ANISOU 3317 CA ALA A 411 1923 3263 1390 -42 -200 215 C
ATOM 3318 C ALA A 411 -18.858 24.946 -7.536 1.00 21.90 C
ANISOU 3318 C ALA A 411 2539 3818 1963 -106 -193 274 C
ATOM 3319 O ALA A 411 -19.446 25.281 -8.557 1.00 21.77 O
ANISOU 3319 O ALA A 411 2546 3798 1927 -94 -197 328 O
ATOM 3320 CB ALA A 411 -20.421 24.117 -5.739 1.00 17.68 C
ANISOU 3320 CB ALA A 411 2006 3234 1478 2 -215 198 C
ATOM 3321 N THR A 412 -17.792 25.610 -7.054 1.00 19.15 N
ANISOU 3321 N THR A 412 2194 3458 1624 -181 -183 264 N
ATOM 3322 CA THR A 412 -17.172 26.766 -7.705 1.00 19.36 C
ANISOU 3322 CA THR A 412 2259 3454 1643 -270 -168 320 C
ATOM 3323 C THR A 412 -16.298 26.323 -8.883 1.00 22.48 C
ANISOU 3323 C THR A 412 2598 3968 1975 -318 -145 347 C
ATOM 3324 O THR A 412 -16.289 27.012 -9.897 1.00 22.04 O
ANISOU 3324 O THR A 412 2578 3903 1893 -363 -135 420 O
ATOM 3325 CB THR A 412 -16.270 27.569 -6.718 1.00 24.79 C
ANISOU 3325 CB THR A 412 2960 4103 2357 -357 -162 284 C
ATOM 3326 OG1 THR A 412 -16.831 27.554 -5.410 1.00 29.54 O
ANISOU 3326 OG1 THR A 412 3579 4646 3000 -306 -180 224 O
ATOM 3327 CG2 THR A 412 -16.036 29.008 -7.168 1.00 19.86 C
ANISOU 3327 CG2 THR A 412 2418 3381 1746 -451 -150 343 C
ATOM 3328 N ILE A 413 -15.523 25.223 -8.727 1.00 18.51 N
ANISOU 3328 N ILE A 413 2009 3579 1444 -306 -136 291 N
ATOM 3329 CA ILE A 413 -14.551 24.813 -9.741 1.00 18.38 C
ANISOU 3329 CA ILE A 413 1926 3693 1365 -347 -109 299 C
ATOM 3330 C ILE A 413 -15.170 23.889 -10.825 1.00 24.47 C
ANISOU 3330 C ILE A 413 2680 4522 2095 -279 -108 305 C
ATOM 3331 O ILE A 413 -14.591 23.788 -11.914 1.00 23.94 O
ANISOU 3331 O ILE A 413 2574 4556 1965 -316 -83 325 O
ATOM 3332 CB ILE A 413 -13.210 24.262 -9.147 1.00 20.44 C
ANISOU 3332 CB ILE A 413 2094 4065 1607 -369 -97 235 C
ATOM 3333 CG1 ILE A 413 -13.372 22.923 -8.403 1.00 20.65 C
ANISOU 3333 CG1 ILE A 413 2085 4115 1648 -258 -114 170 C
ATOM 3334 CG2 ILE A 413 -12.523 25.310 -8.262 1.00 19.19 C
ANISOU 3334 CG2 ILE A 413 1943 3875 1472 -468 -97 227 C
ATOM 3335 CD1 ILE A 413 -12.032 22.210 -8.123 1.00 19.12 C
ANISOU 3335 CD1 ILE A 413 1791 4056 1419 -248 -104 117 C
ATOM 3336 N ASN A 414 -16.358 23.294 -10.575 1.00 22.17 N
ANISOU 3336 N ASN A 414 2417 4175 1830 -193 -131 288 N
ATOM 3337 CA ASN A 414 -17.035 22.465 -11.587 1.00 22.66 C
ANISOU 3337 CA ASN A 414 2467 4292 1852 -144 -132 283 C
ATOM 3338 C ASN A 414 -17.311 23.211 -12.915 1.00 26.92 C
ANISOU 3338 C ASN A 414 3029 4862 2338 -180 -128 361 C
ATOM 3339 O ASN A 414 -16.933 22.674 -13.960 1.00 25.99 O
ANISOU 3339 O ASN A 414 2868 4854 2153 -189 -109 353 O
ATOM 3340 CB ASN A 414 -18.313 21.818 -11.047 1.00 24.41 C
ANISOU 3340 CB ASN A 414 2711 4454 2110 -69 -156 250 C
ATOM 3341 CG ASN A 414 -18.120 20.414 -10.554 1.00 49.86 C
ANISOU 3341 CG ASN A 414 5902 7702 5342 -22 -151 174 C
ATOM 3342 OD1 ASN A 414 -17.178 19.717 -10.934 1.00 47.54 O
ANISOU 3342 OD1 ASN A 414 5563 7483 5015 -19 -131 139 O
ATOM 3343 ND2 ASN A 414 -19.019 19.967 -9.700 1.00 42.24 N
ANISOU 3343 ND2 ASN A 414 4961 6673 4417 20 -167 149 N
ATOM 3344 N PRO A 415 -17.913 24.442 -12.917 1.00 23.94 N
ANISOU 3344 N PRO A 415 2721 4393 1981 -197 -144 438 N
ATOM 3345 CA PRO A 415 -18.138 25.149 -14.195 1.00 23.77 C
ANISOU 3345 CA PRO A 415 2729 4402 1900 -224 -142 530 C
ATOM 3346 C PRO A 415 -16.846 25.538 -14.917 1.00 27.67 C
ANISOU 3346 C PRO A 415 3200 4978 2336 -326 -104 569 C
ATOM 3347 O PRO A 415 -16.852 25.666 -16.138 1.00 26.67 O
ANISOU 3347 O PRO A 415 3070 4932 2131 -348 -94 627 O
ATOM 3348 CB PRO A 415 -18.919 26.394 -13.769 1.00 25.42 C
ANISOU 3348 CB PRO A 415 3029 4469 2162 -207 -167 598 C
ATOM 3349 CG PRO A 415 -19.474 26.072 -12.428 1.00 29.24 C
ANISOU 3349 CG PRO A 415 3515 4875 2720 -149 -185 525 C
ATOM 3350 CD PRO A 415 -18.434 25.244 -11.790 1.00 24.91 C
ANISOU 3350 CD PRO A 415 2904 4381 2179 -182 -164 445 C
ATOM 3351 N MET A 416 -15.748 25.722 -14.154 1.00 25.52 N
ANISOU 3351 N MET A 416 2904 4701 2092 -391 -83 534 N
ATOM 3352 CA MET A 416 -14.405 26.051 -14.655 1.00 25.57 C
ANISOU 3352 CA MET A 416 2867 4805 2045 -503 -41 555 C
ATOM 3353 C MET A 416 -13.820 24.868 -15.451 1.00 27.33 C
ANISOU 3353 C MET A 416 2988 5205 2191 -479 -16 496 C
ATOM 3354 O MET A 416 -13.114 25.091 -16.429 1.00 27.26 O
ANISOU 3354 O MET A 416 2943 5311 2103 -553 18 535 O
ATOM 3355 CB MET A 416 -13.454 26.418 -13.499 1.00 28.17 C
ANISOU 3355 CB MET A 416 3178 5102 2424 -570 -32 511 C
ATOM 3356 CG MET A 416 -13.944 27.539 -12.615 1.00 32.26 C
ANISOU 3356 CG MET A 416 3797 5441 3019 -593 -53 543 C
ATOM 3357 SD MET A 416 -12.635 28.021 -11.463 1.00 37.47 S
ANISOU 3357 SD MET A 416 4422 6103 3711 -707 -37 485 S
ATOM 3358 CE MET A 416 -13.564 29.060 -10.319 1.00 34.39 C
ANISOU 3358 CE MET A 416 4160 5488 3418 -687 -69 489 C
ATOM 3359 N CYS A 417 -14.114 23.621 -15.022 1.00 22.08 N
ANISOU 3359 N CYS A 417 2281 4558 1548 -379 -31 403 N
ATOM 3360 CA CYS A 417 -13.694 22.375 -15.668 1.00 21.13 C
ANISOU 3360 CA CYS A 417 2081 4575 1370 -331 -10 329 C
ATOM 3361 C CYS A 417 -14.302 22.260 -17.049 1.00 25.82 C
ANISOU 3361 C CYS A 417 2684 5240 1885 -325 -6 363 C
ATOM 3362 O CYS A 417 -13.595 21.888 -17.978 1.00 28.00 O
ANISOU 3362 O CYS A 417 2898 5663 2077 -349 28 345 O
ATOM 3363 CB CYS A 417 -14.044 21.168 -14.804 1.00 20.97 C
ANISOU 3363 CB CYS A 417 2052 4511 1405 -226 -30 236 C
ATOM 3364 SG CYS A 417 -13.095 21.055 -13.263 1.00 24.17 S
ANISOU 3364 SG CYS A 417 2422 4889 1874 -218 -34 186 S
ATOM 3365 N TYR A 418 -15.595 22.618 -17.202 1.00 21.35 N
ANISOU 3365 N TYR A 418 2188 4587 1336 -293 -42 414 N
ATOM 3366 CA TYR A 418 -16.305 22.640 -18.489 1.00 20.61 C
ANISOU 3366 CA TYR A 418 2105 4566 1161 -286 -49 459 C
ATOM 3367 C TYR A 418 -15.734 23.726 -19.386 1.00 26.50 C
ANISOU 3367 C TYR A 418 2865 5373 1832 -379 -24 570 C
ATOM 3368 O TYR A 418 -15.533 23.476 -20.571 1.00 27.43 O
ANISOU 3368 O TYR A 418 2943 5633 1844 -399 -3 579 O
ATOM 3369 CB TYR A 418 -17.821 22.866 -18.306 1.00 20.68 C
ANISOU 3369 CB TYR A 418 2174 4475 1207 -225 -98 492 C
ATOM 3370 CG TYR A 418 -18.567 21.622 -17.884 1.00 21.41 C
ANISOU 3370 CG TYR A 418 2245 4556 1334 -149 -117 387 C
ATOM 3371 CD1 TYR A 418 -18.650 21.254 -16.541 1.00 22.78 C
ANISOU 3371 CD1 TYR A 418 2429 4624 1601 -116 -125 331 C
ATOM 3372 CD2 TYR A 418 -19.157 20.786 -18.828 1.00 22.22 C
ANISOU 3372 CD2 TYR A 418 2318 4756 1367 -122 -124 341 C
ATOM 3373 CE1 TYR A 418 -19.289 20.081 -16.151 1.00 22.80 C
ANISOU 3373 CE1 TYR A 418 2421 4609 1631 -62 -137 243 C
ATOM 3374 CE2 TYR A 418 -19.824 19.623 -18.447 1.00 23.36 C
ANISOU 3374 CE2 TYR A 418 2451 4879 1544 -74 -137 241 C
ATOM 3375 CZ TYR A 418 -19.874 19.266 -17.108 1.00 32.26 C
ANISOU 3375 CZ TYR A 418 3598 5891 2769 -47 -141 197 C
ATOM 3376 OH TYR A 418 -20.513 18.108 -16.730 1.00 37.46 O
ANISOU 3376 OH TYR A 418 4256 6521 3457 -13 -148 108 O
ATOM 3377 N ALA A 419 -15.475 24.928 -18.833 1.00 23.09 N
ANISOU 3377 N ALA A 419 2493 4833 1449 -444 -23 652 N
ATOM 3378 CA ALA A 419 -14.923 26.048 -19.598 1.00 23.11 C
ANISOU 3378 CA ALA A 419 2529 4863 1389 -552 4 771 C
ATOM 3379 C ALA A 419 -13.489 25.803 -20.084 1.00 27.05 C
ANISOU 3379 C ALA A 419 2937 5528 1813 -644 62 741 C
ATOM 3380 O ALA A 419 -13.169 26.195 -21.197 1.00 27.39 O
ANISOU 3380 O ALA A 419 2973 5679 1753 -714 91 818 O
ATOM 3381 CB ALA A 419 -15.015 27.339 -18.800 1.00 23.85 C
ANISOU 3381 CB ALA A 419 2723 4775 1565 -601 -8 849 C
ATOM 3382 N LEU A 420 -12.648 25.128 -19.281 1.00 23.67 N
ANISOU 3382 N LEU A 420 2432 5137 1425 -638 78 633 N
ATOM 3383 CA LEU A 420 -11.259 24.815 -19.643 1.00 23.52 C
ANISOU 3383 CA LEU A 420 2304 5296 1336 -707 132 588 C
ATOM 3384 C LEU A 420 -11.138 23.688 -20.677 1.00 29.20 C
ANISOU 3384 C LEU A 420 2941 6195 1959 -645 154 516 C
ATOM 3385 O LEU A 420 -10.214 23.724 -21.488 1.00 29.93 O
ANISOU 3385 O LEU A 420 2958 6460 1952 -716 204 522 O
ATOM 3386 CB LEU A 420 -10.418 24.443 -18.402 1.00 23.18 C
ANISOU 3386 CB LEU A 420 2199 5246 1364 -700 135 495 C
ATOM 3387 CG LEU A 420 -10.076 25.553 -17.397 1.00 26.87 C
ANISOU 3387 CG LEU A 420 2715 5591 1902 -798 129 540 C
ATOM 3388 CD1 LEU A 420 -9.740 24.972 -16.047 1.00 25.91 C
ANISOU 3388 CD1 LEU A 420 2552 5432 1860 -737 107 440 C
ATOM 3389 CD2 LEU A 420 -8.945 26.434 -17.892 1.00 28.29 C
ANISOU 3389 CD2 LEU A 420 2854 5878 2016 -966 181 595 C
ATOM 3390 N CYS A 421 -12.034 22.675 -20.614 1.00 25.41 N
ANISOU 3390 N CYS A 421 2472 5678 1506 -520 120 440 N
ATOM 3391 CA CYS A 421 -12.038 21.464 -21.453 1.00 24.63 C
ANISOU 3391 CA CYS A 421 2309 5718 1333 -448 136 342 C
ATOM 3392 C CYS A 421 -12.916 21.523 -22.697 1.00 27.31 C
ANISOU 3392 C CYS A 421 2679 6120 1579 -447 126 390 C
ATOM 3393 O CYS A 421 -12.673 20.743 -23.617 1.00 27.62 O
ANISOU 3393 O CYS A 421 2655 6315 1524 -424 152 318 O
ATOM 3394 CB CYS A 421 -12.412 20.242 -20.614 1.00 24.84 C
ANISOU 3394 CB CYS A 421 2333 5663 1442 -328 110 220 C
ATOM 3395 SG CYS A 421 -11.264 19.869 -19.272 1.00 28.69 S
ANISOU 3395 SG CYS A 421 2762 6130 2009 -299 121 147 S
ATOM 3396 N ASN A 422 -13.984 22.342 -22.691 1.00 23.23 N
ANISOU 3396 N ASN A 422 2252 5488 1086 -453 83 496 N
ATOM 3397 CA ASN A 422 -14.978 22.390 -23.766 1.00 23.19 C
ANISOU 3397 CA ASN A 422 2274 5541 994 -434 59 544 C
ATOM 3398 C ASN A 422 -15.091 23.784 -24.408 1.00 26.96 C
ANISOU 3398 C ASN A 422 2814 6019 1412 -514 58 720 C
ATOM 3399 O ASN A 422 -15.616 24.706 -23.775 1.00 26.56 O
ANISOU 3399 O ASN A 422 2849 5802 1439 -517 27 812 O
ATOM 3400 CB ASN A 422 -16.323 21.939 -23.184 1.00 26.25 C
ANISOU 3400 CB ASN A 422 2707 5806 1461 -341 1 504 C
ATOM 3401 CG ASN A 422 -17.173 21.064 -24.067 1.00 63.14 C
ANISOU 3401 CG ASN A 422 7353 10582 6056 -290 -18 436 C
ATOM 3402 OD1 ASN A 422 -17.768 21.515 -25.057 1.00 58.93 O
ANISOU 3402 OD1 ASN A 422 6830 10135 5424 -303 -36 514 O
ATOM 3403 ND2 ASN A 422 -17.290 19.796 -23.689 1.00 57.73 N
ANISOU 3403 ND2 ASN A 422 6638 9883 5413 -233 -18 291 N
ATOM 3404 N LYS A 423 -14.603 23.929 -25.667 1.00 23.65 N
ANISOU 3404 N LYS A 423 2357 5781 849 -576 95 767 N
ATOM 3405 CA LYS A 423 -14.615 25.175 -26.458 1.00 23.68 C
ANISOU 3405 CA LYS A 423 2423 5807 769 -661 102 947 C
ATOM 3406 C LYS A 423 -16.009 25.819 -26.555 1.00 28.71 C
ANISOU 3406 C LYS A 423 3158 6328 1424 -597 35 1058 C
ATOM 3407 O LYS A 423 -16.134 27.028 -26.352 1.00 28.40 O
ANISOU 3407 O LYS A 423 3216 6156 1418 -636 25 1202 O
ATOM 3408 CB LYS A 423 -14.025 24.944 -27.863 1.00 26.45 C
ANISOU 3408 CB LYS A 423 2702 6405 942 -720 149 958 C
ATOM 3409 CG LYS A 423 -13.910 26.200 -28.737 1.00 42.38 C
ANISOU 3409 CG LYS A 423 4785 8460 2856 -821 165 1157 C
ATOM 3410 CD LYS A 423 -12.546 26.882 -28.622 1.00 53.80 C
ANISOU 3410 CD LYS A 423 6216 9936 4291 -972 235 1213 C
ATOM 3411 CE LYS A 423 -12.542 28.315 -29.102 1.00 64.14 C
ANISOU 3411 CE LYS A 423 7638 11181 5552 -1081 243 1430 C
ATOM 3412 NZ LYS A 423 -12.934 28.432 -30.534 1.00 73.01 N
ANISOU 3412 NZ LYS A 423 8768 12472 6499 -1086 243 1535 N
ATOM 3413 N ALA A 424 -17.043 25.008 -26.855 1.00 26.24 N
ANISOU 3413 N ALA A 424 2819 6065 1087 -497 -9 986 N
ATOM 3414 CA ALA A 424 -18.437 25.455 -26.965 1.00 26.18 C
ANISOU 3414 CA ALA A 424 2876 5987 1085 -416 -78 1068 C
ATOM 3415 C ALA A 424 -18.955 26.070 -25.647 1.00 29.26 C
ANISOU 3415 C ALA A 424 3344 6138 1636 -370 -112 1095 C
ATOM 3416 O ALA A 424 -19.638 27.090 -25.697 1.00 30.08 O
ANISOU 3416 O ALA A 424 3533 6147 1749 -338 -149 1229 O
ATOM 3417 CB ALA A 424 -19.331 24.310 -27.416 1.00 26.88 C
ANISOU 3417 CB ALA A 424 2897 6195 1120 -338 -112 950 C
ATOM 3418 N PHE A 425 -18.582 25.501 -24.485 1.00 23.21 N
ANISOU 3418 N PHE A 425 2553 5279 988 -362 -99 974 N
ATOM 3419 CA PHE A 425 -18.965 26.052 -23.175 1.00 21.75 C
ANISOU 3419 CA PHE A 425 2434 4883 947 -327 -124 985 C
ATOM 3420 C PHE A 425 -18.274 27.392 -22.904 1.00 27.25 C
ANISOU 3420 C PHE A 425 3216 5459 1677 -411 -101 1109 C
ATOM 3421 O PHE A 425 -18.950 28.360 -22.575 1.00 26.31 O
ANISOU 3421 O PHE A 425 3193 5194 1611 -374 -134 1205 O
ATOM 3422 CB PHE A 425 -18.694 25.060 -22.036 1.00 21.68 C
ANISOU 3422 CB PHE A 425 2376 4824 1038 -302 -115 830 C
ATOM 3423 CG PHE A 425 -19.831 24.115 -21.746 1.00 21.42 C
ANISOU 3423 CG PHE A 425 2314 4790 1035 -208 -155 735 C
ATOM 3424 CD1 PHE A 425 -20.962 24.548 -21.066 1.00 23.42 C
ANISOU 3424 CD1 PHE A 425 2614 4922 1361 -138 -202 764 C
ATOM 3425 CD2 PHE A 425 -19.766 22.783 -22.141 1.00 22.41 C
ANISOU 3425 CD2 PHE A 425 2365 5034 1115 -193 -143 609 C
ATOM 3426 CE1 PHE A 425 -22.008 23.662 -20.774 1.00 24.01 C
ANISOU 3426 CE1 PHE A 425 2653 5011 1459 -70 -234 674 C
ATOM 3427 CE2 PHE A 425 -20.806 21.895 -21.838 1.00 25.03 C
ANISOU 3427 CE2 PHE A 425 2678 5356 1478 -129 -175 519 C
ATOM 3428 CZ PHE A 425 -21.917 22.340 -21.147 1.00 23.02 C
ANISOU 3428 CZ PHE A 425 2460 4994 1291 -76 -220 554 C
ATOM 3429 N ARG A 426 -16.940 27.444 -23.088 1.00 25.67 N
ANISOU 3429 N ARG A 426 2982 5330 1443 -525 -43 1103 N
ATOM 3430 CA ARG A 426 -16.079 28.624 -22.930 1.00 25.94 C
ANISOU 3430 CA ARG A 426 3084 5279 1494 -646 -8 1207 C
ATOM 3431 C ARG A 426 -16.581 29.821 -23.775 1.00 29.84 C
ANISOU 3431 C ARG A 426 3689 5722 1926 -664 -23 1395 C
ATOM 3432 O ARG A 426 -16.646 30.948 -23.273 1.00 29.45 O
ANISOU 3432 O ARG A 426 3755 5485 1949 -695 -29 1488 O
ATOM 3433 CB ARG A 426 -14.654 28.254 -23.355 1.00 25.53 C
ANISOU 3433 CB ARG A 426 2937 5394 1367 -762 60 1163 C
ATOM 3434 CG ARG A 426 -13.540 29.198 -22.898 1.00 30.78 C
ANISOU 3434 CG ARG A 426 3636 5993 2065 -912 104 1217 C
ATOM 3435 CD ARG A 426 -12.229 28.796 -23.559 1.00 32.46 C
ANISOU 3435 CD ARG A 426 3735 6425 2173 -1021 172 1182 C
ATOM 3436 NE ARG A 426 -12.051 27.345 -23.501 1.00 39.40 N
ANISOU 3436 NE ARG A 426 4484 7447 3037 -930 175 1017 N
ATOM 3437 CZ ARG A 426 -11.562 26.596 -24.479 1.00 50.75 C
ANISOU 3437 CZ ARG A 426 5823 9107 4355 -934 212 968 C
ATOM 3438 NH1 ARG A 426 -11.140 27.156 -25.605 1.00 41.59 N
ANISOU 3438 NH1 ARG A 426 4661 8077 3065 -1036 252 1074 N
ATOM 3439 NH2 ARG A 426 -11.464 25.282 -24.330 1.00 35.56 N
ANISOU 3439 NH2 ARG A 426 3802 7274 2435 -836 212 811 N
ATOM 3440 N ASP A 427 -16.947 29.569 -25.038 1.00 26.26 N
ANISOU 3440 N ASP A 427 3208 5432 1340 -640 -30 1450 N
ATOM 3441 CA ASP A 427 -17.437 30.621 -25.931 1.00 26.22 C
ANISOU 3441 CA ASP A 427 3305 5400 1256 -643 -49 1640 C
ATOM 3442 C ASP A 427 -18.853 31.073 -25.571 1.00 29.85 C
ANISOU 3442 C ASP A 427 3848 5711 1784 -496 -123 1692 C
ATOM 3443 O ASP A 427 -19.151 32.261 -25.697 1.00 30.57 O
ANISOU 3443 O ASP A 427 4067 5661 1886 -491 -140 1850 O
ATOM 3444 CB ASP A 427 -17.334 30.200 -27.404 1.00 28.00 C
ANISOU 3444 CB ASP A 427 3466 5873 1299 -667 -34 1683 C
ATOM 3445 CG ASP A 427 -15.923 29.916 -27.899 1.00 37.50 C
ANISOU 3445 CG ASP A 427 4588 7243 2416 -812 46 1649 C
ATOM 3446 OD1 ASP A 427 -14.958 30.473 -27.315 1.00 35.69 O
ANISOU 3446 OD1 ASP A 427 4384 6927 2250 -929 92 1662 O
ATOM 3447 OD2 ASP A 427 -15.785 29.158 -28.889 1.00 46.16 O
ANISOU 3447 OD2 ASP A 427 5591 8570 3376 -812 63 1605 O
ATOM 3448 N THR A 428 -19.711 30.147 -25.099 1.00 24.26 N
ANISOU 3448 N THR A 428 3069 5028 1123 -377 -166 1562 N
ATOM 3449 CA THR A 428 -21.069 30.499 -24.697 1.00 23.72 C
ANISOU 3449 CA THR A 428 3053 4846 1115 -233 -234 1592 C
ATOM 3450 C THR A 428 -21.043 31.276 -23.376 1.00 28.83 C
ANISOU 3450 C THR A 428 3792 5244 1918 -226 -234 1591 C
ATOM 3451 O THR A 428 -21.817 32.217 -23.231 1.00 28.68 O
ANISOU 3451 O THR A 428 3874 5085 1939 -142 -273 1692 O
ATOM 3452 CB THR A 428 -22.002 29.283 -24.708 1.00 29.76 C
ANISOU 3452 CB THR A 428 3706 5737 1862 -132 -274 1459 C
ATOM 3453 OG1 THR A 428 -21.807 28.563 -25.926 1.00 25.28 O
ANISOU 3453 OG1 THR A 428 3056 5401 1147 -166 -262 1441 O
ATOM 3454 CG2 THR A 428 -23.464 29.678 -24.617 1.00 30.09 C
ANISOU 3454 CG2 THR A 428 3779 5731 1923 14 -345 1511 C
ATOM 3455 N PHE A 429 -20.128 30.910 -22.436 1.00 25.87 N
ANISOU 3455 N PHE A 429 3384 4821 1626 -308 -192 1477 N
ATOM 3456 CA PHE A 429 -19.939 31.593 -21.146 1.00 25.23 C
ANISOU 3456 CA PHE A 429 3379 4525 1681 -324 -186 1455 C
ATOM 3457 C PHE A 429 -19.533 33.035 -21.445 1.00 30.85 C
ANISOU 3457 C PHE A 429 4234 5094 2394 -402 -169 1616 C
ATOM 3458 O PHE A 429 -20.121 33.962 -20.891 1.00 29.85 O
ANISOU 3458 O PHE A 429 4222 4771 2349 -338 -196 1671 O
ATOM 3459 CB PHE A 429 -18.818 30.922 -20.323 1.00 25.91 C
ANISOU 3459 CB PHE A 429 3388 4638 1817 -420 -140 1320 C
ATOM 3460 CG PHE A 429 -19.132 29.704 -19.484 1.00 26.08 C
ANISOU 3460 CG PHE A 429 3313 4704 1893 -347 -155 1157 C
ATOM 3461 CD1 PHE A 429 -20.166 28.841 -19.833 1.00 28.02 C
ANISOU 3461 CD1 PHE A 429 3500 5044 2103 -238 -193 1111 C
ATOM 3462 CD2 PHE A 429 -18.331 29.366 -18.400 1.00 26.94 C
ANISOU 3462 CD2 PHE A 429 3385 4774 2075 -398 -130 1051 C
ATOM 3463 CE1 PHE A 429 -20.408 27.680 -19.095 1.00 28.61 C
ANISOU 3463 CE1 PHE A 429 3495 5150 2224 -189 -200 968 C
ATOM 3464 CE2 PHE A 429 -18.585 28.215 -17.654 1.00 29.59 C
ANISOU 3464 CE2 PHE A 429 3643 5147 2454 -332 -142 917 C
ATOM 3465 CZ PHE A 429 -19.621 27.379 -18.006 1.00 27.67 C
ANISOU 3465 CZ PHE A 429 3355 4975 2181 -232 -174 879 C
ATOM 3466 N ARG A 430 -18.551 33.204 -22.361 1.00 29.52 N
ANISOU 3466 N ARG A 430 4060 5029 2128 -538 -121 1691 N
ATOM 3467 CA ARG A 430 -18.023 34.487 -22.825 1.00 30.48 C
ANISOU 3467 CA ARG A 430 4316 5039 2225 -649 -92 1857 C
ATOM 3468 C ARG A 430 -19.151 35.314 -23.465 1.00 35.67 C
ANISOU 3468 C ARG A 430 5094 5608 2852 -526 -144 2020 C
ATOM 3469 O ARG A 430 -19.394 36.438 -23.017 1.00 36.18 O
ANISOU 3469 O ARG A 430 5311 5439 2998 -512 -155 2106 O
ATOM 3470 CB ARG A 430 -16.857 34.261 -23.805 1.00 32.23 C
ANISOU 3470 CB ARG A 430 4473 5453 2321 -811 -30 1894 C
ATOM 3471 CG ARG A 430 -15.989 35.488 -24.047 1.00 48.19 C
ANISOU 3471 CG ARG A 430 6616 7363 4330 -985 20 2036 C
ATOM 3472 CD ARG A 430 -14.758 35.162 -24.870 1.00 65.64 C
ANISOU 3472 CD ARG A 430 8731 9794 6414 -1154 90 2047 C
ATOM 3473 NE ARG A 430 -13.729 34.471 -24.082 1.00 81.77 N
ANISOU 3473 NE ARG A 430 10646 11921 8502 -1241 131 1877 N
ATOM 3474 CZ ARG A 430 -13.448 33.172 -24.176 1.00 97.27 C
ANISOU 3474 CZ ARG A 430 12440 14099 10419 -1198 140 1734 C
ATOM 3475 NH1 ARG A 430 -14.119 32.398 -25.023 1.00 84.32 N
ANISOU 3475 NH1 ARG A 430 10739 12611 8687 -1084 113 1725 N
ATOM 3476 NH2 ARG A 430 -12.493 32.638 -23.427 1.00 83.83 N
ANISOU 3476 NH2 ARG A 430 10633 12460 8759 -1266 174 1595 N
ATOM 3477 N LEU A 431 -19.881 34.729 -24.449 1.00 31.65 N
ANISOU 3477 N LEU A 431 4514 5282 2228 -426 -181 2051 N
ATOM 3478 CA LEU A 431 -21.027 35.356 -25.118 1.00 31.60 C
ANISOU 3478 CA LEU A 431 4591 5244 2173 -284 -241 2199 C
ATOM 3479 C LEU A 431 -22.052 35.877 -24.104 1.00 35.79 C
ANISOU 3479 C LEU A 431 5198 5564 2838 -128 -293 2178 C
ATOM 3480 O LEU A 431 -22.453 37.032 -24.206 1.00 35.86 O
ANISOU 3480 O LEU A 431 5359 5397 2870 -68 -316 2324 O
ATOM 3481 CB LEU A 431 -21.702 34.373 -26.096 1.00 31.85 C
ANISOU 3481 CB LEU A 431 4492 5541 2068 -198 -278 2173 C
ATOM 3482 CG LEU A 431 -22.890 34.924 -26.902 1.00 36.80 C
ANISOU 3482 CG LEU A 431 5176 6193 2613 -46 -347 2327 C
ATOM 3483 CD1 LEU A 431 -22.643 34.811 -28.378 1.00 36.94 C
ANISOU 3483 CD1 LEU A 431 5157 6439 2440 -99 -339 2433 C
ATOM 3484 CD2 LEU A 431 -24.185 34.233 -26.523 1.00 39.37 C
ANISOU 3484 CD2 LEU A 431 5412 6574 2973 132 -416 2220 C
ATOM 3485 N LEU A 432 -22.456 35.034 -23.129 1.00 32.01 N
ANISOU 3485 N LEU A 432 4619 5101 2444 -62 -309 1998 N
ATOM 3486 CA LEU A 432 -23.435 35.381 -22.093 1.00 31.81 C
ANISOU 3486 CA LEU A 432 4636 4912 2538 85 -353 1950 C
ATOM 3487 C LEU A 432 -22.957 36.511 -21.170 1.00 38.62 C
ANISOU 3487 C LEU A 432 5651 5497 3525 33 -327 1976 C
ATOM 3488 O LEU A 432 -23.748 37.394 -20.839 1.00 38.89 O
ANISOU 3488 O LEU A 432 5797 5358 3624 161 -363 2036 O
ATOM 3489 CB LEU A 432 -23.854 34.145 -21.267 1.00 31.17 C
ANISOU 3489 CB LEU A 432 4409 4930 2506 137 -365 1753 C
ATOM 3490 CG LEU A 432 -24.613 33.012 -21.989 1.00 34.57 C
ANISOU 3490 CG LEU A 432 4695 5604 2835 210 -400 1699 C
ATOM 3491 CD1 LEU A 432 -24.676 31.768 -21.129 1.00 34.17 C
ANISOU 3491 CD1 LEU A 432 4521 5621 2839 205 -392 1506 C
ATOM 3492 CD2 LEU A 432 -26.003 33.439 -22.427 1.00 35.43 C
ANISOU 3492 CD2 LEU A 432 4820 5738 2906 386 -470 1785 C
ATOM 3493 N LEU A 433 -21.670 36.484 -20.762 1.00 36.39 N
ANISOU 3493 N LEU A 433 5371 5181 3276 -151 -265 1923 N
ATOM 3494 CA LEU A 433 -21.077 37.500 -19.890 1.00 36.14 C
ANISOU 3494 CA LEU A 433 5474 4902 3354 -238 -234 1927 C
ATOM 3495 C LEU A 433 -20.987 38.852 -20.592 1.00 43.30 C
ANISOU 3495 C LEU A 433 6570 5641 4241 -272 -228 2128 C
ATOM 3496 O LEU A 433 -21.303 39.875 -19.980 1.00 43.20 O
ANISOU 3496 O LEU A 433 6709 5377 4327 -225 -238 2161 O
ATOM 3497 CB LEU A 433 -19.707 37.056 -19.347 1.00 35.35 C
ANISOU 3497 CB LEU A 433 5303 4853 3276 -432 -173 1815 C
ATOM 3498 CG LEU A 433 -19.726 35.992 -18.250 1.00 39.16 C
ANISOU 3498 CG LEU A 433 5648 5413 3818 -397 -178 1617 C
ATOM 3499 CD1 LEU A 433 -18.355 35.424 -18.037 1.00 39.52 C
ANISOU 3499 CD1 LEU A 433 5600 5568 3846 -571 -124 1532 C
ATOM 3500 CD2 LEU A 433 -20.269 36.538 -16.937 1.00 40.05 C
ANISOU 3500 CD2 LEU A 433 5833 5323 4061 -314 -200 1542 C
ATOM 3501 N LEU A 434 -20.606 38.847 -21.883 1.00 41.90 N
ANISOU 3501 N LEU A 434 6388 5600 3931 -347 -211 2262 N
ATOM 3502 CA LEU A 434 -20.508 40.045 -22.717 1.00 43.12 C
ANISOU 3502 CA LEU A 434 6722 5622 4040 -388 -203 2479 C
ATOM 3503 C LEU A 434 -21.897 40.635 -23.001 1.00 49.46 C
ANISOU 3503 C LEU A 434 7623 6321 4847 -152 -276 2593 C
ATOM 3504 O LEU A 434 -22.045 41.856 -23.012 1.00 49.28 O
ANISOU 3504 O LEU A 434 7799 6052 4873 -129 -280 2729 O
ATOM 3505 CB LEU A 434 -19.772 39.735 -24.035 1.00 43.50 C
ANISOU 3505 CB LEU A 434 6712 5892 3924 -523 -166 2583 C
ATOM 3506 CG LEU A 434 -18.241 39.632 -23.954 1.00 48.67 C
ANISOU 3506 CG LEU A 434 7326 6604 4561 -783 -82 2539 C
ATOM 3507 CD1 LEU A 434 -17.706 38.682 -24.999 1.00 48.70 C
ANISOU 3507 CD1 LEU A 434 7169 6927 4408 -856 -54 2531 C
ATOM 3508 CD2 LEU A 434 -17.587 40.990 -24.131 1.00 52.17 C
ANISOU 3508 CD2 LEU A 434 7969 6833 5020 -942 -38 2702 C
ATOM 3509 N ALA A 435 -22.909 39.764 -23.204 1.00 48.08 N
ANISOU 3509 N ALA A 435 7309 6335 4624 23 -334 2533 N
ATOM 3510 CA ALA A 435 -24.303 40.146 -23.456 1.00 48.73 C
ANISOU 3510 CA ALA A 435 7435 6382 4697 266 -410 2617 C
ATOM 3511 C ALA A 435 -24.918 40.794 -22.218 1.00 54.01 C
ANISOU 3511 C ALA A 435 8195 6801 5526 394 -432 2545 C
ATOM 3512 O ALA A 435 -25.695 41.734 -22.342 1.00 52.92 O
ANISOU 3512 O ALA A 435 8189 6505 5411 558 -475 2663 O
ATOM 3513 CB ALA A 435 -25.120 38.926 -23.859 1.00 49.45 C
ANISOU 3513 CB ALA A 435 7326 6766 4698 381 -458 2532 C
ATOM 3514 N ARG A 436 -24.570 40.289 -21.029 1.00 52.92 N
ANISOU 3514 N ARG A 436 7985 6633 5490 330 -403 2351 N
ATOM 3515 CA ARG A 436 -25.056 40.819 -19.757 1.00 53.67 C
ANISOU 3515 CA ARG A 436 8151 6512 5730 431 -415 2255 C
ATOM 3516 C ARG A 436 -24.392 42.152 -19.423 1.00 60.18 C
ANISOU 3516 C ARG A 436 9199 7026 6641 334 -377 2334 C
ATOM 3517 O ARG A 436 -25.047 43.028 -18.859 1.00 59.05 O
ANISOU 3517 O ARG A 436 9189 6658 6590 475 -401 2348 O
ATOM 3518 CB ARG A 436 -24.867 39.794 -18.635 1.00 52.95 C
ANISOU 3518 CB ARG A 436 7906 6512 5701 382 -395 2031 C
ATOM 3519 CG ARG A 436 -25.940 38.711 -18.627 1.00 61.40 C
ANISOU 3519 CG ARG A 436 8796 7801 6730 535 -443 1937 C
ATOM 3520 CD ARG A 436 -27.025 39.007 -17.611 1.00 72.28 C
ANISOU 3520 CD ARG A 436 10187 9071 8205 721 -478 1853 C
ATOM 3521 NE ARG A 436 -28.006 39.973 -18.107 1.00 79.71 N
ANISOU 3521 NE ARG A 436 11232 9920 9134 919 -531 1991 N
ATOM 3522 CZ ARG A 436 -29.308 39.727 -18.212 1.00 94.44 C
ANISOU 3522 CZ ARG A 436 13006 11910 10970 1124 -589 1978 C
ATOM 3523 NH1 ARG A 436 -29.799 38.545 -17.855 1.00 81.96 N
ANISOU 3523 NH1 ARG A 436 11233 10538 9368 1140 -599 1833 N
ATOM 3524 NH2 ARG A 436 -30.130 40.661 -18.669 1.00 81.13 N
ANISOU 3524 NH2 ARG A 436 11416 10138 9270 1314 -639 2112 N
ATOM 3525 N TRP A 437 -23.107 42.314 -19.806 1.00 59.94 N
ANISOU 3525 N TRP A 437 9210 6988 6576 94 -316 2385 N
ATOM 3526 CA TRP A 437 -22.337 43.543 -19.617 1.00 61.30 C
ANISOU 3526 CA TRP A 437 9593 6884 6814 -51 -271 2468 C
ATOM 3527 C TRP A 437 -22.942 44.678 -20.448 1.00 66.51 C
ANISOU 3527 C TRP A 437 10456 7365 7450 67 -302 2693 C
ATOM 3528 O TRP A 437 -22.975 45.818 -19.987 1.00 66.60 O
ANISOU 3528 O TRP A 437 10674 7068 7562 82 -294 2738 O
ATOM 3529 CB TRP A 437 -20.857 43.322 -19.959 1.00 60.88 C
ANISOU 3529 CB TRP A 437 9500 6926 6703 -341 -199 2474 C
ATOM 3530 CG TRP A 437 -20.000 44.535 -19.745 1.00 62.67 C
ANISOU 3530 CG TRP A 437 9933 6883 6995 -527 -147 2546 C
ATOM 3531 CD1 TRP A 437 -19.393 45.289 -20.707 1.00 65.81 C
ANISOU 3531 CD1 TRP A 437 10468 7213 7325 -674 -110 2741 C
ATOM 3532 CD2 TRP A 437 -19.713 45.174 -18.492 1.00 62.88 C
ANISOU 3532 CD2 TRP A 437 10064 6664 7164 -588 -125 2427 C
ATOM 3533 NE1 TRP A 437 -18.721 46.343 -20.131 1.00 65.62 N
ANISOU 3533 NE1 TRP A 437 10629 6907 7398 -837 -64 2748 N
ATOM 3534 CE2 TRP A 437 -18.899 46.295 -18.770 1.00 67.07 C
ANISOU 3534 CE2 TRP A 437 10795 6979 7712 -786 -74 2550 C
ATOM 3535 CE3 TRP A 437 -20.057 44.901 -17.153 1.00 64.40 C
ANISOU 3535 CE3 TRP A 437 10199 6805 7466 -503 -142 2224 C
ATOM 3536 CZ2 TRP A 437 -18.422 47.143 -17.762 1.00 66.55 C
ANISOU 3536 CZ2 TRP A 437 10872 6643 7771 -906 -42 2466 C
ATOM 3537 CZ3 TRP A 437 -19.588 45.744 -16.155 1.00 65.98 C
ANISOU 3537 CZ3 TRP A 437 10537 6751 7783 -609 -111 2142 C
ATOM 3538 CH2 TRP A 437 -18.779 46.848 -16.461 1.00 66.64 C
ANISOU 3538 CH2 TRP A 437 10818 6619 7884 -810 -63 2256 C
ATOM 3539 N ASP A 438 -23.445 44.350 -21.656 1.00 63.92 N
ANISOU 3539 N ASP A 438 10070 7231 6987 161 -339 2831 N
ATOM 3540 CA ASP A 438 -24.154 45.255 -22.573 1.00 63.86 C
ANISOU 3540 CA ASP A 438 10223 7115 6926 313 -383 3059 C
ATOM 3541 C ASP A 438 -25.599 45.371 -22.027 1.00 67.19 C
ANISOU 3541 C ASP A 438 10636 7476 7416 621 -458 3004 C
ATOM 3542 O ASP A 438 -26.227 44.344 -21.763 1.00 67.00 O
ANISOU 3542 O ASP A 438 10407 7678 7372 725 -492 2863 O
ATOM 3543 CB ASP A 438 -24.155 44.642 -23.990 1.00 66.00 C
ANISOU 3543 CB ASP A 438 10383 7684 7009 299 -399 3187 C
ATOM 3544 CG ASP A 438 -24.303 45.630 -25.130 1.00 80.15 C
ANISOU 3544 CG ASP A 438 12361 9380 8711 335 -415 3464 C
ATOM 3545 OD1 ASP A 438 -25.260 46.431 -25.101 1.00 82.22 O
ANISOU 3545 OD1 ASP A 438 12757 9469 9012 562 -473 3567 O
ATOM 3546 OD2 ASP A 438 -23.473 45.585 -26.066 1.00 85.64 O
ANISOU 3546 OD2 ASP A 438 13066 10184 9290 144 -369 3582 O
ATOM 3547 N HIS A 439 -26.099 46.605 -21.802 1.00 62.90 N
ANISOU 3547 N HIS A 439 10315 6626 6960 760 -480 3103 N
ATOM 3548 CA HIS A 439 -27.427 46.896 -21.220 1.00 80.30 C
ANISOU 3548 CA HIS A 439 12531 8743 9237 1063 -545 3052 C
ATOM 3549 C HIS A 439 -27.490 46.506 -19.734 1.00100.18 C
ANISOU 3549 C HIS A 439 14959 11221 11885 1064 -526 2793 C
ATOM 3550 O HIS A 439 -26.580 46.816 -18.965 1.00 59.10 O
ANISOU 3550 O HIS A 439 9846 5830 6777 884 -467 2706 O
ATOM 3551 CB HIS A 439 -28.600 46.290 -22.050 1.00 80.88 C
ANISOU 3551 CB HIS A 439 12447 9098 9184 1295 -626 3117 C
ATOM 3552 CG HIS A 439 -29.394 45.204 -21.369 1.00 84.07 C
ANISOU 3552 CG HIS A 439 12608 9736 9600 1413 -659 2906 C
ATOM 3553 ND1 HIS A 439 -28.899 43.918 -21.233 1.00 85.54 N
ANISOU 3553 ND1 HIS A 439 12585 10173 9743 1247 -628 2754 N
ATOM 3554 CD2 HIS A 439 -30.645 45.244 -20.850 1.00 85.49 C
ANISOU 3554 CD2 HIS A 439 12728 9935 9819 1678 -718 2838 C
ATOM 3555 CE1 HIS A 439 -29.846 43.231 -20.614 1.00 84.73 C
ANISOU 3555 CE1 HIS A 439 12316 10215 9661 1400 -667 2603 C
ATOM 3556 NE2 HIS A 439 -30.914 43.985 -20.363 1.00 85.08 N
ANISOU 3556 NE2 HIS A 439 12433 10142 9751 1656 -719 2644 N
TER 3557 HIS A 439
HETATM 3558 C1 QK8 A1201 -20.997 22.084 5.611 1.00 14.29 C
HETATM 3559 N1 QK8 A1201 -24.500 24.107 7.656 1.00 27.00 N
HETATM 3560 O1 QK8 A1201 -23.138 24.075 9.469 1.00 29.79 O
HETATM 3561 C2 QK8 A1201 -21.869 23.165 6.302 1.00 15.62 C
HETATM 3562 N2 QK8 A1201 -21.093 16.675 3.188 1.00 16.15 N
HETATM 3563 O2 QK8 A1201 -21.261 14.329 3.426 1.00 14.53 O
HETATM 3564 C3 QK8 A1201 -22.463 22.680 7.656 1.00 19.16 C
HETATM 3565 N3 QK8 A1201 -21.753 20.717 5.546 1.00 14.20 N
HETATM 3566 O3 QK8 A1201 -22.815 15.477 2.205 1.00 14.27 O
HETATM 3567 C4 QK8 A1201 -23.130 21.269 7.605 1.00 18.04 C
HETATM 3568 C5 QK8 A1201 -22.243 20.197 6.942 1.00 16.34 C
HETATM 3569 C6 QK8 A1201 -23.403 23.701 8.327 1.00 25.29 C
HETATM 3570 C7 QK8 A1201 -25.568 25.010 8.084 1.00 28.09 C
HETATM 3571 C8 QK8 A1201 -26.323 24.523 9.339 1.00 29.81 C
HETATM 3572 C9 QK8 A1201 -27.325 23.823 8.411 1.00 30.61 C
HETATM 3573 C10 QK8 A1201 -21.088 19.668 4.601 1.00 13.88 C
HETATM 3574 C11 QK8 A1201 -22.192 18.925 3.797 1.00 15.13 C
HETATM 3575 C12 QK8 A1201 -21.675 17.958 2.691 1.00 16.01 C
HETATM 3576 C13 QK8 A1201 -19.713 16.683 3.749 1.00 15.12 C
HETATM 3577 C15 QK8 A1201 -20.045 18.760 5.323 1.00 13.84 C
HETATM 3578 C16 QK8 A1201 -21.695 15.406 2.978 1.00 14.95 C
HETATM 3579 C17 QK8 A1201 -23.491 14.334 1.667 1.00 14.88 C
HETATM 3580 C18 QK8 A1201 -22.754 13.744 0.458 1.00 14.56 C
HETATM 3581 C19 QK8 A1201 -26.871 24.783 7.302 1.00 28.47 C
HETATM 3582 C20 QK8 A1201 -25.156 26.493 8.141 1.00 26.78 C
HETATM 3583 C14 QK8 A1201 -19.119 17.981 4.361 1.00 13.65 C
HETATM 3584 C1 OLA A1202 -4.905 16.923 13.479 1.00 30.73 C
HETATM 3585 O1 OLA A1202 -5.233 16.157 14.408 1.00 31.96 O
HETATM 3586 O2 OLA A1202 -4.666 18.131 13.644 1.00 29.90 O
HETATM 3587 C2 OLA A1202 -4.780 16.351 12.075 1.00 30.43 C
HETATM 3588 C3 OLA A1202 -6.031 16.375 11.239 1.00 29.48 C
HETATM 3589 C4 OLA A1202 -5.934 17.346 10.072 1.00 29.07 C
HETATM 3590 C5 OLA A1202 -5.774 16.691 8.720 1.00 28.83 C
HETATM 3591 C6 OLA A1202 -5.898 17.634 7.541 1.00 27.98 C
HETATM 3592 C7 OLA A1202 -6.059 16.928 6.203 1.00 27.87 C
HETATM 3593 C8 OLA A1202 -5.764 17.774 5.003 1.00 30.25 C
HETATM 3594 C9 OLA A1202 -4.683 17.231 4.118 1.00 31.61 C
HETATM 3595 C10 OLA A1202 -4.746 16.187 3.331 1.00 33.03 C
HETATM 3596 C11 OLA A1202 -4.050 14.879 3.551 1.00 34.26 C
HETATM 3597 C12 OLA A1202 -3.180 14.478 2.401 1.00 36.63 C
HETATM 3598 C13 OLA A1202 -3.244 13.006 2.017 1.00 39.21 C
HETATM 3599 C14 OLA A1202 -4.226 12.686 0.905 1.00 42.27 C
HETATM 3600 C15 OLA A1202 -3.612 12.527 -0.473 1.00 42.93 C
HETATM 3601 C16 OLA A1202 -4.361 13.231 -1.585 1.00 41.81 C
HETATM 3602 C17 OLA A1202 -4.745 12.393 -2.784 1.00 38.28 C
HETATM 3603 C18 OLA A1202 -5.617 13.159 -3.754 1.00 35.94 C
HETATM 3604 C1 OLA A1203 -35.049 24.502 -4.459 1.00 59.12 C
HETATM 3605 O1 OLA A1203 -35.108 25.605 -5.045 1.00 59.71 O
HETATM 3606 O2 OLA A1203 -34.748 24.377 -3.250 1.00 60.27 O
HETATM 3607 C2 OLA A1203 -35.388 23.247 -5.251 1.00 56.30 C
HETATM 3608 C3 OLA A1203 -34.391 22.844 -6.299 1.00 52.77 C
HETATM 3609 C4 OLA A1203 -34.370 21.342 -6.545 1.00 48.06 C
HETATM 3610 C5 OLA A1203 -33.736 20.932 -7.853 1.00 43.16 C
HETATM 3611 C6 OLA A1203 -34.426 19.781 -8.550 1.00 38.80 C
HETATM 3612 C7 OLA A1203 -33.590 19.092 -9.621 1.00 35.67 C
HETATM 3613 C8 OLA A1203 -33.796 19.624 -11.004 1.00 35.68 C
HETATM 3614 C9 OLA A1203 -32.743 19.200 -11.982 1.00 35.22 C
HETATM 3615 C10 OLA A1203 -32.753 19.421 -13.277 1.00 33.67 C
HETATM 3616 C11 OLA A1203 -33.432 18.568 -14.304 1.00 34.17 C
HETATM 3617 C12 OLA A1203 -32.676 18.458 -15.592 1.00 35.89 C
HETATM 3618 C13 OLA A1203 -33.318 19.188 -16.762 1.00 37.05 C
HETATM 3619 C14 OLA A1203 -32.410 19.376 -17.954 1.00 37.63 C
HETATM 3620 C15 OLA A1203 -33.001 20.227 -19.056 1.00 39.35 C
HETATM 3621 C16 OLA A1203 -31.994 20.734 -20.068 1.00 40.09 C
HETATM 3622 C17 OLA A1203 -32.589 21.327 -21.324 1.00 39.84 C
HETATM 3623 C18 OLA A1203 -32.115 20.685 -22.610 1.00 39.11 C
HETATM 3624 C1 OLA A1204 -12.392 30.387 10.240 1.00 57.47 C
HETATM 3625 O1 OLA A1204 -12.902 30.492 11.379 1.00 60.16 O
HETATM 3626 O2 OLA A1204 -11.157 30.344 10.036 1.00 57.60 O
HETATM 3627 C2 OLA A1204 -13.324 30.329 9.039 1.00 52.47 C
HETATM 3628 C3 OLA A1204 -13.421 31.623 8.295 1.00 48.84 C
HETATM 3629 C4 OLA A1204 -14.014 31.458 6.910 1.00 46.42 C
HETATM 3630 C5 OLA A1204 -13.035 31.654 5.777 1.00 43.11 C
HETATM 3631 C6 OLA A1204 -13.630 32.311 4.552 1.00 40.79 C
HETATM 3632 C7 OLA A1204 -14.116 31.340 3.482 1.00 38.78 C
HETATM 3633 C8 OLA A1204 -13.264 31.293 2.254 1.00 38.00 C
HETATM 3634 C9 OLA A1204 -13.369 30.002 1.499 1.00 37.99 C
HETATM 3635 C10 OLA A1204 -12.385 29.218 1.116 1.00 38.21 C
HETATM 3636 C11 OLA A1204 -11.269 28.708 1.976 1.00 39.35 C
HETATM 3637 C12 OLA A1204 -10.971 27.258 1.771 1.00 40.64 C
HETATM 3638 C13 OLA A1204 -9.963 26.680 2.752 1.00 41.75 C
HETATM 3639 C14 OLA A1204 -8.561 26.527 2.203 1.00 41.15 C
HETATM 3640 C15 OLA A1204 -7.532 26.138 3.241 1.00 40.00 C
HETATM 3641 C16 OLA A1204 -6.312 27.030 3.279 1.00 37.82 C
HETATM 3642 C17 OLA A1204 -5.302 26.684 4.344 1.00 35.40 C
HETATM 3643 C18 OLA A1204 -4.821 27.875 5.137 1.00 33.87 C
HETATM 3644 C1 OLA A1205 -27.498 3.404 -16.147 1.00 53.78 C
HETATM 3645 O1 OLA A1205 -27.360 4.267 -17.042 1.00 56.05 O
HETATM 3646 O2 OLA A1205 -28.386 2.529 -16.164 1.00 54.57 O
HETATM 3647 C2 OLA A1205 -26.533 3.421 -14.974 1.00 50.00 C
HETATM 3648 C3 OLA A1205 -26.737 4.561 -14.027 1.00 47.49 C
HETATM 3649 C4 OLA A1205 -26.280 4.235 -12.618 1.00 46.32 C
HETATM 3650 C5 OLA A1205 -25.649 5.400 -11.904 1.00 45.64 C
HETATM 3651 C6 OLA A1205 -25.347 5.162 -10.441 1.00 44.72 C
HETATM 3652 C7 OLA A1205 -26.404 5.675 -9.471 1.00 44.97 C
HETATM 3653 C8 OLA A1205 -26.744 7.135 -9.588 1.00 45.71 C
HETATM 3654 C9 OLA A1205 -28.196 7.398 -9.862 1.00 46.46 C
HETATM 3655 C10 OLA A1205 -29.245 6.992 -9.185 1.00 46.87 C
HETATM 3656 C11 OLA A1205 -30.536 6.517 -9.776 1.00 47.55 C
HETATM 3657 C12 OLA A1205 -30.639 5.027 -9.870 1.00 50.05 C
HETATM 3658 C13 OLA A1205 -30.071 4.445 -11.156 1.00 53.54 C
HETATM 3659 C14 OLA A1205 -30.791 3.216 -11.666 1.00 56.03 C
HETATM 3660 C15 OLA A1205 -30.098 2.522 -12.815 1.00 57.49 C
HETATM 3661 C16 OLA A1205 -30.586 1.117 -13.079 1.00 59.02 C
HETATM 3662 C17 OLA A1205 -29.720 0.323 -14.026 1.00 60.11 C
HETATM 3663 C18 OLA A1205 -30.419 -0.091 -15.301 1.00 60.39 C
HETATM 3664 C1 OLA A1206 -31.108 36.077 12.273 1.00 62.04 C
HETATM 3665 O1 OLA A1206 -30.247 36.883 12.688 1.00 63.26 O
HETATM 3666 O2 OLA A1206 -31.724 35.287 13.016 1.00 63.54 O
HETATM 3667 C2 OLA A1206 -31.443 36.074 10.791 1.00 59.15 C
HETATM 3668 C3 OLA A1206 -30.278 35.914 9.860 1.00 57.74 C
HETATM 3669 C4 OLA A1206 -30.352 34.634 9.043 1.00 57.13 C
HETATM 3670 C5 OLA A1206 -30.873 34.818 7.637 1.00 55.50 C
HETATM 3671 C6 OLA A1206 -30.400 33.769 6.663 1.00 54.72 C
HETATM 3672 C7 OLA A1206 -30.213 34.276 5.238 1.00 54.63 C
HETATM 3673 C8 OLA A1206 -28.831 34.085 4.682 1.00 54.11 C
HETATM 3674 C9 OLA A1206 -28.631 32.765 4.002 1.00 54.67 C
HETATM 3675 C10 OLA A1206 -28.930 32.469 2.762 1.00 56.21 C
HETATM 3676 C11 OLA A1206 -29.948 31.461 2.332 1.00 58.23 C
HETATM 3677 C12 OLA A1206 -30.869 31.966 1.262 1.00 61.05 C
HETATM 3678 C13 OLA A1206 -30.504 31.525 -0.150 1.00 63.04 C
HETATM 3679 C14 OLA A1206 -31.636 30.883 -0.925 1.00 62.88 C
HETATM 3680 C15 OLA A1206 -31.188 29.994 -2.062 1.00 61.75 C
HETATM 3681 C16 OLA A1206 -32.050 28.767 -2.288 1.00 60.34 C
HETATM 3682 C17 OLA A1206 -31.452 27.697 -3.175 1.00 59.08 C
HETATM 3683 C18 OLA A1206 -31.504 27.976 -4.665 1.00 58.07 C
HETATM 3684 C1 OLA A1207 -20.330 -2.345 -42.067 1.00 71.30 C
HETATM 3685 O1 OLA A1207 -21.232 -2.789 -42.810 1.00 72.68 O
HETATM 3686 O2 OLA A1207 -20.108 -2.781 -40.915 1.00 70.89 O
HETATM 3687 C2 OLA A1207 -19.456 -1.220 -42.596 1.00 69.52 C
HETATM 3688 C3 OLA A1207 -18.636 -1.594 -43.792 1.00 69.17 C
HETATM 3689 C4 OLA A1207 -17.535 -0.590 -44.096 1.00 68.97 C
HETATM 3690 C5 OLA A1207 -16.475 -1.102 -45.051 1.00 68.54 C
HETATM 3691 C6 OLA A1207 -16.638 -0.677 -46.499 1.00 68.35 C
HETATM 3692 C7 OLA A1207 -17.677 -1.458 -47.300 1.00 68.57 C
HETATM 3693 C8 OLA A1207 -17.178 -2.703 -47.973 1.00 69.01 C
HETATM 3694 C9 OLA A1207 -18.291 -3.602 -48.420 1.00 69.91 C
HETATM 3695 C10 OLA A1207 -18.329 -4.919 -48.414 1.00 70.70 C
HETATM 3696 C11 OLA A1207 -18.163 -5.861 -47.257 1.00 70.79 C
HETATM 3697 C12 OLA A1207 -19.304 -5.863 -46.286 1.00 71.46 C
HETATM 3698 C13 OLA A1207 -18.875 -5.942 -44.828 1.00 72.62 C
HETATM 3699 C14 OLA A1207 -20.011 -6.096 -43.844 1.00 73.12 C
HETATM 3700 C15 OLA A1207 -19.966 -7.367 -43.028 1.00 73.21 C
HETATM 3701 C16 OLA A1207 -20.962 -8.421 -43.459 1.00 73.53 C
HETATM 3702 C17 OLA A1207 -22.052 -8.720 -42.460 1.00 73.99 C
HETATM 3703 C18 OLA A1207 -23.377 -9.093 -43.082 1.00 73.82 C
HETATM 3704 C1 PGE A1208 -17.516 28.686 15.495 1.00 54.54 C
HETATM 3705 O1 PGE A1208 -16.915 28.446 16.760 1.00 53.30 O
HETATM 3706 C2 PGE A1208 -18.966 28.286 15.455 1.00 53.59 C
HETATM 3707 O2 PGE A1208 -19.447 28.304 14.114 1.00 51.81 O
HETATM 3708 C3 PGE A1208 -19.961 27.044 13.688 1.00 50.81 C
HETATM 3709 C4 PGE A1208 -19.255 26.584 12.445 1.00 49.99 C
HETATM 3710 O4 PGE A1208 -17.365 22.787 13.084 1.00 46.75 O
HETATM 3711 C6 PGE A1208 -18.568 23.097 12.398 1.00 47.84 C
HETATM 3712 C5 PGE A1208 -18.525 24.436 11.724 1.00 48.59 C
HETATM 3713 O3 PGE A1208 -19.624 25.241 12.145 1.00 50.13 O
HETATM 3714 P PO4 A1209 -7.076 -21.337 -45.774 1.00 69.23 P
HETATM 3715 O1 PO4 A1209 -7.787 -20.581 -46.992 1.00 68.96 O
HETATM 3716 O2 PO4 A1209 -5.712 -21.906 -46.219 1.00 70.21 O
HETATM 3717 O3 PO4 A1209 -7.998 -22.547 -45.274 1.00 68.76 O
HETATM 3718 O4 PO4 A1209 -6.822 -20.288 -44.594 1.00 69.21 O
HETATM 3719 P PO4 A1210 -4.377 -1.332 -52.630 1.00 80.98 P
HETATM 3720 O1 PO4 A1210 -5.736 -1.467 -53.466 1.00 82.01 O
HETATM 3721 O2 PO4 A1210 -4.081 0.172 -52.351 1.00 82.05 O
HETATM 3722 O3 PO4 A1210 -3.164 -1.960 -53.463 1.00 80.31 O
HETATM 3723 O4 PO4 A1210 -4.529 -2.101 -51.237 1.00 79.81 O
HETATM 3724 C1 OLA A1211 -8.410 30.402 14.000 1.00 75.80 C
HETATM 3725 O1 OLA A1211 -9.370 30.931 13.399 1.00 76.86 O
HETATM 3726 O2 OLA A1211 -8.414 30.163 15.225 1.00 75.38 O
HETATM 3727 C2 OLA A1211 -7.174 30.013 13.204 1.00 74.97 C
HETATM 3728 C3 OLA A1211 -6.994 30.691 11.877 1.00 74.33 C
HETATM 3729 C4 OLA A1211 -6.474 29.744 10.809 1.00 73.95 C
HETATM 3730 C5 OLA A1211 -6.180 30.402 9.481 1.00 73.61 C
HETATM 3731 C6 OLA A1211 -7.216 30.143 8.414 1.00 73.26 C
HETATM 3732 C7 OLA A1211 -8.303 31.207 8.336 1.00 73.63 C
HETATM 3733 C8 OLA A1211 -9.218 31.079 7.161 1.00 73.74 C
HETATM 3734 C9 OLA A1211 -8.790 31.904 5.989 1.00 73.16 C
HETATM 3735 C10 OLA A1211 -8.195 31.444 4.920 1.00 73.03 C
HETATM 3736 C11 OLA A1211 -8.844 31.180 3.597 1.00 74.07 C
HETATM 3737 C12 OLA A1211 -9.050 32.416 2.769 1.00 75.52 C
HETATM 3738 C13 OLA A1211 -7.893 32.768 1.842 1.00 76.60 C
HETATM 3739 C14 OLA A1211 -7.978 32.155 0.460 1.00 77.40 C
HETATM 3740 C15 OLA A1211 -8.686 33.008 -0.570 1.00 77.43 C
HETATM 3741 C16 OLA A1211 -10.075 32.527 -0.926 1.00 77.21 C
HETATM 3742 C17 OLA A1211 -10.183 31.778 -2.231 1.00 76.84 C
HETATM 3743 C18 OLA A1211 -11.043 30.536 -2.164 1.00 76.39 C
HETATM 3744 C1 OLA A1212 -6.885 34.995 14.020 1.00 81.63 C
HETATM 3745 O1 OLA A1212 -7.985 34.424 13.881 1.00 82.38 O
HETATM 3746 O2 OLA A1212 -6.677 35.897 14.860 1.00 82.50 O
HETATM 3747 C2 OLA A1212 -5.736 34.565 13.123 1.00 79.31 C
HETATM 3748 C3 OLA A1212 -5.536 35.418 11.910 1.00 77.36 C
HETATM 3749 C4 OLA A1212 -5.246 34.599 10.665 1.00 76.10 C
HETATM 3750 C5 OLA A1212 -5.807 35.187 9.393 1.00 75.01 C
HETATM 3751 C6 OLA A1212 -5.958 34.195 8.267 1.00 74.55 C
HETATM 3752 C7 OLA A1212 -5.491 34.709 6.912 1.00 74.41 C
HETATM 3753 C8 OLA A1212 -5.143 33.630 5.929 1.00 74.70 C
HETATM 3754 C9 OLA A1212 -4.129 34.051 4.909 1.00 74.88 C
HETATM 3755 C10 OLA A1212 -4.388 34.543 3.722 1.00 75.47 C
HETATM 3756 C11 OLA A1212 -4.754 35.963 3.414 1.00 75.84 C
HETATM 3757 C12 OLA A1212 -6.233 36.183 3.290 1.00 76.12 C
HETATM 3758 C13 OLA A1212 -6.666 37.635 3.424 1.00 75.69 C
HETATM 3759 C14 OLA A1212 -8.135 37.877 3.164 1.00 74.37 C
HETATM 3760 C15 OLA A1212 -8.429 38.597 1.866 1.00 72.91 C
HETATM 3761 C16 OLA A1212 -8.801 40.056 2.022 1.00 70.62 C
HETATM 3762 C17 OLA A1212 -10.268 40.353 1.835 1.00 68.65 C
HETATM 3763 C18 OLA A1212 -10.566 41.659 1.141 1.00 67.54 C
HETATM 3764 C1 OLA A1213 -34.202 25.478 19.727 1.00 58.91 C
HETATM 3765 O1 OLA A1213 -33.939 26.692 19.581 1.00 59.22 O
HETATM 3766 O2 OLA A1213 -33.501 24.706 20.418 1.00 59.79 O
HETATM 3767 C2 OLA A1213 -35.435 24.897 19.045 1.00 57.14 C
HETATM 3768 C3 OLA A1213 -36.427 25.857 18.458 1.00 55.54 C
HETATM 3769 C4 OLA A1213 -37.085 25.352 17.184 1.00 55.66 C
HETATM 3770 C5 OLA A1213 -37.774 26.427 16.377 1.00 55.88 C
HETATM 3771 C6 OLA A1213 -37.992 26.094 14.926 1.00 56.43 C
HETATM 3772 C7 OLA A1213 -37.587 27.184 13.939 1.00 56.37 C
HETATM 3773 C8 OLA A1213 -38.592 27.436 12.848 1.00 57.89 C
HETATM 3774 C9 OLA A1213 -38.064 28.269 11.717 1.00 59.45 C
HETATM 3775 C10 OLA A1213 -38.486 28.281 10.471 1.00 59.39 C
HETATM 3776 C11 OLA A1213 -38.169 27.273 9.407 1.00 58.96 C
HETATM 3777 C12 OLA A1213 -38.378 27.784 8.012 1.00 58.83 C
HETATM 3778 C13 OLA A1213 -39.358 26.970 7.177 1.00 58.25 C
HETATM 3779 C14 OLA A1213 -39.132 27.057 5.683 1.00 57.31 C
HETATM 3780 C15 OLA A1213 -40.042 26.180 4.852 1.00 56.18 C
HETATM 3781 C16 OLA A1213 -39.413 24.886 4.382 1.00 55.24 C
HETATM 3782 C17 OLA A1213 -40.098 24.233 3.203 1.00 53.97 C
HETATM 3783 C18 OLA A1213 -39.487 22.919 2.770 1.00 51.99 C
HETATM 3784 C1 OLA A1214 -7.076 26.658 -21.630 1.00 53.63 C
HETATM 3785 O1 OLA A1214 -6.022 27.295 -21.842 1.00 54.38 O
HETATM 3786 O2 OLA A1214 -7.099 25.434 -21.389 1.00 52.66 O
HETATM 3787 C2 OLA A1214 -8.403 27.399 -21.702 1.00 53.14 C
HETATM 3788 C3 OLA A1214 -8.521 28.641 -20.864 1.00 52.39 C
HETATM 3789 C4 OLA A1214 -9.965 28.996 -20.545 1.00 51.88 C
HETATM 3790 C5 OLA A1214 -10.136 30.005 -19.432 1.00 50.58 C
HETATM 3791 C6 OLA A1214 -11.447 29.900 -18.691 1.00 49.48 C
HETATM 3792 C7 OLA A1214 -11.305 29.630 -17.199 1.00 50.14 C
HETATM 3793 C8 OLA A1214 -12.442 28.857 -16.598 1.00 51.88 C
HETATM 3794 C9 OLA A1214 -13.242 29.635 -15.596 1.00 52.79 C
HETATM 3795 C10 OLA A1214 -14.428 30.169 -15.781 1.00 52.56 C
HETATM 3796 C11 OLA A1214 -15.755 29.526 -15.507 1.00 51.56 C
HETATM 3797 C12 OLA A1214 -16.393 29.971 -14.224 1.00 50.27 C
HETATM 3798 C13 OLA A1214 -17.365 31.131 -14.367 1.00 49.09 C
HETATM 3799 C14 OLA A1214 -16.845 32.449 -13.842 1.00 48.35 C
HETATM 3800 C15 OLA A1214 -17.396 32.848 -12.496 1.00 47.15 C
HETATM 3801 C16 OLA A1214 -16.649 33.975 -11.828 1.00 47.34 C
HETATM 3802 C17 OLA A1214 -17.520 35.142 -11.430 1.00 48.35 C
HETATM 3803 C18 OLA A1214 -16.969 36.003 -10.312 1.00 48.34 C
HETATM 3804 C1 OLA A1215 -40.827 8.255 12.040 1.00 51.06 C
HETATM 3805 O1 OLA A1215 -41.849 8.083 11.353 1.00 52.16 O
HETATM 3806 O2 OLA A1215 -40.772 9.051 12.995 1.00 51.33 O
HETATM 3807 C2 OLA A1215 -39.588 7.441 11.706 1.00 50.13 C
HETATM 3808 C3 OLA A1215 -38.825 7.899 10.500 1.00 49.62 C
HETATM 3809 C4 OLA A1215 -37.654 6.986 10.176 1.00 49.78 C
HETATM 3810 C5 OLA A1215 -36.406 7.709 9.732 1.00 49.91 C
HETATM 3811 C6 OLA A1215 -35.365 6.816 9.107 1.00 49.51 C
HETATM 3812 C7 OLA A1215 -34.072 6.713 9.904 1.00 51.23 C
HETATM 3813 C8 OLA A1215 -33.187 5.574 9.498 1.00 54.81 C
HETATM 3814 C9 OLA A1215 -32.218 5.931 8.413 1.00 57.67 C
HETATM 3815 C10 OLA A1215 -31.494 5.096 7.703 1.00 59.18 C
HETATM 3816 C11 OLA A1215 -30.806 5.419 6.411 1.00 59.22 C
HETATM 3817 C12 OLA A1215 -29.344 5.718 6.572 1.00 58.53 C
HETATM 3818 C13 OLA A1215 -29.013 7.199 6.695 1.00 56.52 C
HETATM 3819 C14 OLA A1215 -27.546 7.529 6.542 1.00 53.72 C
HETATM 3820 C15 OLA A1215 -27.190 8.179 5.225 1.00 49.65 C
HETATM 3821 C16 OLA A1215 -25.969 7.602 4.556 1.00 46.30 C
HETATM 3822 C17 OLA A1215 -26.192 7.110 3.152 1.00 44.52 C
HETATM 3823 C18 OLA A1215 -25.410 7.864 2.103 1.00 42.65 C
HETATM 3824 P PO4 A1216 -20.862 13.302 -27.413 1.00118.42 P
HETATM 3825 O1 PO4 A1216 -21.463 13.348 -28.896 1.00118.83 O
HETATM 3826 O2 PO4 A1216 -19.327 13.545 -27.461 1.00117.89 O
HETATM 3827 O3 PO4 A1216 -21.175 11.868 -26.775 1.00118.42 O
HETATM 3828 O4 PO4 A1216 -21.550 14.445 -26.530 1.00117.90 O
HETATM 3829 O HOH A1301 -21.644 22.300 -11.632 1.00 17.51 O
HETATM 3830 O HOH A1302 -29.286 4.289 -51.675 1.00 23.64 O
HETATM 3831 O HOH A1303 -16.797 17.550 -9.446 1.00 15.70 O
HETATM 3832 O HOH A1304 -18.343 3.289 -40.682 1.00 19.34 O
HETATM 3833 O HOH A1305 -21.255 32.907 1.546 1.00 24.97 O
HETATM 3834 O HOH A1306 -25.110 14.826 19.689 1.00 25.96 O
HETATM 3835 O HOH A1307 -12.951 5.554 -32.548 1.00 20.12 O
HETATM 3836 O HOH A1308 2.950 -6.711 -52.399 1.00 33.83 O
HETATM 3837 O HOH A1309 -20.269 16.016 8.096 1.00 29.91 O
HETATM 3838 O HOH A1310 -18.168 28.830 -10.705 1.00 13.12 O
HETATM 3839 O HOH A1311 -8.472 12.720 -20.827 1.00 31.08 O
HETATM 3840 O HOH A1312 -12.523 19.039 2.130 1.00 5.52 O
HETATM 3841 O HOH A1313 -31.377 28.626 17.551 1.00 17.95 O
HETATM 3842 O HOH A1314 -21.018 16.588 -19.162 1.00 39.75 O
HETATM 3843 O HOH A1315 -31.048 22.254 19.632 1.00 24.42 O
HETATM 3844 O HOH A1316 -5.195 -19.241 -49.327 1.00 38.28 O
HETATM 3845 O HOH A1317 -38.622 10.519 -18.488 1.00 28.04 O
HETATM 3846 O HOH A1318 -4.364 -16.309 -30.814 1.00 33.14 O
HETATM 3847 O HOH A1319 -12.557 11.865 -35.516 1.00 35.20 O
HETATM 3848 O HOH A1320 -32.562 8.696 5.800 1.00 24.04 O
HETATM 3849 O HOH A1321 -23.179 -3.378 -28.116 1.00 22.25 O
HETATM 3850 O HOH A1322 -18.264 6.259 -40.794 1.00 9.36 O
HETATM 3851 O HOH A1323 -11.905 -10.075 -57.290 1.00 46.65 O
HETATM 3852 O HOH A1324 -12.317 6.035 -29.720 1.00 25.93 O
HETATM 3853 O HOH A1325 -3.496 -7.513 -59.199 1.00 38.89 O
HETATM 3854 O HOH A1326 -23.576 13.676 -24.859 1.00 37.96 O
HETATM 3855 O HOH A1327 -22.143 22.505 11.480 1.00 27.12 O
HETATM 3856 O HOH A1328 -21.932 -2.820 -50.385 1.00 33.92 O
HETATM 3857 O HOH A1329 -20.097 20.713 -2.740 1.00 24.69 O
HETATM 3858 O HOH A1330 -30.391 23.724 17.072 1.00 15.66 O
HETATM 3859 O HOH A1331 -19.846 -2.033 -21.082 1.00 42.82 O
HETATM 3860 O HOH A1332 -7.642 22.512 -21.169 1.00 25.00 O
HETATM 3861 O HOH A1333 -12.723 22.129 -26.630 1.00 34.20 O
HETATM 3862 O HOH A1334 -31.358 16.033 16.014 1.00 8.71 O
HETATM 3863 O HOH A1335 -24.036 9.590 -31.466 1.00 33.74 O
HETATM 3864 O HOH A1336 -29.744 17.654 14.183 1.00 14.38 O
HETATM 3865 O HOH A1337 -4.774 11.576 -19.854 1.00 41.69 O
HETATM 3866 O HOH A1338 1.313 -3.676 -38.068 1.00 32.45 O
HETATM 3867 O HOH A1339 -20.879 -11.851 -44.878 1.00 32.95 O
HETATM 3868 O HOH A1340 -23.764 9.388 16.604 1.00 37.73 O
HETATM 3869 O HOH A1341 -8.755 -6.360 -44.987 1.00 35.49 O
HETATM 3870 O HOH A1342 -23.441 17.819 10.635 1.00 16.08 O
HETATM 3871 O HOH A1343 -32.483 33.254 -21.460 1.00 33.13 O
HETATM 3872 O HOH A1344 2.532 -12.897 -46.028 1.00 37.06 O
HETATM 3873 O HOH A1345 -4.718 1.242 -49.423 1.00 30.51 O
HETATM 3874 O HOH A1346 -26.923 32.057 12.859 1.00 26.08 O
HETATM 3875 O HOH A1347 -24.899 25.190 4.895 1.00 21.21 O
HETATM 3876 O HOH A1348 -37.350 14.492 25.049 1.00 23.67 O
HETATM 3877 O HOH A1349 -32.834 14.357 14.458 1.00 7.79 O
HETATM 3878 O HOH A1350 -38.929 17.959 19.215 1.00 44.37 O
HETATM 3879 O HOH A1351 -21.721 16.350 -24.340 1.00 32.98 O
HETATM 3880 O HOH A1352 -7.982 -1.916 -30.662 1.00 51.36 O
HETATM 3881 O HOH A1353 -17.916 12.367 2.251 1.00 22.55 O
HETATM 3882 O HOH A1354 -21.509 19.859 11.289 1.00 25.37 O
HETATM 3883 O HOH A1355 -9.394 -1.731 -50.013 1.00 27.17 O
HETATM 3884 O HOH A1356 -11.686 10.873 -26.751 1.00 20.86 O
HETATM 3885 O HOH A1357 3.559 -10.166 -48.680 1.00 38.64 O
HETATM 3886 O HOH A1358 1.766 -2.607 -47.558 1.00 29.97 O
HETATM 3887 O HOH A1359 -8.312 19.643 18.799 1.00 20.55 O
HETATM 3888 O HOH A1360 -17.178 4.433 -28.954 1.00 28.28 O
HETATM 3889 O HOH A1361 -20.966 18.864 -24.990 1.00 26.72 O
HETATM 3890 O HOH A1362 2.595 -1.680 -49.957 1.00 36.07 O
HETATM 3891 O HOH A1363 -18.181 14.364 -19.755 1.00 32.58 O
HETATM 3892 O HOH A1364 -6.078 12.084 -16.712 1.00 26.85 O
HETATM 3893 O HOH A1365 -23.549 0.602 -41.892 1.00 37.89 O
HETATM 3894 O HOH A1366 -1.818 2.010 -50.020 1.00 47.45 O
HETATM 3895 O HOH A1367 -1.386 4.340 -30.694 1.00 35.97 O
HETATM 3896 O HOH A1368 -35.551 16.825 23.278 1.00 21.90 O
HETATM 3897 O HOH A1369 -37.034 11.489 -25.455 1.00 27.96 O
HETATM 3898 O HOH A1370 -8.236 3.972 -49.531 1.00 40.64 O
HETATM 3899 O HOH A1371 -5.956 -7.196 -60.304 1.00 30.68 O
HETATM 3900 O HOH A1372 -32.486 34.937 -19.311 1.00 46.45 O
CONECT 591 1232
CONECT 1232 591
CONECT 3152 3175
CONECT 3175 3152
CONECT 3558 3561 3565
CONECT 3559 3569 3570
CONECT 3560 3569
CONECT 3561 3558 3564
CONECT 3562 3575 3576 3578
CONECT 3563 3578
CONECT 3564 3561 3567 3569
CONECT 3565 3558 3568 3573
CONECT 3566 3578 3579
CONECT 3567 3564 3568
CONECT 3568 3565 3567
CONECT 3569 3559 3560 3564
CONECT 3570 3559 3571 3581 3582
CONECT 3571 3570 3572
CONECT 3572 3571 3581
CONECT 3573 3565 3574 3577
CONECT 3574 3573 3575
CONECT 3575 3562 3574
CONECT 3576 3562 3583
CONECT 3577 3573 3583
CONECT 3578 3562 3563 3566
CONECT 3579 3566 3580
CONECT 3580 3579
CONECT 3581 3570 3572
CONECT 3582 3570
CONECT 3583 3576 3577
CONECT 3584 3585 3586 3587
CONECT 3585 3584
CONECT 3586 3584
CONECT 3587 3584 3588
CONECT 3588 3587 3589
CONECT 3589 3588 3590
CONECT 3590 3589 3591
CONECT 3591 3590 3592
CONECT 3592 3591 3593
CONECT 3593 3592 3594
CONECT 3594 3593 3595
CONECT 3595 3594 3596
CONECT 3596 3595 3597
CONECT 3597 3596 3598
CONECT 3598 3597 3599
CONECT 3599 3598 3600
CONECT 3600 3599 3601
CONECT 3601 3600 3602
CONECT 3602 3601 3603
CONECT 3603 3602
CONECT 3604 3605 3606 3607
CONECT 3605 3604
CONECT 3606 3604
CONECT 3607 3604 3608
CONECT 3608 3607 3609
CONECT 3609 3608 3610
CONECT 3610 3609 3611
CONECT 3611 3610 3612
CONECT 3612 3611 3613
CONECT 3613 3612 3614
CONECT 3614 3613 3615
CONECT 3615 3614 3616
CONECT 3616 3615 3617
CONECT 3617 3616 3618
CONECT 3618 3617 3619
CONECT 3619 3618 3620
CONECT 3620 3619 3621
CONECT 3621 3620 3622
CONECT 3622 3621 3623
CONECT 3623 3622
CONECT 3624 3625 3626 3627
CONECT 3625 3624
CONECT 3626 3624
CONECT 3627 3624 3628
CONECT 3628 3627 3629
CONECT 3629 3628 3630
CONECT 3630 3629 3631
CONECT 3631 3630 3632
CONECT 3632 3631 3633
CONECT 3633 3632 3634
CONECT 3634 3633 3635
CONECT 3635 3634 3636
CONECT 3636 3635 3637
CONECT 3637 3636 3638
CONECT 3638 3637 3639
CONECT 3639 3638 3640
CONECT 3640 3639 3641
CONECT 3641 3640 3642
CONECT 3642 3641 3643
CONECT 3643 3642
CONECT 3644 3645 3646 3647
CONECT 3645 3644
CONECT 3646 3644
CONECT 3647 3644 3648
CONECT 3648 3647 3649
CONECT 3649 3648 3650
CONECT 3650 3649 3651
CONECT 3651 3650 3652
CONECT 3652 3651 3653
CONECT 3653 3652 3654
CONECT 3654 3653 3655
CONECT 3655 3654 3656
CONECT 3656 3655 3657
CONECT 3657 3656 3658
CONECT 3658 3657 3659
CONECT 3659 3658 3660
CONECT 3660 3659 3661
CONECT 3661 3660 3662
CONECT 3662 3661 3663
CONECT 3663 3662
CONECT 3664 3665 3666 3667
CONECT 3665 3664
CONECT 3666 3664
CONECT 3667 3664 3668
CONECT 3668 3667 3669
CONECT 3669 3668 3670
CONECT 3670 3669 3671
CONECT 3671 3670 3672
CONECT 3672 3671 3673
CONECT 3673 3672 3674
CONECT 3674 3673 3675
CONECT 3675 3674 3676
CONECT 3676 3675 3677
CONECT 3677 3676 3678
CONECT 3678 3677 3679
CONECT 3679 3678 3680
CONECT 3680 3679 3681
CONECT 3681 3680 3682
CONECT 3682 3681 3683
CONECT 3683 3682
CONECT 3684 3685 3686 3687
CONECT 3685 3684
CONECT 3686 3684
CONECT 3687 3684 3688
CONECT 3688 3687 3689
CONECT 3689 3688 3690
CONECT 3690 3689 3691
CONECT 3691 3690 3692
CONECT 3692 3691 3693
CONECT 3693 3692 3694
CONECT 3694 3693 3695
CONECT 3695 3694 3696
CONECT 3696 3695 3697
CONECT 3697 3696 3698
CONECT 3698 3697 3699
CONECT 3699 3698 3700
CONECT 3700 3699 3701
CONECT 3701 3700 3702
CONECT 3702 3701 3703
CONECT 3703 3702
CONECT 3704 3705 3706
CONECT 3705 3704
CONECT 3706 3704 3707
CONECT 3707 3706 3708
CONECT 3708 3707 3709
CONECT 3709 3708 3713
CONECT 3710 3711
CONECT 3711 3710 3712
CONECT 3712 3711 3713
CONECT 3713 3709 3712
CONECT 3714 3715 3716 3717 3718
CONECT 3715 3714
CONECT 3716 3714
CONECT 3717 3714
CONECT 3718 3714
CONECT 3719 3720 3721 3722 3723
CONECT 3720 3719
CONECT 3721 3719
CONECT 3722 3719
CONECT 3723 3719
CONECT 3724 3725 3726 3727
CONECT 3725 3724
CONECT 3726 3724
CONECT 3727 3724 3728
CONECT 3728 3727 3729
CONECT 3729 3728 3730
CONECT 3730 3729 3731
CONECT 3731 3730 3732
CONECT 3732 3731 3733
CONECT 3733 3732 3734
CONECT 3734 3733 3735
CONECT 3735 3734 3736
CONECT 3736 3735 3737
CONECT 3737 3736 3738
CONECT 3738 3737 3739
CONECT 3739 3738 3740
CONECT 3740 3739 3741
CONECT 3741 3740 3742
CONECT 3742 3741 3743
CONECT 3743 3742
CONECT 3744 3745 3746 3747
CONECT 3745 3744
CONECT 3746 3744
CONECT 3747 3744 3748
CONECT 3748 3747 3749
CONECT 3749 3748 3750
CONECT 3750 3749 3751
CONECT 3751 3750 3752
CONECT 3752 3751 3753
CONECT 3753 3752 3754
CONECT 3754 3753 3755
CONECT 3755 3754 3756
CONECT 3756 3755 3757
CONECT 3757 3756 3758
CONECT 3758 3757 3759
CONECT 3759 3758 3760
CONECT 3760 3759 3761
CONECT 3761 3760 3762
CONECT 3762 3761 3763
CONECT 3763 3762
CONECT 3764 3765 3766 3767
CONECT 3765 3764
CONECT 3766 3764
CONECT 3767 3764 3768
CONECT 3768 3767 3769
CONECT 3769 3768 3770
CONECT 3770 3769 3771
CONECT 3771 3770 3772
CONECT 3772 3771 3773
CONECT 3773 3772 3774
CONECT 3774 3773 3775
CONECT 3775 3774 3776
CONECT 3776 3775 3777
CONECT 3777 3776 3778
CONECT 3778 3777 3779
CONECT 3779 3778 3780
CONECT 3780 3779 3781
CONECT 3781 3780 3782
CONECT 3782 3781 3783
CONECT 3783 3782
CONECT 3784 3785 3786 3787
CONECT 3785 3784
CONECT 3786 3784
CONECT 3787 3784 3788
CONECT 3788 3787 3789
CONECT 3789 3788 3790
CONECT 3790 3789 3791
CONECT 3791 3790 3792
CONECT 3792 3791 3793
CONECT 3793 3792 3794
CONECT 3794 3793 3795
CONECT 3795 3794 3796
CONECT 3796 3795 3797
CONECT 3797 3796 3798
CONECT 3798 3797 3799
CONECT 3799 3798 3800
CONECT 3800 3799 3801
CONECT 3801 3800 3802
CONECT 3802 3801 3803
CONECT 3803 3802
CONECT 3804 3805 3806 3807
CONECT 3805 3804
CONECT 3806 3804
CONECT 3807 3804 3808
CONECT 3808 3807 3809
CONECT 3809 3808 3810
CONECT 3810 3809 3811
CONECT 3811 3810 3812
CONECT 3812 3811 3813
CONECT 3813 3812 3814
CONECT 3814 3813 3815
CONECT 3815 3814 3816
CONECT 3816 3815 3817
CONECT 3817 3816 3818
CONECT 3818 3817 3819
CONECT 3819 3818 3820
CONECT 3820 3819 3821
CONECT 3821 3820 3822
CONECT 3822 3821 3823
CONECT 3823 3822
CONECT 3824 3825 3826 3827 3828
CONECT 3825 3824
CONECT 3826 3824
CONECT 3827 3824
CONECT 3828 3824
MASTER 353 0 16 22 3 0 25 6 3899 1 275 35
END