HEADER MEMBRANE PROTEIN 08-MAY-19 6RNK
TITLE CRYSTAL STRUCTURE OF A HUMANIZED (K18E, K269N) RAT SUCCINATE RECEPTOR
TITLE 2 SUCNR1 (GPR91) IN COMPLEX WITH A NANOBODY AND ANTAGONIST NF-56-EJ40.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINATE RECEPTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 91;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NANOBODY6;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: SUCNR1, GPR91;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS;
SOURCE 10 ORGANISM_TAXID: 30538;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS SUCNR1, GPR91, GPCR, G-PROTEIN COUPLED RECEPTOR, NANOBODY,
KEYWDS 2 ANTAGONIST, SUCCINATE, COMPLEX, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAFFKE,V.-P.JAAKOLA
REVDAT 3 06-NOV-19 6RNK 1 JRNL
REVDAT 2 16-OCT-19 6RNK 1 JRNL
REVDAT 1 14-AUG-19 6RNK 0
JRNL AUTH M.HAFFKE,D.FEHLMANN,G.RUMMEL,J.BOIVINEAU,M.DUCKELY,
JRNL AUTH 2 N.GOMMERMANN,S.COTESTA,F.SIROCKIN,F.FREULER,
JRNL AUTH 3 A.LITTLEWOOD-EVANS,K.KAUPMANN,V.P.JAAKOLA
JRNL TITL STRUCTURAL BASIS OF SPECIES-SELECTIVE ANTAGONIST BINDING TO
JRNL TITL 2 THE SUCCINATE RECEPTOR.
JRNL REF NATURE V. 574 581 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 31645725
JRNL DOI 10.1038/S41586-019-1663-8
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.6
REMARK 3 NUMBER OF REFLECTIONS : 40585
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1980
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 11.92
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 812
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2058
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 773
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE : 0.2212
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 39
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3281
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 286
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18150
REMARK 3 B22 (A**2) : -1.61380
REMARK 3 B33 (A**2) : 1.43230
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.57610
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.230
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.144
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.128
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.145
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.129
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 : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3638 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4869 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1309 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 572 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3638 ; 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 : 449 ; 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 : 4359 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.97
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1974 23.2309 18.5300
REMARK 3 T TENSOR
REMARK 3 T11: -0.0367 T22: -0.0462
REMARK 3 T33: -0.0452 T12: -0.0032
REMARK 3 T13: 0.0481 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.6328 L22: 2.3597
REMARK 3 L33: 0.7668 L12: -0.2005
REMARK 3 L13: -0.1680 L23: 0.3512
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 0.0617 S13: 0.0440
REMARK 3 S21: -0.2674 S22: 0.0041 S23: -0.0691
REMARK 3 S31: -0.0266 S32: 0.0444 S33: -0.0013
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6069 63.8335 25.0224
REMARK 3 T TENSOR
REMARK 3 T11: -0.0481 T22: -0.1527
REMARK 3 T33: -0.0248 T12: -0.0592
REMARK 3 T13: 0.0561 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 2.4404 L22: 5.8352
REMARK 3 L33: 2.2320 L12: 0.1628
REMARK 3 L13: -0.3926 L23: 1.7161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0209 S12: 0.0548 S13: 0.0519
REMARK 3 S21: -0.4302 S22: 0.0823 S23: -0.2496
REMARK 3 S31: -0.1451 S32: 0.0769 S33: -0.0613
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6RNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100.00
REMARK 200 PH : 7.0
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) : 1.00002
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS BUILT 20190315
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 20190301
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88565
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 75.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 67.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.21300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 8.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 8.75600
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 2.8.0
REMARK 200 STARTING MODEL: 6IBB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ADA, PH 7.0, 28% PEG MME 550,
REMARK 280 0.55 M (NH4)2SO4, 100-400 MICROM COMPOUND 3, 1-4 % (V/V) DMSO,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.41500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.41500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 75.46500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 209 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A -6
REMARK 465 TYR A -5
REMARK 465 LYS A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 ASP A 0
REMARK 465 LYS A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 ASN A 4
REMARK 465 LEU A 5
REMARK 465 SER A 6
REMARK 465 GLN A 215
REMARK 465 GLN A 216
REMARK 465 GLN A 217
REMARK 465 ALA A 218
REMARK 465 THR A 219
REMARK 465 VAL A 220
REMARK 465 LEU A 221
REMARK 465 SER A 222
REMARK 465 LEU A 223
REMARK 465 ASP A 257
REMARK 465 SER A 258
REMARK 465 TRP A 259
REMARK 465 PRO A 260
REMARK 465 GLN A 261
REMARK 465 ARG A 306
REMARK 465 GLN A 307
REMARK 465 TYR A 308
REMARK 465 PHE A 309
REMARK 465 LYS A 310
REMARK 465 SER A 311
REMARK 465 LEU A 312
REMARK 465 THR A 313
REMARK 465 SER A 314
REMARK 465 PHE A 315
REMARK 465 ARG A 316
REMARK 465 LEU A 317
REMARK 465 LEU A 318
REMARK 465 GLU A 319
REMARK 465 VAL A 320
REMARK 465 LEU A 321
REMARK 465 PHE A 322
REMARK 465 GLN A 323
REMARK 465 GLY A 324
REMARK 465 PRO A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
REMARK 465 HIS A 330
REMARK 465 HIS A 331
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 HIS A 334
REMARK 465 HIS A 335
REMARK 465 ASP B 1
REMARK 465 TYR B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 ASP B 5
REMARK 465 ASP B 6
REMARK 465 ASP B 7
REMARK 465 LYS B 8
REMARK 465 GLU B 138
REMARK 465 VAL B 139
REMARK 465 LEU B 140
REMARK 465 PHE B 141
REMARK 465 GLN B 142
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 214 OG
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 TYR B 35 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 137 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 168 84.09 -154.25
REMARK 500 ARG B 74 -32.46 -132.61
REMARK 500 ALA B 99 168.07 179.49
REMARK 500 ARG B 111 -64.54 -91.66
REMARK 500 ASP B 115 71.52 -153.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC A 402
REMARK 610 OLC A 403
REMARK 610 OLC A 405
REMARK 610 OLC A 406
REMARK 610 OLC A 407
REMARK 610 OLC A 409
REMARK 610 OLC A 410
REMARK 610 OLC A 411
REMARK 610 OLC A 413
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KAZ A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6IBB RELATED DB: PDB
REMARK 900 6IBB CONTAINS THE SAME PROTEIN WITHOUT K18E, K269N MUTATIONS
DBREF 6RNK A 2 317 UNP Q6IYF9 SUCR1_RAT 2 317
DBREF 6RNK B 1 142 PDB 6RNK 6RNK 1 142
SEQADV 6RNK ASP A -6 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK TYR A -5 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK LYS A -4 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK ASP A -3 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK ASP A -2 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK ASP A -1 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK ASP A 0 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK LYS A 1 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK GLU A 18 UNP Q6IYF9 LYS 18 ENGINEERED MUTATION
SEQADV 6RNK ASN A 269 UNP Q6IYF9 LYS 269 ENGINEERED MUTATION
SEQADV 6RNK LEU A 318 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK GLU A 319 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK VAL A 320 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK LEU A 321 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK PHE A 322 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK GLN A 323 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK GLY A 324 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK PRO A 325 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 326 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 327 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 328 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 329 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 330 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 331 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 332 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 333 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 334 UNP Q6IYF9 EXPRESSION TAG
SEQADV 6RNK HIS A 335 UNP Q6IYF9 EXPRESSION TAG
SEQRES 1 A 342 ASP TYR LYS ASP ASP ASP ASP LYS ALA GLN ASN LEU SER
SEQRES 2 A 342 CYS GLU ASN TRP LEU ALA LEU GLU ASN ILE LEU GLU LYS
SEQRES 3 A 342 TYR TYR LEU SER ALA PHE TYR GLY ILE GLU PHE ILE VAL
SEQRES 4 A 342 GLY MET LEU GLY ASN PHE THR VAL VAL PHE GLY TYR LEU
SEQRES 5 A 342 PHE CYS MET LYS ASN TRP ASN SER SER ASN VAL TYR LEU
SEQRES 6 A 342 PHE ASN LEU SER ILE SER ASP LEU ALA PHE LEU CYS THR
SEQRES 7 A 342 LEU PRO MET LEU ILE ARG SER TYR ALA THR GLY ASN TRP
SEQRES 8 A 342 THR TYR GLY ASP VAL LEU CYS ILE SER ASN ARG TYR VAL
SEQRES 9 A 342 LEU HIS ALA ASN LEU TYR THR SER ILE LEU PHE LEU THR
SEQRES 10 A 342 PHE ILE SER ILE ASP ARG TYR LEU LEU MET LYS PHE PRO
SEQRES 11 A 342 PHE ARG GLU HIS ILE LEU GLN LYS LYS GLU PHE ALA ILE
SEQRES 12 A 342 LEU ILE SER LEU ALA VAL TRP VAL LEU VAL THR LEU GLU
SEQRES 13 A 342 VAL LEU PRO MET LEU THR PHE ILE THR SER THR PRO ILE
SEQRES 14 A 342 GLU LYS GLY ASP SER CYS VAL ASP TYR ALA SER SER GLY
SEQRES 15 A 342 ASN PRO LYS TYR SER LEU ILE TYR SER LEU CYS LEU THR
SEQRES 16 A 342 LEU LEU GLY PHE LEU ILE PRO LEU SER VAL MET CYS PHE
SEQRES 17 A 342 PHE TYR TYR LYS MET VAL VAL PHE LEU LYS LYS ARG SER
SEQRES 18 A 342 GLN GLN GLN ALA THR VAL LEU SER LEU ASN LYS PRO LEU
SEQRES 19 A 342 ARG LEU VAL VAL LEU ALA VAL VAL ILE PHE SER VAL LEU
SEQRES 20 A 342 PHE THR PRO TYR HIS ILE MET ARG ASN VAL ARG ILE ALA
SEQRES 21 A 342 SER ARG LEU ASP SER TRP PRO GLN GLY CYS SER GLN LYS
SEQRES 22 A 342 ALA ILE ASN CYS LEU TYR ILE LEU THR ARG PRO LEU ALA
SEQRES 23 A 342 PHE LEU ASN SER ALA VAL ASN PRO ILE PHE TYR PHE LEU
SEQRES 24 A 342 VAL GLY ASP HIS PHE ARG ASP MET LEU PHE SER LYS LEU
SEQRES 25 A 342 ARG GLN TYR PHE LYS SER LEU THR SER PHE ARG LEU LEU
SEQRES 26 A 342 GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS
SEQRES 27 A 342 HIS HIS HIS HIS
SEQRES 1 B 142 ASP TYR LYS ASP ASP ASP ASP LYS GLU VAL GLN LEU VAL
SEQRES 2 B 142 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU
SEQRES 3 B 142 ARG LEU SER CYS GLU ALA SER GLY TYR THR LEU ALA ASN
SEQRES 4 B 142 TYR ALA ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU
SEQRES 5 B 142 ARG GLU GLY VAL SER CYS ILE SER SER GLY GLY SER THR
SEQRES 6 B 142 VAL TYR SER GLU SER VAL LYS ASP ARG PHE THR ILE SER
SEQRES 7 B 142 ARG ASP ASN ALA LYS LYS ILE VAL TYR LEU GLN MET ASN
SEQRES 8 B 142 SER LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA
SEQRES 9 B 142 ALA ASP PRO PHE GLY GLU ARG LEU CYS ILE ASP PRO ASN
SEQRES 10 B 142 THR PHE ALA GLY TYR LEU GLU THR TRP GLY GLN GLY THR
SEQRES 11 B 142 GLN VAL THR VAL SER SER LEU GLU VAL LEU PHE GLN
HET KAZ A 401 33
HET OLC A 402 19
HET OLC A 403 19
HET OLC A 404 25
HET OLC A 405 19
HET OLC A 406 21
HET OLC A 407 14
HET OLC A 408 25
HET OLC A 409 10
HET OLC A 410 12
HET OLC A 411 11
HET OLC A 412 25
HET OLC A 413 17
HET OLC A 414 25
HET GOL A 415 6
HET SO4 A 416 5
HETNAM KAZ 2-[2-[[3-[4-[(4-METHYLPIPERAZIN-1-YL)
HETNAM 2 KAZ METHYL]PHENYL]PHENYL]CARBONYLAMINO]PHENYL]ETHANOIC
HETNAM 3 KAZ ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN OLC 1-OLEOYL-R-GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 KAZ C27 H29 N3 O3
FORMUL 4 OLC 13(C21 H40 O4)
FORMUL 17 GOL C3 H8 O3
FORMUL 18 SO4 O4 S 2-
FORMUL 19 HOH *242(H2 O)
HELIX 1 AA1 CYS A 7 TYR A 20 1 14
HELIX 2 AA2 TYR A 20 MET A 48 1 29
HELIX 3 AA3 ASN A 52 GLY A 82 1 31
HELIX 4 AA4 GLY A 87 PHE A 122 1 36
HELIX 5 AA5 HIS A 127 GLN A 130 5 4
HELIX 6 AA6 LYS A 131 THR A 160 1 30
HELIX 7 AA7 PRO A 161 GLY A 165 5 5
HELIX 8 AA8 ASN A 176 PHE A 192 1 17
HELIX 9 AA9 PHE A 192 SER A 214 1 23
HELIX 10 AB1 LYS A 225 SER A 254 1 30
HELIX 11 AB2 CYS A 263 ASN A 286 1 24
HELIX 12 AB3 PRO A 287 LEU A 292 5 6
HELIX 13 AB4 HIS A 296 LEU A 305 1 10
HELIX 14 AB5 GLN B 94 THR B 98 5 5
HELIX 15 AB6 ARG B 111 ILE B 114 5 4
HELIX 16 AB7 ASP B 115 ALA B 120 1 6
HELIX 17 AB8 GLY B 121 LEU B 123 5 3
SHEET 1 AA1 4 VAL B 10 SER B 15 0
SHEET 2 AA1 4 LEU B 26 GLY B 34 -1 O SER B 29 N SER B 15
SHEET 3 AA1 4 ILE B 85 MET B 90 -1 O MET B 90 N LEU B 26
SHEET 4 AA1 4 PHE B 75 ASP B 80 -1 N THR B 76 O GLN B 89
SHEET 1 AA2 6 GLY B 18 VAL B 20 0
SHEET 2 AA2 6 THR B 130 VAL B 134 1 O THR B 133 N VAL B 20
SHEET 3 AA2 6 ALA B 99 ASP B 106 -1 N TYR B 101 O THR B 130
SHEET 4 AA2 6 ALA B 41 GLN B 47 -1 N PHE B 45 O TYR B 102
SHEET 5 AA2 6 GLU B 54 ILE B 59 -1 O SER B 57 N TRP B 44
SHEET 6 AA2 6 THR B 65 TYR B 67 -1 O VAL B 66 N CYS B 58
SHEET 1 AA3 4 GLY B 18 VAL B 20 0
SHEET 2 AA3 4 THR B 130 VAL B 134 1 O THR B 133 N VAL B 20
SHEET 3 AA3 4 ALA B 99 ASP B 106 -1 N TYR B 101 O THR B 130
SHEET 4 AA3 4 THR B 125 TRP B 126 -1 O THR B 125 N ALA B 105
SSBOND 1 CYS A 7 CYS A 263 1555 1555 2.04
SSBOND 2 CYS A 91 CYS A 168 1555 1555 2.06
SSBOND 3 CYS B 30 CYS B 103 1555 1555 2.05
SSBOND 4 CYS B 58 CYS B 113 1555 1555 2.08
SITE 1 AC1 15 GLU A 18 TYR A 26 SER A 78 TYR A 79
SITE 2 AC1 15 GLY A 82 TRP A 84 ASN A 94 ARG A 95
SITE 3 AC1 15 LEU A 98 CYS A 168 TYR A 244 ARG A 276
SITE 4 AC1 15 PHE A 280 GOL A 415 HOH A 510
SITE 1 AC2 9 TYR A 57 PHE A 111 ILE A 114 ASP A 115
SITE 2 AC2 9 LEU A 129 PHE A 134 ILE A 138 OLC A 403
SITE 3 AC2 9 OLC A 408
SITE 1 AC3 9 ILE A 114 TYR A 117 ILE A 128 LEU A 129
SITE 2 AC3 9 LEU A 137 PHE A 201 OLC A 402 OLC A 404
SITE 3 AC3 9 HOH A 564
SITE 1 AC4 10 TRP A 51 LYS A 131 LYS A 132 GLU A 133
SITE 2 AC4 10 PHE A 201 OLC A 403 OLC A 408 HOH A 521
SITE 3 AC4 10 HOH A 550 THR B 118
SITE 1 AC5 7 PHE A 156 THR A 158 GLY A 175 ASN A 176
SITE 2 AC5 7 TYR A 179 SER A 180 TYR A 183
SITE 1 AC6 8 LYS A 49 TRP A 51 ASN A 60 LYS A 132
SITE 2 AC6 8 ILE A 136 SER A 139 TRP A 143 OLC A 409
SITE 1 AC7 3 ALA A 67 SER A 93 ASN A 94
SITE 1 AC8 5 SER A 197 VAL A 198 TYR A 204 OLC A 402
SITE 2 AC8 5 OLC A 404
SITE 1 AC9 4 LEU A 45 TRP A 51 PHE A 59 OLC A 406
SITE 1 AD1 4 LEU A 185 PHE A 192 VAL A 250 HOH A 548
SITE 1 AD2 3 ILE A 182 CYS A 186 LEU A 189
SITE 1 AD3 4 TYR A 21 ILE A 246 MET A 247 VAL A 250
SITE 1 AD4 4 TRP A 10 LEU A 17 TYR A 20 ALA A 267
SITE 1 AD5 9 TYR A 86 GLY A 87 ASP A 88 VAL A 89
SITE 2 AD5 9 LEU A 90 TYR A 96 HOH A 541 HOH A 554
SITE 3 AD5 9 GLY B 17
SITE 1 AD6 8 TYR A 79 ARG A 95 CYS A 168 ASP A 170
SITE 2 AD6 8 ARG A 276 KAZ A 401 HOH A 524 HOH A 559
SITE 1 AD7 3 HIS A 127 ILE A 128 LEU A 129
CRYST1 76.830 150.930 68.230 90.00 112.42 90.00 C 1 2 1 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 0.013016 0.000000 0.005370 0.00000
SCALE2 0.000000 0.006626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015855 0.00000
ATOM 1 N CYS A 7 -8.279 -7.491 2.946 1.00 66.09 N
ANISOU 1 N CYS A 7 10337 7014 7759 -166 228 -1253 N
ATOM 2 CA CYS A 7 -7.860 -6.102 2.763 1.00 65.85 C
ANISOU 2 CA CYS A 7 10306 7078 7635 -128 237 -1188 C
ATOM 3 C CYS A 7 -6.348 -5.945 3.024 1.00 64.69 C
ANISOU 3 C CYS A 7 10162 6964 7453 -57 435 -1119 C
ATOM 4 O CYS A 7 -5.917 -4.953 3.620 1.00 63.05 O
ANISOU 4 O CYS A 7 9853 6841 7264 -34 481 -1036 O
ATOM 5 CB CYS A 7 -8.691 -5.169 3.646 1.00 67.32 C
ANISOU 5 CB CYS A 7 10314 7339 7926 -162 145 -1131 C
ATOM 6 SG CYS A 7 -10.481 -5.283 3.376 1.00 72.02 S
ANISOU 6 SG CYS A 7 10870 7894 8600 -244 -88 -1215 S
ATOM 7 N GLU A 8 -5.548 -6.933 2.562 1.00 58.60 N
ANISOU 7 N GLU A 8 9504 6122 6642 -23 549 -1161 N
ATOM 8 CA GLU A 8 -4.087 -6.976 2.720 1.00 57.45 C
ANISOU 8 CA GLU A 8 9358 5987 6484 48 741 -1114 C
ATOM 9 C GLU A 8 -3.387 -5.784 2.038 1.00 56.85 C
ANISOU 9 C GLU A 8 9351 5969 6279 85 800 -1080 C
ATOM 10 O GLU A 8 -2.326 -5.358 2.497 1.00 56.07 O
ANISOU 10 O GLU A 8 9175 5915 6216 132 934 -1016 O
ATOM 11 CB GLU A 8 -3.501 -8.300 2.191 1.00 59.37 C
ANISOU 11 CB GLU A 8 9724 6126 6706 76 841 -1182 C
ATOM 12 CG GLU A 8 -4.289 -9.554 2.558 1.00 75.06 C
ANISOU 12 CG GLU A 8 11695 8030 8795 31 774 -1236 C
ATOM 13 CD GLU A 8 -5.297 -10.010 1.517 1.00 99.74 C
ANISOU 13 CD GLU A 8 14970 11084 11841 -23 635 -1345 C
ATOM 14 OE1 GLU A 8 -4.875 -10.335 0.383 1.00106.37 O
ANISOU 14 OE1 GLU A 8 16002 11867 12545 4 676 -1413 O
ATOM 15 OE2 GLU A 8 -6.507 -10.051 1.837 1.00 88.45 O
ANISOU 15 OE2 GLU A 8 13468 9650 10490 -91 485 -1367 O
ATOM 16 N ASN A 9 -3.978 -5.265 0.942 1.00 50.24 N
ANISOU 16 N ASN A 9 8667 5126 5298 66 698 -1125 N
ATOM 17 CA ASN A 9 -3.446 -4.123 0.192 1.00 48.46 C
ANISOU 17 CA ASN A 9 8541 4941 4932 96 748 -1094 C
ATOM 18 C ASN A 9 -3.553 -2.844 1.009 1.00 49.29 C
ANISOU 18 C ASN A 9 8481 5146 5100 89 716 -1003 C
ATOM 19 O ASN A 9 -2.601 -2.060 1.044 1.00 48.07 O
ANISOU 19 O ASN A 9 8307 5036 4923 124 842 -945 O
ATOM 20 CB ASN A 9 -4.121 -3.976 -1.185 1.00 47.77 C
ANISOU 20 CB ASN A 9 8684 4807 4661 83 630 -1167 C
ATOM 21 CG ASN A 9 -5.631 -3.818 -1.180 1.00 69.21 C
ANISOU 21 CG ASN A 9 11372 7527 7398 27 387 -1202 C
ATOM 22 OD1 ASN A 9 -6.347 -4.339 -0.313 1.00 64.87 O
ANISOU 22 OD1 ASN A 9 10666 6978 7006 -15 306 -1209 O
ATOM 23 ND2 ASN A 9 -6.152 -3.100 -2.171 1.00 57.16 N
ANISOU 23 ND2 ASN A 9 10003 5997 5716 27 265 -1227 N
ATOM 24 N TRP A 10 -4.697 -2.650 1.686 1.00 44.93 N
ANISOU 24 N TRP A 10 7806 4626 4639 42 557 -993 N
ATOM 25 CA TRP A 10 -4.939 -1.493 2.545 1.00 44.69 C
ANISOU 25 CA TRP A 10 7615 4684 4680 31 516 -913 C
ATOM 26 C TRP A 10 -4.106 -1.548 3.821 1.00 46.91 C
ANISOU 26 C TRP A 10 7719 5008 5097 54 642 -844 C
ATOM 27 O TRP A 10 -3.704 -0.494 4.327 1.00 44.17 O
ANISOU 27 O TRP A 10 7279 4731 4771 67 678 -774 O
ATOM 28 CB TRP A 10 -6.425 -1.298 2.818 1.00 43.37 C
ANISOU 28 CB TRP A 10 7377 4529 4575 -23 319 -934 C
ATOM 29 CG TRP A 10 -7.193 -0.931 1.582 1.00 44.33 C
ANISOU 29 CG TRP A 10 7662 4622 4559 -34 170 -991 C
ATOM 30 CD1 TRP A 10 -7.940 -1.767 0.809 1.00 47.52 C
ANISOU 30 CD1 TRP A 10 8183 4950 4921 -60 52 -1086 C
ATOM 31 CD2 TRP A 10 -7.268 0.364 0.963 1.00 43.86 C
ANISOU 31 CD2 TRP A 10 7682 4602 4382 -15 116 -958 C
ATOM 32 NE1 TRP A 10 -8.482 -1.077 -0.249 1.00 47.34 N
ANISOU 32 NE1 TRP A 10 8310 4920 4757 -54 -85 -1116 N
ATOM 33 CE2 TRP A 10 -8.107 0.241 -0.165 1.00 48.40 C
ANISOU 33 CE2 TRP A 10 8426 5123 4841 -26 -48 -1035 C
ATOM 34 CE3 TRP A 10 -6.709 1.617 1.253 1.00 44.61 C
ANISOU 34 CE3 TRP A 10 7726 4766 4458 10 187 -873 C
ATOM 35 CZ2 TRP A 10 -8.394 1.320 -1.008 1.00 47.35 C
ANISOU 35 CZ2 TRP A 10 8423 5002 4566 -5 -144 -1023 C
ATOM 36 CZ3 TRP A 10 -7.001 2.688 0.427 1.00 46.08 C
ANISOU 36 CZ3 TRP A 10 8035 4963 4511 24 104 -861 C
ATOM 37 CH2 TRP A 10 -7.839 2.538 -0.685 1.00 47.00 C
ANISOU 37 CH2 TRP A 10 8328 5024 4507 20 -61 -932 C
ATOM 38 N LEU A 11 -3.774 -2.774 4.288 1.00 44.52 N
ANISOU 38 N LEU A 11 7383 4654 4877 63 709 -865 N
ATOM 39 CA LEU A 11 -2.894 -2.993 5.443 1.00 45.01 C
ANISOU 39 CA LEU A 11 7302 4740 5058 97 822 -805 C
ATOM 40 C LEU A 11 -1.456 -2.611 5.046 1.00 47.14 C
ANISOU 40 C LEU A 11 7606 5023 5281 156 981 -781 C
ATOM 41 O LEU A 11 -0.740 -2.021 5.844 1.00 47.02 O
ANISOU 41 O LEU A 11 7464 5063 5338 183 1043 -718 O
ATOM 42 CB LEU A 11 -2.969 -4.450 5.954 1.00 45.40 C
ANISOU 42 CB LEU A 11 7333 4716 5200 96 844 -835 C
ATOM 43 CG LEU A 11 -2.146 -4.782 7.228 1.00 50.48 C
ANISOU 43 CG LEU A 11 7840 5373 5967 139 936 -773 C
ATOM 44 CD1 LEU A 11 -2.632 -3.979 8.463 1.00 49.84 C
ANISOU 44 CD1 LEU A 11 7603 5366 5967 115 872 -701 C
ATOM 45 CD2 LEU A 11 -2.125 -6.297 7.507 1.00 51.31 C
ANISOU 45 CD2 LEU A 11 7970 5386 6140 147 970 -807 C
ATOM 46 N ALA A 12 -1.056 -2.911 3.801 1.00 42.50 N
ANISOU 46 N ALA A 12 7192 4380 4575 175 1047 -837 N
ATOM 47 CA ALA A 12 0.254 -2.515 3.271 1.00 41.57 C
ANISOU 47 CA ALA A 12 7120 4264 4412 225 1215 -823 C
ATOM 48 C ALA A 12 0.346 -0.983 3.230 1.00 45.51 C
ANISOU 48 C ALA A 12 7586 4839 4868 216 1209 -765 C
ATOM 49 O ALA A 12 1.381 -0.440 3.616 1.00 45.55 O
ANISOU 49 O ALA A 12 7496 4877 4933 247 1326 -718 O
ATOM 50 CB ALA A 12 0.465 -3.091 1.879 1.00 41.69 C
ANISOU 50 CB ALA A 12 7356 4197 4286 240 1281 -899 C
ATOM 51 N LEU A 13 -0.745 -0.287 2.791 1.00 41.54 N
ANISOU 51 N LEU A 13 7153 4357 4275 175 1064 -769 N
ATOM 52 CA LEU A 13 -0.800 1.178 2.742 1.00 40.94 C
ANISOU 52 CA LEU A 13 7058 4344 4155 166 1041 -713 C
ATOM 53 C LEU A 13 -0.694 1.766 4.150 1.00 43.16 C
ANISOU 53 C LEU A 13 7115 4701 4584 161 1025 -643 C
ATOM 54 O LEU A 13 0.115 2.674 4.353 1.00 41.36 O
ANISOU 54 O LEU A 13 6827 4513 4376 177 1115 -593 O
ATOM 55 CB LEU A 13 -2.062 1.701 2.016 1.00 41.57 C
ANISOU 55 CB LEU A 13 7256 4421 4118 131 867 -736 C
ATOM 56 CG LEU A 13 -2.286 3.239 2.011 1.00 47.09 C
ANISOU 56 CG LEU A 13 7937 5180 4777 123 819 -676 C
ATOM 57 CD1 LEU A 13 -1.203 3.947 1.271 1.00 47.46 C
ANISOU 57 CD1 LEU A 13 8089 5216 4726 152 980 -650 C
ATOM 58 CD2 LEU A 13 -3.595 3.621 1.364 1.00 49.17 C
ANISOU 58 CD2 LEU A 13 8305 5433 4945 98 625 -704 C
ATOM 59 N GLU A 14 -1.480 1.233 5.124 1.00 39.98 N
ANISOU 59 N GLU A 14 6597 4309 4285 137 921 -641 N
ATOM 60 CA GLU A 14 -1.458 1.684 6.522 1.00 39.77 C
ANISOU 60 CA GLU A 14 6378 4344 4387 133 902 -579 C
ATOM 61 C GLU A 14 -0.028 1.628 7.060 1.00 41.76 C
ANISOU 61 C GLU A 14 6543 4609 4716 181 1048 -546 C
ATOM 62 O GLU A 14 0.440 2.611 7.616 1.00 42.57 O
ANISOU 62 O GLU A 14 6546 4768 4861 188 1073 -495 O
ATOM 63 CB GLU A 14 -2.363 0.800 7.414 1.00 41.30 C
ANISOU 63 CB GLU A 14 6493 4522 4677 106 811 -591 C
ATOM 64 CG GLU A 14 -3.853 1.097 7.354 1.00 51.43 C
ANISOU 64 CG GLU A 14 7777 5812 5951 53 653 -609 C
ATOM 65 CD GLU A 14 -4.746 0.163 8.158 1.00 69.29 C
ANISOU 65 CD GLU A 14 9966 8043 8319 18 589 -627 C
ATOM 66 OE1 GLU A 14 -4.416 -1.040 8.272 1.00 57.12 O
ANISOU 66 OE1 GLU A 14 8449 6444 6813 30 645 -653 O
ATOM 67 OE2 GLU A 14 -5.793 0.632 8.660 1.00 60.58 O
ANISOU 67 OE2 GLU A 14 8785 6966 7269 -21 488 -615 O
ATOM 68 N ASN A 15 0.662 0.493 6.860 1.00 36.67 N
ANISOU 68 N ASN A 15 5935 3906 4094 216 1140 -581 N
ATOM 69 CA ASN A 15 2.024 0.258 7.319 1.00 36.53 C
ANISOU 69 CA ASN A 15 5829 3884 4166 271 1271 -562 C
ATOM 70 C ASN A 15 3.019 1.215 6.699 1.00 40.36 C
ANISOU 70 C ASN A 15 6328 4389 4620 289 1391 -548 C
ATOM 71 O ASN A 15 3.838 1.769 7.421 1.00 39.18 O
ANISOU 71 O ASN A 15 6041 4278 4566 311 1439 -507 O
ATOM 72 CB ASN A 15 2.434 -1.217 7.121 1.00 36.29 C
ANISOU 72 CB ASN A 15 5850 3775 4165 307 1338 -610 C
ATOM 73 CG ASN A 15 1.717 -2.174 8.067 1.00 54.29 C
ANISOU 73 CG ASN A 15 8076 6032 6519 297 1247 -608 C
ATOM 74 OD1 ASN A 15 1.324 -1.816 9.177 1.00 51.28 O
ANISOU 74 OD1 ASN A 15 7580 5697 6205 283 1172 -559 O
ATOM 75 ND2 ASN A 15 1.523 -3.417 7.649 1.00 45.78 N
ANISOU 75 ND2 ASN A 15 7091 4875 5430 302 1260 -662 N
ATOM 76 N ILE A 16 2.932 1.431 5.370 1.00 37.83 N
ANISOU 76 N ILE A 16 6177 4033 4162 277 1436 -583 N
ATOM 77 CA ILE A 16 3.783 2.373 4.641 1.00 36.66 C
ANISOU 77 CA ILE A 16 6075 3889 3964 286 1566 -569 C
ATOM 78 C ILE A 16 3.517 3.819 5.086 1.00 38.77 C
ANISOU 78 C ILE A 16 6264 4229 4239 256 1504 -509 C
ATOM 79 O ILE A 16 4.473 4.563 5.315 1.00 38.34 O
ANISOU 79 O ILE A 16 6119 4197 4251 267 1606 -478 O
ATOM 80 CB ILE A 16 3.682 2.176 3.115 1.00 39.49 C
ANISOU 80 CB ILE A 16 6669 4181 4153 284 1629 -620 C
ATOM 81 CG1 ILE A 16 4.518 0.947 2.667 1.00 40.46 C
ANISOU 81 CG1 ILE A 16 6848 4227 4296 329 1772 -675 C
ATOM 82 CG2 ILE A 16 4.129 3.436 2.373 1.00 39.79 C
ANISOU 82 CG2 ILE A 16 6785 4228 4106 276 1724 -591 C
ATOM 83 CD1 ILE A 16 4.015 0.219 1.383 1.00 45.98 C
ANISOU 83 CD1 ILE A 16 7794 4849 4829 325 1771 -746 C
ATOM 84 N LEU A 17 2.235 4.216 5.228 1.00 35.07 N
ANISOU 84 N LEU A 17 5818 3791 3716 217 1339 -497 N
ATOM 85 CA LEU A 17 1.882 5.571 5.686 1.00 33.74 C
ANISOU 85 CA LEU A 17 5576 3685 3557 190 1271 -443 C
ATOM 86 C LEU A 17 2.463 5.868 7.056 1.00 37.14 C
ANISOU 86 C LEU A 17 5799 4168 4142 201 1282 -400 C
ATOM 87 O LEU A 17 2.984 6.962 7.287 1.00 36.48 O
ANISOU 87 O LEU A 17 5649 4121 4092 196 1325 -362 O
ATOM 88 CB LEU A 17 0.361 5.814 5.707 1.00 33.38 C
ANISOU 88 CB LEU A 17 5570 3659 3456 153 1087 -444 C
ATOM 89 CG LEU A 17 -0.339 5.930 4.348 1.00 38.22 C
ANISOU 89 CG LEU A 17 6391 4229 3903 141 1031 -479 C
ATOM 90 CD1 LEU A 17 -1.840 6.169 4.534 1.00 36.25 C
ANISOU 90 CD1 LEU A 17 6134 3999 3641 108 832 -484 C
ATOM 91 CD2 LEU A 17 0.336 7.002 3.429 1.00 39.40 C
ANISOU 91 CD2 LEU A 17 6656 4367 3946 150 1139 -454 C
ATOM 92 N GLU A 18 2.406 4.883 7.961 1.00 33.91 N
ANISOU 92 N GLU A 18 5299 3757 3827 217 1244 -408 N
ATOM 93 CA GLU A 18 2.923 5.071 9.320 1.00 33.61 C
ANISOU 93 CA GLU A 18 5084 3762 3924 235 1235 -369 C
ATOM 94 C GLU A 18 4.443 5.116 9.327 1.00 38.17 C
ANISOU 94 C GLU A 18 5588 4329 4584 276 1377 -369 C
ATOM 95 O GLU A 18 5.023 6.029 9.906 1.00 37.41 O
ANISOU 95 O GLU A 18 5380 4274 4560 277 1392 -337 O
ATOM 96 CB GLU A 18 2.439 3.947 10.235 1.00 34.54 C
ANISOU 96 CB GLU A 18 5153 3867 4105 245 1161 -375 C
ATOM 97 CG GLU A 18 0.974 4.084 10.606 1.00 38.97 C
ANISOU 97 CG GLU A 18 5724 4448 4636 199 1023 -367 C
ATOM 98 CD GLU A 18 0.459 3.040 11.570 1.00 49.02 C
ANISOU 98 CD GLU A 18 6951 5700 5975 202 967 -367 C
ATOM 99 OE1 GLU A 18 1.260 2.185 12.017 1.00 39.98 O
ANISOU 99 OE1 GLU A 18 5770 4525 4894 246 1024 -368 O
ATOM 100 OE2 GLU A 18 -0.751 3.081 11.887 1.00 38.69 O
ANISOU 100 OE2 GLU A 18 5642 4399 4661 161 870 -365 O
ATOM 101 N LYS A 19 5.077 4.151 8.652 1.00 34.84 N
ANISOU 101 N LYS A 19 5230 3848 4160 310 1481 -411 N
ATOM 102 CA LYS A 19 6.521 4.014 8.632 1.00 36.37 C
ANISOU 102 CA LYS A 19 5343 4019 4456 356 1623 -421 C
ATOM 103 C LYS A 19 7.237 5.128 7.870 1.00 41.32 C
ANISOU 103 C LYS A 19 5988 4648 5065 340 1748 -414 C
ATOM 104 O LYS A 19 8.277 5.594 8.333 1.00 40.47 O
ANISOU 104 O LYS A 19 5740 4554 5083 358 1818 -403 O
ATOM 105 CB LYS A 19 6.918 2.613 8.096 1.00 38.95 C
ANISOU 105 CB LYS A 19 5741 4271 4786 399 1706 -472 C
ATOM 106 CG LYS A 19 8.406 2.316 8.111 1.00 53.56 C
ANISOU 106 CG LYS A 19 7493 6089 6768 456 1854 -490 C
ATOM 107 CD LYS A 19 8.691 0.811 8.064 1.00 63.28 C
ANISOU 107 CD LYS A 19 8752 7253 8041 510 1891 -531 C
ATOM 108 CE LYS A 19 10.168 0.492 7.937 1.00 72.04 C
ANISOU 108 CE LYS A 19 9766 8319 9288 573 2048 -557 C
ATOM 109 NZ LYS A 19 10.935 0.877 9.158 1.00 85.34 N
ANISOU 109 NZ LYS A 19 11235 10045 11144 607 2001 -525 N
ATOM 110 N TYR A 20 6.698 5.537 6.710 1.00 38.47 N
ANISOU 110 N TYR A 20 5800 4265 4549 307 1776 -424 N
ATOM 111 CA TYR A 20 7.351 6.506 5.833 1.00 37.79 C
ANISOU 111 CA TYR A 20 5773 4162 4422 292 1918 -416 C
ATOM 112 C TYR A 20 6.705 7.884 5.787 1.00 39.45 C
ANISOU 112 C TYR A 20 6014 4415 4561 244 1846 -371 C
ATOM 113 O TYR A 20 7.412 8.884 5.913 1.00 39.65 O
ANISOU 113 O TYR A 20 5961 4454 4650 231 1926 -345 O
ATOM 114 CB TYR A 20 7.484 5.928 4.413 1.00 39.35 C
ANISOU 114 CB TYR A 20 6178 4283 4491 302 2044 -462 C
ATOM 115 CG TYR A 20 8.350 4.694 4.366 1.00 43.03 C
ANISOU 115 CG TYR A 20 6609 4697 5045 354 2157 -509 C
ATOM 116 CD1 TYR A 20 9.735 4.793 4.248 1.00 46.07 C
ANISOU 116 CD1 TYR A 20 6901 5051 5553 383 2347 -520 C
ATOM 117 CD2 TYR A 20 7.788 3.420 4.432 1.00 43.40 C
ANISOU 117 CD2 TYR A 20 6710 4717 5065 374 2079 -545 C
ATOM 118 CE1 TYR A 20 10.541 3.655 4.221 1.00 47.10 C
ANISOU 118 CE1 TYR A 20 6987 5128 5780 438 2450 -566 C
ATOM 119 CE2 TYR A 20 8.588 2.278 4.434 1.00 44.63 C
ANISOU 119 CE2 TYR A 20 6831 4818 5309 428 2181 -586 C
ATOM 120 CZ TYR A 20 9.963 2.402 4.313 1.00 55.90 C
ANISOU 120 CZ TYR A 20 8165 6217 6858 463 2365 -597 C
ATOM 121 OH TYR A 20 10.759 1.287 4.286 1.00 64.70 O
ANISOU 121 OH TYR A 20 9241 7272 8070 523 2466 -640 O
ATOM 122 N TYR A 21 5.392 7.965 5.585 1.00 34.47 N
ANISOU 122 N TYR A 21 5492 3799 3807 219 1699 -365 N
ATOM 123 CA TYR A 21 4.745 9.280 5.530 1.00 33.09 C
ANISOU 123 CA TYR A 21 5347 3659 3568 182 1624 -323 C
ATOM 124 C TYR A 21 4.777 10.009 6.885 1.00 36.65 C
ANISOU 124 C TYR A 21 5599 4176 4152 170 1547 -282 C
ATOM 125 O TYR A 21 5.186 11.172 6.933 1.00 35.92 O
ANISOU 125 O TYR A 21 5467 4098 4084 151 1595 -250 O
ATOM 126 CB TYR A 21 3.312 9.145 4.990 1.00 34.04 C
ANISOU 126 CB TYR A 21 5619 3773 3544 165 1472 -334 C
ATOM 127 CG TYR A 21 2.469 10.401 5.077 1.00 34.69 C
ANISOU 127 CG TYR A 21 5714 3890 3576 135 1360 -291 C
ATOM 128 CD1 TYR A 21 2.533 11.377 4.088 1.00 35.81 C
ANISOU 128 CD1 TYR A 21 6003 4004 3600 126 1415 -270 C
ATOM 129 CD2 TYR A 21 1.543 10.569 6.101 1.00 34.93 C
ANISOU 129 CD2 TYR A 21 5628 3974 3670 120 1200 -274 C
ATOM 130 CE1 TYR A 21 1.711 12.498 4.125 1.00 35.95 C
ANISOU 130 CE1 TYR A 21 6044 4045 3569 106 1303 -231 C
ATOM 131 CE2 TYR A 21 0.736 11.699 6.165 1.00 35.05 C
ANISOU 131 CE2 TYR A 21 5654 4017 3648 98 1098 -239 C
ATOM 132 CZ TYR A 21 0.833 12.666 5.180 1.00 36.38 C
ANISOU 132 CZ TYR A 21 5962 4156 3705 93 1145 -217 C
ATOM 133 OH TYR A 21 0.021 13.760 5.224 1.00 31.90 O
ANISOU 133 OH TYR A 21 5410 3607 3102 79 1038 -183 O
ATOM 134 N LEU A 22 4.350 9.336 7.983 1.00 33.10 N
ANISOU 134 N LEU A 22 5036 3760 3782 180 1433 -284 N
ATOM 135 CA LEU A 22 4.311 9.981 9.309 1.00 32.50 C
ANISOU 135 CA LEU A 22 4794 3742 3812 172 1352 -249 C
ATOM 136 C LEU A 22 5.703 10.351 9.802 1.00 37.86 C
ANISOU 136 C LEU A 22 5333 4428 4626 189 1457 -243 C
ATOM 137 O LEU A 22 5.907 11.488 10.232 1.00 34.79 O
ANISOU 137 O LEU A 22 4869 4070 4281 168 1448 -214 O
ATOM 138 CB LEU A 22 3.525 9.152 10.353 1.00 31.65 C
ANISOU 138 CB LEU A 22 4623 3657 3746 180 1222 -251 C
ATOM 139 CG LEU A 22 2.006 8.971 10.095 1.00 34.64 C
ANISOU 139 CG LEU A 22 5096 4035 4030 152 1096 -257 C
ATOM 140 CD1 LEU A 22 1.320 8.276 11.288 1.00 32.89 C
ANISOU 140 CD1 LEU A 22 4790 3832 3875 153 994 -253 C
ATOM 141 CD2 LEU A 22 1.308 10.310 9.894 1.00 33.07 C
ANISOU 141 CD2 LEU A 22 4926 3865 3775 119 1033 -228 C
ATOM 142 N SER A 23 6.679 9.419 9.644 1.00 37.72 N
ANISOU 142 N SER A 23 5283 4372 4675 228 1560 -275 N
ATOM 143 CA SER A 23 8.092 9.628 9.995 1.00 38.77 C
ANISOU 143 CA SER A 23 5273 4499 4959 251 1666 -282 C
ATOM 144 C SER A 23 8.675 10.858 9.343 1.00 42.96 C
ANISOU 144 C SER A 23 5814 5018 5491 217 1785 -270 C
ATOM 145 O SER A 23 9.302 11.663 10.025 1.00 44.21 O
ANISOU 145 O SER A 23 5831 5201 5766 207 1787 -256 O
ATOM 146 CB SER A 23 8.940 8.418 9.594 1.00 42.66 C
ANISOU 146 CB SER A 23 5765 4938 5508 300 1778 -324 C
ATOM 147 OG SER A 23 8.598 7.340 10.447 1.00 55.45 O
ANISOU 147 OG SER A 23 7340 6565 7163 336 1668 -330 O
ATOM 148 N ALA A 24 8.497 10.987 8.021 1.00 39.26 N
ANISOU 148 N ALA A 24 5520 4504 4891 200 1885 -276 N
ATOM 149 CA ALA A 24 9.041 12.088 7.226 1.00 38.67 C
ANISOU 149 CA ALA A 24 5498 4401 4796 168 2026 -261 C
ATOM 150 C ALA A 24 8.365 13.413 7.562 1.00 40.79 C
ANISOU 150 C ALA A 24 5765 4709 5025 125 1929 -215 C
ATOM 151 O ALA A 24 9.065 14.387 7.832 1.00 40.39 O
ANISOU 151 O ALA A 24 5615 4660 5070 101 1993 -200 O
ATOM 152 CB ALA A 24 8.919 11.783 5.740 1.00 39.36 C
ANISOU 152 CB ALA A 24 5809 4422 4724 168 2147 -278 C
ATOM 153 N PHE A 25 7.015 13.437 7.578 1.00 35.06 N
ANISOU 153 N PHE A 25 5138 4010 4173 115 1772 -197 N
ATOM 154 CA PHE A 25 6.224 14.627 7.892 1.00 33.74 C
ANISOU 154 CA PHE A 25 4977 3877 3966 82 1667 -156 C
ATOM 155 C PHE A 25 6.484 15.128 9.320 1.00 36.76 C
ANISOU 155 C PHE A 25 5156 4313 4497 76 1591 -143 C
ATOM 156 O PHE A 25 6.736 16.323 9.494 1.00 34.89 O
ANISOU 156 O PHE A 25 4876 4082 4298 46 1613 -118 O
ATOM 157 CB PHE A 25 4.715 14.403 7.614 1.00 34.96 C
ANISOU 157 CB PHE A 25 5262 4044 3978 81 1511 -150 C
ATOM 158 CG PHE A 25 3.885 15.591 7.136 1.00 36.47 C
ANISOU 158 CG PHE A 25 5563 4233 4063 55 1449 -113 C
ATOM 159 CD1 PHE A 25 2.749 15.396 6.357 1.00 39.58 C
ANISOU 159 CD1 PHE A 25 6123 4609 4309 59 1351 -118 C
ATOM 160 CD2 PHE A 25 4.205 16.894 7.523 1.00 38.68 C
ANISOU 160 CD2 PHE A 25 5773 4524 4399 30 1474 -78 C
ATOM 161 CE1 PHE A 25 1.930 16.478 5.999 1.00 41.91 C
ANISOU 161 CE1 PHE A 25 6508 4900 4517 46 1269 -83 C
ATOM 162 CE2 PHE A 25 3.401 17.983 7.138 1.00 41.86 C
ANISOU 162 CE2 PHE A 25 6275 4919 4709 13 1408 -41 C
ATOM 163 CZ PHE A 25 2.260 17.768 6.398 1.00 40.61 C
ANISOU 163 CZ PHE A 25 6277 4746 4408 25 1302 -42 C
ATOM 164 N TYR A 26 6.452 14.231 10.336 1.00 33.73 N
ANISOU 164 N TYR A 26 4659 3962 4193 104 1504 -160 N
ATOM 165 CA TYR A 26 6.762 14.648 11.711 1.00 32.20 C
ANISOU 165 CA TYR A 26 4292 3813 4128 105 1429 -151 C
ATOM 166 C TYR A 26 8.250 15.034 11.861 1.00 37.02 C
ANISOU 166 C TYR A 26 4772 4406 4888 107 1547 -166 C
ATOM 167 O TYR A 26 8.559 15.941 12.623 1.00 37.34 O
ANISOU 167 O TYR A 26 4702 4470 5014 88 1511 -156 O
ATOM 168 CB TYR A 26 6.332 13.620 12.768 1.00 31.81 C
ANISOU 168 CB TYR A 26 4181 3794 4113 138 1308 -159 C
ATOM 169 CG TYR A 26 4.831 13.533 12.966 1.00 31.83 C
ANISOU 169 CG TYR A 26 4261 3819 4014 124 1178 -143 C
ATOM 170 CD1 TYR A 26 4.080 14.669 13.271 1.00 32.10 C
ANISOU 170 CD1 TYR A 26 4297 3882 4018 92 1104 -114 C
ATOM 171 CD2 TYR A 26 4.162 12.311 12.874 1.00 31.38 C
ANISOU 171 CD2 TYR A 26 4265 3749 3908 143 1132 -159 C
ATOM 172 CE1 TYR A 26 2.700 14.599 13.446 1.00 30.07 C
ANISOU 172 CE1 TYR A 26 4094 3641 3691 81 992 -104 C
ATOM 173 CE2 TYR A 26 2.782 12.225 13.089 1.00 31.20 C
ANISOU 173 CE2 TYR A 26 4292 3742 3820 125 1017 -150 C
ATOM 174 CZ TYR A 26 2.054 13.377 13.351 1.00 34.71 C
ANISOU 174 CZ TYR A 26 4730 4215 4241 96 949 -124 C
ATOM 175 OH TYR A 26 0.691 13.335 13.525 1.00 30.42 O
ANISOU 175 OH TYR A 26 4223 3682 3653 79 844 -119 O
ATOM 176 N GLY A 27 9.136 14.366 11.126 1.00 34.62 N
ANISOU 176 N GLY A 27 4478 4057 4621 128 1687 -195 N
ATOM 177 CA GLY A 27 10.568 14.671 11.119 1.00 35.82 C
ANISOU 177 CA GLY A 27 4499 4180 4932 128 1821 -218 C
ATOM 178 C GLY A 27 10.860 16.098 10.673 1.00 41.39 C
ANISOU 178 C GLY A 27 5215 4866 5646 73 1912 -198 C
ATOM 179 O GLY A 27 11.669 16.788 11.301 1.00 40.72 O
ANISOU 179 O GLY A 27 4974 4785 5713 57 1926 -207 O
ATOM 180 N ILE A 28 10.167 16.563 9.597 1.00 38.78 N
ANISOU 180 N ILE A 28 5076 4509 5151 45 1963 -171 N
ATOM 181 CA ILE A 28 10.260 17.927 9.036 1.00 38.37 C
ANISOU 181 CA ILE A 28 5084 4426 5068 -6 2050 -141 C
ATOM 182 C ILE A 28 9.658 18.943 10.043 1.00 39.85 C
ANISOU 182 C ILE A 28 5198 4664 5279 -32 1897 -113 C
ATOM 183 O ILE A 28 10.244 19.996 10.286 1.00 39.11 O
ANISOU 183 O ILE A 28 5021 4557 5281 -69 1948 -107 O
ATOM 184 CB ILE A 28 9.592 18.007 7.626 1.00 41.90 C
ANISOU 184 CB ILE A 28 5785 4827 5310 -14 2121 -118 C
ATOM 185 CG1 ILE A 28 10.398 17.166 6.606 1.00 43.25 C
ANISOU 185 CG1 ILE A 28 6030 4934 5470 6 2312 -150 C
ATOM 186 CG2 ILE A 28 9.488 19.477 7.127 1.00 43.09 C
ANISOU 186 CG2 ILE A 28 6022 4943 5406 -62 2181 -74 C
ATOM 187 CD1 ILE A 28 9.621 16.705 5.356 1.00 53.56 C
ANISOU 187 CD1 ILE A 28 7599 6200 6552 20 2333 -144 C
ATOM 188 N GLU A 29 8.510 18.605 10.639 1.00 33.68 N
ANISOU 188 N GLU A 29 4445 3935 4419 -13 1718 -101 N
ATOM 189 CA GLU A 29 7.857 19.450 11.638 1.00 32.29 C
ANISOU 189 CA GLU A 29 4206 3803 4258 -31 1575 -79 C
ATOM 190 C GLU A 29 8.751 19.603 12.860 1.00 36.50 C
ANISOU 190 C GLU A 29 4536 4362 4969 -29 1543 -103 C
ATOM 191 O GLU A 29 8.824 20.690 13.403 1.00 35.68 O
ANISOU 191 O GLU A 29 4370 4266 4919 -60 1510 -93 O
ATOM 192 CB GLU A 29 6.500 18.869 12.049 1.00 32.93 C
ANISOU 192 CB GLU A 29 4345 3927 4238 -9 1412 -69 C
ATOM 193 CG GLU A 29 5.479 19.031 10.944 1.00 39.91 C
ANISOU 193 CG GLU A 29 5420 4787 4955 -16 1402 -46 C
ATOM 194 CD GLU A 29 4.094 18.468 11.183 1.00 48.99 C
ANISOU 194 CD GLU A 29 6626 5968 6020 1 1249 -43 C
ATOM 195 OE1 GLU A 29 3.818 17.896 12.264 1.00 33.36 O
ANISOU 195 OE1 GLU A 29 4547 4029 4100 16 1155 -55 O
ATOM 196 OE2 GLU A 29 3.263 18.636 10.270 1.00 35.58 O
ANISOU 196 OE2 GLU A 29 5076 4248 4195 -2 1222 -30 O
ATOM 197 N PHE A 30 9.445 18.520 13.275 1.00 34.11 N
ANISOU 197 N PHE A 30 4135 4065 4758 11 1545 -137 N
ATOM 198 CA PHE A 30 10.370 18.545 14.401 1.00 33.29 C
ANISOU 198 CA PHE A 30 3843 3979 4827 25 1499 -167 C
ATOM 199 C PHE A 30 11.472 19.563 14.123 1.00 36.90 C
ANISOU 199 C PHE A 30 4208 4397 5415 -17 1624 -181 C
ATOM 200 O PHE A 30 11.718 20.396 14.972 1.00 35.66 O
ANISOU 200 O PHE A 30 3946 4256 5347 -39 1555 -188 O
ATOM 201 CB PHE A 30 11.004 17.150 14.650 1.00 34.39 C
ANISOU 201 CB PHE A 30 3910 4114 5041 84 1500 -200 C
ATOM 202 CG PHE A 30 11.984 17.161 15.801 1.00 35.19 C
ANISOU 202 CG PHE A 30 3821 4229 5322 108 1432 -232 C
ATOM 203 CD1 PHE A 30 13.354 17.184 15.568 1.00 38.39 C
ANISOU 203 CD1 PHE A 30 4091 4593 5900 112 1544 -272 C
ATOM 204 CD2 PHE A 30 11.535 17.231 17.120 1.00 36.10 C
ANISOU 204 CD2 PHE A 30 3891 4389 5435 125 1255 -226 C
ATOM 205 CE1 PHE A 30 14.260 17.218 16.635 1.00 39.24 C
ANISOU 205 CE1 PHE A 30 4015 4710 6184 137 1457 -308 C
ATOM 206 CE2 PHE A 30 12.439 17.263 18.183 1.00 38.74 C
ANISOU 206 CE2 PHE A 30 4066 4731 5923 152 1172 -258 C
ATOM 207 CZ PHE A 30 13.795 17.258 17.936 1.00 37.46 C
ANISOU 207 CZ PHE A 30 3762 4531 5938 159 1263 -301 C
ATOM 208 N ILE A 31 12.113 19.503 12.936 1.00 34.93 N
ANISOU 208 N ILE A 31 4006 4089 5175 -31 1813 -189 N
ATOM 209 CA ILE A 31 13.206 20.415 12.572 1.00 36.09 C
ANISOU 209 CA ILE A 31 4067 4184 5460 -77 1966 -204 C
ATOM 210 C ILE A 31 12.745 21.886 12.463 1.00 42.10 C
ANISOU 210 C ILE A 31 4891 4935 6169 -138 1966 -168 C
ATOM 211 O ILE A 31 13.324 22.742 13.129 1.00 42.94 O
ANISOU 211 O ILE A 31 4862 5038 6416 -172 1948 -185 O
ATOM 212 CB ILE A 31 13.965 19.945 11.304 1.00 39.26 C
ANISOU 212 CB ILE A 31 4522 4518 5877 -76 2192 -220 C
ATOM 213 CG1 ILE A 31 14.685 18.602 11.555 1.00 40.22 C
ANISOU 213 CG1 ILE A 31 4533 4641 6109 -15 2200 -267 C
ATOM 214 CG2 ILE A 31 14.961 21.042 10.816 1.00 39.60 C
ANISOU 214 CG2 ILE A 31 4502 4494 6050 -138 2378 -228 C
ATOM 215 CD1 ILE A 31 15.132 17.837 10.251 1.00 48.20 C
ANISOU 215 CD1 ILE A 31 5645 5587 7082 2 2410 -282 C
ATOM 216 N VAL A 32 11.728 22.166 11.619 1.00 38.79 N
ANISOU 216 N VAL A 32 4678 4506 5556 -149 1981 -121 N
ATOM 217 CA VAL A 32 11.184 23.513 11.376 1.00 38.70 C
ANISOU 217 CA VAL A 32 4757 4474 5473 -197 1983 -80 C
ATOM 218 C VAL A 32 10.602 24.115 12.666 1.00 41.39 C
ANISOU 218 C VAL A 32 5012 4871 5844 -202 1793 -77 C
ATOM 219 O VAL A 32 10.846 25.281 12.976 1.00 41.77 O
ANISOU 219 O VAL A 32 5009 4899 5962 -246 1803 -72 O
ATOM 220 CB VAL A 32 10.175 23.521 10.183 1.00 42.66 C
ANISOU 220 CB VAL A 32 5508 4950 5752 -191 2013 -33 C
ATOM 221 CG1 VAL A 32 9.524 24.898 10.003 1.00 42.60 C
ANISOU 221 CG1 VAL A 32 5597 4920 5668 -228 1989 14 C
ATOM 222 CG2 VAL A 32 10.863 23.084 8.878 1.00 42.11 C
ANISOU 222 CG2 VAL A 32 5543 4811 5647 -192 2226 -39 C
ATOM 223 N GLY A 33 9.874 23.301 13.413 1.00 35.97 N
ANISOU 223 N GLY A 33 4314 4246 5107 -157 1634 -81 N
ATOM 224 CA GLY A 33 9.249 23.719 14.660 1.00 34.80 C
ANISOU 224 CA GLY A 33 4104 4149 4970 -154 1462 -80 C
ATOM 225 C GLY A 33 10.248 24.081 15.737 1.00 37.62 C
ANISOU 225 C GLY A 33 4272 4514 5509 -166 1426 -121 C
ATOM 226 O GLY A 33 10.079 25.100 16.400 1.00 35.42 O
ANISOU 226 O GLY A 33 3958 4241 5261 -194 1360 -120 O
ATOM 227 N MET A 34 11.272 23.238 15.949 1.00 36.79 N
ANISOU 227 N MET A 34 4045 4406 5526 -139 1456 -162 N
ATOM 228 CA MET A 34 12.287 23.493 16.980 1.00 38.21 C
ANISOU 228 CA MET A 34 4036 4590 5892 -141 1399 -211 C
ATOM 229 C MET A 34 13.062 24.772 16.692 1.00 44.82 C
ANISOU 229 C MET A 34 4805 5374 6850 -209 1506 -224 C
ATOM 230 O MET A 34 13.203 25.601 17.589 1.00 44.85 O
ANISOU 230 O MET A 34 4726 5386 6931 -233 1414 -244 O
ATOM 231 CB MET A 34 13.254 22.301 17.163 1.00 40.38 C
ANISOU 231 CB MET A 34 4193 4864 6287 -91 1410 -253 C
ATOM 232 CG MET A 34 12.651 21.130 17.923 1.00 44.23 C
ANISOU 232 CG MET A 34 4706 5401 6697 -23 1263 -249 C
ATOM 233 SD MET A 34 12.294 21.532 19.654 1.00 49.61 S
ANISOU 233 SD MET A 34 5328 6132 7391 -8 1040 -259 S
ATOM 234 CE MET A 34 12.037 19.931 20.320 1.00 46.74 C
ANISOU 234 CE MET A 34 4983 5799 6979 76 930 -259 C
ATOM 235 N LEU A 35 13.531 24.947 15.440 1.00 42.22 N
ANISOU 235 N LEU A 35 4525 4984 6531 -241 1705 -213 N
ATOM 236 CA LEU A 35 14.292 26.128 15.037 1.00 43.03 C
ANISOU 236 CA LEU A 35 4576 5022 6752 -311 1842 -222 C
ATOM 237 C LEU A 35 13.462 27.399 15.112 1.00 44.32 C
ANISOU 237 C LEU A 35 4840 5177 6822 -355 1799 -182 C
ATOM 238 O LEU A 35 13.946 28.409 15.622 1.00 42.64 O
ANISOU 238 O LEU A 35 4528 4939 6734 -403 1791 -206 O
ATOM 239 CB LEU A 35 14.915 25.960 13.636 1.00 44.28 C
ANISOU 239 CB LEU A 35 4794 5108 6922 -332 2086 -214 C
ATOM 240 CG LEU A 35 16.016 24.888 13.494 1.00 51.39 C
ANISOU 240 CG LEU A 35 5562 5994 7972 -298 2174 -265 C
ATOM 241 CD1 LEU A 35 16.356 24.638 12.012 1.00 52.43 C
ANISOU 241 CD1 LEU A 35 5812 6055 8055 -312 2424 -248 C
ATOM 242 CD2 LEU A 35 17.288 25.289 14.252 1.00 55.44 C
ANISOU 242 CD2 LEU A 35 5821 6484 8760 -325 2170 -332 C
ATOM 243 N GLY A 36 12.221 27.334 14.635 1.00 39.09 N
ANISOU 243 N GLY A 36 4366 4534 5951 -335 1764 -127 N
ATOM 244 CA GLY A 36 11.318 28.474 14.670 1.00 38.19 C
ANISOU 244 CA GLY A 36 4358 4412 5741 -363 1714 -86 C
ATOM 245 C GLY A 36 10.942 28.877 16.079 1.00 41.77 C
ANISOU 245 C GLY A 36 4723 4915 6233 -357 1528 -108 C
ATOM 246 O GLY A 36 11.054 30.050 16.437 1.00 41.37 O
ANISOU 246 O GLY A 36 4640 4835 6243 -403 1520 -113 O
ATOM 247 N ASN A 37 10.534 27.900 16.906 1.00 38.71 N
ANISOU 247 N ASN A 37 4300 4596 5813 -302 1385 -124 N
ATOM 248 CA ASN A 37 10.119 28.171 18.278 1.00 38.43 C
ANISOU 248 CA ASN A 37 4206 4605 5791 -289 1212 -144 C
ATOM 249 C ASN A 37 11.254 28.604 19.176 1.00 42.96 C
ANISOU 249 C ASN A 37 4606 5167 6551 -313 1175 -204 C
ATOM 250 O ASN A 37 11.042 29.529 19.956 1.00 40.10 O
ANISOU 250 O ASN A 37 4223 4804 6209 -337 1091 -217 O
ATOM 251 CB ASN A 37 9.341 27.010 18.877 1.00 36.69 C
ANISOU 251 CB ASN A 37 4018 4449 5475 -226 1087 -139 C
ATOM 252 CG ASN A 37 7.923 27.044 18.390 1.00 48.73 C
ANISOU 252 CG ASN A 37 5700 5985 6828 -214 1065 -88 C
ATOM 253 OD1 ASN A 37 7.122 27.853 18.854 1.00 43.38 O
ANISOU 253 OD1 ASN A 37 5064 5314 6103 -224 994 -73 O
ATOM 254 ND2 ASN A 37 7.600 26.230 17.397 1.00 35.80 N
ANISOU 254 ND2 ASN A 37 4156 4344 5102 -193 1127 -64 N
ATOM 255 N PHE A 38 12.456 27.991 19.061 1.00 42.37 N
ANISOU 255 N PHE A 38 4402 5076 6620 -307 1234 -245 N
ATOM 256 CA PHE A 38 13.582 28.412 19.897 1.00 43.78 C
ANISOU 256 CA PHE A 38 4399 5239 6999 -330 1183 -311 C
ATOM 257 C PHE A 38 14.041 29.826 19.545 1.00 45.15 C
ANISOU 257 C PHE A 38 4541 5345 7271 -412 1285 -320 C
ATOM 258 O PHE A 38 14.384 30.567 20.459 1.00 44.07 O
ANISOU 258 O PHE A 38 4310 5201 7235 -438 1189 -365 O
ATOM 259 CB PHE A 38 14.746 27.386 19.935 1.00 47.48 C
ANISOU 259 CB PHE A 38 4717 5703 7618 -295 1204 -360 C
ATOM 260 CG PHE A 38 14.516 26.309 20.987 1.00 51.40 C
ANISOU 260 CG PHE A 38 5193 6261 8074 -216 1023 -375 C
ATOM 261 CD1 PHE A 38 14.420 26.638 22.342 1.00 56.86 C
ANISOU 261 CD1 PHE A 38 5842 6981 8782 -202 836 -405 C
ATOM 262 CD2 PHE A 38 14.344 24.978 20.620 1.00 54.42 C
ANISOU 262 CD2 PHE A 38 5621 6667 8390 -156 1042 -356 C
ATOM 263 CE1 PHE A 38 14.167 25.650 23.307 1.00 58.09 C
ANISOU 263 CE1 PHE A 38 6008 7183 8879 -127 677 -412 C
ATOM 264 CE2 PHE A 38 14.123 23.987 21.589 1.00 57.67 C
ANISOU 264 CE2 PHE A 38 6028 7124 8761 -84 884 -364 C
ATOM 265 CZ PHE A 38 14.029 24.330 22.924 1.00 56.58 C
ANISOU 265 CZ PHE A 38 5856 7010 8631 -69 705 -388 C
ATOM 266 N THR A 39 13.935 30.238 18.256 1.00 40.89 N
ANISOU 266 N THR A 39 4103 4751 6680 -451 1470 -275 N
ATOM 267 CA THR A 39 14.288 31.596 17.798 1.00 40.21 C
ANISOU 267 CA THR A 39 4020 4588 6670 -531 1591 -271 C
ATOM 268 C THR A 39 13.371 32.671 18.431 1.00 43.15 C
ANISOU 268 C THR A 39 4470 4967 6958 -549 1478 -252 C
ATOM 269 O THR A 39 13.875 33.687 18.931 1.00 43.23 O
ANISOU 269 O THR A 39 4393 4936 7098 -604 1465 -290 O
ATOM 270 CB THR A 39 14.305 31.679 16.258 1.00 45.05 C
ANISOU 270 CB THR A 39 4763 5139 7215 -557 1815 -218 C
ATOM 271 OG1 THR A 39 15.259 30.745 15.760 1.00 43.60 O
ANISOU 271 OG1 THR A 39 4491 4941 7134 -543 1931 -247 O
ATOM 272 CG2 THR A 39 14.654 33.091 15.728 1.00 44.48 C
ANISOU 272 CG2 THR A 39 4717 4973 7212 -641 1960 -204 C
ATOM 273 N VAL A 40 12.045 32.452 18.397 1.00 38.52 N
ANISOU 273 N VAL A 40 4040 4426 6170 -504 1400 -198 N
ATOM 274 CA VAL A 40 11.062 33.407 18.934 1.00 37.66 C
ANISOU 274 CA VAL A 40 4012 4321 5975 -512 1303 -178 C
ATOM 275 C VAL A 40 11.083 33.437 20.479 1.00 42.03 C
ANISOU 275 C VAL A 40 4465 4921 6585 -494 1118 -234 C
ATOM 276 O VAL A 40 10.891 34.508 21.061 1.00 41.43 O
ANISOU 276 O VAL A 40 4389 4821 6533 -526 1066 -249 O
ATOM 277 CB VAL A 40 9.619 33.243 18.360 1.00 40.06 C
ANISOU 277 CB VAL A 40 4505 4648 6067 -471 1283 -107 C
ATOM 278 CG1 VAL A 40 9.586 33.504 16.858 1.00 39.29 C
ANISOU 278 CG1 VAL A 40 4537 4488 5902 -492 1453 -52 C
ATOM 279 CG2 VAL A 40 9.002 31.883 18.702 1.00 39.42 C
ANISOU 279 CG2 VAL A 40 4441 4646 5891 -401 1181 -105 C
ATOM 280 N VAL A 41 11.313 32.272 21.126 1.00 38.35 N
ANISOU 280 N VAL A 41 3926 4514 6131 -441 1021 -264 N
ATOM 281 CA VAL A 41 11.411 32.141 22.589 1.00 38.81 C
ANISOU 281 CA VAL A 41 3907 4612 6227 -413 843 -317 C
ATOM 282 C VAL A 41 12.653 32.881 23.083 1.00 45.78 C
ANISOU 282 C VAL A 41 4632 5449 7313 -465 829 -389 C
ATOM 283 O VAL A 41 12.545 33.707 23.979 1.00 43.55 O
ANISOU 283 O VAL A 41 4338 5158 7052 -484 728 -423 O
ATOM 284 CB VAL A 41 11.355 30.661 23.067 1.00 42.28 C
ANISOU 284 CB VAL A 41 4330 5115 6621 -339 752 -323 C
ATOM 285 CG1 VAL A 41 11.846 30.501 24.506 1.00 41.96 C
ANISOU 285 CG1 VAL A 41 4195 5097 6650 -311 580 -386 C
ATOM 286 CG2 VAL A 41 9.945 30.111 22.928 1.00 41.86 C
ANISOU 286 CG2 VAL A 41 4429 5105 6371 -294 726 -264 C
ATOM 287 N PHE A 42 13.818 32.630 22.462 1.00 47.05 N
ANISOU 287 N PHE A 42 4672 5573 7631 -491 938 -416 N
ATOM 288 CA PHE A 42 15.041 33.326 22.845 1.00 49.36 C
ANISOU 288 CA PHE A 42 4795 5814 8148 -547 934 -491 C
ATOM 289 C PHE A 42 14.950 34.823 22.517 1.00 50.41 C
ANISOU 289 C PHE A 42 4965 5875 8314 -629 1022 -484 C
ATOM 290 O PHE A 42 15.443 35.640 23.292 1.00 49.16 O
ANISOU 290 O PHE A 42 4714 5686 8280 -671 942 -546 O
ATOM 291 CB PHE A 42 16.288 32.636 22.269 1.00 53.44 C
ANISOU 291 CB PHE A 42 5159 6304 8841 -551 1039 -525 C
ATOM 292 CG PHE A 42 16.729 31.475 23.140 1.00 57.89 C
ANISOU 292 CG PHE A 42 5621 6922 9453 -475 880 -571 C
ATOM 293 CD1 PHE A 42 15.957 30.321 23.241 1.00 62.19 C
ANISOU 293 CD1 PHE A 42 6271 7533 9826 -395 818 -527 C
ATOM 294 CD2 PHE A 42 17.892 31.556 23.898 1.00 63.27 C
ANISOU 294 CD2 PHE A 42 6105 7582 10352 -482 780 -660 C
ATOM 295 CE1 PHE A 42 16.345 29.265 24.071 1.00 64.10 C
ANISOU 295 CE1 PHE A 42 6437 7815 10103 -321 670 -563 C
ATOM 296 CE2 PHE A 42 18.294 30.484 24.708 1.00 66.76 C
ANISOU 296 CE2 PHE A 42 6466 8068 10831 -402 619 -698 C
ATOM 297 CZ PHE A 42 17.514 29.349 24.791 1.00 64.45 C
ANISOU 297 CZ PHE A 42 6295 7838 10354 -321 569 -646 C
ATOM 298 N GLY A 43 14.226 35.159 21.445 1.00 45.03 N
ANISOU 298 N GLY A 43 4435 5168 7506 -646 1165 -407 N
ATOM 299 CA GLY A 43 13.948 36.533 21.046 1.00 43.79 C
ANISOU 299 CA GLY A 43 4355 4940 7345 -712 1251 -382 C
ATOM 300 C GLY A 43 13.191 37.259 22.140 1.00 47.00 C
ANISOU 300 C GLY A 43 4808 5364 7686 -704 1089 -398 C
ATOM 301 O GLY A 43 13.534 38.395 22.476 1.00 46.79 O
ANISOU 301 O GLY A 43 4739 5277 7762 -766 1088 -435 O
ATOM 302 N TYR A 44 12.191 36.586 22.761 1.00 40.97 N
ANISOU 302 N TYR A 44 4125 4680 6761 -630 953 -378 N
ATOM 303 CA TYR A 44 11.422 37.174 23.861 1.00 39.58 C
ANISOU 303 CA TYR A 44 4002 4522 6513 -615 807 -396 C
ATOM 304 C TYR A 44 12.229 37.245 25.139 1.00 47.16 C
ANISOU 304 C TYR A 44 4831 5490 7599 -621 660 -488 C
ATOM 305 O TYR A 44 12.243 38.287 25.787 1.00 46.25 O
ANISOU 305 O TYR A 44 4711 5336 7527 -659 602 -529 O
ATOM 306 CB TYR A 44 10.103 36.430 24.094 1.00 37.65 C
ANISOU 306 CB TYR A 44 3885 4350 6070 -539 731 -346 C
ATOM 307 CG TYR A 44 8.933 37.022 23.338 1.00 35.51 C
ANISOU 307 CG TYR A 44 3767 4058 5668 -538 802 -274 C
ATOM 308 CD1 TYR A 44 9.121 37.685 22.124 1.00 36.55 C
ANISOU 308 CD1 TYR A 44 3944 4120 5821 -584 956 -232 C
ATOM 309 CD2 TYR A 44 7.632 36.911 23.827 1.00 33.71 C
ANISOU 309 CD2 TYR A 44 3642 3872 5297 -487 716 -247 C
ATOM 310 CE1 TYR A 44 8.050 38.239 21.430 1.00 35.01 C
ANISOU 310 CE1 TYR A 44 3898 3899 5503 -574 1002 -164 C
ATOM 311 CE2 TYR A 44 6.547 37.400 23.105 1.00 33.18 C
ANISOU 311 CE2 TYR A 44 3702 3783 5123 -477 767 -184 C
ATOM 312 CZ TYR A 44 6.764 38.081 21.916 1.00 35.76 C
ANISOU 312 CZ TYR A 44 4077 4041 5468 -518 899 -142 C
ATOM 313 OH TYR A 44 5.714 38.587 21.199 1.00 32.00 O
ANISOU 313 OH TYR A 44 3735 3537 4886 -500 931 -80 O
ATOM 314 N LEU A 45 12.931 36.155 25.481 1.00 47.46 N
ANISOU 314 N LEU A 45 4765 5570 7697 -582 594 -523 N
ATOM 315 CA LEU A 45 13.772 36.085 26.677 1.00 49.15 C
ANISOU 315 CA LEU A 45 4852 5790 8031 -576 431 -614 C
ATOM 316 C LEU A 45 14.878 37.147 26.696 1.00 56.29 C
ANISOU 316 C LEU A 45 5617 6615 9156 -661 460 -685 C
ATOM 317 O LEU A 45 15.178 37.654 27.772 1.00 55.47 O
ANISOU 317 O LEU A 45 5465 6498 9111 -672 311 -758 O
ATOM 318 CB LEU A 45 14.365 34.673 26.882 1.00 49.24 C
ANISOU 318 CB LEU A 45 4779 5853 8079 -511 366 -631 C
ATOM 319 CG LEU A 45 13.365 33.538 27.149 1.00 54.20 C
ANISOU 319 CG LEU A 45 5531 6555 8506 -425 304 -577 C
ATOM 320 CD1 LEU A 45 14.074 32.192 27.262 1.00 54.16 C
ANISOU 320 CD1 LEU A 45 5437 6584 8558 -365 254 -596 C
ATOM 321 CD2 LEU A 45 12.490 33.823 28.370 1.00 56.43 C
ANISOU 321 CD2 LEU A 45 5924 6865 8653 -392 153 -587 C
ATOM 322 N PHE A 46 15.414 37.530 25.514 1.00 56.51 N
ANISOU 322 N PHE A 46 5596 6581 9293 -725 656 -663 N
ATOM 323 CA PHE A 46 16.499 38.512 25.379 1.00 59.10 C
ANISOU 323 CA PHE A 46 5783 6819 9852 -818 721 -727 C
ATOM 324 C PHE A 46 16.131 39.921 24.830 1.00 65.18 C
ANISOU 324 C PHE A 46 6642 7507 10618 -897 851 -696 C
ATOM 325 O PHE A 46 16.929 40.835 25.031 1.00 66.29 O
ANISOU 325 O PHE A 46 6671 7571 10944 -975 865 -762 O
ATOM 326 CB PHE A 46 17.628 37.923 24.521 1.00 62.12 C
ANISOU 326 CB PHE A 46 6015 7174 10414 -840 864 -741 C
ATOM 327 CG PHE A 46 18.459 36.887 25.235 1.00 65.21 C
ANISOU 327 CG PHE A 46 6245 7609 10921 -785 719 -811 C
ATOM 328 CD1 PHE A 46 18.129 35.539 25.165 1.00 69.23 C
ANISOU 328 CD1 PHE A 46 6799 8195 11309 -695 684 -771 C
ATOM 329 CD2 PHE A 46 19.589 37.256 25.959 1.00 69.12 C
ANISOU 329 CD2 PHE A 46 6543 8064 11654 -823 613 -918 C
ATOM 330 CE1 PHE A 46 18.898 34.579 25.827 1.00 71.07 C
ANISOU 330 CE1 PHE A 46 6893 8461 11648 -637 546 -831 C
ATOM 331 CE2 PHE A 46 20.361 36.294 26.619 1.00 72.57 C
ANISOU 331 CE2 PHE A 46 6832 8538 12202 -762 461 -982 C
ATOM 332 CZ PHE A 46 20.011 34.962 26.549 1.00 70.80 C
ANISOU 332 CZ PHE A 46 6666 8388 11848 -667 431 -935 C
ATOM 333 N CYS A 47 14.981 40.113 24.144 1.00 62.79 N
ANISOU 333 N CYS A 47 6529 7210 10119 -878 940 -601 N
ATOM 334 CA CYS A 47 14.620 41.427 23.564 1.00 63.13 C
ANISOU 334 CA CYS A 47 6669 7166 10151 -943 1062 -564 C
ATOM 335 C CYS A 47 13.447 42.118 24.243 1.00 68.16 C
ANISOU 335 C CYS A 47 7446 7815 10637 -917 953 -547 C
ATOM 336 O CYS A 47 13.455 43.343 24.330 1.00 68.69 O
ANISOU 336 O CYS A 47 7535 7803 10760 -977 982 -563 O
ATOM 337 CB CYS A 47 14.382 41.330 22.058 1.00 63.78 C
ANISOU 337 CB CYS A 47 6859 7214 10161 -952 1277 -471 C
ATOM 338 SG CYS A 47 15.682 40.467 21.147 1.00 68.25 S
ANISOU 338 SG CYS A 47 7283 7759 10888 -976 1443 -485 S
ATOM 339 N MET A 48 12.401 41.364 24.621 1.00 65.39 N
ANISOU 339 N MET A 48 7197 7552 10097 -831 851 -510 N
ATOM 340 CA MET A 48 11.198 41.929 25.232 1.00 65.28 C
ANISOU 340 CA MET A 48 7315 7550 9938 -798 764 -491 C
ATOM 341 C MET A 48 11.384 42.206 26.716 1.00 70.45 C
ANISOU 341 C MET A 48 7917 8218 10633 -794 585 -581 C
ATOM 342 O MET A 48 11.665 41.280 27.482 1.00 71.92 O
ANISOU 342 O MET A 48 8043 8470 10814 -748 460 -622 O
ATOM 343 CB MET A 48 9.975 41.025 24.998 1.00 67.58 C
ANISOU 343 CB MET A 48 7732 7920 10026 -713 743 -417 C
ATOM 344 CG MET A 48 9.610 40.836 23.541 1.00 71.66 C
ANISOU 344 CG MET A 48 8337 8419 10472 -710 898 -329 C
ATOM 345 SD MET A 48 9.140 42.336 22.659 1.00 76.16 S
ANISOU 345 SD MET A 48 9031 8882 11025 -759 1026 -272 S
ATOM 346 CE MET A 48 8.621 41.689 21.170 1.00 72.30 C
ANISOU 346 CE MET A 48 8663 8401 10408 -724 1149 -174 C
ATOM 347 N LYS A 49 11.201 43.470 27.129 1.00 65.53 N
ANISOU 347 N LYS A 49 7332 7528 10040 -838 569 -611 N
ATOM 348 CA LYS A 49 11.321 43.850 28.538 1.00 64.75 C
ANISOU 348 CA LYS A 49 7209 7430 9963 -836 399 -701 C
ATOM 349 C LYS A 49 9.954 44.070 29.228 1.00 63.33 C
ANISOU 349 C LYS A 49 7185 7278 9598 -776 328 -679 C
ATOM 350 O LYS A 49 9.808 43.682 30.387 1.00 64.33 O
ANISOU 350 O LYS A 49 7326 7450 9664 -731 181 -729 O
ATOM 351 CB LYS A 49 12.249 45.065 28.713 1.00 68.69 C
ANISOU 351 CB LYS A 49 7619 7828 10653 -931 411 -778 C
ATOM 352 CG LYS A 49 12.903 45.156 30.099 1.00 89.77 C
ANISOU 352 CG LYS A 49 10206 10501 13402 -937 217 -896 C
ATOM 353 CD LYS A 49 13.310 46.593 30.471 1.00102.29 C
ANISOU 353 CD LYS A 49 11768 11981 15117 -1021 206 -970 C
ATOM 354 CE LYS A 49 14.603 47.063 29.836 1.00112.62 C
ANISOU 354 CE LYS A 49 12909 13205 16675 -1122 302 -1013 C
ATOM 355 NZ LYS A 49 14.826 48.516 30.060 1.00120.85 N
ANISOU 355 NZ LYS A 49 13953 14133 17831 -1208 319 -1070 N
ATOM 356 N ASN A 50 8.975 44.689 28.537 1.00 54.22 N
ANISOU 356 N ASN A 50 6150 6091 8359 -772 431 -605 N
ATOM 357 CA ASN A 50 7.638 44.945 29.102 1.00 52.24 C
ANISOU 357 CA ASN A 50 6034 5858 7955 -714 383 -583 C
ATOM 358 C ASN A 50 6.563 44.261 28.246 1.00 51.67 C
ANISOU 358 C ASN A 50 6049 5835 7747 -654 453 -484 C
ATOM 359 O ASN A 50 6.226 44.738 27.160 1.00 52.97 O
ANISOU 359 O ASN A 50 6267 5954 7905 -668 566 -417 O
ATOM 360 CB ASN A 50 7.381 46.457 29.270 1.00 54.29 C
ANISOU 360 CB ASN A 50 6351 6021 8254 -758 409 -605 C
ATOM 361 CG ASN A 50 7.146 47.226 27.985 1.00 78.17 C
ANISOU 361 CG ASN A 50 9429 8971 11302 -792 562 -530 C
ATOM 362 OD1 ASN A 50 7.951 47.204 27.042 1.00 68.43 O
ANISOU 362 OD1 ASN A 50 8136 7704 10161 -843 665 -506 O
ATOM 363 ND2 ASN A 50 6.016 47.907 27.923 1.00 73.78 N
ANISOU 363 ND2 ASN A 50 8993 8383 10658 -758 582 -489 N
ATOM 364 N TRP A 51 6.059 43.122 28.714 1.00 42.54 N
ANISOU 364 N TRP A 51 4910 4766 6487 -587 383 -474 N
ATOM 365 CA TRP A 51 5.112 42.312 27.948 1.00 40.05 C
ANISOU 365 CA TRP A 51 4659 4501 6057 -532 434 -391 C
ATOM 366 C TRP A 51 3.687 42.807 27.987 1.00 37.82 C
ANISOU 366 C TRP A 51 4490 4207 5675 -490 442 -352 C
ATOM 367 O TRP A 51 3.222 43.241 29.033 1.00 37.26 O
ANISOU 367 O TRP A 51 4455 4128 5573 -473 378 -395 O
ATOM 368 CB TRP A 51 5.139 40.860 28.452 1.00 39.30 C
ANISOU 368 CB TRP A 51 4534 4495 5902 -480 360 -399 C
ATOM 369 CG TRP A 51 6.411 40.109 28.192 1.00 40.73 C
ANISOU 369 CG TRP A 51 4602 4697 6176 -502 361 -422 C
ATOM 370 CD1 TRP A 51 7.670 40.625 28.078 1.00 43.97 C
ANISOU 370 CD1 TRP A 51 4909 5059 6740 -566 378 -470 C
ATOM 371 CD2 TRP A 51 6.547 38.692 28.066 1.00 40.32 C
ANISOU 371 CD2 TRP A 51 4521 4714 6086 -458 342 -403 C
ATOM 372 NE1 TRP A 51 8.572 39.619 27.833 1.00 43.72 N
ANISOU 372 NE1 TRP A 51 4779 5062 6772 -561 377 -481 N
ATOM 373 CE2 TRP A 51 7.918 38.417 27.863 1.00 44.30 C
ANISOU 373 CE2 TRP A 51 4900 5208 6724 -493 349 -441 C
ATOM 374 CE3 TRP A 51 5.638 37.625 28.063 1.00 41.41 C
ANISOU 374 CE3 TRP A 51 4720 4914 6098 -395 327 -359 C
ATOM 375 CZ2 TRP A 51 8.404 37.118 27.682 1.00 43.23 C
ANISOU 375 CZ2 TRP A 51 4706 5124 6595 -459 338 -435 C
ATOM 376 CZ3 TRP A 51 6.130 36.333 27.920 1.00 42.50 C
ANISOU 376 CZ3 TRP A 51 4808 5102 6238 -367 313 -354 C
ATOM 377 CH2 TRP A 51 7.494 36.093 27.722 1.00 42.81 C
ANISOU 377 CH2 TRP A 51 4729 5131 6406 -395 319 -390 C
ATOM 378 N ASN A 52 2.978 42.701 26.863 1.00 30.27 N
ANISOU 378 N ASN A 52 3590 3247 4665 -468 517 -274 N
ATOM 379 CA ASN A 52 1.557 42.997 26.851 1.00 29.63 C
ANISOU 379 CA ASN A 52 3599 3161 4498 -417 513 -236 C
ATOM 380 C ASN A 52 0.810 41.631 26.766 1.00 31.15 C
ANISOU 380 C ASN A 52 3801 3438 4598 -357 486 -203 C
ATOM 381 O ASN A 52 1.461 40.586 26.824 1.00 29.78 O
ANISOU 381 O ASN A 52 3572 3317 4425 -358 469 -214 O
ATOM 382 CB ASN A 52 1.162 43.981 25.724 1.00 29.69 C
ANISOU 382 CB ASN A 52 3676 3091 4513 -427 593 -177 C
ATOM 383 CG ASN A 52 1.402 43.496 24.317 1.00 39.55 C
ANISOU 383 CG ASN A 52 4944 4340 5742 -433 667 -111 C
ATOM 384 OD1 ASN A 52 1.365 42.304 24.014 1.00 38.92 O
ANISOU 384 OD1 ASN A 52 4846 4329 5614 -406 658 -92 O
ATOM 385 ND2 ASN A 52 1.620 44.427 23.409 1.00 33.19 N
ANISOU 385 ND2 ASN A 52 4192 3451 4966 -465 748 -72 N
ATOM 386 N SER A 53 -0.528 41.653 26.609 1.00 26.92 N
ANISOU 386 N SER A 53 3327 2904 3995 -306 483 -166 N
ATOM 387 CA SER A 53 -1.391 40.473 26.504 1.00 26.83 C
ANISOU 387 CA SER A 53 3326 2959 3911 -254 462 -138 C
ATOM 388 C SER A 53 -1.011 39.576 25.345 1.00 30.83 C
ANISOU 388 C SER A 53 3822 3495 4399 -257 496 -93 C
ATOM 389 O SER A 53 -0.877 38.373 25.537 1.00 30.83 O
ANISOU 389 O SER A 53 3789 3555 4368 -241 474 -98 O
ATOM 390 CB SER A 53 -2.843 40.905 26.342 1.00 28.65 C
ANISOU 390 CB SER A 53 3611 3167 4109 -207 461 -109 C
ATOM 391 OG SER A 53 -3.178 41.794 27.384 1.00 32.98 O
ANISOU 391 OG SER A 53 4175 3678 4678 -202 445 -153 O
ATOM 392 N SER A 54 -0.828 40.166 24.141 1.00 28.36 N
ANISOU 392 N SER A 54 3548 3131 4097 -277 555 -48 N
ATOM 393 CA SER A 54 -0.415 39.453 22.931 1.00 27.75 C
ANISOU 393 CA SER A 54 3485 3066 3994 -283 605 -6 C
ATOM 394 C SER A 54 0.922 38.725 23.142 1.00 31.40 C
ANISOU 394 C SER A 54 3864 3560 4505 -318 624 -40 C
ATOM 395 O SER A 54 1.025 37.583 22.739 1.00 31.25 O
ANISOU 395 O SER A 54 3834 3589 4451 -301 629 -27 O
ATOM 396 CB SER A 54 -0.328 40.414 21.751 1.00 30.95 C
ANISOU 396 CB SER A 54 3967 3392 4400 -302 675 44 C
ATOM 397 OG SER A 54 -1.621 40.678 21.236 1.00 36.85 O
ANISOU 397 OG SER A 54 4797 4121 5084 -251 643 88 O
ATOM 398 N ASN A 55 1.913 39.353 23.819 1.00 28.23 N
ANISOU 398 N ASN A 55 3400 3131 4193 -365 626 -90 N
ATOM 399 CA ASN A 55 3.201 38.710 24.100 1.00 28.35 C
ANISOU 399 CA ASN A 55 3318 3173 4281 -394 628 -132 C
ATOM 400 C ASN A 55 3.020 37.507 24.988 1.00 30.30 C
ANISOU 400 C ASN A 55 3530 3497 4486 -350 544 -158 C
ATOM 401 O ASN A 55 3.618 36.466 24.728 1.00 29.94 O
ANISOU 401 O ASN A 55 3438 3487 4449 -343 553 -159 O
ATOM 402 CB ASN A 55 4.200 39.667 24.764 1.00 29.09 C
ANISOU 402 CB ASN A 55 3343 3217 4490 -450 621 -192 C
ATOM 403 CG ASN A 55 4.508 40.926 24.023 1.00 37.01 C
ANISOU 403 CG ASN A 55 4377 4132 5554 -503 712 -173 C
ATOM 404 OD1 ASN A 55 4.580 41.977 24.639 1.00 31.73 O
ANISOU 404 OD1 ASN A 55 3704 3413 4937 -532 690 -209 O
ATOM 405 ND2 ASN A 55 4.735 40.857 22.711 1.00 29.70 N
ANISOU 405 ND2 ASN A 55 3489 3175 4621 -519 821 -118 N
ATOM 406 N VAL A 56 2.216 37.655 26.054 1.00 26.01 N
ANISOU 406 N VAL A 56 3015 2969 3897 -320 470 -180 N
ATOM 407 CA VAL A 56 1.905 36.555 26.982 1.00 25.18 C
ANISOU 407 CA VAL A 56 2903 2927 3737 -276 398 -200 C
ATOM 408 C VAL A 56 1.310 35.346 26.218 1.00 29.05 C
ANISOU 408 C VAL A 56 3417 3461 4160 -240 423 -151 C
ATOM 409 O VAL A 56 1.788 34.217 26.396 1.00 27.18 O
ANISOU 409 O VAL A 56 3144 3265 3917 -223 401 -159 O
ATOM 410 CB VAL A 56 0.980 37.023 28.136 1.00 27.00 C
ANISOU 410 CB VAL A 56 3186 3154 3921 -250 346 -225 C
ATOM 411 CG1 VAL A 56 0.450 35.838 28.948 1.00 25.97 C
ANISOU 411 CG1 VAL A 56 3075 3076 3715 -202 299 -229 C
ATOM 412 CG2 VAL A 56 1.704 38.032 29.045 1.00 26.09 C
ANISOU 412 CG2 VAL A 56 3050 2998 3865 -283 303 -288 C
ATOM 413 N TYR A 57 0.302 35.603 25.354 1.00 25.64 N
ANISOU 413 N TYR A 57 3046 3012 3682 -227 460 -102 N
ATOM 414 CA TYR A 57 -0.361 34.557 24.582 1.00 26.02 C
ANISOU 414 CA TYR A 57 3124 3094 3670 -195 472 -62 C
ATOM 415 C TYR A 57 0.586 33.902 23.598 1.00 31.39 C
ANISOU 415 C TYR A 57 3782 3779 4364 -212 524 -47 C
ATOM 416 O TYR A 57 0.545 32.686 23.458 1.00 30.79 O
ANISOU 416 O TYR A 57 3699 3744 4255 -189 516 -41 O
ATOM 417 CB TYR A 57 -1.595 35.083 23.844 1.00 26.23 C
ANISOU 417 CB TYR A 57 3218 3092 3656 -175 481 -21 C
ATOM 418 CG TYR A 57 -2.654 35.676 24.745 1.00 26.35 C
ANISOU 418 CG TYR A 57 3248 3098 3667 -152 443 -37 C
ATOM 419 CD1 TYR A 57 -2.989 35.068 25.953 1.00 26.92 C
ANISOU 419 CD1 TYR A 57 3300 3205 3723 -131 407 -69 C
ATOM 420 CD2 TYR A 57 -3.337 36.837 24.382 1.00 25.87 C
ANISOU 420 CD2 TYR A 57 3230 2984 3617 -146 450 -18 C
ATOM 421 CE1 TYR A 57 -3.954 35.611 26.787 1.00 27.02 C
ANISOU 421 CE1 TYR A 57 3332 3200 3733 -110 394 -86 C
ATOM 422 CE2 TYR A 57 -4.319 37.378 25.198 1.00 25.89 C
ANISOU 422 CE2 TYR A 57 3240 2971 3626 -121 426 -36 C
ATOM 423 CZ TYR A 57 -4.638 36.747 26.392 1.00 31.60 C
ANISOU 423 CZ TYR A 57 3940 3731 4336 -104 404 -71 C
ATOM 424 OH TYR A 57 -5.607 37.244 27.204 1.00 32.11 O
ANISOU 424 OH TYR A 57 4016 3775 4408 -79 400 -91 O
ATOM 425 N LEU A 58 1.438 34.708 22.919 1.00 26.32 N
ANISOU 425 N LEU A 58 3134 3090 3776 -254 588 -42 N
ATOM 426 CA LEU A 58 2.399 34.185 21.960 1.00 25.23 C
ANISOU 426 CA LEU A 58 2978 2946 3662 -274 664 -30 C
ATOM 427 C LEU A 58 3.429 33.292 22.633 1.00 28.84 C
ANISOU 427 C LEU A 58 3337 3440 4179 -274 640 -74 C
ATOM 428 O LEU A 58 3.792 32.281 22.070 1.00 27.46 O
ANISOU 428 O LEU A 58 3152 3287 3995 -261 674 -65 O
ATOM 429 CB LEU A 58 3.097 35.330 21.186 1.00 24.93 C
ANISOU 429 CB LEU A 58 2956 2837 3681 -324 756 -17 C
ATOM 430 CG LEU A 58 2.249 35.986 20.107 1.00 28.98 C
ANISOU 430 CG LEU A 58 3590 3303 4118 -316 796 41 C
ATOM 431 CD1 LEU A 58 2.831 37.373 19.706 1.00 29.11 C
ANISOU 431 CD1 LEU A 58 3630 3235 4196 -368 877 51 C
ATOM 432 CD2 LEU A 58 2.039 35.034 18.895 1.00 27.35 C
ANISOU 432 CD2 LEU A 58 3456 3109 3828 -292 839 82 C
ATOM 433 N PHE A 59 3.918 33.677 23.820 1.00 28.16 N
ANISOU 433 N PHE A 59 3186 3358 4158 -284 577 -124 N
ATOM 434 CA PHE A 59 4.911 32.898 24.554 1.00 28.45 C
ANISOU 434 CA PHE A 59 3130 3423 4256 -276 529 -170 C
ATOM 435 C PHE A 59 4.304 31.556 24.967 1.00 31.28 C
ANISOU 435 C PHE A 59 3516 3838 4533 -220 474 -159 C
ATOM 436 O PHE A 59 4.940 30.515 24.784 1.00 29.60 O
ANISOU 436 O PHE A 59 3258 3646 4341 -202 480 -165 O
ATOM 437 CB PHE A 59 5.427 33.669 25.772 1.00 30.26 C
ANISOU 437 CB PHE A 59 3306 3638 4554 -295 450 -228 C
ATOM 438 CG PHE A 59 6.714 33.097 26.319 1.00 33.11 C
ANISOU 438 CG PHE A 59 3557 4010 5013 -293 399 -281 C
ATOM 439 CD1 PHE A 59 7.937 33.359 25.694 1.00 36.87 C
ANISOU 439 CD1 PHE A 59 3935 4451 5623 -338 467 -303 C
ATOM 440 CD2 PHE A 59 6.709 32.298 27.458 1.00 36.19 C
ANISOU 440 CD2 PHE A 59 3943 4441 5368 -246 286 -309 C
ATOM 441 CE1 PHE A 59 9.131 32.844 26.209 1.00 38.04 C
ANISOU 441 CE1 PHE A 59 3963 4606 5885 -332 409 -358 C
ATOM 442 CE2 PHE A 59 7.902 31.746 27.950 1.00 39.23 C
ANISOU 442 CE2 PHE A 59 4227 4833 5847 -234 221 -357 C
ATOM 443 CZ PHE A 59 9.105 32.048 27.339 1.00 37.71 C
ANISOU 443 CZ PHE A 59 3919 4606 5803 -277 276 -385 C
ATOM 444 N ASN A 60 3.047 31.578 25.445 1.00 26.66 N
ANISOU 444 N ASN A 60 3002 3268 3859 -193 432 -143 N
ATOM 445 CA ASN A 60 2.306 30.356 25.801 1.00 25.83 C
ANISOU 445 CA ASN A 60 2932 3205 3678 -147 397 -128 C
ATOM 446 C ASN A 60 2.133 29.447 24.588 1.00 28.57 C
ANISOU 446 C ASN A 60 3301 3563 3994 -138 455 -92 C
ATOM 447 O ASN A 60 2.301 28.241 24.713 1.00 28.50 O
ANISOU 447 O ASN A 60 3280 3580 3968 -110 440 -93 O
ATOM 448 CB ASN A 60 0.954 30.697 26.382 1.00 22.31 C
ANISOU 448 CB ASN A 60 2551 2760 3166 -130 369 -118 C
ATOM 449 CG ASN A 60 1.024 30.926 27.849 1.00 40.39 C
ANISOU 449 CG ASN A 60 4844 5053 5451 -118 302 -158 C
ATOM 450 OD1 ASN A 60 0.931 29.990 28.641 1.00 35.79 O
ANISOU 450 OD1 ASN A 60 4277 4494 4826 -85 261 -166 O
ATOM 451 ND2 ASN A 60 1.199 32.176 28.240 1.00 33.73 N
ANISOU 451 ND2 ASN A 60 3998 4178 4642 -143 290 -184 N
ATOM 452 N LEU A 61 1.815 30.028 23.423 1.00 25.02 N
ANISOU 452 N LEU A 61 2893 3085 3529 -158 517 -60 N
ATOM 453 CA LEU A 61 1.682 29.303 22.170 1.00 26.09 C
ANISOU 453 CA LEU A 61 3069 3220 3623 -151 572 -29 C
ATOM 454 C LEU A 61 3.001 28.543 21.854 1.00 32.46 C
ANISOU 454 C LEU A 61 3815 4031 4486 -155 619 -46 C
ATOM 455 O LEU A 61 2.956 27.373 21.452 1.00 32.67 O
ANISOU 455 O LEU A 61 3857 4077 4480 -131 631 -39 O
ATOM 456 CB LEU A 61 1.350 30.301 21.061 1.00 26.19 C
ANISOU 456 CB LEU A 61 3149 3189 3613 -173 627 5 C
ATOM 457 CG LEU A 61 1.180 29.734 19.645 1.00 31.01 C
ANISOU 457 CG LEU A 61 3834 3787 4161 -166 682 38 C
ATOM 458 CD1 LEU A 61 -0.164 28.971 19.504 1.00 30.13 C
ANISOU 458 CD1 LEU A 61 3777 3700 3970 -129 620 53 C
ATOM 459 CD2 LEU A 61 1.257 30.859 18.622 1.00 34.31 C
ANISOU 459 CD2 LEU A 61 4325 4148 4565 -191 748 70 C
ATOM 460 N SER A 62 4.165 29.195 22.082 1.00 29.26 N
ANISOU 460 N SER A 62 3335 3603 4179 -186 644 -75 N
ATOM 461 CA SER A 62 5.470 28.568 21.846 1.00 29.50 C
ANISOU 461 CA SER A 62 3284 3631 4294 -189 690 -99 C
ATOM 462 C SER A 62 5.744 27.447 22.845 1.00 33.88 C
ANISOU 462 C SER A 62 3784 4225 4862 -146 606 -127 C
ATOM 463 O SER A 62 6.283 26.426 22.454 1.00 33.73 O
ANISOU 463 O SER A 62 3739 4214 4864 -124 638 -131 O
ATOM 464 CB SER A 62 6.582 29.603 21.890 1.00 30.18 C
ANISOU 464 CB SER A 62 3287 3675 4503 -237 733 -129 C
ATOM 465 OG SER A 62 6.472 30.448 20.767 1.00 38.44 O
ANISOU 465 OG SER A 62 4398 4674 5534 -275 839 -96 O
ATOM 466 N ILE A 63 5.352 27.615 24.108 1.00 30.84 N
ANISOU 466 N ILE A 63 3398 3859 4459 -129 503 -145 N
ATOM 467 CA ILE A 63 5.507 26.564 25.124 1.00 31.78 C
ANISOU 467 CA ILE A 63 3497 4008 4568 -82 417 -164 C
ATOM 468 C ILE A 63 4.673 25.308 24.738 1.00 33.81 C
ANISOU 468 C ILE A 63 3824 4288 4735 -46 433 -129 C
ATOM 469 O ILE A 63 5.168 24.186 24.852 1.00 31.70 O
ANISOU 469 O ILE A 63 3531 4030 4482 -12 420 -136 O
ATOM 470 CB ILE A 63 5.209 27.066 26.551 1.00 35.65 C
ANISOU 470 CB ILE A 63 4003 4506 5038 -71 314 -188 C
ATOM 471 CG1 ILE A 63 6.153 28.221 26.982 1.00 37.30 C
ANISOU 471 CG1 ILE A 63 4136 4688 5348 -107 283 -234 C
ATOM 472 CG2 ILE A 63 5.207 25.906 27.577 1.00 37.18 C
ANISOU 472 CG2 ILE A 63 4214 4722 5189 -15 230 -196 C
ATOM 473 CD1 ILE A 63 7.764 28.026 26.736 1.00 50.53 C
ANISOU 473 CD1 ILE A 63 5678 6348 7172 -116 289 -275 C
ATOM 474 N SER A 64 3.439 25.532 24.245 1.00 28.45 N
ANISOU 474 N SER A 64 3226 3609 3975 -56 459 -96 N
ATOM 475 CA SER A 64 2.533 24.502 23.763 1.00 28.25 C
ANISOU 475 CA SER A 64 3263 3595 3874 -34 474 -69 C
ATOM 476 C SER A 64 3.191 23.813 22.557 1.00 30.72 C
ANISOU 476 C SER A 64 3569 3898 4204 -34 548 -64 C
ATOM 477 O SER A 64 3.247 22.592 22.531 1.00 29.97 O
ANISOU 477 O SER A 64 3481 3813 4095 -4 545 -64 O
ATOM 478 CB SER A 64 1.204 25.138 23.350 1.00 31.57 C
ANISOU 478 CB SER A 64 3751 4009 4235 -49 480 -44 C
ATOM 479 OG SER A 64 0.297 24.182 22.830 1.00 38.83 O
ANISOU 479 OG SER A 64 4722 4935 5096 -33 485 -25 O
ATOM 480 N ASP A 65 3.712 24.595 21.572 1.00 26.96 N
ANISOU 480 N ASP A 65 3089 3396 3759 -67 624 -59 N
ATOM 481 CA ASP A 65 4.364 24.006 20.413 1.00 26.30 C
ANISOU 481 CA ASP A 65 3013 3295 3687 -68 714 -56 C
ATOM 482 C ASP A 65 5.578 23.182 20.847 1.00 30.52 C
ANISOU 482 C ASP A 65 3453 3834 4311 -44 716 -88 C
ATOM 483 O ASP A 65 5.761 22.095 20.336 1.00 30.01 O
ANISOU 483 O ASP A 65 3403 3768 4233 -19 752 -89 O
ATOM 484 CB ASP A 65 4.843 25.069 19.419 1.00 26.30 C
ANISOU 484 CB ASP A 65 3027 3254 3710 -110 810 -46 C
ATOM 485 CG ASP A 65 3.801 25.896 18.697 1.00 35.04 C
ANISOU 485 CG ASP A 65 4241 4342 4730 -128 820 -10 C
ATOM 486 OD1 ASP A 65 2.600 25.492 18.684 1.00 32.53 O
ANISOU 486 OD1 ASP A 65 3989 4043 4329 -106 759 6 O
ATOM 487 OD2 ASP A 65 4.175 26.940 18.142 1.00 37.86 O
ANISOU 487 OD2 ASP A 65 4615 4661 5109 -162 886 1 O
ATOM 488 N LEU A 66 6.410 23.708 21.753 1.00 26.82 N
ANISOU 488 N LEU A 66 2888 3365 3937 -49 672 -119 N
ATOM 489 CA LEU A 66 7.623 23.014 22.177 1.00 28.51 C
ANISOU 489 CA LEU A 66 2998 3578 4255 -20 656 -155 C
ATOM 490 C LEU A 66 7.337 21.689 22.886 1.00 32.94 C
ANISOU 490 C LEU A 66 3579 4162 4772 38 578 -153 C
ATOM 491 O LEU A 66 8.088 20.725 22.692 1.00 33.06 O
ANISOU 491 O LEU A 66 3550 4170 4842 72 599 -167 O
ATOM 492 CB LEU A 66 8.516 23.923 23.037 1.00 28.79 C
ANISOU 492 CB LEU A 66 2927 3605 4406 -38 600 -195 C
ATOM 493 CG LEU A 66 9.306 24.989 22.279 1.00 33.90 C
ANISOU 493 CG LEU A 66 3514 4212 5154 -95 703 -209 C
ATOM 494 CD1 LEU A 66 9.773 26.099 23.225 1.00 32.90 C
ANISOU 494 CD1 LEU A 66 3310 4076 5115 -124 627 -247 C
ATOM 495 CD2 LEU A 66 10.490 24.370 21.530 1.00 38.37 C
ANISOU 495 CD2 LEU A 66 3992 4752 5833 -90 803 -231 C
ATOM 496 N ALA A 67 6.259 21.644 23.695 1.00 27.79 N
ANISOU 496 N ALA A 67 2998 3531 4028 50 499 -135 N
ATOM 497 CA ALA A 67 5.845 20.427 24.397 1.00 28.25 C
ANISOU 497 CA ALA A 67 3098 3602 4034 100 438 -126 C
ATOM 498 C ALA A 67 5.521 19.335 23.346 1.00 32.36 C
ANISOU 498 C ALA A 67 3669 4114 4512 111 512 -108 C
ATOM 499 O ALA A 67 6.010 18.199 23.465 1.00 32.57 O
ANISOU 499 O ALA A 67 3679 4133 4562 154 504 -115 O
ATOM 500 CB ALA A 67 4.631 20.711 25.290 1.00 28.79 C
ANISOU 500 CB ALA A 67 3243 3685 4012 98 377 -109 C
ATOM 501 N PHE A 68 4.753 19.704 22.297 1.00 26.80 N
ANISOU 501 N PHE A 68 3027 3405 3749 76 577 -88 N
ATOM 502 CA PHE A 68 4.430 18.810 21.188 1.00 27.16 C
ANISOU 502 CA PHE A 68 3134 3438 3748 81 641 -77 C
ATOM 503 C PHE A 68 5.715 18.362 20.454 1.00 31.45 C
ANISOU 503 C PHE A 68 3624 3959 4366 93 723 -98 C
ATOM 504 O PHE A 68 5.878 17.175 20.197 1.00 30.21 O
ANISOU 504 O PHE A 68 3483 3791 4205 126 743 -104 O
ATOM 505 CB PHE A 68 3.416 19.457 20.200 1.00 27.93 C
ANISOU 505 CB PHE A 68 3315 3530 3767 43 675 -56 C
ATOM 506 CG PHE A 68 3.522 18.971 18.769 1.00 28.88 C
ANISOU 506 CG PHE A 68 3497 3626 3851 39 760 -54 C
ATOM 507 CD1 PHE A 68 3.101 17.686 18.416 1.00 31.02 C
ANISOU 507 CD1 PHE A 68 3821 3889 4076 62 761 -58 C
ATOM 508 CD2 PHE A 68 4.104 19.769 17.784 1.00 29.56 C
ANISOU 508 CD2 PHE A 68 3596 3687 3946 12 848 -52 C
ATOM 509 CE1 PHE A 68 3.221 17.231 17.094 1.00 31.40 C
ANISOU 509 CE1 PHE A 68 3942 3910 4080 60 837 -62 C
ATOM 510 CE2 PHE A 68 4.231 19.301 16.460 1.00 31.84 C
ANISOU 510 CE2 PHE A 68 3966 3946 4184 11 936 -51 C
ATOM 511 CZ PHE A 68 3.774 18.045 16.121 1.00 29.09 C
ANISOU 511 CZ PHE A 68 3676 3595 3783 36 925 -59 C
ATOM 512 N LEU A 69 6.611 19.298 20.137 1.00 29.05 N
ANISOU 512 N LEU A 69 3255 3642 4139 66 777 -112 N
ATOM 513 CA LEU A 69 7.843 18.996 19.394 1.00 29.99 C
ANISOU 513 CA LEU A 69 3313 3732 4348 72 879 -135 C
ATOM 514 C LEU A 69 8.765 18.020 20.132 1.00 37.15 C
ANISOU 514 C LEU A 69 4125 4638 5352 127 836 -164 C
ATOM 515 O LEU A 69 9.428 17.189 19.495 1.00 36.60 O
ANISOU 515 O LEU A 69 4035 4544 5327 152 913 -180 O
ATOM 516 CB LEU A 69 8.578 20.291 18.996 1.00 29.42 C
ANISOU 516 CB LEU A 69 3184 3638 4356 24 954 -145 C
ATOM 517 CG LEU A 69 7.840 21.195 17.996 1.00 32.97 C
ANISOU 517 CG LEU A 69 3744 4071 4711 -23 1023 -113 C
ATOM 518 CD1 LEU A 69 8.326 22.664 18.119 1.00 31.88 C
ANISOU 518 CD1 LEU A 69 3550 3914 4647 -72 1051 -118 C
ATOM 519 CD2 LEU A 69 8.001 20.680 16.556 1.00 31.37 C
ANISOU 519 CD2 LEU A 69 3627 3833 4459 -24 1156 -106 C
ATOM 520 N CYS A 70 8.739 18.070 21.467 1.00 36.04 N
ANISOU 520 N CYS A 70 3942 4520 5232 150 709 -170 N
ATOM 521 CA CYS A 70 9.501 17.164 22.326 1.00 38.17 C
ANISOU 521 CA CYS A 70 4140 4787 5577 213 633 -192 C
ATOM 522 C CYS A 70 8.988 15.715 22.294 1.00 39.56 C
ANISOU 522 C CYS A 70 4394 4956 5679 260 625 -174 C
ATOM 523 O CYS A 70 9.758 14.825 22.629 1.00 40.08 O
ANISOU 523 O CYS A 70 4407 5005 5817 317 597 -192 O
ATOM 524 CB CYS A 70 9.579 17.708 23.749 1.00 40.42 C
ANISOU 524 CB CYS A 70 4386 5089 5881 225 494 -203 C
ATOM 525 SG CYS A 70 10.702 19.119 23.921 1.00 45.68 S
ANISOU 525 SG CYS A 70 4913 5747 6697 184 488 -247 S
ATOM 526 N THR A 71 7.712 15.474 21.888 1.00 33.38 N
ANISOU 526 N THR A 71 3733 4181 4769 238 644 -143 N
ATOM 527 CA THR A 71 7.141 14.123 21.796 1.00 32.51 C
ANISOU 527 CA THR A 71 3701 4056 4594 272 643 -130 C
ATOM 528 C THR A 71 7.501 13.455 20.486 1.00 35.31 C
ANISOU 528 C THR A 71 4075 4382 4959 275 757 -143 C
ATOM 529 O THR A 71 7.402 12.237 20.405 1.00 33.54 O
ANISOU 529 O THR A 71 3891 4136 4717 312 762 -143 O
ATOM 530 CB THR A 71 5.594 14.122 21.801 1.00 35.87 C
ANISOU 530 CB THR A 71 4237 4494 4898 241 622 -101 C
ATOM 531 OG1 THR A 71 5.098 14.589 20.534 1.00 34.07 O
ANISOU 531 OG1 THR A 71 4060 4263 4621 195 699 -97 O
ATOM 532 CG2 THR A 71 4.987 14.861 22.975 1.00 29.66 C
ANISOU 532 CG2 THR A 71 3456 3732 4081 230 535 -87 C
ATOM 533 N LEU A 72 7.826 14.252 19.430 1.00 32.06 N
ANISOU 533 N LEU A 72 3655 3964 4563 234 856 -151 N
ATOM 534 CA LEU A 72 8.052 13.713 18.079 1.00 30.85 C
ANISOU 534 CA LEU A 72 3554 3777 4390 231 979 -163 C
ATOM 535 C LEU A 72 9.164 12.660 17.975 1.00 34.55 C
ANISOU 535 C LEU A 72 3957 4213 4958 287 1030 -192 C
ATOM 536 O LEU A 72 8.892 11.647 17.336 1.00 35.59 O
ANISOU 536 O LEU A 72 4168 4318 5037 305 1077 -197 O
ATOM 537 CB LEU A 72 8.225 14.801 17.033 1.00 30.13 C
ANISOU 537 CB LEU A 72 3486 3676 4288 180 1083 -162 C
ATOM 538 CG LEU A 72 6.978 15.679 16.816 1.00 33.10 C
ANISOU 538 CG LEU A 72 3958 4071 4547 133 1043 -131 C
ATOM 539 CD1 LEU A 72 7.204 16.665 15.684 1.00 32.19 C
ANISOU 539 CD1 LEU A 72 3890 3932 4409 90 1153 -125 C
ATOM 540 CD2 LEU A 72 5.726 14.838 16.555 1.00 32.17 C
ANISOU 540 CD2 LEU A 72 3957 3956 4312 139 996 -119 C
ATOM 541 N PRO A 73 10.349 12.743 18.616 1.00 30.45 N
ANISOU 541 N PRO A 73 3298 3689 4584 320 1011 -216 N
ATOM 542 CA PRO A 73 11.300 11.609 18.490 1.00 29.68 C
ANISOU 542 CA PRO A 73 3141 3552 4583 383 1054 -245 C
ATOM 543 C PRO A 73 10.676 10.256 18.919 1.00 34.40 C
ANISOU 543 C PRO A 73 3820 4140 5111 433 985 -231 C
ATOM 544 O PRO A 73 10.830 9.272 18.208 1.00 35.23 O
ANISOU 544 O PRO A 73 3968 4207 5212 461 1063 -245 O
ATOM 545 CB PRO A 73 12.488 12.042 19.351 1.00 30.93 C
ANISOU 545 CB PRO A 73 3128 3713 4910 412 995 -273 C
ATOM 546 CG PRO A 73 12.418 13.564 19.347 1.00 35.76 C
ANISOU 546 CG PRO A 73 3710 4350 5528 342 1002 -269 C
ATOM 547 CD PRO A 73 10.929 13.843 19.425 1.00 31.78 C
ANISOU 547 CD PRO A 73 3350 3877 4846 304 949 -226 C
ATOM 548 N MET A 74 9.861 10.243 19.990 1.00 30.46 N
ANISOU 548 N MET A 74 3362 3667 4543 437 855 -202 N
ATOM 549 CA MET A 74 9.150 9.061 20.473 1.00 29.95 C
ANISOU 549 CA MET A 74 3385 3586 4408 473 797 -182 C
ATOM 550 C MET A 74 8.070 8.585 19.493 1.00 33.06 C
ANISOU 550 C MET A 74 3910 3967 4685 435 863 -174 C
ATOM 551 O MET A 74 7.968 7.393 19.248 1.00 31.86 O
ANISOU 551 O MET A 74 3812 3776 4518 468 886 -180 O
ATOM 552 CB MET A 74 8.504 9.331 21.834 1.00 31.96 C
ANISOU 552 CB MET A 74 3662 3868 4614 477 666 -152 C
ATOM 553 CG MET A 74 9.454 9.159 23.014 1.00 35.41 C
ANISOU 553 CG MET A 74 4015 4298 5142 545 563 -159 C
ATOM 554 SD MET A 74 8.596 9.469 24.595 1.00 38.72 S
ANISOU 554 SD MET A 74 4505 4740 5468 548 422 -122 S
ATOM 555 CE MET A 74 8.420 11.257 24.529 1.00 34.84 C
ANISOU 555 CE MET A 74 3962 4299 4975 472 421 -131 C
ATOM 556 N LEU A 75 7.262 9.506 18.951 1.00 29.39 N
ANISOU 556 N LEU A 75 3497 3529 4141 369 882 -163 N
ATOM 557 CA LEU A 75 6.199 9.158 18.006 1.00 29.52 C
ANISOU 557 CA LEU A 75 3635 3532 4049 333 920 -162 C
ATOM 558 C LEU A 75 6.769 8.657 16.679 1.00 33.28 C
ANISOU 558 C LEU A 75 4149 3968 4526 340 1041 -192 C
ATOM 559 O LEU A 75 6.269 7.655 16.157 1.00 32.41 O
ANISOU 559 O LEU A 75 4129 3825 4361 347 1061 -204 O
ATOM 560 CB LEU A 75 5.263 10.356 17.797 1.00 29.68 C
ANISOU 560 CB LEU A 75 3693 3588 3996 271 895 -144 C
ATOM 561 CG LEU A 75 3.968 10.390 18.631 1.00 34.42 C
ANISOU 561 CG LEU A 75 4332 4208 4539 251 799 -119 C
ATOM 562 CD1 LEU A 75 4.160 9.892 20.071 1.00 33.79 C
ANISOU 562 CD1 LEU A 75 4209 4129 4500 292 726 -105 C
ATOM 563 CD2 LEU A 75 3.331 11.744 18.580 1.00 35.43 C
ANISOU 563 CD2 LEU A 75 4462 4369 4629 202 773 -104 C
ATOM 564 N ILE A 76 7.834 9.331 16.150 1.00 29.74 N
ANISOU 564 N ILE A 76 3635 3517 4149 338 1131 -209 N
ATOM 565 CA ILE A 76 8.514 8.922 14.923 1.00 28.80 C
ANISOU 565 CA ILE A 76 3551 3353 4040 348 1272 -240 C
ATOM 566 C ILE A 76 9.104 7.502 15.134 1.00 36.31 C
ANISOU 566 C ILE A 76 4476 4262 5058 416 1287 -263 C
ATOM 567 O ILE A 76 8.891 6.635 14.292 1.00 37.05 O
ANISOU 567 O ILE A 76 4668 4313 5094 424 1352 -283 O
ATOM 568 CB ILE A 76 9.598 9.948 14.482 1.00 31.23 C
ANISOU 568 CB ILE A 76 3774 3657 4434 331 1378 -252 C
ATOM 569 CG1 ILE A 76 8.961 11.334 14.168 1.00 31.97 C
ANISOU 569 CG1 ILE A 76 3918 3781 4450 264 1371 -225 C
ATOM 570 CG2 ILE A 76 10.428 9.408 13.265 1.00 29.64 C
ANISOU 570 CG2 ILE A 76 3607 3398 4258 348 1551 -288 C
ATOM 571 CD1 ILE A 76 9.980 12.595 14.257 1.00 32.66 C
ANISOU 571 CD1 ILE A 76 3885 3872 4652 239 1435 -229 C
ATOM 572 N ARG A 77 9.835 7.267 16.249 1.00 32.15 N
ANISOU 572 N ARG A 77 3826 3740 4650 467 1220 -261 N
ATOM 573 CA ARG A 77 10.413 5.949 16.508 1.00 32.34 C
ANISOU 573 CA ARG A 77 3826 3719 4744 541 1222 -279 C
ATOM 574 C ARG A 77 9.320 4.862 16.610 1.00 34.91 C
ANISOU 574 C ARG A 77 4280 4022 4964 545 1171 -266 C
ATOM 575 O ARG A 77 9.519 3.779 16.094 1.00 35.20 O
ANISOU 575 O ARG A 77 4364 4005 5005 581 1232 -289 O
ATOM 576 CB ARG A 77 11.328 5.954 17.752 1.00 35.99 C
ANISOU 576 CB ARG A 77 4142 4188 5344 601 1130 -278 C
ATOM 577 CG ARG A 77 12.232 4.708 17.853 1.00 52.92 C
ANISOU 577 CG ARG A 77 6238 6274 7595 689 1151 -303 C
ATOM 578 CD ARG A 77 11.969 3.873 19.096 1.00 64.10 C
ANISOU 578 CD ARG A 77 7672 7679 9004 749 1010 -275 C
ATOM 579 NE ARG A 77 12.388 2.478 18.932 1.00 78.04 N
ANISOU 579 NE ARG A 77 9458 9376 10817 823 1043 -291 N
ATOM 580 CZ ARG A 77 13.601 2.014 19.215 1.00 92.91 C
ANISOU 580 CZ ARG A 77 11225 11223 12855 908 1037 -316 C
ATOM 581 NH1 ARG A 77 13.890 0.735 19.017 1.00 82.85 N
ANISOU 581 NH1 ARG A 77 9982 9880 11616 976 1073 -329 N
ATOM 582 NH2 ARG A 77 14.535 2.825 19.695 1.00 75.90 N
ANISOU 582 NH2 ARG A 77 8915 9094 10831 925 992 -331 N
ATOM 583 N SER A 78 8.159 5.162 17.221 1.00 29.26 N
ANISOU 583 N SER A 78 3620 3340 4159 506 1071 -232 N
ATOM 584 CA SER A 78 7.073 4.184 17.336 1.00 27.80 C
ANISOU 584 CA SER A 78 3545 3129 3891 499 1030 -222 C
ATOM 585 C SER A 78 6.481 3.844 15.960 1.00 33.76 C
ANISOU 585 C SER A 78 4415 3854 4557 460 1109 -251 C
ATOM 586 O SER A 78 6.374 2.666 15.636 1.00 35.08 O
ANISOU 586 O SER A 78 4649 3968 4714 484 1136 -271 O
ATOM 587 CB SER A 78 6.005 4.662 18.310 1.00 26.49 C
ANISOU 587 CB SER A 78 3396 3000 3668 464 923 -184 C
ATOM 588 OG SER A 78 6.643 5.058 19.510 1.00 33.37 O
ANISOU 588 OG SER A 78 4176 3895 4608 502 852 -164 O
ATOM 589 N TYR A 79 6.163 4.859 15.133 1.00 30.45 N
ANISOU 589 N TYR A 79 4030 3464 4075 406 1143 -255 N
ATOM 590 CA TYR A 79 5.676 4.635 13.772 1.00 30.62 C
ANISOU 590 CA TYR A 79 4178 3456 4001 374 1207 -284 C
ATOM 591 C TYR A 79 6.722 3.947 12.876 1.00 36.08 C
ANISOU 591 C TYR A 79 4890 4092 4726 415 1339 -324 C
ATOM 592 O TYR A 79 6.361 3.054 12.108 1.00 35.73 O
ANISOU 592 O TYR A 79 4958 3999 4619 416 1374 -356 O
ATOM 593 CB TYR A 79 5.218 5.948 13.120 1.00 29.69 C
ANISOU 593 CB TYR A 79 4099 3375 3807 317 1211 -274 C
ATOM 594 CG TYR A 79 3.885 6.424 13.644 1.00 30.28 C
ANISOU 594 CG TYR A 79 4193 3486 3825 273 1090 -248 C
ATOM 595 CD1 TYR A 79 2.735 5.645 13.495 1.00 30.75 C
ANISOU 595 CD1 TYR A 79 4337 3522 3825 252 1030 -261 C
ATOM 596 CD2 TYR A 79 3.756 7.675 14.247 1.00 29.37 C
ANISOU 596 CD2 TYR A 79 4010 3424 3726 249 1042 -215 C
ATOM 597 CE1 TYR A 79 1.501 6.086 13.961 1.00 28.03 C
ANISOU 597 CE1 TYR A 79 3995 3205 3451 211 930 -242 C
ATOM 598 CE2 TYR A 79 2.528 8.122 14.724 1.00 29.70 C
ANISOU 598 CE2 TYR A 79 4064 3493 3727 212 944 -195 C
ATOM 599 CZ TYR A 79 1.404 7.328 14.567 1.00 31.53 C
ANISOU 599 CZ TYR A 79 4368 3701 3910 194 891 -208 C
ATOM 600 OH TYR A 79 0.190 7.778 14.984 1.00 30.58 O
ANISOU 600 OH TYR A 79 4248 3603 3768 157 805 -194 O
ATOM 601 N ALA A 80 8.001 4.348 12.979 1.00 33.66 N
ANISOU 601 N ALA A 80 4473 3788 4527 448 1414 -329 N
ATOM 602 CA ALA A 80 9.075 3.731 12.192 1.00 35.02 C
ANISOU 602 CA ALA A 80 4645 3904 4757 491 1557 -370 C
ATOM 603 C ALA A 80 9.264 2.242 12.503 1.00 41.40 C
ANISOU 603 C ALA A 80 5460 4657 5613 553 1549 -389 C
ATOM 604 O ALA A 80 9.524 1.483 11.577 1.00 43.41 O
ANISOU 604 O ALA A 80 5796 4854 5846 573 1653 -429 O
ATOM 605 CB ALA A 80 10.394 4.474 12.384 1.00 35.51 C
ANISOU 605 CB ALA A 80 4555 3977 4959 513 1631 -373 C
ATOM 606 N THR A 81 9.133 1.829 13.781 1.00 37.37 N
ANISOU 606 N THR A 81 4880 4159 5159 586 1430 -361 N
ATOM 607 CA THR A 81 9.330 0.435 14.234 1.00 38.16 C
ANISOU 607 CA THR A 81 4988 4202 5311 652 1411 -369 C
ATOM 608 C THR A 81 8.029 -0.420 14.233 1.00 42.26 C
ANISOU 608 C THR A 81 5643 4692 5723 622 1350 -365 C
ATOM 609 O THR A 81 8.112 -1.641 14.328 1.00 43.14 O
ANISOU 609 O THR A 81 5793 4739 5858 667 1359 -379 O
ATOM 610 CB THR A 81 10.028 0.378 15.630 1.00 45.25 C
ANISOU 610 CB THR A 81 5750 5112 6332 716 1318 -341 C
ATOM 611 OG1 THR A 81 9.151 0.919 16.609 1.00 49.27 O
ANISOU 611 OG1 THR A 81 6265 5672 6785 680 1190 -295 O
ATOM 612 CG2 THR A 81 11.368 1.120 15.674 1.00 42.15 C
ANISOU 612 CG2 THR A 81 5202 4737 6076 749 1367 -356 C
ATOM 613 N GLY A 82 6.861 0.216 14.169 1.00 36.32 N
ANISOU 613 N GLY A 82 4951 3982 4869 548 1286 -348 N
ATOM 614 CA GLY A 82 5.599 -0.510 14.112 1.00 35.40 C
ANISOU 614 CA GLY A 82 4944 3836 4671 510 1231 -352 C
ATOM 615 C GLY A 82 4.968 -0.869 15.440 1.00 41.00 C
ANISOU 615 C GLY A 82 5630 4547 5401 513 1128 -310 C
ATOM 616 O GLY A 82 3.997 -1.630 15.454 1.00 41.31 O
ANISOU 616 O GLY A 82 5750 4546 5398 484 1098 -316 O
ATOM 617 N ASN A 83 5.482 -0.325 16.569 1.00 37.14 N
ANISOU 617 N ASN A 83 5039 4098 4974 546 1075 -269 N
ATOM 618 CA ASN A 83 4.897 -0.623 17.885 1.00 38.36 C
ANISOU 618 CA ASN A 83 5194 4249 5132 552 985 -225 C
ATOM 619 C ASN A 83 5.185 0.443 18.939 1.00 41.22 C
ANISOU 619 C ASN A 83 5465 4676 5522 561 915 -185 C
ATOM 620 O ASN A 83 6.102 1.251 18.774 1.00 41.70 O
ANISOU 620 O ASN A 83 5439 4775 5631 578 933 -194 O
ATOM 621 CB ASN A 83 5.331 -2.025 18.402 1.00 45.27 C
ANISOU 621 CB ASN A 83 6097 5046 6059 624 989 -220 C
ATOM 622 CG ASN A 83 6.818 -2.294 18.371 1.00 76.10 C
ANISOU 622 CG ASN A 83 9923 8930 10062 712 1026 -234 C
ATOM 623 OD1 ASN A 83 7.657 -1.382 18.370 1.00 72.98 O
ANISOU 623 OD1 ASN A 83 9425 8583 9719 728 1030 -237 O
ATOM 624 ND2 ASN A 83 7.173 -3.566 18.346 1.00 70.98 N
ANISOU 624 ND2 ASN A 83 9316 8200 9453 772 1055 -246 N
ATOM 625 N TRP A 84 4.409 0.428 20.023 1.00 35.77 N
ANISOU 625 N TRP A 84 4799 3989 4802 547 843 -146 N
ATOM 626 CA TRP A 84 4.604 1.330 21.155 1.00 34.61 C
ANISOU 626 CA TRP A 84 4591 3893 4668 559 770 -110 C
ATOM 627 C TRP A 84 5.444 0.549 22.136 1.00 37.88 C
ANISOU 627 C TRP A 84 4994 4264 5135 649 726 -89 C
ATOM 628 O TRP A 84 5.076 -0.572 22.463 1.00 37.46 O
ANISOU 628 O TRP A 84 5020 4145 5067 671 728 -74 O
ATOM 629 CB TRP A 84 3.261 1.687 21.806 1.00 33.02 C
ANISOU 629 CB TRP A 84 4439 3708 4398 499 728 -81 C
ATOM 630 CG TRP A 84 3.416 2.580 23.000 1.00 33.33 C
ANISOU 630 CG TRP A 84 4437 3791 4436 513 657 -47 C
ATOM 631 CD1 TRP A 84 3.176 2.259 24.306 1.00 36.02 C
ANISOU 631 CD1 TRP A 84 4823 4107 4754 542 606 -8 C
ATOM 632 CD2 TRP A 84 3.918 3.921 23.000 1.00 32.74 C
ANISOU 632 CD2 TRP A 84 4276 3783 4379 501 632 -53 C
ATOM 633 NE1 TRP A 84 3.480 3.331 25.118 1.00 35.08 N
ANISOU 633 NE1 TRP A 84 4657 4039 4632 550 543 7 N
ATOM 634 CE2 TRP A 84 3.949 4.359 24.342 1.00 36.17 C
ANISOU 634 CE2 TRP A 84 4707 4233 4802 524 556 -22 C
ATOM 635 CE3 TRP A 84 4.348 4.801 21.988 1.00 33.98 C
ANISOU 635 CE3 TRP A 84 4371 3981 4558 473 672 -82 C
ATOM 636 CZ2 TRP A 84 4.349 5.650 24.696 1.00 35.65 C
ANISOU 636 CZ2 TRP A 84 4569 4225 4752 515 511 -24 C
ATOM 637 CZ3 TRP A 84 4.783 6.065 22.347 1.00 35.41 C
ANISOU 637 CZ3 TRP A 84 4477 4215 4762 463 637 -79 C
ATOM 638 CH2 TRP A 84 4.752 6.489 23.683 1.00 35.81 C
ANISOU 638 CH2 TRP A 84 4517 4282 4806 482 553 -53 C
ATOM 639 N THR A 85 6.584 1.094 22.571 1.00 33.98 N
ANISOU 639 N THR A 85 4403 3798 4712 703 684 -89 N
ATOM 640 CA THR A 85 7.455 0.367 23.503 1.00 33.31 C
ANISOU 640 CA THR A 85 4304 3669 4685 801 620 -72 C
ATOM 641 C THR A 85 7.812 1.214 24.707 1.00 34.98 C
ANISOU 641 C THR A 85 4467 3920 4903 827 509 -47 C
ATOM 642 O THR A 85 8.555 0.730 25.555 1.00 34.48 O
ANISOU 642 O THR A 85 4395 3823 4884 913 430 -33 O
ATOM 643 CB THR A 85 8.791 -0.055 22.809 1.00 38.29 C
ANISOU 643 CB THR A 85 4844 4272 5433 867 666 -113 C
ATOM 644 OG1 THR A 85 9.480 1.108 22.369 1.00 38.94 O
ANISOU 644 OG1 THR A 85 4807 4413 5577 845 685 -142 O
ATOM 645 CG2 THR A 85 8.605 -1.024 21.663 1.00 36.48 C
ANISOU 645 CG2 THR A 85 4674 3988 5198 858 776 -142 C
ATOM 646 N TYR A 86 7.324 2.474 24.777 1.00 29.11 N
ANISOU 646 N TYR A 86 3698 3245 4120 758 496 -46 N
ATOM 647 CA TYR A 86 7.739 3.411 25.819 1.00 27.95 C
ANISOU 647 CA TYR A 86 3499 3137 3983 778 393 -34 C
ATOM 648 C TYR A 86 7.041 3.256 27.165 1.00 33.06 C
ANISOU 648 C TYR A 86 4255 3767 4539 792 315 12 C
ATOM 649 O TYR A 86 7.524 3.833 28.140 1.00 34.36 O
ANISOU 649 O TYR A 86 4398 3951 4708 828 214 20 O
ATOM 650 CB TYR A 86 7.645 4.863 25.328 1.00 28.20 C
ANISOU 650 CB TYR A 86 3455 3239 4020 704 416 -56 C
ATOM 651 CG TYR A 86 8.643 5.202 24.250 1.00 28.91 C
ANISOU 651 CG TYR A 86 3430 3342 4214 703 483 -100 C
ATOM 652 CD1 TYR A 86 9.938 5.590 24.570 1.00 30.29 C
ANISOU 652 CD1 TYR A 86 3479 3523 4508 754 432 -125 C
ATOM 653 CD2 TYR A 86 8.287 5.159 22.902 1.00 29.29 C
ANISOU 653 CD2 TYR A 86 3496 3389 4242 651 601 -120 C
ATOM 654 CE1 TYR A 86 10.871 5.887 23.576 1.00 30.67 C
ANISOU 654 CE1 TYR A 86 3414 3572 4666 749 517 -168 C
ATOM 655 CE2 TYR A 86 9.213 5.449 21.898 1.00 28.69 C
ANISOU 655 CE2 TYR A 86 3333 3314 4253 650 686 -158 C
ATOM 656 CZ TYR A 86 10.498 5.827 22.242 1.00 36.36 C
ANISOU 656 CZ TYR A 86 4171 4290 5354 696 654 -182 C
ATOM 657 OH TYR A 86 11.410 6.125 21.260 1.00 39.43 O
ANISOU 657 OH TYR A 86 4468 4671 5842 691 758 -221 O
ATOM 658 N GLY A 87 5.982 2.456 27.250 1.00 29.31 N
ANISOU 658 N GLY A 87 3900 3250 3987 767 362 41 N
ATOM 659 CA GLY A 87 5.326 2.227 28.534 1.00 28.22 C
ANISOU 659 CA GLY A 87 3879 3081 3761 781 313 88 C
ATOM 660 C GLY A 87 4.120 3.096 28.820 1.00 32.13 C
ANISOU 660 C GLY A 87 4414 3614 4179 698 339 101 C
ATOM 661 O GLY A 87 3.772 3.987 28.032 1.00 31.56 O
ANISOU 661 O GLY A 87 4272 3597 4120 629 378 74 O
ATOM 662 N ASP A 88 3.507 2.870 29.988 1.00 29.94 N
ANISOU 662 N ASP A 88 4253 3300 3821 709 317 144 N
ATOM 663 CA ASP A 88 2.269 3.537 30.382 1.00 29.92 C
ANISOU 663 CA ASP A 88 4301 3317 3751 636 358 158 C
ATOM 664 C ASP A 88 2.385 5.022 30.690 1.00 33.28 C
ANISOU 664 C ASP A 88 4664 3814 4166 612 308 142 C
ATOM 665 O ASP A 88 1.521 5.756 30.237 1.00 33.97 O
ANISOU 665 O ASP A 88 4720 3938 4248 536 360 129 O
ATOM 666 CB ASP A 88 1.547 2.816 31.525 1.00 30.56 C
ANISOU 666 CB ASP A 88 4538 3326 3749 651 379 208 C
ATOM 667 CG ASP A 88 2.351 2.403 32.737 1.00 43.22 C
ANISOU 667 CG ASP A 88 6234 4884 5302 750 286 242 C
ATOM 668 OD1 ASP A 88 3.440 2.979 32.962 1.00 44.12 O
ANISOU 668 OD1 ASP A 88 6282 5037 5445 805 178 224 O
ATOM 669 OD2 ASP A 88 1.873 1.535 33.488 1.00 48.76 O
ANISOU 669 OD2 ASP A 88 7080 5507 5939 771 319 287 O
ATOM 670 N VAL A 89 3.402 5.467 31.440 1.00 30.74 N
ANISOU 670 N VAL A 89 4324 3509 3849 675 202 139 N
ATOM 671 CA VAL A 89 3.567 6.881 31.833 1.00 31.12 C
ANISOU 671 CA VAL A 89 4321 3616 3889 653 145 120 C
ATOM 672 C VAL A 89 3.719 7.767 30.586 1.00 33.30 C
ANISOU 672 C VAL A 89 4456 3954 4242 593 185 79 C
ATOM 673 O VAL A 89 3.031 8.780 30.471 1.00 30.66 O
ANISOU 673 O VAL A 89 4104 3658 3887 531 213 71 O
ATOM 674 CB VAL A 89 4.731 7.071 32.865 1.00 36.00 C
ANISOU 674 CB VAL A 89 4943 4228 4506 739 3 116 C
ATOM 675 CG1 VAL A 89 5.004 8.555 33.160 1.00 35.47 C
ANISOU 675 CG1 VAL A 89 4808 4219 4449 711 -59 85 C
ATOM 676 CG2 VAL A 89 4.431 6.328 34.166 1.00 35.99 C
ANISOU 676 CG2 VAL A 89 5118 4161 4396 796 -35 164 C
ATOM 677 N LEU A 90 4.591 7.338 29.638 1.00 29.43 N
ANISOU 677 N LEU A 90 3879 3464 3840 616 197 55 N
ATOM 678 CA LEU A 90 4.851 8.058 28.405 1.00 29.75 C
ANISOU 678 CA LEU A 90 3807 3549 3947 567 249 19 C
ATOM 679 C LEU A 90 3.676 7.989 27.430 1.00 34.20 C
ANISOU 679 C LEU A 90 4401 4117 4478 493 348 21 C
ATOM 680 O LEU A 90 3.503 8.913 26.647 1.00 33.80 O
ANISOU 680 O LEU A 90 4295 4107 4443 440 382 2 O
ATOM 681 CB LEU A 90 6.181 7.632 27.762 1.00 29.28 C
ANISOU 681 CB LEU A 90 3652 3480 3994 616 245 -10 C
ATOM 682 CG LEU A 90 7.440 8.143 28.517 1.00 33.53 C
ANISOU 682 CG LEU A 90 4106 4028 4604 674 134 -30 C
ATOM 683 CD1 LEU A 90 8.720 7.499 27.976 1.00 31.95 C
ANISOU 683 CD1 LEU A 90 3808 3804 4529 735 135 -59 C
ATOM 684 CD2 LEU A 90 7.541 9.697 28.494 1.00 34.54 C
ANISOU 684 CD2 LEU A 90 4158 4212 4755 618 117 -54 C
ATOM 685 N CYS A 91 2.824 6.957 27.530 1.00 31.51 N
ANISOU 685 N CYS A 91 4151 3730 4091 488 388 43 N
ATOM 686 CA CYS A 91 1.605 6.870 26.727 1.00 32.40 C
ANISOU 686 CA CYS A 91 4292 3841 4180 418 462 39 C
ATOM 687 C CYS A 91 0.674 8.020 27.150 1.00 32.86 C
ANISOU 687 C CYS A 91 4351 3934 4199 364 457 45 C
ATOM 688 O CYS A 91 0.172 8.726 26.294 1.00 31.86 O
ANISOU 688 O CYS A 91 4185 3839 4081 311 484 28 O
ATOM 689 CB CYS A 91 0.902 5.524 26.910 1.00 34.49 C
ANISOU 689 CB CYS A 91 4648 4038 4419 421 502 58 C
ATOM 690 SG CYS A 91 -0.768 5.477 26.190 1.00 39.36 S
ANISOU 690 SG CYS A 91 5290 4646 5020 330 571 47 S
ATOM 691 N ILE A 92 0.415 8.158 28.465 1.00 27.36 N
ANISOU 691 N ILE A 92 3714 3226 3457 382 425 71 N
ATOM 692 CA ILE A 92 -0.489 9.171 29.001 1.00 27.90 C
ANISOU 692 CA ILE A 92 3794 3317 3489 339 431 76 C
ATOM 693 C ILE A 92 0.063 10.582 28.734 1.00 30.62 C
ANISOU 693 C ILE A 92 4053 3721 3860 325 391 53 C
ATOM 694 O ILE A 92 -0.686 11.433 28.244 1.00 29.05 O
ANISOU 694 O ILE A 92 3825 3549 3665 271 418 43 O
ATOM 695 CB ILE A 92 -0.802 8.935 30.506 1.00 31.13 C
ANISOU 695 CB ILE A 92 4309 3689 3832 368 418 108 C
ATOM 696 CG1 ILE A 92 -1.511 7.567 30.732 1.00 32.50 C
ANISOU 696 CG1 ILE A 92 4575 3791 3984 369 482 135 C
ATOM 697 CG2 ILE A 92 -1.631 10.109 31.106 1.00 31.35 C
ANISOU 697 CG2 ILE A 92 4347 3740 3827 328 431 107 C
ATOM 698 CD1 ILE A 92 -1.500 7.110 32.227 1.00 48.58 C
ANISOU 698 CD1 ILE A 92 6744 5773 5942 418 471 175 C
ATOM 699 N SER A 93 1.361 10.817 29.043 1.00 26.93 N
ANISOU 699 N SER A 93 3545 3268 3420 373 324 43 N
ATOM 700 CA SER A 93 1.974 12.127 28.832 1.00 27.92 C
ANISOU 700 CA SER A 93 3586 3440 3584 357 289 18 C
ATOM 701 C SER A 93 1.958 12.536 27.356 1.00 31.07 C
ANISOU 701 C SER A 93 3915 3863 4029 311 348 -1 C
ATOM 702 O SER A 93 1.555 13.666 27.066 1.00 30.88 O
ANISOU 702 O SER A 93 3863 3867 4003 266 359 -9 O
ATOM 703 CB SER A 93 3.366 12.220 29.458 1.00 31.16 C
ANISOU 703 CB SER A 93 3952 3851 4035 416 201 3 C
ATOM 704 OG SER A 93 4.311 11.406 28.800 1.00 45.08 O
ANISOU 704 OG SER A 93 5661 5600 5866 454 207 -9 O
ATOM 705 N ASN A 94 2.291 11.607 26.424 1.00 26.09 N
ANISOU 705 N ASN A 94 3273 3214 3427 322 390 -8 N
ATOM 706 CA ASN A 94 2.241 11.922 24.988 1.00 25.68 C
ANISOU 706 CA ASN A 94 3186 3176 3397 282 451 -25 C
ATOM 707 C ASN A 94 0.823 12.139 24.503 1.00 28.74 C
ANISOU 707 C ASN A 94 3620 3565 3736 228 482 -18 C
ATOM 708 O ASN A 94 0.591 13.087 23.761 1.00 27.68 O
ANISOU 708 O ASN A 94 3464 3454 3601 190 499 -26 O
ATOM 709 CB ASN A 94 2.892 10.846 24.134 1.00 25.71 C
ANISOU 709 CB ASN A 94 3185 3152 3433 310 495 -38 C
ATOM 710 CG ASN A 94 4.396 10.775 24.193 1.00 47.30 C
ANISOU 710 CG ASN A 94 5841 5883 6247 359 482 -56 C
ATOM 711 OD1 ASN A 94 5.082 11.674 24.644 1.00 44.55 O
ANISOU 711 OD1 ASN A 94 5425 5558 5943 363 442 -66 O
ATOM 712 ND2 ASN A 94 4.942 9.691 23.719 1.00 48.60 N
ANISOU 712 ND2 ASN A 94 6006 6015 6444 396 517 -66 N
ATOM 713 N ARG A 95 -0.142 11.278 24.928 1.00 25.13 N
ANISOU 713 N ARG A 95 3225 3078 3245 224 490 -4 N
ATOM 714 CA ARG A 95 -1.531 11.465 24.508 1.00 25.86 C
ANISOU 714 CA ARG A 95 3343 3167 3317 173 511 -5 C
ATOM 715 C ARG A 95 -2.048 12.834 25.003 1.00 28.03 C
ANISOU 715 C ARG A 95 3593 3472 3583 147 489 0 C
ATOM 716 O ARG A 95 -2.788 13.510 24.304 1.00 25.97 O
ANISOU 716 O ARG A 95 3320 3224 3324 109 494 -8 O
ATOM 717 CB ARG A 95 -2.422 10.332 25.051 1.00 26.22 C
ANISOU 717 CB ARG A 95 3446 3166 3349 170 531 6 C
ATOM 718 CG ARG A 95 -2.159 9.012 24.350 1.00 28.74 C
ANISOU 718 CG ARG A 95 3795 3447 3679 184 558 -4 C
ATOM 719 CD ARG A 95 -2.910 8.926 23.046 1.00 25.68 C
ANISOU 719 CD ARG A 95 3409 3054 3294 139 574 -31 C
ATOM 720 NE ARG A 95 -2.579 7.677 22.375 1.00 31.54 N
ANISOU 720 NE ARG A 95 4187 3756 4041 155 600 -47 N
ATOM 721 CZ ARG A 95 -2.761 7.449 21.082 1.00 39.32 C
ANISOU 721 CZ ARG A 95 5190 4732 5017 133 611 -77 C
ATOM 722 NH1 ARG A 95 -2.370 6.305 20.546 1.00 30.44 N
ANISOU 722 NH1 ARG A 95 4105 3565 3895 152 640 -95 N
ATOM 723 NH2 ARG A 95 -3.317 8.374 20.310 1.00 29.93 N
ANISOU 723 NH2 ARG A 95 3990 3570 3812 97 590 -91 N
ATOM 724 N TYR A 96 -1.647 13.225 26.205 1.00 24.86 N
ANISOU 724 N TYR A 96 3194 3078 3173 172 459 11 N
ATOM 725 CA TYR A 96 -2.051 14.507 26.774 1.00 24.59 C
ANISOU 725 CA TYR A 96 3147 3067 3130 152 441 11 C
ATOM 726 C TYR A 96 -1.544 15.646 25.901 1.00 27.46 C
ANISOU 726 C TYR A 96 3452 3462 3520 132 434 -3 C
ATOM 727 O TYR A 96 -2.339 16.427 25.362 1.00 26.91 O
ANISOU 727 O TYR A 96 3373 3400 3450 97 444 -6 O
ATOM 728 CB TYR A 96 -1.564 14.672 28.238 1.00 25.60 C
ANISOU 728 CB TYR A 96 3305 3190 3231 188 401 19 C
ATOM 729 CG TYR A 96 -1.747 16.095 28.742 1.00 29.68 C
ANISOU 729 CG TYR A 96 3806 3730 3743 170 380 10 C
ATOM 730 CD1 TYR A 96 -3.000 16.561 29.147 1.00 31.65 C
ANISOU 730 CD1 TYR A 96 4083 3970 3972 142 413 15 C
ATOM 731 CD2 TYR A 96 -0.680 16.990 28.764 1.00 30.51 C
ANISOU 731 CD2 TYR A 96 3859 3859 3874 178 333 -7 C
ATOM 732 CE1 TYR A 96 -3.182 17.881 29.562 1.00 32.14 C
ANISOU 732 CE1 TYR A 96 4132 4046 4032 127 399 4 C
ATOM 733 CE2 TYR A 96 -0.857 18.321 29.146 1.00 31.61 C
ANISOU 733 CE2 TYR A 96 3985 4013 4012 157 317 -19 C
ATOM 734 CZ TYR A 96 -2.107 18.760 29.557 1.00 40.03 C
ANISOU 734 CZ TYR A 96 5091 5070 5050 134 349 -12 C
ATOM 735 OH TYR A 96 -2.254 20.066 29.966 1.00 36.35 O
ANISOU 735 OH TYR A 96 4616 4611 4583 119 334 -26 O
ATOM 736 N VAL A 97 -0.223 15.694 25.710 1.00 24.57 N
ANISOU 736 N VAL A 97 3045 3106 3184 156 420 -13 N
ATOM 737 CA VAL A 97 0.477 16.770 25.002 1.00 24.34 C
ANISOU 737 CA VAL A 97 2961 3097 3191 137 426 -26 C
ATOM 738 C VAL A 97 -0.039 16.986 23.573 1.00 29.27 C
ANISOU 738 C VAL A 97 3597 3719 3803 102 473 -26 C
ATOM 739 O VAL A 97 -0.161 18.133 23.145 1.00 28.00 O
ANISOU 739 O VAL A 97 3424 3569 3646 75 478 -26 O
ATOM 740 CB VAL A 97 2.007 16.551 25.055 1.00 28.30 C
ANISOU 740 CB VAL A 97 3404 3598 3749 169 415 -42 C
ATOM 741 CG1 VAL A 97 2.726 17.452 24.066 1.00 28.64 C
ANISOU 741 CG1 VAL A 97 3392 3649 3841 142 456 -56 C
ATOM 742 CG2 VAL A 97 2.546 16.757 26.464 1.00 27.60 C
ANISOU 742 CG2 VAL A 97 3303 3512 3671 201 340 -49 C
ATOM 743 N LEU A 98 -0.329 15.902 22.837 1.00 27.31 N
ANISOU 743 N LEU A 98 3385 3454 3538 106 500 -27 N
ATOM 744 CA LEU A 98 -0.798 16.008 21.450 1.00 27.08 C
ANISOU 744 CA LEU A 98 3388 3416 3483 80 530 -31 C
ATOM 745 C LEU A 98 -2.145 16.683 21.356 1.00 30.54 C
ANISOU 745 C LEU A 98 3848 3858 3898 51 502 -24 C
ATOM 746 O LEU A 98 -2.263 17.662 20.623 1.00 29.95 O
ANISOU 746 O LEU A 98 3782 3787 3812 32 504 -21 O
ATOM 747 CB LEU A 98 -0.778 14.667 20.708 1.00 26.77 C
ANISOU 747 CB LEU A 98 3390 3352 3428 92 558 -42 C
ATOM 748 CG LEU A 98 0.542 14.260 19.999 1.00 31.66 C
ANISOU 748 CG LEU A 98 3999 3962 4070 114 614 -55 C
ATOM 749 CD1 LEU A 98 0.698 14.953 18.645 1.00 31.36 C
ANISOU 749 CD1 LEU A 98 3993 3918 4003 90 661 -59 C
ATOM 750 CD2 LEU A 98 1.773 14.421 20.891 1.00 31.28 C
ANISOU 750 CD2 LEU A 98 3875 3924 4085 145 608 -56 C
ATOM 751 N HIS A 99 -3.121 16.250 22.159 1.00 27.03 N
ANISOU 751 N HIS A 99 3410 3405 3454 49 480 -22 N
ATOM 752 CA HIS A 99 -4.418 16.935 22.176 1.00 27.49 C
ANISOU 752 CA HIS A 99 3468 3462 3515 24 456 -21 C
ATOM 753 C HIS A 99 -4.282 18.327 22.800 1.00 28.93 C
ANISOU 753 C HIS A 99 3620 3662 3708 20 444 -13 C
ATOM 754 O HIS A 99 -4.884 19.260 22.282 1.00 30.03 O
ANISOU 754 O HIS A 99 3758 3802 3849 5 428 -11 O
ATOM 755 CB HIS A 99 -5.469 16.121 22.949 1.00 28.87 C
ANISOU 755 CB HIS A 99 3648 3616 3707 18 458 -23 C
ATOM 756 CG HIS A 99 -6.330 15.265 22.079 1.00 33.17 C
ANISOU 756 CG HIS A 99 4212 4134 4259 0 450 -39 C
ATOM 757 ND1 HIS A 99 -5.790 14.267 21.279 1.00 35.08 N
ANISOU 757 ND1 HIS A 99 4487 4361 4479 8 461 -50 N
ATOM 758 CD2 HIS A 99 -7.678 15.243 21.957 1.00 35.33 C
ANISOU 758 CD2 HIS A 99 4470 4388 4568 -24 430 -53 C
ATOM 759 CE1 HIS A 99 -6.819 13.686 20.683 1.00 34.94 C
ANISOU 759 CE1 HIS A 99 4482 4317 4476 -14 440 -71 C
ATOM 760 NE2 HIS A 99 -7.975 14.257 21.037 1.00 35.15 N
ANISOU 760 NE2 HIS A 99 4472 4339 4543 -35 417 -74 N
ATOM 761 N ALA A 100 -3.492 18.480 23.888 1.00 24.25 N
ANISOU 761 N ALA A 100 3010 3080 3122 38 444 -10 N
ATOM 762 CA ALA A 100 -3.359 19.799 24.535 1.00 25.12 C
ANISOU 762 CA ALA A 100 3099 3203 3243 33 428 -10 C
ATOM 763 C ALA A 100 -2.769 20.838 23.594 1.00 31.22 C
ANISOU 763 C ALA A 100 3855 3981 4026 17 434 -10 C
ATOM 764 O ALA A 100 -3.283 21.957 23.518 1.00 30.50 O
ANISOU 764 O ALA A 100 3761 3887 3940 2 425 -7 O
ATOM 765 CB ALA A 100 -2.546 19.723 25.813 1.00 25.45 C
ANISOU 765 CB ALA A 100 3135 3250 3284 57 410 -15 C
ATOM 766 N ASN A 101 -1.750 20.451 22.816 1.00 28.51 N
ANISOU 766 N ASN A 101 3505 3638 3688 21 460 -13 N
ATOM 767 CA ASN A 101 -1.153 21.392 21.883 1.00 28.16 C
ANISOU 767 CA ASN A 101 3457 3589 3654 3 488 -10 C
ATOM 768 C ASN A 101 -2.140 21.859 20.810 1.00 32.02 C
ANISOU 768 C ASN A 101 3998 4063 4105 -13 487 3 C
ATOM 769 O ASN A 101 -2.216 23.047 20.518 1.00 31.05 O
ANISOU 769 O ASN A 101 3882 3930 3984 -28 489 13 O
ATOM 770 CB ASN A 101 0.141 20.857 21.289 1.00 28.16 C
ANISOU 770 CB ASN A 101 3438 3584 3677 10 536 -18 C
ATOM 771 CG ASN A 101 0.631 21.670 20.115 1.00 39.53 C
ANISOU 771 CG ASN A 101 4897 5006 5117 -13 593 -12 C
ATOM 772 OD1 ASN A 101 0.675 21.187 18.995 1.00 32.24 O
ANISOU 772 OD1 ASN A 101 4024 4067 4157 -13 638 -8 O
ATOM 773 ND2 ASN A 101 0.969 22.925 20.334 1.00 30.12 N
ANISOU 773 ND2 ASN A 101 3677 3809 3958 -34 598 -10 N
ATOM 774 N LEU A 102 -2.938 20.949 20.298 1.00 29.15 N
ANISOU 774 N LEU A 102 3671 3693 3711 -8 473 2 N
ATOM 775 CA LEU A 102 -3.901 21.240 19.257 1.00 29.62 C
ANISOU 775 CA LEU A 102 3784 3735 3736 -15 448 8 C
ATOM 776 C LEU A 102 -4.965 22.267 19.713 1.00 30.22 C
ANISOU 776 C LEU A 102 3843 3808 3832 -20 402 14 C
ATOM 777 O LEU A 102 -5.169 23.266 19.031 1.00 27.58 O
ANISOU 777 O LEU A 102 3540 3458 3481 -23 390 27 O
ATOM 778 CB LEU A 102 -4.542 19.916 18.843 1.00 31.10 C
ANISOU 778 CB LEU A 102 4000 3914 3904 -10 429 -6 C
ATOM 779 CG LEU A 102 -5.228 19.858 17.490 1.00 38.75 C
ANISOU 779 CG LEU A 102 5041 4859 4824 -13 395 -10 C
ATOM 780 CD1 LEU A 102 -4.199 19.813 16.346 1.00 39.25 C
ANISOU 780 CD1 LEU A 102 5175 4908 4830 -10 450 -5 C
ATOM 781 CD2 LEU A 102 -6.078 18.618 17.403 1.00 43.49 C
ANISOU 781 CD2 LEU A 102 5647 5448 5429 -14 360 -33 C
ATOM 782 N TYR A 103 -5.575 22.040 20.891 1.00 24.42 N
ANISOU 782 N TYR A 103 3063 3082 3132 -17 387 5 N
ATOM 783 CA TYR A 103 -6.658 22.865 21.399 1.00 24.38 C
ANISOU 783 CA TYR A 103 3036 3069 3160 -18 358 5 C
ATOM 784 C TYR A 103 -6.188 24.119 22.162 1.00 28.43 C
ANISOU 784 C TYR A 103 3528 3585 3689 -20 371 9 C
ATOM 785 O TYR A 103 -6.911 25.111 22.110 1.00 27.58 O
ANISOU 785 O TYR A 103 3417 3462 3600 -19 350 13 O
ATOM 786 CB TYR A 103 -7.640 22.003 22.191 1.00 24.41 C
ANISOU 786 CB TYR A 103 3012 3068 3196 -17 356 -10 C
ATOM 787 CG TYR A 103 -8.279 20.978 21.269 1.00 27.35 C
ANISOU 787 CG TYR A 103 3400 3426 3566 -22 330 -21 C
ATOM 788 CD1 TYR A 103 -8.025 19.618 21.426 1.00 29.25 C
ANISOU 788 CD1 TYR A 103 3650 3665 3798 -23 354 -29 C
ATOM 789 CD2 TYR A 103 -8.995 21.379 20.139 1.00 28.62 C
ANISOU 789 CD2 TYR A 103 3581 3570 3724 -21 273 -24 C
ATOM 790 CE1 TYR A 103 -8.541 18.677 20.532 1.00 30.53 C
ANISOU 790 CE1 TYR A 103 3834 3809 3958 -31 327 -46 C
ATOM 791 CE2 TYR A 103 -9.540 20.448 19.254 1.00 29.50 C
ANISOU 791 CE2 TYR A 103 3716 3665 3829 -25 234 -42 C
ATOM 792 CZ TYR A 103 -9.326 19.097 19.466 1.00 34.57 C
ANISOU 792 CZ TYR A 103 4360 4305 4470 -33 264 -56 C
ATOM 793 OH TYR A 103 -9.877 18.188 18.607 1.00 31.73 O
ANISOU 793 OH TYR A 103 4026 3924 4108 -41 222 -80 O
ATOM 794 N THR A 104 -4.978 24.126 22.785 1.00 25.54 N
ANISOU 794 N THR A 104 3148 3234 3322 -21 397 6 N
ATOM 795 CA THR A 104 -4.461 25.374 23.395 1.00 26.33 C
ANISOU 795 CA THR A 104 3232 3332 3442 -28 400 3 C
ATOM 796 C THR A 104 -4.023 26.328 22.263 1.00 31.10 C
ANISOU 796 C THR A 104 3858 3917 4043 -43 414 18 C
ATOM 797 O THR A 104 -4.194 27.545 22.395 1.00 30.31 O
ANISOU 797 O THR A 104 3758 3798 3960 -50 409 22 O
ATOM 798 CB THR A 104 -3.241 25.153 24.350 1.00 27.95 C
ANISOU 798 CB THR A 104 3410 3552 3658 -25 405 -13 C
ATOM 799 OG1 THR A 104 -2.235 24.417 23.687 1.00 27.80 O
ANISOU 799 OG1 THR A 104 3383 3540 3640 -24 426 -12 O
ATOM 800 CG2 THR A 104 -3.593 24.426 25.622 1.00 22.42 C
ANISOU 800 CG2 THR A 104 2714 2859 2946 -7 392 -23 C
ATOM 801 N SER A 105 -3.461 25.783 21.146 1.00 25.81 N
ANISOU 801 N SER A 105 3216 3244 3347 -46 440 28 N
ATOM 802 CA SER A 105 -2.964 26.643 20.071 1.00 25.72 C
ANISOU 802 CA SER A 105 3245 3205 3322 -61 473 46 C
ATOM 803 C SER A 105 -4.053 27.505 19.439 1.00 30.20 C
ANISOU 803 C SER A 105 3864 3745 3866 -54 437 67 C
ATOM 804 O SER A 105 -3.875 28.714 19.325 1.00 29.21 O
ANISOU 804 O SER A 105 3754 3591 3752 -64 451 80 O
ATOM 805 CB SER A 105 -2.188 25.862 19.008 1.00 28.66 C
ANISOU 805 CB SER A 105 3654 3573 3663 -63 523 51 C
ATOM 806 OG SER A 105 -3.061 25.042 18.254 1.00 38.56 O
ANISOU 806 OG SER A 105 4962 4824 4864 -48 492 55 O
ATOM 807 N ILE A 106 -5.195 26.910 19.085 1.00 26.84 N
ANISOU 807 N ILE A 106 3460 3319 3418 -36 386 66 N
ATOM 808 CA ILE A 106 -6.262 27.712 18.496 1.00 26.32 C
ANISOU 808 CA ILE A 106 3435 3224 3343 -21 332 81 C
ATOM 809 C ILE A 106 -6.806 28.724 19.536 1.00 28.25 C
ANISOU 809 C ILE A 106 3627 3461 3644 -17 316 75 C
ATOM 810 O ILE A 106 -7.149 29.834 19.158 1.00 26.91 O
ANISOU 810 O ILE A 106 3490 3257 3477 -8 297 93 O
ATOM 811 CB ILE A 106 -7.356 26.827 17.823 1.00 29.01 C
ANISOU 811 CB ILE A 106 3799 3561 3662 -2 265 73 C
ATOM 812 CG1 ILE A 106 -8.362 27.672 16.992 1.00 28.44 C
ANISOU 812 CG1 ILE A 106 3779 3451 3578 22 190 89 C
ATOM 813 CG2 ILE A 106 -8.068 25.925 18.846 1.00 28.83 C
ANISOU 813 CG2 ILE A 106 3698 3564 3694 -2 249 44 C
ATOM 814 CD1 ILE A 106 -9.164 26.819 15.911 1.00 33.28 C
ANISOU 814 CD1 ILE A 106 4446 4050 4150 40 110 78 C
ATOM 815 N LEU A 107 -6.863 28.347 20.833 1.00 25.78 N
ANISOU 815 N LEU A 107 3249 3175 3373 -20 327 51 N
ATOM 816 CA LEU A 107 -7.354 29.246 21.899 1.00 24.58 C
ANISOU 816 CA LEU A 107 3059 3012 3266 -16 325 39 C
ATOM 817 C LEU A 107 -6.409 30.430 22.129 1.00 29.63 C
ANISOU 817 C LEU A 107 3709 3635 3914 -33 355 43 C
ATOM 818 O LEU A 107 -6.868 31.560 22.277 1.00 30.95 O
ANISOU 818 O LEU A 107 3882 3770 4106 -26 345 47 O
ATOM 819 CB LEU A 107 -7.590 28.514 23.209 1.00 23.91 C
ANISOU 819 CB LEU A 107 2930 2951 3203 -14 340 14 C
ATOM 820 CG LEU A 107 -8.933 27.805 23.355 1.00 29.21 C
ANISOU 820 CG LEU A 107 3574 3619 3906 -1 322 3 C
ATOM 821 CD1 LEU A 107 -8.945 27.007 24.631 1.00 29.59 C
ANISOU 821 CD1 LEU A 107 3601 3682 3958 -3 360 -15 C
ATOM 822 CD2 LEU A 107 -10.126 28.807 23.387 1.00 28.44 C
ANISOU 822 CD2 LEU A 107 3454 3488 3863 17 297 -1 C
ATOM 823 N PHE A 108 -5.100 30.191 22.147 1.00 25.69 N
ANISOU 823 N PHE A 108 3205 3150 3405 -54 391 40 N
ATOM 824 CA PHE A 108 -4.176 31.318 22.272 1.00 26.47 C
ANISOU 824 CA PHE A 108 3304 3225 3529 -78 421 39 C
ATOM 825 C PHE A 108 -4.340 32.286 21.112 1.00 30.25 C
ANISOU 825 C PHE A 108 3844 3656 3993 -81 432 72 C
ATOM 826 O PHE A 108 -4.304 33.486 21.357 1.00 30.65 O
ANISOU 826 O PHE A 108 3901 3672 4073 -90 439 73 O
ATOM 827 CB PHE A 108 -2.709 30.869 22.466 1.00 27.81 C
ANISOU 827 CB PHE A 108 3438 3412 3715 -102 456 23 C
ATOM 828 CG PHE A 108 -2.506 30.345 23.874 1.00 28.78 C
ANISOU 828 CG PHE A 108 3515 3566 3854 -94 428 -11 C
ATOM 829 CD1 PHE A 108 -2.819 31.132 24.979 1.00 31.85 C
ANISOU 829 CD1 PHE A 108 3897 3945 4261 -93 405 -34 C
ATOM 830 CD2 PHE A 108 -2.031 29.055 24.093 1.00 29.38 C
ANISOU 830 CD2 PHE A 108 3569 3675 3918 -83 425 -20 C
ATOM 831 CE1 PHE A 108 -2.674 30.632 26.277 1.00 32.91 C
ANISOU 831 CE1 PHE A 108 4016 4101 4388 -80 378 -63 C
ATOM 832 CE2 PHE A 108 -1.857 28.567 25.392 1.00 31.90 C
ANISOU 832 CE2 PHE A 108 3867 4015 4238 -68 393 -46 C
ATOM 833 CZ PHE A 108 -2.187 29.353 26.475 1.00 30.11 C
ANISOU 833 CZ PHE A 108 3647 3777 4016 -67 369 -66 C
ATOM 834 N LEU A 109 -4.607 31.779 19.881 1.00 26.97 N
ANISOU 834 N LEU A 109 3486 3234 3527 -69 428 99 N
ATOM 835 CA LEU A 109 -4.805 32.632 18.706 1.00 28.93 C
ANISOU 835 CA LEU A 109 3822 3431 3739 -63 431 136 C
ATOM 836 C LEU A 109 -6.141 33.347 18.756 1.00 30.67 C
ANISOU 836 C LEU A 109 4057 3624 3973 -29 362 145 C
ATOM 837 O LEU A 109 -6.249 34.457 18.269 1.00 29.58 O
ANISOU 837 O LEU A 109 3977 3433 3829 -23 362 171 O
ATOM 838 CB LEU A 109 -4.591 31.898 17.350 1.00 29.52 C
ANISOU 838 CB LEU A 109 3978 3499 3740 -58 448 159 C
ATOM 839 CG LEU A 109 -3.223 32.069 16.655 1.00 35.79 C
ANISOU 839 CG LEU A 109 4815 4267 4515 -92 549 174 C
ATOM 840 CD1 LEU A 109 -2.870 33.576 16.368 1.00 36.69 C
ANISOU 840 CD1 LEU A 109 4980 4316 4644 -111 596 202 C
ATOM 841 CD2 LEU A 109 -2.126 31.391 17.417 1.00 38.11 C
ANISOU 841 CD2 LEU A 109 5015 4601 4865 -118 600 141 C
ATOM 842 N THR A 110 -7.134 32.730 19.363 1.00 27.09 N
ANISOU 842 N THR A 110 3548 3200 3545 -6 309 122 N
ATOM 843 CA THR A 110 -8.439 33.358 19.564 1.00 27.11 C
ANISOU 843 CA THR A 110 3536 3177 3589 28 249 120 C
ATOM 844 C THR A 110 -8.289 34.553 20.528 1.00 29.84 C
ANISOU 844 C THR A 110 3855 3498 3986 21 279 108 C
ATOM 845 O THR A 110 -8.817 35.626 20.253 1.00 28.84 O
ANISOU 845 O THR A 110 3759 3321 3878 43 255 125 O
ATOM 846 CB THR A 110 -9.439 32.327 20.115 1.00 31.77 C
ANISOU 846 CB THR A 110 4056 3799 4214 44 212 90 C
ATOM 847 OG1 THR A 110 -9.568 31.265 19.177 1.00 31.68 O
ANISOU 847 OG1 THR A 110 4075 3803 4157 49 178 95 O
ATOM 848 CG2 THR A 110 -10.804 32.929 20.405 1.00 28.39 C
ANISOU 848 CG2 THR A 110 3589 3342 3856 80 161 79 C
ATOM 849 N PHE A 111 -7.572 34.365 21.647 1.00 27.42 N
ANISOU 849 N PHE A 111 3498 3220 3698 -7 324 79 N
ATOM 850 CA PHE A 111 -7.396 35.442 22.623 1.00 27.50 C
ANISOU 850 CA PHE A 111 3491 3206 3751 -16 347 58 C
ATOM 851 C PHE A 111 -6.493 36.558 22.075 1.00 30.26 C
ANISOU 851 C PHE A 111 3889 3508 4100 -42 380 79 C
ATOM 852 O PHE A 111 -6.788 37.726 22.338 1.00 28.59 O
ANISOU 852 O PHE A 111 3693 3249 3922 -36 380 78 O
ATOM 853 CB PHE A 111 -6.957 34.907 23.991 1.00 29.25 C
ANISOU 853 CB PHE A 111 3663 3467 3983 -33 368 17 C
ATOM 854 CG PHE A 111 -8.118 34.209 24.682 1.00 31.16 C
ANISOU 854 CG PHE A 111 3871 3730 4240 -5 354 -2 C
ATOM 855 CD1 PHE A 111 -9.248 34.928 25.088 1.00 33.77 C
ANISOU 855 CD1 PHE A 111 4189 4026 4617 23 349 -13 C
ATOM 856 CD2 PHE A 111 -8.103 32.828 24.884 1.00 31.74 C
ANISOU 856 CD2 PHE A 111 3924 3848 4290 -6 356 -8 C
ATOM 857 CE1 PHE A 111 -10.335 34.279 25.691 1.00 34.54 C
ANISOU 857 CE1 PHE A 111 4246 4133 4745 44 356 -32 C
ATOM 858 CE2 PHE A 111 -9.185 32.183 25.507 1.00 34.60 C
ANISOU 858 CE2 PHE A 111 4255 4217 4675 13 361 -25 C
ATOM 859 CZ PHE A 111 -10.295 32.913 25.908 1.00 32.66 C
ANISOU 859 CZ PHE A 111 3990 3937 4483 36 365 -37 C
ATOM 860 N ILE A 112 -5.482 36.216 21.233 1.00 27.11 N
ANISOU 860 N ILE A 112 3521 3114 3668 -70 416 100 N
ATOM 861 CA ILE A 112 -4.635 37.229 20.569 1.00 27.71 C
ANISOU 861 CA ILE A 112 3650 3133 3747 -100 468 124 C
ATOM 862 C ILE A 112 -5.547 38.090 19.665 1.00 33.65 C
ANISOU 862 C ILE A 112 4487 3823 4476 -64 438 167 C
ATOM 863 O ILE A 112 -5.484 39.313 19.739 1.00 33.94 O
ANISOU 863 O ILE A 112 4554 3801 4543 -71 456 176 O
ATOM 864 CB ILE A 112 -3.437 36.629 19.766 1.00 29.96 C
ANISOU 864 CB ILE A 112 3951 3426 4005 -134 532 137 C
ATOM 865 CG1 ILE A 112 -2.464 35.900 20.679 1.00 29.08 C
ANISOU 865 CG1 ILE A 112 3750 3365 3935 -162 550 93 C
ATOM 866 CG2 ILE A 112 -2.664 37.714 18.925 1.00 29.67 C
ANISOU 866 CG2 ILE A 112 3985 3315 3974 -167 608 170 C
ATOM 867 CD1 ILE A 112 -1.568 34.863 19.907 1.00 29.65 C
ANISOU 867 CD1 ILE A 112 3822 3461 3984 -177 601 101 C
ATOM 868 N SER A 113 -6.427 37.444 18.873 1.00 29.28 N
ANISOU 868 N SER A 113 3971 3280 3873 -23 381 190 N
ATOM 869 CA SER A 113 -7.379 38.121 17.976 1.00 28.93 C
ANISOU 869 CA SER A 113 4010 3179 3802 23 324 229 C
ATOM 870 C SER A 113 -8.284 39.101 18.747 1.00 32.46 C
ANISOU 870 C SER A 113 4420 3593 4321 54 285 214 C
ATOM 871 O SER A 113 -8.483 40.229 18.282 1.00 32.08 O
ANISOU 871 O SER A 113 4442 3473 4274 74 277 246 O
ATOM 872 CB SER A 113 -8.211 37.095 17.206 1.00 31.51 C
ANISOU 872 CB SER A 113 4360 3533 4081 62 247 237 C
ATOM 873 OG SER A 113 -7.352 36.251 16.444 1.00 36.92 O
ANISOU 873 OG SER A 113 5095 4238 4694 36 292 249 O
ATOM 874 N ILE A 114 -8.805 38.687 19.938 1.00 28.29 N
ANISOU 874 N ILE A 114 3790 3109 3850 60 271 167 N
ATOM 875 CA ILE A 114 -9.652 39.558 20.758 1.00 27.66 C
ANISOU 875 CA ILE A 114 3671 2997 3842 89 253 145 C
ATOM 876 C ILE A 114 -8.807 40.738 21.256 1.00 31.53 C
ANISOU 876 C ILE A 114 4185 3441 4355 54 314 139 C
ATOM 877 O ILE A 114 -9.277 41.873 21.247 1.00 32.50 O
ANISOU 877 O ILE A 114 4337 3498 4514 80 304 149 O
ATOM 878 CB ILE A 114 -10.357 38.794 21.916 1.00 29.82 C
ANISOU 878 CB ILE A 114 3846 3320 4163 99 249 96 C
ATOM 879 CG1 ILE A 114 -11.276 37.659 21.365 1.00 29.15 C
ANISOU 879 CG1 ILE A 114 3731 3269 4075 129 187 99 C
ATOM 880 CG2 ILE A 114 -11.150 39.785 22.811 1.00 29.74 C
ANISOU 880 CG2 ILE A 114 3803 3267 4229 127 254 69 C
ATOM 881 CD1 ILE A 114 -11.759 36.601 22.413 1.00 28.06 C
ANISOU 881 CD1 ILE A 114 3504 3183 3974 123 207 55 C
ATOM 882 N ASP A 115 -7.547 40.466 21.649 1.00 27.73 N
ANISOU 882 N ASP A 115 3687 2989 3861 -3 372 121 N
ATOM 883 CA ASP A 115 -6.618 41.493 22.094 1.00 27.10 C
ANISOU 883 CA ASP A 115 3618 2865 3814 -46 425 107 C
ATOM 884 C ASP A 115 -6.374 42.516 20.996 1.00 31.18 C
ANISOU 884 C ASP A 115 4229 3300 4319 -50 450 158 C
ATOM 885 O ASP A 115 -6.335 43.691 21.307 1.00 30.80 O
ANISOU 885 O ASP A 115 4203 3187 4314 -57 469 153 O
ATOM 886 CB ASP A 115 -5.281 40.904 22.575 1.00 27.79 C
ANISOU 886 CB ASP A 115 3659 2997 3903 -104 467 75 C
ATOM 887 CG ASP A 115 -4.396 41.955 23.232 1.00 32.19 C
ANISOU 887 CG ASP A 115 4207 3509 4515 -151 505 43 C
ATOM 888 OD1 ASP A 115 -4.800 42.500 24.280 1.00 32.38 O
ANISOU 888 OD1 ASP A 115 4212 3520 4571 -142 487 3 O
ATOM 889 OD2 ASP A 115 -3.308 42.246 22.686 1.00 32.25 O
ANISOU 889 OD2 ASP A 115 4227 3486 4538 -200 558 55 O
ATOM 890 N ARG A 116 -6.192 42.076 19.723 1.00 28.91 N
ANISOU 890 N ARG A 116 4009 3008 3967 -46 455 207 N
ATOM 891 CA ARG A 116 -5.932 42.988 18.593 1.00 27.79 C
ANISOU 891 CA ARG A 116 3987 2780 3794 -47 490 265 C
ATOM 892 C ARG A 116 -7.165 43.846 18.348 1.00 33.35 C
ANISOU 892 C ARG A 116 4745 3421 4504 20 419 292 C
ATOM 893 O ARG A 116 -7.022 45.039 18.105 1.00 33.38 O
ANISOU 893 O ARG A 116 4821 3339 4525 17 450 318 O
ATOM 894 CB ARG A 116 -5.509 42.237 17.305 1.00 26.42 C
ANISOU 894 CB ARG A 116 3894 2614 3532 -52 514 309 C
ATOM 895 CG ARG A 116 -4.362 41.200 17.440 1.00 29.05 C
ANISOU 895 CG ARG A 116 4165 3010 3862 -107 581 282 C
ATOM 896 CD ARG A 116 -3.179 41.630 18.324 1.00 30.76 C
ANISOU 896 CD ARG A 116 4302 3223 4164 -174 655 239 C
ATOM 897 NE ARG A 116 -2.486 42.812 17.792 1.00 30.09 N
ANISOU 897 NE ARG A 116 4289 3042 4101 -214 741 269 N
ATOM 898 CZ ARG A 116 -1.541 43.481 18.441 1.00 37.66 C
ANISOU 898 CZ ARG A 116 5189 3971 5149 -275 802 233 C
ATOM 899 NH1 ARG A 116 -1.162 43.101 19.654 1.00 29.05 N
ANISOU 899 NH1 ARG A 116 3975 2940 4122 -297 772 166 N
ATOM 900 NH2 ARG A 116 -0.955 44.524 17.878 1.00 25.09 N
ANISOU 900 NH2 ARG A 116 3668 2284 3583 -314 890 263 N
ATOM 901 N TYR A 117 -8.379 43.269 18.514 1.00 30.54 N
ANISOU 901 N TYR A 117 4343 3105 4155 79 328 278 N
ATOM 902 CA TYR A 117 -9.627 44.028 18.373 1.00 31.02 C
ANISOU 902 CA TYR A 117 4428 3110 4250 151 250 294 C
ATOM 903 C TYR A 117 -9.762 45.100 19.470 1.00 33.99 C
ANISOU 903 C TYR A 117 4758 3443 4712 149 280 259 C
ATOM 904 O TYR A 117 -10.175 46.226 19.175 1.00 31.74 O
ANISOU 904 O TYR A 117 4537 3071 4451 185 264 286 O
ATOM 905 CB TYR A 117 -10.846 43.089 18.393 1.00 32.50 C
ANISOU 905 CB TYR A 117 4546 3350 4453 206 154 275 C
ATOM 906 CG TYR A 117 -12.172 43.812 18.494 1.00 36.15 C
ANISOU 906 CG TYR A 117 4988 3759 4988 282 74 273 C
ATOM 907 CD1 TYR A 117 -12.712 44.476 17.399 1.00 38.97 C
ANISOU 907 CD1 TYR A 117 5449 4039 5318 342 -3 325 C
ATOM 908 CD2 TYR A 117 -12.900 43.808 19.677 1.00 37.93 C
ANISOU 908 CD2 TYR A 117 5096 4005 5310 298 77 217 C
ATOM 909 CE1 TYR A 117 -13.921 45.161 17.494 1.00 41.86 C
ANISOU 909 CE1 TYR A 117 5787 4351 5767 420 -84 321 C
ATOM 910 CE2 TYR A 117 -14.135 44.450 19.769 1.00 39.41 C
ANISOU 910 CE2 TYR A 117 5250 4140 5584 371 13 210 C
ATOM 911 CZ TYR A 117 -14.653 45.101 18.666 1.00 48.43 C
ANISOU 911 CZ TYR A 117 6480 5209 6713 433 -75 261 C
ATOM 912 OH TYR A 117 -15.863 45.740 18.758 1.00 55.11 O
ANISOU 912 OH TYR A 117 7283 5998 7659 512 -147 251 O
ATOM 913 N LEU A 118 -9.500 44.727 20.744 1.00 29.06 N
ANISOU 913 N LEU A 118 4033 2876 4132 113 317 197 N
ATOM 914 CA LEU A 118 -9.629 45.702 21.827 1.00 28.81 C
ANISOU 914 CA LEU A 118 3972 2803 4172 111 346 155 C
ATOM 915 C LEU A 118 -8.598 46.828 21.700 1.00 33.68 C
ANISOU 915 C LEU A 118 4657 3344 4795 61 410 168 C
ATOM 916 O LEU A 118 -8.885 47.969 22.041 1.00 34.44 O
ANISOU 916 O LEU A 118 4779 3365 4943 77 420 160 O
ATOM 917 CB LEU A 118 -9.549 45.025 23.189 1.00 28.57 C
ANISOU 917 CB LEU A 118 3846 2843 4164 87 368 88 C
ATOM 918 CG LEU A 118 -10.749 44.125 23.536 1.00 32.94 C
ANISOU 918 CG LEU A 118 4328 3449 4738 137 325 68 C
ATOM 919 CD1 LEU A 118 -10.434 43.211 24.703 1.00 32.38 C
ANISOU 919 CD1 LEU A 118 4193 3452 4659 104 359 15 C
ATOM 920 CD2 LEU A 118 -12.039 44.953 23.766 1.00 32.35 C
ANISOU 920 CD2 LEU A 118 4237 3312 4741 204 299 59 C
ATOM 921 N LEU A 119 -7.423 46.502 21.186 1.00 30.16 N
ANISOU 921 N LEU A 119 4238 2913 4310 0 460 186 N
ATOM 922 CA LEU A 119 -6.334 47.440 20.994 1.00 30.95 C
ANISOU 922 CA LEU A 119 4389 2940 4429 -60 536 195 C
ATOM 923 C LEU A 119 -6.635 48.427 19.883 1.00 35.82 C
ANISOU 923 C LEU A 119 5134 3453 5025 -29 542 266 C
ATOM 924 O LEU A 119 -6.199 49.567 19.948 1.00 34.08 O
ANISOU 924 O LEU A 119 4960 3143 4846 -59 595 270 O
ATOM 925 CB LEU A 119 -5.035 46.675 20.705 1.00 30.80 C
ANISOU 925 CB LEU A 119 4348 2968 4387 -130 595 193 C
ATOM 926 CG LEU A 119 -3.748 47.516 20.724 1.00 33.97 C
ANISOU 926 CG LEU A 119 4763 3302 4841 -210 686 182 C
ATOM 927 CD1 LEU A 119 -3.450 48.033 22.137 1.00 31.66 C
ANISOU 927 CD1 LEU A 119 4392 3008 4628 -243 679 104 C
ATOM 928 CD2 LEU A 119 -2.578 46.700 20.186 1.00 34.56 C
ANISOU 928 CD2 LEU A 119 4815 3415 4901 -266 750 189 C
ATOM 929 N MET A 120 -7.382 47.992 18.871 1.00 35.67 N
ANISOU 929 N MET A 120 5177 3437 4940 32 483 320 N
ATOM 930 CA MET A 120 -7.817 48.821 17.752 1.00 37.90 C
ANISOU 930 CA MET A 120 5600 3619 5181 80 463 392 C
ATOM 931 C MET A 120 -8.804 49.893 18.280 1.00 40.19 C
ANISOU 931 C MET A 120 5887 3840 5544 141 413 382 C
ATOM 932 O MET A 120 -8.750 51.041 17.857 1.00 40.76 O
ANISOU 932 O MET A 120 6062 3802 5623 152 438 422 O
ATOM 933 CB MET A 120 -8.461 47.890 16.725 1.00 41.72 C
ANISOU 933 CB MET A 120 6134 4141 5578 137 382 434 C
ATOM 934 CG MET A 120 -9.255 48.556 15.653 1.00 47.74 C
ANISOU 934 CG MET A 120 7036 4812 6290 215 309 502 C
ATOM 935 SD MET A 120 -10.262 47.303 14.804 1.00 54.68 S
ANISOU 935 SD MET A 120 7927 5757 7093 289 170 518 S
ATOM 936 CE MET A 120 -9.061 46.584 13.792 1.00 51.68 C
ANISOU 936 CE MET A 120 7656 5393 6588 228 259 556 C
ATOM 937 N LYS A 121 -9.665 49.521 19.236 1.00 34.73 N
ANISOU 937 N LYS A 121 5078 3206 4910 178 357 326 N
ATOM 938 CA LYS A 121 -10.643 50.429 19.817 1.00 34.87 C
ANISOU 938 CA LYS A 121 5076 3164 5009 239 320 305 C
ATOM 939 C LYS A 121 -10.037 51.268 20.957 1.00 37.27 C
ANISOU 939 C LYS A 121 5348 3433 5380 184 400 250 C
ATOM 940 O LYS A 121 -10.407 52.421 21.110 1.00 37.88 O
ANISOU 940 O LYS A 121 5468 3415 5510 215 404 252 O
ATOM 941 CB LYS A 121 -11.835 49.629 20.371 1.00 36.73 C
ANISOU 941 CB LYS A 121 5197 3472 5289 298 246 264 C
ATOM 942 CG LYS A 121 -12.751 49.040 19.307 1.00 45.39 C
ANISOU 942 CG LYS A 121 6315 4578 6351 371 137 308 C
ATOM 943 CD LYS A 121 -13.821 48.150 19.922 1.00 50.85 C
ANISOU 943 CD LYS A 121 6871 5342 7106 411 81 257 C
ATOM 944 CE LYS A 121 -14.925 48.879 20.652 1.00 60.68 C
ANISOU 944 CE LYS A 121 8047 6537 8470 477 62 221 C
ATOM 945 NZ LYS A 121 -15.587 47.971 21.624 1.00 73.67 N
ANISOU 945 NZ LYS A 121 9550 8259 10180 479 73 156 N
ATOM 946 N PHE A 122 -9.164 50.660 21.785 1.00 31.94 N
ANISOU 946 N PHE A 122 4598 2832 4704 109 451 194 N
ATOM 947 CA PHE A 122 -8.575 51.262 22.979 1.00 30.57 C
ANISOU 947 CA PHE A 122 4388 2640 4587 55 506 126 C
ATOM 948 C PHE A 122 -7.060 51.066 22.953 1.00 33.83 C
ANISOU 948 C PHE A 122 4798 3071 4984 -43 569 114 C
ATOM 949 O PHE A 122 -6.523 50.181 23.629 1.00 32.34 O
ANISOU 949 O PHE A 122 4530 2970 4786 -83 571 66 O
ATOM 950 CB PHE A 122 -9.206 50.651 24.245 1.00 31.92 C
ANISOU 950 CB PHE A 122 4460 2885 4783 78 484 54 C
ATOM 951 CG PHE A 122 -10.709 50.546 24.188 1.00 34.12 C
ANISOU 951 CG PHE A 122 4712 3161 5091 172 428 63 C
ATOM 952 CD1 PHE A 122 -11.506 51.686 24.241 1.00 37.14 C
ANISOU 952 CD1 PHE A 122 5127 3447 5538 231 420 66 C
ATOM 953 CD2 PHE A 122 -11.333 49.304 24.095 1.00 37.43 C
ANISOU 953 CD2 PHE A 122 5065 3670 5489 202 385 64 C
ATOM 954 CE1 PHE A 122 -12.891 51.587 24.167 1.00 37.87 C
ANISOU 954 CE1 PHE A 122 5175 3532 5680 321 366 69 C
ATOM 955 CE2 PHE A 122 -12.723 49.205 24.072 1.00 39.60 C
ANISOU 955 CE2 PHE A 122 5294 3937 5816 284 335 63 C
ATOM 956 CZ PHE A 122 -13.489 50.348 24.112 1.00 37.53 C
ANISOU 956 CZ PHE A 122 5053 3579 5626 344 324 65 C
ATOM 957 N PRO A 123 -6.346 51.902 22.161 1.00 32.09 N
ANISOU 957 N PRO A 123 4663 2759 4769 -82 625 158 N
ATOM 958 CA PRO A 123 -4.881 51.715 22.021 1.00 31.18 C
ANISOU 958 CA PRO A 123 4533 2653 4663 -179 698 148 C
ATOM 959 C PRO A 123 -4.075 51.792 23.311 1.00 33.08 C
ANISOU 959 C PRO A 123 4684 2918 4967 -246 712 56 C
ATOM 960 O PRO A 123 -3.025 51.158 23.402 1.00 32.92 O
ANISOU 960 O PRO A 123 4604 2948 4956 -309 738 30 O
ATOM 961 CB PRO A 123 -4.468 52.819 21.031 1.00 33.51 C
ANISOU 961 CB PRO A 123 4947 2819 4966 -202 769 210 C
ATOM 962 CG PRO A 123 -5.736 53.182 20.295 1.00 37.72 C
ANISOU 962 CG PRO A 123 5575 3302 5454 -103 711 277 C
ATOM 963 CD PRO A 123 -6.851 52.988 21.291 1.00 32.61 C
ANISOU 963 CD PRO A 123 4847 2706 4835 -37 628 224 C
ATOM 964 N PHE A 124 -4.592 52.523 24.323 1.00 28.10 N
ANISOU 964 N PHE A 124 4045 2251 4381 -226 688 2 N
ATOM 965 CA PHE A 124 -3.919 52.772 25.602 1.00 26.75 C
ANISOU 965 CA PHE A 124 3816 2085 4262 -282 687 -92 C
ATOM 966 C PHE A 124 -4.151 51.685 26.657 1.00 32.07 C
ANISOU 966 C PHE A 124 4413 2873 4899 -262 631 -150 C
ATOM 967 O PHE A 124 -3.587 51.791 27.746 1.00 31.27 O
ANISOU 967 O PHE A 124 4277 2781 4824 -301 615 -230 O
ATOM 968 CB PHE A 124 -4.268 54.182 26.129 1.00 27.40 C
ANISOU 968 CB PHE A 124 3952 2056 4404 -275 701 -124 C
ATOM 969 CG PHE A 124 -3.642 55.260 25.263 1.00 28.11 C
ANISOU 969 CG PHE A 124 4114 2023 4543 -323 770 -80 C
ATOM 970 CD1 PHE A 124 -4.264 55.688 24.093 1.00 29.47 C
ANISOU 970 CD1 PHE A 124 4381 2128 4687 -271 790 13 C
ATOM 971 CD2 PHE A 124 -2.424 55.833 25.608 1.00 29.96 C
ANISOU 971 CD2 PHE A 124 4326 2203 4853 -421 814 -133 C
ATOM 972 CE1 PHE A 124 -3.669 56.648 23.276 1.00 30.48 C
ANISOU 972 CE1 PHE A 124 4596 2136 4850 -317 867 60 C
ATOM 973 CE2 PHE A 124 -1.837 56.811 24.797 1.00 32.49 C
ANISOU 973 CE2 PHE A 124 4715 2402 5228 -473 896 -91 C
ATOM 974 CZ PHE A 124 -2.470 57.227 23.646 1.00 31.08 C
ANISOU 974 CZ PHE A 124 4646 2154 5009 -420 929 8 C
ATOM 975 N ARG A 125 -4.875 50.585 26.298 1.00 28.71 N
ANISOU 975 N ARG A 125 3966 2532 4412 -206 599 -112 N
ATOM 976 CA ARG A 125 -5.114 49.414 27.163 1.00 27.75 C
ANISOU 976 CA ARG A 125 3781 2515 4248 -187 558 -154 C
ATOM 977 C ARG A 125 -5.655 49.758 28.546 1.00 31.11 C
ANISOU 977 C ARG A 125 4206 2932 4682 -163 543 -226 C
ATOM 978 O ARG A 125 -5.203 49.175 29.531 1.00 30.74 O
ANISOU 978 O ARG A 125 4129 2941 4611 -185 521 -285 O
ATOM 979 CB ARG A 125 -3.855 48.520 27.292 1.00 27.38 C
ANISOU 979 CB ARG A 125 3676 2537 4190 -249 553 -177 C
ATOM 980 CG ARG A 125 -3.252 48.004 25.959 1.00 28.51 C
ANISOU 980 CG ARG A 125 3817 2695 4320 -273 585 -111 C
ATOM 981 CD ARG A 125 -2.083 47.064 26.227 1.00 24.18 C
ANISOU 981 CD ARG A 125 3195 2215 3777 -324 579 -145 C
ATOM 982 NE ARG A 125 -1.752 46.295 25.029 1.00 29.04 N
ANISOU 982 NE ARG A 125 3810 2861 4362 -329 613 -84 N
ATOM 983 CZ ARG A 125 -2.324 45.147 24.680 1.00 30.25 C
ANISOU 983 CZ ARG A 125 3957 3089 4450 -284 587 -53 C
ATOM 984 NH1 ARG A 125 -1.987 44.554 23.551 1.00 25.86 N
ANISOU 984 NH1 ARG A 125 3416 2547 3863 -290 622 -2 N
ATOM 985 NH2 ARG A 125 -3.217 44.564 25.482 1.00 21.61 N
ANISOU 985 NH2 ARG A 125 2843 2049 3320 -235 533 -77 N
ATOM 986 N GLU A 126 -6.628 50.673 28.636 1.00 27.85 N
ANISOU 986 N GLU A 126 3835 2447 4299 -114 556 -224 N
ATOM 987 CA GLU A 126 -7.175 51.022 29.954 1.00 29.12 C
ANISOU 987 CA GLU A 126 4006 2592 4465 -89 560 -297 C
ATOM 988 C GLU A 126 -8.056 49.953 30.549 1.00 33.21 C
ANISOU 988 C GLU A 126 4490 3189 4940 -38 552 -309 C
ATOM 989 O GLU A 126 -8.223 49.935 31.764 1.00 32.42 O
ANISOU 989 O GLU A 126 4404 3094 4819 -32 563 -376 O
ATOM 990 CB GLU A 126 -7.965 52.326 29.938 1.00 30.87 C
ANISOU 990 CB GLU A 126 4279 2705 4744 -47 586 -297 C
ATOM 991 CG GLU A 126 -7.130 53.502 29.496 1.00 44.52 C
ANISOU 991 CG GLU A 126 6056 4336 6522 -100 606 -291 C
ATOM 992 CD GLU A 126 -7.404 53.840 28.049 1.00 56.49 C
ANISOU 992 CD GLU A 126 7605 5804 8053 -75 613 -197 C
ATOM 993 OE1 GLU A 126 -7.443 55.047 27.752 1.00 39.27 O
ANISOU 993 OE1 GLU A 126 5487 3512 5922 -73 639 -183 O
ATOM 994 OE2 GLU A 126 -7.621 52.921 27.226 1.00 54.92 O
ANISOU 994 OE2 GLU A 126 7384 5671 7813 -52 591 -138 O
ATOM 995 N HIS A 127 -8.661 49.102 29.713 1.00 29.16 N
ANISOU 995 N HIS A 127 3939 2728 4412 -1 538 -249 N
ATOM 996 CA HIS A 127 -9.575 48.078 30.218 1.00 28.99 C
ANISOU 996 CA HIS A 127 3877 2772 4367 44 541 -260 C
ATOM 997 C HIS A 127 -8.832 46.957 30.954 1.00 31.60 C
ANISOU 997 C HIS A 127 4190 3186 4629 6 530 -293 C
ATOM 998 O HIS A 127 -7.723 46.587 30.571 1.00 30.05 O
ANISOU 998 O HIS A 127 3984 3024 4411 -45 504 -281 O
ATOM 999 CB HIS A 127 -10.398 47.503 29.052 1.00 30.14 C
ANISOU 999 CB HIS A 127 3985 2940 4526 90 515 -192 C
ATOM 1000 CG HIS A 127 -11.306 48.519 28.445 1.00 33.57 C
ANISOU 1000 CG HIS A 127 4437 3291 5027 146 509 -163 C
ATOM 1001 ND1 HIS A 127 -12.614 48.646 28.853 1.00 35.67 N
ANISOU 1001 ND1 HIS A 127 4669 3533 5351 213 523 -183 N
ATOM 1002 CD2 HIS A 127 -11.048 49.448 27.502 1.00 36.19 C
ANISOU 1002 CD2 HIS A 127 4821 3552 5379 146 494 -117 C
ATOM 1003 CE1 HIS A 127 -13.108 49.662 28.175 1.00 36.21 C
ANISOU 1003 CE1 HIS A 127 4763 3518 5478 256 504 -151 C
ATOM 1004 NE2 HIS A 127 -12.197 50.182 27.351 1.00 36.92 N
ANISOU 1004 NE2 HIS A 127 4915 3574 5539 219 485 -109 N
ATOM 1005 N ILE A 128 -9.467 46.403 31.993 1.00 29.25 N
ANISOU 1005 N ILE A 128 3892 2917 4304 33 555 -333 N
ATOM 1006 CA ILE A 128 -8.971 45.257 32.748 1.00 28.64 C
ANISOU 1006 CA ILE A 128 3814 2913 4154 13 545 -358 C
ATOM 1007 C ILE A 128 -8.631 44.114 31.777 1.00 31.29 C
ANISOU 1007 C ILE A 128 4098 3321 4471 1 512 -302 C
ATOM 1008 O ILE A 128 -7.545 43.553 31.890 1.00 29.20 O
ANISOU 1008 O ILE A 128 3828 3099 4167 -39 480 -310 O
ATOM 1009 CB ILE A 128 -9.972 44.800 33.843 1.00 32.42 C
ANISOU 1009 CB ILE A 128 4312 3400 4607 55 600 -394 C
ATOM 1010 CG1 ILE A 128 -10.149 45.908 34.934 1.00 32.39 C
ANISOU 1010 CG1 ILE A 128 4382 3322 4605 64 640 -461 C
ATOM 1011 CG2 ILE A 128 -9.517 43.442 34.461 1.00 34.07 C
ANISOU 1011 CG2 ILE A 128 4529 3683 4731 40 588 -402 C
ATOM 1012 CD1 ILE A 128 -11.538 45.900 35.657 1.00 40.56 C
ANISOU 1012 CD1 ILE A 128 5426 4325 5659 121 730 -485 C
ATOM 1013 N LEU A 129 -9.527 43.826 30.792 1.00 28.86 N
ANISOU 1013 N LEU A 129 3749 3018 4197 36 513 -249 N
ATOM 1014 CA LEU A 129 -9.350 42.764 29.785 1.00 29.63 C
ANISOU 1014 CA LEU A 129 3809 3176 4274 30 483 -198 C
ATOM 1015 C LEU A 129 -8.057 42.933 28.955 1.00 30.23 C
ANISOU 1015 C LEU A 129 3895 3255 4338 -19 458 -172 C
ATOM 1016 O LEU A 129 -7.660 41.996 28.290 1.00 26.88 O
ANISOU 1016 O LEU A 129 3448 2881 3885 -32 442 -141 O
ATOM 1017 CB LEU A 129 -10.557 42.741 28.793 1.00 30.84 C
ANISOU 1017 CB LEU A 129 3930 3312 4474 79 470 -153 C
ATOM 1018 CG LEU A 129 -11.917 42.160 29.242 1.00 37.35 C
ANISOU 1018 CG LEU A 129 4708 4147 5336 126 494 -168 C
ATOM 1019 CD1 LEU A 129 -12.956 42.354 28.151 1.00 37.61 C
ANISOU 1019 CD1 LEU A 129 4704 4150 5434 174 454 -130 C
ATOM 1020 CD2 LEU A 129 -11.851 40.693 29.438 1.00 42.76 C
ANISOU 1020 CD2 LEU A 129 5365 4905 5977 113 497 -167 C
ATOM 1021 N GLN A 130 -7.441 44.142 28.954 1.00 26.84 N
ANISOU 1021 N GLN A 130 3497 2761 3938 -47 465 -185 N
ATOM 1022 CA GLN A 130 -6.241 44.473 28.154 1.00 24.90 C
ANISOU 1022 CA GLN A 130 3259 2499 3703 -100 465 -163 C
ATOM 1023 C GLN A 130 -4.975 44.443 29.001 1.00 28.59 C
ANISOU 1023 C GLN A 130 3712 2981 4171 -154 454 -218 C
ATOM 1024 O GLN A 130 -3.887 44.684 28.482 1.00 27.29 O
ANISOU 1024 O GLN A 130 3534 2800 4035 -205 462 -212 O
ATOM 1025 CB GLN A 130 -6.408 45.865 27.523 1.00 25.37 C
ANISOU 1025 CB GLN A 130 3365 2465 3811 -98 484 -138 C
ATOM 1026 CG GLN A 130 -7.593 45.985 26.558 1.00 28.90 C
ANISOU 1026 CG GLN A 130 3832 2886 4261 -37 473 -80 C
ATOM 1027 CD GLN A 130 -7.659 47.380 25.997 1.00 31.99 C
ANISOU 1027 CD GLN A 130 4284 3175 4694 -32 489 -54 C
ATOM 1028 OE1 GLN A 130 -8.188 48.285 26.625 1.00 27.95 O
ANISOU 1028 OE1 GLN A 130 3789 2605 4224 -8 498 -84 O
ATOM 1029 NE2 GLN A 130 -7.097 47.602 24.806 1.00 28.71 N
ANISOU 1029 NE2 GLN A 130 3915 2728 4265 -54 501 3 N
ATOM 1030 N LYS A 131 -5.109 44.163 30.308 1.00 26.06 N
ANISOU 1030 N LYS A 131 3397 2684 3821 -144 437 -275 N
ATOM 1031 CA LYS A 131 -3.938 44.123 31.190 1.00 26.17 C
ANISOU 1031 CA LYS A 131 3405 2709 3831 -187 401 -336 C
ATOM 1032 C LYS A 131 -3.115 42.860 31.052 1.00 31.47 C
ANISOU 1032 C LYS A 131 4027 3453 4476 -202 370 -327 C
ATOM 1033 O LYS A 131 -3.678 41.793 30.830 1.00 29.94 O
ANISOU 1033 O LYS A 131 3823 3314 4239 -169 375 -294 O
ATOM 1034 CB LYS A 131 -4.327 44.357 32.664 1.00 26.06 C
ANISOU 1034 CB LYS A 131 3442 2681 3778 -166 387 -402 C
ATOM 1035 CG LYS A 131 -5.073 45.661 32.890 1.00 33.08 C
ANISOU 1035 CG LYS A 131 4380 3489 4702 -150 424 -421 C
ATOM 1036 CD LYS A 131 -4.343 46.940 32.391 1.00 36.12 C
ANISOU 1036 CD LYS A 131 4767 3797 5162 -198 426 -429 C
ATOM 1037 CE LYS A 131 -5.163 48.160 32.803 1.00 39.70 C
ANISOU 1037 CE LYS A 131 5278 4164 5640 -172 460 -454 C
ATOM 1038 NZ LYS A 131 -4.638 49.432 32.247 1.00 41.88 N
ANISOU 1038 NZ LYS A 131 5567 4352 5992 -214 475 -453 N
ATOM 1039 N LYS A 132 -1.775 42.986 31.206 1.00 30.26 N
ANISOU 1039 N LYS A 132 3839 3295 4362 -253 336 -363 N
ATOM 1040 CA LYS A 132 -0.831 41.873 31.168 1.00 30.71 C
ANISOU 1040 CA LYS A 132 3840 3413 4414 -267 300 -367 C
ATOM 1041 C LYS A 132 -1.234 40.786 32.174 1.00 34.73 C
ANISOU 1041 C LYS A 132 4377 3980 4838 -222 259 -385 C
ATOM 1042 O LYS A 132 -1.274 39.611 31.801 1.00 34.72 O
ANISOU 1042 O LYS A 132 4352 4035 4806 -202 261 -349 O
ATOM 1043 CB LYS A 132 0.586 42.356 31.476 1.00 32.95 C
ANISOU 1043 CB LYS A 132 4076 3670 4774 -324 258 -424 C
ATOM 1044 CG LYS A 132 1.654 41.263 31.305 1.00 45.01 C
ANISOU 1044 CG LYS A 132 5527 5251 6324 -335 222 -428 C
ATOM 1045 CD LYS A 132 2.495 41.083 32.558 1.00 51.19 C
ANISOU 1045 CD LYS A 132 6294 6043 7113 -340 117 -506 C
ATOM 1046 CE LYS A 132 3.753 41.902 32.539 1.00 61.42 C
ANISOU 1046 CE LYS A 132 7517 7288 8533 -405 89 -562 C
ATOM 1047 NZ LYS A 132 4.455 41.851 33.845 1.00 70.44 N
ANISOU 1047 NZ LYS A 132 8656 8430 9676 -404 -38 -648 N
ATOM 1048 N GLU A 133 -1.560 41.185 33.427 1.00 30.00 N
ANISOU 1048 N GLU A 133 3842 3359 4197 -205 231 -438 N
ATOM 1049 CA GLU A 133 -1.963 40.271 34.512 1.00 30.34 C
ANISOU 1049 CA GLU A 133 3941 3440 4147 -162 204 -457 C
ATOM 1050 C GLU A 133 -3.243 39.490 34.184 1.00 33.08 C
ANISOU 1050 C GLU A 133 4301 3816 4450 -119 270 -402 C
ATOM 1051 O GLU A 133 -3.372 38.337 34.570 1.00 32.23 O
ANISOU 1051 O GLU A 133 4210 3754 4283 -93 261 -392 O
ATOM 1052 CB GLU A 133 -2.105 41.014 35.853 1.00 31.45 C
ANISOU 1052 CB GLU A 133 4171 3536 4243 -154 177 -526 C
ATOM 1053 CG GLU A 133 -0.813 41.673 36.323 1.00 42.59 C
ANISOU 1053 CG GLU A 133 5569 4916 5696 -197 88 -595 C
ATOM 1054 CD GLU A 133 -0.444 43.019 35.710 1.00 72.59 C
ANISOU 1054 CD GLU A 133 9328 8653 9601 -248 108 -609 C
ATOM 1055 OE1 GLU A 133 0.695 43.481 35.954 1.00 76.40 O
ANISOU 1055 OE1 GLU A 133 9775 9109 10144 -293 38 -665 O
ATOM 1056 OE2 GLU A 133 -1.279 43.607 34.981 1.00 56.40 O
ANISOU 1056 OE2 GLU A 133 7280 6571 7577 -243 189 -565 O
ATOM 1057 N PHE A 134 -4.172 40.112 33.458 1.00 28.64 N
ANISOU 1057 N PHE A 134 3731 3225 3926 -111 330 -369 N
ATOM 1058 CA PHE A 134 -5.395 39.450 33.027 1.00 26.45 C
ANISOU 1058 CA PHE A 134 3445 2968 3635 -73 381 -323 C
ATOM 1059 C PHE A 134 -5.066 38.399 31.943 1.00 29.64 C
ANISOU 1059 C PHE A 134 3793 3425 4046 -80 371 -271 C
ATOM 1060 O PHE A 134 -5.647 37.324 31.957 1.00 28.36 O
ANISOU 1060 O PHE A 134 3626 3300 3850 -55 386 -250 O
ATOM 1061 CB PHE A 134 -6.386 40.496 32.501 1.00 27.11 C
ANISOU 1061 CB PHE A 134 3529 2999 3774 -58 426 -306 C
ATOM 1062 CG PHE A 134 -7.780 39.946 32.375 1.00 27.58 C
ANISOU 1062 CG PHE A 134 3576 3068 3836 -14 471 -280 C
ATOM 1063 CD1 PHE A 134 -8.623 39.886 33.483 1.00 29.44 C
ANISOU 1063 CD1 PHE A 134 3852 3286 4047 15 519 -313 C
ATOM 1064 CD2 PHE A 134 -8.238 39.437 31.160 1.00 28.98 C
ANISOU 1064 CD2 PHE A 134 3703 3266 4041 -4 469 -226 C
ATOM 1065 CE1 PHE A 134 -9.916 39.363 33.375 1.00 30.29 C
ANISOU 1065 CE1 PHE A 134 3931 3397 4182 50 572 -295 C
ATOM 1066 CE2 PHE A 134 -9.520 38.888 31.056 1.00 31.59 C
ANISOU 1066 CE2 PHE A 134 4007 3603 4392 33 500 -211 C
ATOM 1067 CZ PHE A 134 -10.350 38.857 32.162 1.00 29.90 C
ANISOU 1067 CZ PHE A 134 3815 3371 4177 57 555 -246 C
ATOM 1068 N ALA A 135 -4.098 38.700 31.026 1.00 26.84 N
ANISOU 1068 N ALA A 135 3398 3067 3734 -116 354 -255 N
ATOM 1069 CA ALA A 135 -3.669 37.766 29.984 1.00 26.19 C
ANISOU 1069 CA ALA A 135 3272 3026 3654 -124 355 -213 C
ATOM 1070 C ALA A 135 -3.013 36.551 30.612 1.00 31.01 C
ANISOU 1070 C ALA A 135 3870 3686 4224 -118 319 -230 C
ATOM 1071 O ALA A 135 -3.183 35.453 30.096 1.00 30.11 O
ANISOU 1071 O ALA A 135 3739 3612 4089 -104 328 -197 O
ATOM 1072 CB ALA A 135 -2.700 38.432 29.033 1.00 26.42 C
ANISOU 1072 CB ALA A 135 3272 3026 3738 -166 365 -200 C
ATOM 1073 N ILE A 136 -2.296 36.738 31.746 1.00 29.29 N
ANISOU 1073 N ILE A 136 3669 3463 3995 -126 272 -283 N
ATOM 1074 CA ILE A 136 -1.691 35.623 32.474 1.00 29.99 C
ANISOU 1074 CA ILE A 136 3763 3593 4040 -109 222 -300 C
ATOM 1075 C ILE A 136 -2.820 34.733 33.034 1.00 32.52 C
ANISOU 1075 C ILE A 136 4139 3932 4284 -67 252 -283 C
ATOM 1076 O ILE A 136 -2.749 33.516 32.892 1.00 31.46 O
ANISOU 1076 O ILE A 136 3996 3835 4123 -50 248 -259 O
ATOM 1077 CB ILE A 136 -0.696 36.111 33.555 1.00 33.43 C
ANISOU 1077 CB ILE A 136 4214 4010 4479 -122 144 -366 C
ATOM 1078 CG1 ILE A 136 0.553 36.747 32.873 1.00 33.66 C
ANISOU 1078 CG1 ILE A 136 4159 4020 4610 -172 122 -383 C
ATOM 1079 CG2 ILE A 136 -0.279 34.935 34.498 1.00 33.44 C
ANISOU 1079 CG2 ILE A 136 4249 4044 4411 -87 79 -382 C
ATOM 1080 CD1 ILE A 136 1.375 37.677 33.794 1.00 38.91 C
ANISOU 1080 CD1 ILE A 136 4828 4646 5309 -197 47 -457 C
ATOM 1081 N LEU A 137 -3.871 35.356 33.621 1.00 28.65 N
ANISOU 1081 N LEU A 137 3703 3410 3772 -51 292 -295 N
ATOM 1082 CA LEU A 137 -5.043 34.653 34.153 1.00 28.64 C
ANISOU 1082 CA LEU A 137 3748 3413 3720 -17 346 -282 C
ATOM 1083 C LEU A 137 -5.738 33.852 33.038 1.00 30.90 C
ANISOU 1083 C LEU A 137 3980 3725 4037 -12 384 -230 C
ATOM 1084 O LEU A 137 -6.019 32.676 33.230 1.00 29.70 O
ANISOU 1084 O LEU A 137 3839 3596 3848 4 400 -213 O
ATOM 1085 CB LEU A 137 -6.025 35.645 34.808 1.00 29.03 C
ANISOU 1085 CB LEU A 137 3848 3413 3769 -5 398 -308 C
ATOM 1086 CG LEU A 137 -7.415 35.096 35.192 1.00 35.29 C
ANISOU 1086 CG LEU A 137 4667 4196 4545 26 483 -295 C
ATOM 1087 CD1 LEU A 137 -7.307 34.022 36.303 1.00 36.97 C
ANISOU 1087 CD1 LEU A 137 4962 4421 4663 45 492 -304 C
ATOM 1088 CD2 LEU A 137 -8.351 36.225 35.673 1.00 36.30 C
ANISOU 1088 CD2 LEU A 137 4824 4268 4699 39 544 -324 C
ATOM 1089 N ILE A 138 -5.985 34.485 31.876 1.00 27.35 N
ANISOU 1089 N ILE A 138 3480 3264 3649 -25 394 -205 N
ATOM 1090 CA ILE A 138 -6.597 33.832 30.706 1.00 27.32 C
ANISOU 1090 CA ILE A 138 3432 3279 3670 -20 410 -161 C
ATOM 1091 C ILE A 138 -5.734 32.653 30.186 1.00 31.47 C
ANISOU 1091 C ILE A 138 3935 3848 4174 -28 385 -141 C
ATOM 1092 O ILE A 138 -6.287 31.615 29.809 1.00 31.23 O
ANISOU 1092 O ILE A 138 3893 3838 4134 -17 399 -119 O
ATOM 1093 CB ILE A 138 -6.888 34.885 29.586 1.00 29.24 C
ANISOU 1093 CB ILE A 138 3651 3491 3967 -27 410 -139 C
ATOM 1094 CG1 ILE A 138 -8.047 35.842 30.022 1.00 28.03 C
ANISOU 1094 CG1 ILE A 138 3511 3291 3849 -4 441 -154 C
ATOM 1095 CG2 ILE A 138 -7.161 34.211 28.210 1.00 27.61 C
ANISOU 1095 CG2 ILE A 138 3416 3303 3770 -24 402 -96 C
ATOM 1096 CD1 ILE A 138 -9.423 35.128 30.278 1.00 34.42 C
ANISOU 1096 CD1 ILE A 138 4302 4102 4673 26 479 -152 C
ATOM 1097 N SER A 139 -4.393 32.817 30.179 1.00 25.75 N
ANISOU 1097 N SER A 139 3199 3133 3453 -49 349 -155 N
ATOM 1098 CA SER A 139 -3.476 31.759 29.719 1.00 24.86 C
ANISOU 1098 CA SER A 139 3057 3055 3334 -54 329 -142 C
ATOM 1099 C SER A 139 -3.589 30.557 30.628 1.00 29.87 C
ANISOU 1099 C SER A 139 3723 3713 3916 -27 319 -148 C
ATOM 1100 O SER A 139 -3.714 29.421 30.147 1.00 29.06 O
ANISOU 1100 O SER A 139 3609 3633 3801 -17 330 -123 O
ATOM 1101 CB SER A 139 -2.039 32.265 29.659 1.00 25.73 C
ANISOU 1101 CB SER A 139 3133 3161 3484 -81 297 -165 C
ATOM 1102 OG SER A 139 -1.924 33.327 28.726 1.00 32.61 O
ANISOU 1102 OG SER A 139 3986 4002 4404 -109 324 -153 O
ATOM 1103 N LEU A 140 -3.611 30.805 31.936 1.00 27.80 N
ANISOU 1103 N LEU A 140 3512 3436 3614 -14 302 -179 N
ATOM 1104 CA LEU A 140 -3.794 29.746 32.923 1.00 29.72 C
ANISOU 1104 CA LEU A 140 3815 3687 3791 16 300 -181 C
ATOM 1105 C LEU A 140 -5.197 29.083 32.701 1.00 31.97 C
ANISOU 1105 C LEU A 140 4109 3968 4069 26 373 -152 C
ATOM 1106 O LEU A 140 -5.280 27.863 32.704 1.00 32.21 O
ANISOU 1106 O LEU A 140 4151 4013 4075 39 384 -133 O
ATOM 1107 CB LEU A 140 -3.635 30.325 34.358 1.00 30.67 C
ANISOU 1107 CB LEU A 140 4015 3783 3857 29 271 -223 C
ATOM 1108 CG LEU A 140 -3.922 29.390 35.543 1.00 38.68 C
ANISOU 1108 CG LEU A 140 5129 4789 4779 64 280 -224 C
ATOM 1109 CD1 LEU A 140 -3.018 28.136 35.533 1.00 38.11 C
ANISOU 1109 CD1 LEU A 140 5055 4743 4683 85 223 -208 C
ATOM 1110 CD2 LEU A 140 -3.818 30.153 36.878 1.00 44.32 C
ANISOU 1110 CD2 LEU A 140 5943 5470 5428 78 253 -269 C
ATOM 1111 N ALA A 141 -6.261 29.881 32.439 1.00 26.41 N
ANISOU 1111 N ALA A 141 3391 3241 3403 20 419 -152 N
ATOM 1112 CA ALA A 141 -7.609 29.358 32.158 1.00 25.32 C
ANISOU 1112 CA ALA A 141 3236 3093 3290 27 480 -133 C
ATOM 1113 C ALA A 141 -7.604 28.463 30.902 1.00 29.82 C
ANISOU 1113 C ALA A 141 3753 3689 3888 19 466 -102 C
ATOM 1114 O ALA A 141 -8.256 27.412 30.910 1.00 30.09 O
ANISOU 1114 O ALA A 141 3788 3724 3922 23 499 -91 O
ATOM 1115 CB ALA A 141 -8.602 30.489 31.991 1.00 24.87 C
ANISOU 1115 CB ALA A 141 3156 3004 3289 27 513 -142 C
ATOM 1116 N VAL A 142 -6.861 28.867 29.844 1.00 24.86 N
ANISOU 1116 N VAL A 142 3089 3075 3281 4 425 -91 N
ATOM 1117 CA VAL A 142 -6.695 28.099 28.606 1.00 24.60 C
ANISOU 1117 CA VAL A 142 3025 3063 3259 -3 412 -66 C
ATOM 1118 C VAL A 142 -6.070 26.718 28.925 1.00 28.76 C
ANISOU 1118 C VAL A 142 3567 3612 3748 6 408 -62 C
ATOM 1119 O VAL A 142 -6.607 25.695 28.481 1.00 28.53 O
ANISOU 1119 O VAL A 142 3532 3586 3721 8 424 -49 O
ATOM 1120 CB VAL A 142 -5.861 28.855 27.527 1.00 27.32 C
ANISOU 1120 CB VAL A 142 3350 3409 3621 -20 388 -56 C
ATOM 1121 CG1 VAL A 142 -5.399 27.901 26.412 1.00 26.54 C
ANISOU 1121 CG1 VAL A 142 3241 3330 3513 -24 384 -36 C
ATOM 1122 CG2 VAL A 142 -6.659 30.012 26.942 1.00 26.56 C
ANISOU 1122 CG2 VAL A 142 3249 3283 3560 -21 389 -49 C
ATOM 1123 N TRP A 143 -4.950 26.694 29.682 1.00 24.28 N
ANISOU 1123 N TRP A 143 3019 3054 3153 12 380 -77 N
ATOM 1124 CA TRP A 143 -4.312 25.432 30.062 1.00 25.41 C
ANISOU 1124 CA TRP A 143 3181 3210 3262 30 366 -72 C
ATOM 1125 C TRP A 143 -5.238 24.528 30.886 1.00 28.79 C
ANISOU 1125 C TRP A 143 3663 3623 3654 46 406 -65 C
ATOM 1126 O TRP A 143 -5.262 23.316 30.671 1.00 27.87 O
ANISOU 1126 O TRP A 143 3553 3509 3526 55 417 -49 O
ATOM 1127 CB TRP A 143 -2.982 25.675 30.789 1.00 25.24 C
ANISOU 1127 CB TRP A 143 3166 3195 3228 41 309 -95 C
ATOM 1128 CG TRP A 143 -1.876 26.075 29.850 1.00 27.51 C
ANISOU 1128 CG TRP A 143 3387 3495 3570 22 286 -100 C
ATOM 1129 CD1 TRP A 143 -1.333 27.319 29.694 1.00 30.06 C
ANISOU 1129 CD1 TRP A 143 3678 3808 3934 -2 271 -119 C
ATOM 1130 CD2 TRP A 143 -1.209 25.223 28.902 1.00 28.01 C
ANISOU 1130 CD2 TRP A 143 3412 3574 3658 24 293 -86 C
ATOM 1131 NE1 TRP A 143 -0.365 27.295 28.713 1.00 28.85 N
ANISOU 1131 NE1 TRP A 143 3466 3662 3833 -18 277 -116 N
ATOM 1132 CE2 TRP A 143 -0.252 26.018 28.227 1.00 31.36 C
ANISOU 1132 CE2 TRP A 143 3779 3996 4139 -1 291 -98 C
ATOM 1133 CE3 TRP A 143 -1.289 23.853 28.597 1.00 29.79 C
ANISOU 1133 CE3 TRP A 143 3648 3807 3865 43 308 -68 C
ATOM 1134 CZ2 TRP A 143 0.592 25.496 27.244 1.00 31.29 C
ANISOU 1134 CZ2 TRP A 143 3726 3993 4168 -5 314 -91 C
ATOM 1135 CZ3 TRP A 143 -0.483 23.347 27.584 1.00 31.73 C
ANISOU 1135 CZ3 TRP A 143 3850 4061 4144 40 321 -63 C
ATOM 1136 CH2 TRP A 143 0.450 24.160 26.928 1.00 32.35 C
ANISOU 1136 CH2 TRP A 143 3875 4138 4277 18 329 -75 C
ATOM 1137 N VAL A 144 -6.019 25.115 31.802 1.00 25.18 N
ANISOU 1137 N VAL A 144 3245 3141 3180 49 439 -77 N
ATOM 1138 CA VAL A 144 -6.921 24.342 32.652 1.00 25.36 C
ANISOU 1138 CA VAL A 144 3326 3138 3171 61 501 -71 C
ATOM 1139 C VAL A 144 -8.093 23.784 31.799 1.00 31.07 C
ANISOU 1139 C VAL A 144 3997 3852 3955 43 552 -57 C
ATOM 1140 O VAL A 144 -8.394 22.596 31.885 1.00 30.39 O
ANISOU 1140 O VAL A 144 3930 3754 3861 44 585 -44 O
ATOM 1141 CB VAL A 144 -7.427 25.191 33.855 1.00 28.94 C
ANISOU 1141 CB VAL A 144 3843 3561 3592 69 539 -93 C
ATOM 1142 CG1 VAL A 144 -8.638 24.522 34.529 1.00 28.97 C
ANISOU 1142 CG1 VAL A 144 3895 3526 3588 71 640 -86 C
ATOM 1143 CG2 VAL A 144 -6.300 25.445 34.863 1.00 28.37 C
ANISOU 1143 CG2 VAL A 144 3846 3489 3444 91 476 -111 C
ATOM 1144 N LEU A 145 -8.743 24.648 30.999 1.00 27.06 N
ANISOU 1144 N LEU A 145 3426 3344 3511 28 550 -63 N
ATOM 1145 CA LEU A 145 -9.859 24.262 30.158 1.00 27.83 C
ANISOU 1145 CA LEU A 145 3467 3431 3678 14 572 -59 C
ATOM 1146 C LEU A 145 -9.468 23.091 29.227 1.00 29.24 C
ANISOU 1146 C LEU A 145 3631 3626 3851 8 543 -44 C
ATOM 1147 O LEU A 145 -10.216 22.122 29.119 1.00 27.34 O
ANISOU 1147 O LEU A 145 3380 3369 3640 -1 576 -43 O
ATOM 1148 CB LEU A 145 -10.351 25.491 29.327 1.00 28.75 C
ANISOU 1148 CB LEU A 145 3527 3544 3852 10 542 -65 C
ATOM 1149 CG LEU A 145 -11.288 25.195 28.109 1.00 35.22 C
ANISOU 1149 CG LEU A 145 4285 4357 4742 2 518 -63 C
ATOM 1150 CD1 LEU A 145 -12.681 24.718 28.591 1.00 34.96 C
ANISOU 1150 CD1 LEU A 145 4214 4288 4782 -3 579 -79 C
ATOM 1151 CD2 LEU A 145 -11.479 26.441 27.218 1.00 35.56 C
ANISOU 1151 CD2 LEU A 145 4298 4394 4818 9 466 -61 C
ATOM 1152 N VAL A 146 -8.302 23.214 28.553 1.00 24.60 N
ANISOU 1152 N VAL A 146 3043 3069 3236 10 490 -36 N
ATOM 1153 CA VAL A 146 -7.831 22.234 27.584 1.00 24.93 C
ANISOU 1153 CA VAL A 146 3076 3124 3270 7 468 -26 C
ATOM 1154 C VAL A 146 -7.455 20.952 28.286 1.00 27.73 C
ANISOU 1154 C VAL A 146 3473 3473 3591 19 490 -19 C
ATOM 1155 O VAL A 146 -7.850 19.894 27.799 1.00 26.41 O
ANISOU 1155 O VAL A 146 3303 3295 3438 12 504 -15 O
ATOM 1156 CB VAL A 146 -6.727 22.773 26.652 1.00 28.26 C
ANISOU 1156 CB VAL A 146 3487 3569 3682 5 428 -21 C
ATOM 1157 CG1 VAL A 146 -6.175 21.663 25.743 1.00 27.52 C
ANISOU 1157 CG1 VAL A 146 3398 3485 3576 6 423 -14 C
ATOM 1158 CG2 VAL A 146 -7.262 23.937 25.827 1.00 27.76 C
ANISOU 1158 CG2 VAL A 146 3401 3499 3647 -5 410 -20 C
ATOM 1159 N THR A 147 -6.813 21.048 29.478 1.00 23.31 N
ANISOU 1159 N THR A 147 2959 2912 2985 39 491 -19 N
ATOM 1160 CA THR A 147 -6.499 19.863 30.274 1.00 24.58 C
ANISOU 1160 CA THR A 147 3179 3057 3102 60 506 -8 C
ATOM 1161 C THR A 147 -7.817 19.105 30.558 1.00 30.06 C
ANISOU 1161 C THR A 147 3892 3714 3817 46 580 -3 C
ATOM 1162 O THR A 147 -7.862 17.876 30.413 1.00 30.13 O
ANISOU 1162 O THR A 147 3920 3705 3824 47 600 9 O
ATOM 1163 CB THR A 147 -5.727 20.245 31.560 1.00 31.05 C
ANISOU 1163 CB THR A 147 4061 3875 3862 89 480 -13 C
ATOM 1164 OG1 THR A 147 -4.463 20.770 31.146 1.00 27.76 O
ANISOU 1164 OG1 THR A 147 3604 3488 3454 97 410 -23 O
ATOM 1165 CG2 THR A 147 -5.471 19.056 32.479 1.00 32.41 C
ANISOU 1165 CG2 THR A 147 4319 4020 3975 120 490 4 C
ATOM 1166 N LEU A 148 -8.891 19.846 30.885 1.00 25.30 N
ANISOU 1166 N LEU A 148 3272 3092 3248 30 625 -14 N
ATOM 1167 CA LEU A 148 -10.194 19.246 31.168 1.00 26.32 C
ANISOU 1167 CA LEU A 148 3398 3178 3424 10 707 -16 C
ATOM 1168 C LEU A 148 -10.851 18.662 29.918 1.00 28.31 C
ANISOU 1168 C LEU A 148 3576 3428 3754 -17 694 -24 C
ATOM 1169 O LEU A 148 -11.441 17.595 30.008 1.00 26.28 O
ANISOU 1169 O LEU A 148 3324 3134 3525 -33 745 -22 O
ATOM 1170 CB LEU A 148 -11.145 20.228 31.873 1.00 26.99 C
ANISOU 1170 CB LEU A 148 3476 3240 3541 4 767 -32 C
ATOM 1171 CG LEU A 148 -10.743 20.715 33.276 1.00 31.61 C
ANISOU 1171 CG LEU A 148 4159 3810 4041 29 798 -32 C
ATOM 1172 CD1 LEU A 148 -11.625 21.863 33.717 1.00 30.82 C
ANISOU 1172 CD1 LEU A 148 4039 3690 3982 24 851 -54 C
ATOM 1173 CD2 LEU A 148 -10.761 19.590 34.304 1.00 32.51 C
ANISOU 1173 CD2 LEU A 148 4380 3883 4091 40 868 -12 C
ATOM 1174 N GLU A 149 -10.695 19.307 28.753 1.00 24.35 N
ANISOU 1174 N GLU A 149 3016 2957 3279 -21 623 -32 N
ATOM 1175 CA GLU A 149 -11.277 18.782 27.507 1.00 25.44 C
ANISOU 1175 CA GLU A 149 3101 3090 3474 -41 591 -44 C
ATOM 1176 C GLU A 149 -10.680 17.423 27.113 1.00 29.34 C
ANISOU 1176 C GLU A 149 3630 3582 3937 -42 585 -36 C
ATOM 1177 O GLU A 149 -11.343 16.624 26.470 1.00 27.77 O
ANISOU 1177 O GLU A 149 3406 3359 3785 -63 584 -50 O
ATOM 1178 CB GLU A 149 -11.019 19.747 26.333 1.00 26.39 C
ANISOU 1178 CB GLU A 149 3190 3240 3596 -37 513 -47 C
ATOM 1179 CG GLU A 149 -11.879 20.994 26.344 1.00 31.53 C
ANISOU 1179 CG GLU A 149 3794 3883 4303 -37 504 -59 C
ATOM 1180 CD GLU A 149 -11.473 22.063 25.346 1.00 34.62 C
ANISOU 1180 CD GLU A 149 4180 4296 4678 -27 434 -53 C
ATOM 1181 OE1 GLU A 149 -10.394 21.948 24.718 1.00 35.16 O
ANISOU 1181 OE1 GLU A 149 4284 4388 4687 -23 406 -40 O
ATOM 1182 OE2 GLU A 149 -12.239 23.037 25.207 1.00 34.23 O
ANISOU 1182 OE2 GLU A 149 4093 4232 4679 -21 415 -61 O
ATOM 1183 N VAL A 150 -9.420 17.210 27.485 1.00 26.73 N
ANISOU 1183 N VAL A 150 3352 3271 3534 -16 576 -18 N
ATOM 1184 CA VAL A 150 -8.551 16.081 27.153 1.00 27.85 C
ANISOU 1184 CA VAL A 150 3528 3413 3641 -3 565 -9 C
ATOM 1185 C VAL A 150 -8.657 14.926 28.196 1.00 34.19 C
ANISOU 1185 C VAL A 150 4391 4174 4424 5 624 6 C
ATOM 1186 O VAL A 150 -8.401 13.769 27.861 1.00 32.73 O
ANISOU 1186 O VAL A 150 4230 3970 4237 8 629 10 O
ATOM 1187 CB VAL A 150 -7.129 16.703 27.055 1.00 32.08 C
ANISOU 1187 CB VAL A 150 4070 3988 4131 24 520 -1 C
ATOM 1188 CG1 VAL A 150 -6.010 15.701 27.278 1.00 33.71 C
ANISOU 1188 CG1 VAL A 150 4315 4193 4302 55 515 10 C
ATOM 1189 CG2 VAL A 150 -6.951 17.470 25.746 1.00 31.15 C
ANISOU 1189 CG2 VAL A 150 3912 3896 4027 12 480 -11 C
ATOM 1190 N LEU A 151 -9.043 15.258 29.444 1.00 33.03 N
ANISOU 1190 N LEU A 151 4281 4007 4260 10 673 15 N
ATOM 1191 CA LEU A 151 -9.190 14.321 30.554 1.00 34.14 C
ANISOU 1191 CA LEU A 151 4505 4099 4368 21 740 35 C
ATOM 1192 C LEU A 151 -10.138 13.105 30.276 1.00 34.42 C
ANISOU 1192 C LEU A 151 4535 4080 4462 -13 804 31 C
ATOM 1193 O LEU A 151 -9.774 12.006 30.683 1.00 32.46 O
ANISOU 1193 O LEU A 151 4359 3795 4178 2 831 52 O
ATOM 1194 CB LEU A 151 -9.611 15.077 31.812 1.00 35.62 C
ANISOU 1194 CB LEU A 151 4740 4270 4524 27 792 39 C
ATOM 1195 CG LEU A 151 -8.699 14.927 33.027 1.00 42.78 C
ANISOU 1195 CG LEU A 151 5763 5166 5325 73 782 62 C
ATOM 1196 CD1 LEU A 151 -7.296 15.504 32.749 1.00 43.04 C
ANISOU 1196 CD1 LEU A 151 5778 5254 5322 107 670 57 C
ATOM 1197 CD2 LEU A 151 -9.311 15.643 34.252 1.00 44.52 C
ANISOU 1197 CD2 LEU A 151 6050 5358 5509 75 851 61 C
ATOM 1198 N PRO A 152 -11.295 13.207 29.569 1.00 29.77 N
ANISOU 1198 N PRO A 152 3863 3478 3970 -58 821 4 N
ATOM 1199 CA PRO A 152 -12.063 11.977 29.282 1.00 28.68 C
ANISOU 1199 CA PRO A 152 3716 3284 3899 -93 871 -6 C
ATOM 1200 C PRO A 152 -11.271 10.992 28.423 1.00 31.16 C
ANISOU 1200 C PRO A 152 4050 3601 4186 -82 818 -6 C
ATOM 1201 O PRO A 152 -11.433 9.783 28.595 1.00 28.73 O
ANISOU 1201 O PRO A 152 3785 3239 3891 -94 868 1 O
ATOM 1202 CB PRO A 152 -13.324 12.488 28.567 1.00 29.75 C
ANISOU 1202 CB PRO A 152 3739 3414 4151 -136 862 -46 C
ATOM 1203 CG PRO A 152 -13.422 13.927 28.977 1.00 33.61 C
ANISOU 1203 CG PRO A 152 4203 3937 4630 -120 853 -46 C
ATOM 1204 CD PRO A 152 -12.000 14.393 29.038 1.00 29.46 C
ANISOU 1204 CD PRO A 152 3735 3465 3994 -76 790 -22 C
ATOM 1205 N MET A 153 -10.417 11.494 27.503 1.00 28.67 N
ANISOU 1205 N MET A 153 3712 3344 3838 -61 730 -12 N
ATOM 1206 CA MET A 153 -9.594 10.612 26.675 1.00 28.94 C
ANISOU 1206 CA MET A 153 3770 3379 3845 -46 692 -15 C
ATOM 1207 C MET A 153 -8.575 9.888 27.563 1.00 30.67 C
ANISOU 1207 C MET A 153 4073 3582 3999 -1 715 19 C
ATOM 1208 O MET A 153 -8.374 8.695 27.391 1.00 30.62 O
ANISOU 1208 O MET A 153 4106 3536 3994 4 733 22 O
ATOM 1209 CB MET A 153 -8.890 11.378 25.554 1.00 32.54 C
ANISOU 1209 CB MET A 153 4191 3892 4279 -33 616 -28 C
ATOM 1210 CG MET A 153 -7.682 10.617 25.005 1.00 38.15 C
ANISOU 1210 CG MET A 153 4940 4608 4948 -1 597 -24 C
ATOM 1211 SD MET A 153 -6.600 11.560 23.966 1.00 45.97 S
ANISOU 1211 SD MET A 153 5906 5656 5904 19 543 -31 S
ATOM 1212 CE MET A 153 -5.849 12.643 25.148 1.00 43.25 C
ANISOU 1212 CE MET A 153 5553 5348 5533 49 536 -6 C
ATOM 1213 N LEU A 154 -7.952 10.602 28.510 1.00 26.24 N
ANISOU 1213 N LEU A 154 3541 3045 3382 34 706 41 N
ATOM 1214 CA LEU A 154 -6.985 10.005 29.427 1.00 27.27 C
ANISOU 1214 CA LEU A 154 3755 3157 3448 86 704 72 C
ATOM 1215 C LEU A 154 -7.637 8.979 30.353 1.00 32.69 C
ANISOU 1215 C LEU A 154 4528 3768 4124 81 787 96 C
ATOM 1216 O LEU A 154 -7.036 7.935 30.629 1.00 31.52 O
ANISOU 1216 O LEU A 154 4451 3582 3945 116 789 118 O
ATOM 1217 CB LEU A 154 -6.249 11.087 30.234 1.00 27.21 C
ANISOU 1217 CB LEU A 154 3762 3189 3386 122 659 82 C
ATOM 1218 CG LEU A 154 -5.388 12.068 29.418 1.00 31.64 C
ANISOU 1218 CG LEU A 154 4246 3815 3959 130 586 62 C
ATOM 1219 CD1 LEU A 154 -4.631 13.017 30.354 1.00 31.77 C
ANISOU 1219 CD1 LEU A 154 4282 3859 3931 163 539 67 C
ATOM 1220 CD2 LEU A 154 -4.418 11.327 28.453 1.00 28.20 C
ANISOU 1220 CD2 LEU A 154 3788 3388 3539 152 554 55 C
ATOM 1221 N THR A 155 -8.881 9.264 30.807 1.00 29.76 N
ANISOU 1221 N THR A 155 4150 3368 3789 37 862 91 N
ATOM 1222 CA THR A 155 -9.656 8.345 31.654 1.00 29.48 C
ANISOU 1222 CA THR A 155 4194 3248 3759 19 970 112 C
ATOM 1223 C THR A 155 -9.885 7.052 30.884 1.00 32.43 C
ANISOU 1223 C THR A 155 4557 3574 4189 -6 990 102 C
ATOM 1224 O THR A 155 -9.643 5.977 31.422 1.00 31.78 O
ANISOU 1224 O THR A 155 4572 3430 4074 14 1033 132 O
ATOM 1225 CB THR A 155 -10.989 8.975 32.100 1.00 31.48 C
ANISOU 1225 CB THR A 155 4411 3478 4070 -30 1058 98 C
ATOM 1226 OG1 THR A 155 -10.722 10.242 32.698 1.00 30.47 O
ANISOU 1226 OG1 THR A 155 4290 3396 3889 -5 1032 100 O
ATOM 1227 CG2 THR A 155 -11.772 8.065 33.065 1.00 28.61 C
ANISOU 1227 CG2 THR A 155 4137 3018 3714 -52 1196 122 C
ATOM 1228 N PHE A 156 -10.311 7.158 29.618 1.00 29.95 N
ANISOU 1228 N PHE A 156 4140 3286 3954 -46 950 60 N
ATOM 1229 CA PHE A 156 -10.483 5.991 28.764 1.00 30.79 C
ANISOU 1229 CA PHE A 156 4238 3350 4112 -71 952 40 C
ATOM 1230 C PHE A 156 -9.140 5.217 28.614 1.00 35.88 C
ANISOU 1230 C PHE A 156 4950 3995 4688 -12 909 61 C
ATOM 1231 O PHE A 156 -9.137 3.993 28.707 1.00 35.50 O
ANISOU 1231 O PHE A 156 4964 3879 4648 -11 952 71 O
ATOM 1232 CB PHE A 156 -11.005 6.404 27.382 1.00 32.13 C
ANISOU 1232 CB PHE A 156 4299 3555 4352 -111 887 -12 C
ATOM 1233 CG PHE A 156 -10.742 5.383 26.305 1.00 33.23 C
ANISOU 1233 CG PHE A 156 4446 3672 4509 -119 853 -39 C
ATOM 1234 CD1 PHE A 156 -11.378 4.151 26.322 1.00 36.24 C
ANISOU 1234 CD1 PHE A 156 4851 3970 4950 -156 912 -51 C
ATOM 1235 CD2 PHE A 156 -9.832 5.645 25.284 1.00 35.93 C
ANISOU 1235 CD2 PHE A 156 4777 4068 4807 -89 772 -53 C
ATOM 1236 CE1 PHE A 156 -11.108 3.189 25.337 1.00 37.56 C
ANISOU 1236 CE1 PHE A 156 5034 4109 5127 -162 880 -80 C
ATOM 1237 CE2 PHE A 156 -9.571 4.689 24.293 1.00 39.06 C
ANISOU 1237 CE2 PHE A 156 5194 4438 5210 -92 750 -81 C
ATOM 1238 CZ PHE A 156 -10.217 3.474 24.323 1.00 36.94 C
ANISOU 1238 CZ PHE A 156 4952 4088 4997 -128 799 -96 C
ATOM 1239 N ILE A 157 -8.031 5.926 28.358 1.00 32.63 N
ANISOU 1239 N ILE A 157 4522 3654 4223 36 829 64 N
ATOM 1240 CA ILE A 157 -6.724 5.277 28.190 1.00 33.29 C
ANISOU 1240 CA ILE A 157 4647 3737 4263 97 788 78 C
ATOM 1241 C ILE A 157 -6.332 4.477 29.457 1.00 34.35 C
ANISOU 1241 C ILE A 157 4896 3812 4345 145 822 125 C
ATOM 1242 O ILE A 157 -5.898 3.332 29.336 1.00 31.78 O
ANISOU 1242 O ILE A 157 4622 3434 4018 172 831 135 O
ATOM 1243 CB ILE A 157 -5.632 6.273 27.718 1.00 36.46 C
ANISOU 1243 CB ILE A 157 4993 4220 4640 133 708 68 C
ATOM 1244 CG1 ILE A 157 -5.906 6.703 26.258 1.00 36.98 C
ANISOU 1244 CG1 ILE A 157 4982 4324 4747 93 682 26 C
ATOM 1245 CG2 ILE A 157 -4.197 5.661 27.853 1.00 36.09 C
ANISOU 1245 CG2 ILE A 157 4982 4168 4564 206 670 84 C
ATOM 1246 CD1 ILE A 157 -5.308 7.977 25.893 1.00 38.27 C
ANISOU 1246 CD1 ILE A 157 5088 4557 4894 104 631 18 C
ATOM 1247 N THR A 158 -6.538 5.059 30.654 1.00 30.93 N
ANISOU 1247 N THR A 158 4514 3376 3862 156 843 153 N
ATOM 1248 CA THR A 158 -6.229 4.362 31.917 1.00 31.77 C
ANISOU 1248 CA THR A 158 4757 3417 3897 206 872 202 C
ATOM 1249 C THR A 158 -7.071 3.089 32.096 1.00 37.24 C
ANISOU 1249 C THR A 158 5522 4009 4618 172 977 218 C
ATOM 1250 O THR A 158 -6.638 2.172 32.801 1.00 37.34 O
ANISOU 1250 O THR A 158 5656 3955 4578 221 994 259 O
ATOM 1251 CB THR A 158 -6.312 5.284 33.131 1.00 40.13 C
ANISOU 1251 CB THR A 158 5875 4489 4883 224 876 224 C
ATOM 1252 OG1 THR A 158 -7.675 5.634 33.374 1.00 40.57 O
ANISOU 1252 OG1 THR A 158 5919 4522 4976 156 977 216 O
ATOM 1253 CG2 THR A 158 -5.410 6.496 33.014 1.00 38.09 C
ANISOU 1253 CG2 THR A 158 5550 4319 4602 257 769 206 C
ATOM 1254 N SER A 159 -8.243 3.006 31.419 1.00 34.81 N
ANISOU 1254 N SER A 159 5139 3685 4402 91 1040 183 N
ATOM 1255 CA SER A 159 -9.089 1.800 31.466 1.00 35.20 C
ANISOU 1255 CA SER A 159 5234 3633 4506 45 1143 187 C
ATOM 1256 C SER A 159 -8.531 0.710 30.522 1.00 39.67 C
ANISOU 1256 C SER A 159 5798 4173 5101 59 1106 171 C
ATOM 1257 O SER A 159 -8.888 -0.442 30.676 1.00 41.37 O
ANISOU 1257 O SER A 159 6081 4295 5343 41 1178 183 O
ATOM 1258 CB SER A 159 -10.548 2.122 31.128 1.00 37.37 C
ANISOU 1258 CB SER A 159 5416 3895 4888 -47 1213 147 C
ATOM 1259 OG SER A 159 -10.770 2.150 29.723 1.00 45.05 O
ANISOU 1259 OG SER A 159 6271 4904 5942 -86 1149 90 O
ATOM 1260 N THR A 160 -7.715 1.070 29.527 1.00 36.06 N
ANISOU 1260 N THR A 160 5267 3791 4644 86 1007 141 N
ATOM 1261 CA THR A 160 -7.103 0.098 28.600 1.00 36.21 C
ANISOU 1261 CA THR A 160 5289 3785 4684 106 979 120 C
ATOM 1262 C THR A 160 -5.857 -0.552 29.275 1.00 40.73 C
ANISOU 1262 C THR A 160 5959 4328 5190 201 952 167 C
ATOM 1263 O THR A 160 -5.374 -0.005 30.273 1.00 38.68 O
ANISOU 1263 O THR A 160 5744 4090 4863 251 924 205 O
ATOM 1264 CB THR A 160 -6.831 0.733 27.216 1.00 42.09 C
ANISOU 1264 CB THR A 160 5926 4609 5456 91 905 67 C
ATOM 1265 OG1 THR A 160 -5.688 1.601 27.289 1.00 35.70 O
ANISOU 1265 OG1 THR A 160 5091 3878 4595 152 834 79 O
ATOM 1266 CG2 THR A 160 -8.068 1.463 26.645 1.00 38.22 C
ANISOU 1266 CG2 THR A 160 5348 4147 5027 10 909 25 C
ATOM 1267 N PRO A 161 -5.321 -1.712 28.796 1.00 39.51 N
ANISOU 1267 N PRO A 161 5843 4117 5052 232 953 162 N
ATOM 1268 CA PRO A 161 -4.187 -2.339 29.517 1.00 39.43 C
ANISOU 1268 CA PRO A 161 5924 4068 4988 331 920 208 C
ATOM 1269 C PRO A 161 -2.815 -1.697 29.256 1.00 41.45 C
ANISOU 1269 C PRO A 161 6116 4405 5228 406 817 199 C
ATOM 1270 O PRO A 161 -1.885 -2.386 28.819 1.00 40.22 O
ANISOU 1270 O PRO A 161 5962 4229 5093 465 788 192 O
ATOM 1271 CB PRO A 161 -4.253 -3.794 29.057 1.00 41.51 C
ANISOU 1271 CB PRO A 161 6245 4234 5293 330 970 201 C
ATOM 1272 CG PRO A 161 -4.740 -3.682 27.620 1.00 46.16 C
ANISOU 1272 CG PRO A 161 6732 4857 5950 258 972 131 C
ATOM 1273 CD PRO A 161 -5.751 -2.539 27.648 1.00 41.36 C
ANISOU 1273 CD PRO A 161 6050 4310 5355 183 980 114 C
ATOM 1274 N ILE A 162 -2.674 -0.388 29.576 1.00 35.21 N
ANISOU 1274 N ILE A 162 5269 3699 4409 405 768 198 N
ATOM 1275 CA ILE A 162 -1.423 0.369 29.367 1.00 34.19 C
ANISOU 1275 CA ILE A 162 5063 3645 4280 464 676 185 C
ATOM 1276 C ILE A 162 -0.251 -0.152 30.206 1.00 36.56 C
ANISOU 1276 C ILE A 162 5427 3911 4553 570 609 220 C
ATOM 1277 O ILE A 162 0.890 0.055 29.800 1.00 35.99 O
ANISOU 1277 O ILE A 162 5279 3877 4518 624 544 199 O
ATOM 1278 CB ILE A 162 -1.587 1.904 29.529 1.00 36.12 C
ANISOU 1278 CB ILE A 162 5238 3979 4509 432 641 173 C
ATOM 1279 CG1 ILE A 162 -2.169 2.279 30.932 1.00 35.91 C
ANISOU 1279 CG1 ILE A 162 5301 3932 4412 432 653 214 C
ATOM 1280 CG2 ILE A 162 -2.410 2.458 28.377 1.00 36.02 C
ANISOU 1280 CG2 ILE A 162 5138 4010 4540 348 677 130 C
ATOM 1281 CD1 ILE A 162 -2.131 3.792 31.222 1.00 38.70 C
ANISOU 1281 CD1 ILE A 162 5594 4366 4745 417 607 202 C
ATOM 1282 N GLU A 163 -0.536 -0.838 31.338 1.00 31.83 N
ANISOU 1282 N GLU A 163 4967 3233 3894 602 628 271 N
ATOM 1283 CA GLU A 163 0.444 -1.445 32.246 1.00 32.45 C
ANISOU 1283 CA GLU A 163 5138 3260 3933 710 555 312 C
ATOM 1284 C GLU A 163 1.285 -2.479 31.493 1.00 37.17 C
ANISOU 1284 C GLU A 163 5708 3818 4598 767 541 296 C
ATOM 1285 O GLU A 163 2.421 -2.730 31.886 1.00 37.71 O
ANISOU 1285 O GLU A 163 5783 3872 4673 867 450 309 O
ATOM 1286 CB GLU A 163 -0.245 -2.142 33.451 1.00 34.10 C
ANISOU 1286 CB GLU A 163 5531 3370 4055 721 609 374 C
ATOM 1287 CG GLU A 163 -0.880 -1.203 34.456 1.00 47.28 C
ANISOU 1287 CG GLU A 163 7261 5062 5641 692 621 396 C
ATOM 1288 CD GLU A 163 -2.269 -0.667 34.130 1.00 70.62 C
ANISOU 1288 CD GLU A 163 10172 8039 8620 575 734 375 C
ATOM 1289 OE1 GLU A 163 -2.846 -1.019 33.073 1.00 48.14 O
ANISOU 1289 OE1 GLU A 163 7246 5191 5856 507 799 340 O
ATOM 1290 OE2 GLU A 163 -2.785 0.115 34.959 1.00 77.14 O
ANISOU 1290 OE2 GLU A 163 11047 8880 9384 554 754 390 O
ATOM 1291 N LYS A 164 0.730 -3.063 30.411 1.00 33.82 N
ANISOU 1291 N LYS A 164 5249 3371 4229 705 626 265 N
ATOM 1292 CA LYS A 164 1.410 -4.028 29.534 1.00 34.15 C
ANISOU 1292 CA LYS A 164 5265 3372 4337 746 635 239 C
ATOM 1293 C LYS A 164 2.658 -3.443 28.854 1.00 38.38 C
ANISOU 1293 C LYS A 164 5666 3982 4935 795 567 198 C
ATOM 1294 O LYS A 164 3.492 -4.198 28.349 1.00 37.29 O
ANISOU 1294 O LYS A 164 5507 3807 4855 857 563 180 O
ATOM 1295 CB LYS A 164 0.453 -4.620 28.480 1.00 37.16 C
ANISOU 1295 CB LYS A 164 5643 3721 4757 657 735 202 C
ATOM 1296 CG LYS A 164 -0.581 -5.559 29.084 1.00 46.92 C
ANISOU 1296 CG LYS A 164 7009 4853 5967 621 814 239 C
ATOM 1297 CD LYS A 164 -1.352 -6.302 28.008 1.00 55.86 C
ANISOU 1297 CD LYS A 164 8132 5938 7155 544 894 193 C
ATOM 1298 CE LYS A 164 -2.351 -7.247 28.628 1.00 63.64 C
ANISOU 1298 CE LYS A 164 9237 6810 8134 502 981 226 C
ATOM 1299 NZ LYS A 164 -3.046 -8.057 27.598 1.00 70.83 N
ANISOU 1299 NZ LYS A 164 10139 7664 9111 429 1046 174 N
ATOM 1300 N GLY A 165 2.770 -2.115 28.851 1.00 35.98 N
ANISOU 1300 N GLY A 165 5272 3772 4625 767 526 181 N
ATOM 1301 CA GLY A 165 3.926 -1.402 28.328 1.00 36.36 C
ANISOU 1301 CA GLY A 165 5188 3888 4737 804 470 143 C
ATOM 1302 C GLY A 165 4.002 -1.207 26.830 1.00 41.79 C
ANISOU 1302 C GLY A 165 5782 4613 5482 755 535 88 C
ATOM 1303 O GLY A 165 4.769 -0.357 26.369 1.00 42.51 O
ANISOU 1303 O GLY A 165 5763 4768 5622 761 512 57 O
ATOM 1304 N ASP A 166 3.228 -1.972 26.061 1.00 38.76 N
ANISOU 1304 N ASP A 166 5447 4185 5094 704 616 72 N
ATOM 1305 CA ASP A 166 3.238 -1.849 24.604 1.00 39.86 C
ANISOU 1305 CA ASP A 166 5528 4351 5267 659 676 18 C
ATOM 1306 C ASP A 166 1.840 -1.515 24.045 1.00 43.43 C
ANISOU 1306 C ASP A 166 6006 4821 5677 552 720 2 C
ATOM 1307 O ASP A 166 1.513 -1.828 22.891 1.00 42.81 O
ANISOU 1307 O ASP A 166 5932 4729 5605 511 769 -40 O
ATOM 1308 CB ASP A 166 3.835 -3.110 23.959 1.00 42.24 C
ANISOU 1308 CB ASP A 166 5856 4578 5616 711 720 -5 C
ATOM 1309 CG ASP A 166 3.010 -4.367 24.139 1.00 55.85 C
ANISOU 1309 CG ASP A 166 7697 6207 7318 696 761 10 C
ATOM 1310 OD1 ASP A 166 3.254 -5.342 23.398 1.00 61.40 O
ANISOU 1310 OD1 ASP A 166 8428 6849 8053 715 810 -20 O
ATOM 1311 OD2 ASP A 166 2.115 -4.376 25.023 1.00 54.90 O
ANISOU 1311 OD2 ASP A 166 7641 6068 7150 662 752 50 O
ATOM 1312 N SER A 167 1.031 -0.864 24.876 1.00 38.73 N
ANISOU 1312 N SER A 167 5426 4250 5040 512 697 32 N
ATOM 1313 CA SER A 167 -0.324 -0.506 24.514 1.00 38.36 C
ANISOU 1313 CA SER A 167 5387 4216 4971 418 727 18 C
ATOM 1314 C SER A 167 -0.524 0.969 24.745 1.00 39.91 C
ANISOU 1314 C SER A 167 5520 4497 5148 387 691 22 C
ATOM 1315 O SER A 167 -0.270 1.472 25.841 1.00 39.63 O
ANISOU 1315 O SER A 167 5488 4481 5091 418 652 56 O
ATOM 1316 CB SER A 167 -1.322 -1.330 25.331 1.00 42.21 C
ANISOU 1316 CB SER A 167 5965 4628 5445 393 763 48 C
ATOM 1317 OG SER A 167 -2.649 -0.858 25.175 1.00 52.80 O
ANISOU 1317 OG SER A 167 7293 5982 6786 304 787 34 O
ATOM 1318 N CYS A 168 -0.935 1.671 23.699 1.00 36.61 N
ANISOU 1318 N CYS A 168 5053 4125 4732 331 699 -14 N
ATOM 1319 CA CYS A 168 -1.249 3.100 23.770 1.00 37.17 C
ANISOU 1319 CA CYS A 168 5067 4268 4787 295 670 -13 C
ATOM 1320 C CYS A 168 -2.241 3.419 22.674 1.00 41.43 C
ANISOU 1320 C CYS A 168 5596 4821 5325 223 683 -49 C
ATOM 1321 O CYS A 168 -1.864 3.810 21.567 1.00 42.68 O
ANISOU 1321 O CYS A 168 5730 5007 5478 217 684 -79 O
ATOM 1322 CB CYS A 168 -0.006 3.978 23.678 1.00 36.70 C
ANISOU 1322 CB CYS A 168 4939 4266 4740 337 639 -16 C
ATOM 1323 SG CYS A 168 -0.332 5.677 24.183 1.00 39.88 S
ANISOU 1323 SG CYS A 168 5288 4742 5123 303 599 -4 S
ATOM 1324 N VAL A 169 -3.496 3.191 22.963 1.00 35.83 N
ANISOU 1324 N VAL A 169 4910 4082 4623 172 694 -48 N
ATOM 1325 CA VAL A 169 -4.549 3.280 21.958 1.00 36.12 C
ANISOU 1325 CA VAL A 169 4937 4114 4671 107 689 -88 C
ATOM 1326 C VAL A 169 -5.057 4.677 21.655 1.00 35.13 C
ANISOU 1326 C VAL A 169 4756 4052 4538 73 651 -96 C
ATOM 1327 O VAL A 169 -5.025 5.589 22.493 1.00 33.03 O
ANISOU 1327 O VAL A 169 4459 3825 4267 80 641 -67 O
ATOM 1328 CB VAL A 169 -5.751 2.352 22.280 1.00 41.42 C
ANISOU 1328 CB VAL A 169 5639 4714 5382 60 719 -96 C
ATOM 1329 CG1 VAL A 169 -5.346 0.876 22.216 1.00 42.24 C
ANISOU 1329 CG1 VAL A 169 5810 4743 5497 86 756 -100 C
ATOM 1330 CG2 VAL A 169 -6.386 2.717 23.614 1.00 40.93 C
ANISOU 1330 CG2 VAL A 169 5572 4649 5333 47 742 -58 C
ATOM 1331 N ASP A 170 -5.612 4.781 20.445 1.00 29.40 N
ANISOU 1331 N ASP A 170 4032 3328 3812 36 626 -137 N
ATOM 1332 CA ASP A 170 -6.278 5.955 19.924 1.00 29.25 C
ANISOU 1332 CA ASP A 170 3974 3352 3787 2 580 -150 C
ATOM 1333 C ASP A 170 -7.792 5.718 20.091 1.00 32.84 C
ANISOU 1333 C ASP A 170 4408 3771 4301 -53 563 -170 C
ATOM 1334 O ASP A 170 -8.322 4.749 19.540 1.00 30.85 O
ANISOU 1334 O ASP A 170 4182 3465 4074 -80 559 -207 O
ATOM 1335 CB ASP A 170 -5.916 6.109 18.429 1.00 29.73 C
ANISOU 1335 CB ASP A 170 4072 3423 3803 4 556 -184 C
ATOM 1336 CG ASP A 170 -6.516 7.317 17.721 1.00 32.21 C
ANISOU 1336 CG ASP A 170 4369 3774 4096 -21 499 -195 C
ATOM 1337 OD1 ASP A 170 -7.271 8.073 18.363 1.00 30.42 O
ANISOU 1337 OD1 ASP A 170 4088 3567 3904 -41 474 -180 O
ATOM 1338 OD2 ASP A 170 -6.235 7.497 16.525 1.00 37.25 O
ANISOU 1338 OD2 ASP A 170 5058 4414 4680 -17 482 -217 O
ATOM 1339 N TYR A 171 -8.492 6.618 20.815 1.00 31.19 N
ANISOU 1339 N TYR A 171 4143 3585 4121 -72 556 -153 N
ATOM 1340 CA TYR A 171 -9.950 6.519 21.007 1.00 30.18 C
ANISOU 1340 CA TYR A 171 3972 3422 4074 -125 549 -177 C
ATOM 1341 C TYR A 171 -10.703 6.545 19.664 1.00 33.23 C
ANISOU 1341 C TYR A 171 4347 3798 4481 -158 470 -231 C
ATOM 1342 O TYR A 171 -11.817 6.034 19.595 1.00 32.11 O
ANISOU 1342 O TYR A 171 4171 3607 4421 -204 457 -267 O
ATOM 1343 CB TYR A 171 -10.491 7.597 21.981 1.00 30.59 C
ANISOU 1343 CB TYR A 171 3966 3501 4154 -131 564 -151 C
ATOM 1344 CG TYR A 171 -10.427 9.024 21.458 1.00 31.71 C
ANISOU 1344 CG TYR A 171 4074 3704 4270 -121 502 -151 C
ATOM 1345 CD1 TYR A 171 -11.453 9.551 20.674 1.00 32.78 C
ANISOU 1345 CD1 TYR A 171 4163 3839 4453 -150 435 -187 C
ATOM 1346 CD2 TYR A 171 -9.383 9.869 21.815 1.00 32.30 C
ANISOU 1346 CD2 TYR A 171 4160 3830 4284 -82 509 -117 C
ATOM 1347 CE1 TYR A 171 -11.393 10.860 20.187 1.00 31.31 C
ANISOU 1347 CE1 TYR A 171 3959 3699 4237 -135 378 -182 C
ATOM 1348 CE2 TYR A 171 -9.351 11.199 21.393 1.00 32.83 C
ANISOU 1348 CE2 TYR A 171 4200 3943 4332 -76 463 -114 C
ATOM 1349 CZ TYR A 171 -10.351 11.686 20.569 1.00 34.53 C
ANISOU 1349 CZ TYR A 171 4384 4153 4582 -101 401 -143 C
ATOM 1350 OH TYR A 171 -10.290 12.991 20.147 1.00 34.00 O
ANISOU 1350 OH TYR A 171 4305 4123 4491 -90 357 -135 O
ATOM 1351 N ALA A 172 -10.094 7.139 18.597 1.00 29.57 N
ANISOU 1351 N ALA A 172 3917 3373 3944 -134 417 -240 N
ATOM 1352 CA ALA A 172 -10.724 7.179 17.268 1.00 30.10 C
ANISOU 1352 CA ALA A 172 4005 3428 4006 -156 329 -291 C
ATOM 1353 C ALA A 172 -10.838 5.766 16.675 1.00 36.12 C
ANISOU 1353 C ALA A 172 4821 4127 4776 -175 328 -336 C
ATOM 1354 O ALA A 172 -11.815 5.460 15.990 1.00 35.15 O
ANISOU 1354 O ALA A 172 4692 3967 4697 -211 254 -389 O
ATOM 1355 CB ALA A 172 -9.940 8.082 16.312 1.00 30.63 C
ANISOU 1355 CB ALA A 172 4126 3539 3974 -123 296 -282 C
ATOM 1356 N SER A 173 -9.852 4.905 16.991 1.00 34.71 N
ANISOU 1356 N SER A 173 4692 3932 4566 -148 405 -317 N
ATOM 1357 CA SER A 173 -9.740 3.536 16.501 1.00 35.51 C
ANISOU 1357 CA SER A 173 4856 3969 4668 -156 422 -355 C
ATOM 1358 C SER A 173 -10.129 2.457 17.514 1.00 41.26 C
ANISOU 1358 C SER A 173 5565 4635 5476 -179 486 -347 C
ATOM 1359 O SER A 173 -10.373 1.331 17.098 1.00 41.11 O
ANISOU 1359 O SER A 173 5588 4549 5483 -202 489 -388 O
ATOM 1360 CB SER A 173 -8.311 3.282 16.023 1.00 38.21 C
ANISOU 1360 CB SER A 173 5273 4323 4922 -103 468 -343 C
ATOM 1361 OG SER A 173 -7.980 4.129 14.931 1.00 49.57 O
ANISOU 1361 OG SER A 173 6753 5801 6282 -88 425 -355 O
ATOM 1362 N SER A 174 -10.166 2.778 18.822 1.00 39.25 N
ANISOU 1362 N SER A 174 5265 4395 5255 -173 542 -295 N
ATOM 1363 CA SER A 174 -10.425 1.795 19.888 1.00 39.89 C
ANISOU 1363 CA SER A 174 5353 4409 5392 -187 622 -275 C
ATOM 1364 C SER A 174 -11.452 2.271 20.904 1.00 45.42 C
ANISOU 1364 C SER A 174 5985 5104 6171 -225 654 -257 C
ATOM 1365 O SER A 174 -11.649 3.469 21.096 1.00 45.24 O
ANISOU 1365 O SER A 174 5907 5139 6141 -220 626 -243 O
ATOM 1366 CB SER A 174 -9.118 1.453 20.602 1.00 43.13 C
ANISOU 1366 CB SER A 174 5819 4826 5741 -122 682 -221 C
ATOM 1367 OG SER A 174 -8.084 1.145 19.680 1.00 50.84 O
ANISOU 1367 OG SER A 174 6846 5813 6658 -81 666 -238 O
ATOM 1368 N GLY A 175 -12.090 1.329 21.570 1.00 44.31 N
ANISOU 1368 N GLY A 175 5849 4884 6103 -262 724 -258 N
ATOM 1369 CA GLY A 175 -13.118 1.664 22.548 1.00 45.66 C
ANISOU 1369 CA GLY A 175 5959 5032 6357 -302 781 -245 C
ATOM 1370 C GLY A 175 -14.477 1.911 21.913 1.00 51.49 C
ANISOU 1370 C GLY A 175 6598 5752 7214 -369 727 -309 C
ATOM 1371 O GLY A 175 -14.593 2.020 20.685 1.00 53.72 O
ANISOU 1371 O GLY A 175 6866 6052 7493 -377 622 -361 O
ATOM 1372 N ASN A 176 -15.515 1.998 22.755 1.00 44.38 N
ANISOU 1372 N ASN A 176 5632 4809 6422 -415 800 -308 N
ATOM 1373 CA ASN A 176 -16.902 2.176 22.351 1.00 42.60 C
ANISOU 1373 CA ASN A 176 5287 4551 6346 -481 762 -372 C
ATOM 1374 C ASN A 176 -17.095 3.329 21.309 1.00 42.06 C
ANISOU 1374 C ASN A 176 5156 4558 6266 -464 614 -408 C
ATOM 1375 O ASN A 176 -16.928 4.499 21.659 1.00 40.20 O
ANISOU 1375 O ASN A 176 4896 4387 5990 -430 606 -374 O
ATOM 1376 CB ASN A 176 -17.795 2.338 23.590 1.00 40.66 C
ANISOU 1376 CB ASN A 176 4982 4260 6207 -518 889 -353 C
ATOM 1377 CG ASN A 176 -19.259 2.120 23.338 1.00 61.74 C
ANISOU 1377 CG ASN A 176 7522 6863 9074 -597 887 -423 C
ATOM 1378 OD1 ASN A 176 -19.810 2.504 22.307 1.00 58.07 O
ANISOU 1378 OD1 ASN A 176 6973 6419 8674 -612 752 -486 O
ATOM 1379 ND2 ASN A 176 -19.934 1.501 24.286 1.00 60.02 N
ANISOU 1379 ND2 ASN A 176 7286 6558 8963 -647 1035 -416 N
ATOM 1380 N PRO A 177 -17.453 2.994 20.034 1.00 36.89 N
ANISOU 1380 N PRO A 177 4488 3887 5642 -487 494 -477 N
ATOM 1381 CA PRO A 177 -17.628 4.046 19.008 1.00 36.50 C
ANISOU 1381 CA PRO A 177 4405 3898 5565 -465 346 -507 C
ATOM 1382 C PRO A 177 -18.690 5.090 19.324 1.00 39.84 C
ANISOU 1382 C PRO A 177 4699 4335 6104 -480 319 -520 C
ATOM 1383 O PRO A 177 -18.507 6.246 18.987 1.00 38.13 O
ANISOU 1383 O PRO A 177 4476 4183 5828 -440 246 -504 O
ATOM 1384 CB PRO A 177 -17.948 3.267 17.729 1.00 38.69 C
ANISOU 1384 CB PRO A 177 4707 4132 5862 -493 231 -584 C
ATOM 1385 CG PRO A 177 -17.514 1.848 18.007 1.00 43.22 C
ANISOU 1385 CG PRO A 177 5353 4639 6428 -513 325 -582 C
ATOM 1386 CD PRO A 177 -17.702 1.647 19.472 1.00 38.52 C
ANISOU 1386 CD PRO A 177 4722 4012 5900 -531 482 -531 C
ATOM 1387 N LYS A 178 -19.764 4.701 20.022 1.00 38.09 N
ANISOU 1387 N LYS A 178 4376 4046 6051 -538 393 -545 N
ATOM 1388 CA LYS A 178 -20.839 5.600 20.431 1.00 38.20 C
ANISOU 1388 CA LYS A 178 4251 4059 6205 -554 392 -562 C
ATOM 1389 C LYS A 178 -20.292 6.702 21.359 1.00 41.21 C
ANISOU 1389 C LYS A 178 4655 4505 6499 -504 471 -489 C
ATOM 1390 O LYS A 178 -20.553 7.875 21.115 1.00 40.66 O
ANISOU 1390 O LYS A 178 4531 4482 6437 -475 396 -491 O
ATOM 1391 CB LYS A 178 -21.971 4.794 21.109 1.00 41.62 C
ANISOU 1391 CB LYS A 178 4580 4394 6840 -631 499 -601 C
ATOM 1392 CG LYS A 178 -23.086 5.635 21.728 1.00 66.62 C
ANISOU 1392 CG LYS A 178 7595 7546 10173 -650 543 -618 C
ATOM 1393 CD LYS A 178 -23.947 4.791 22.687 1.00 78.97 C
ANISOU 1393 CD LYS A 178 9086 9007 11912 -724 718 -634 C
ATOM 1394 CE LYS A 178 -25.088 5.563 23.309 1.00 86.33 C
ANISOU 1394 CE LYS A 178 9859 9914 13030 -746 783 -658 C
ATOM 1395 NZ LYS A 178 -24.623 6.495 24.369 1.00 95.44 N
ANISOU 1395 NZ LYS A 178 11068 11117 14079 -696 901 -582 N
ATOM 1396 N TYR A 179 -19.520 6.327 22.393 1.00 36.52 N
ANISOU 1396 N TYR A 179 4149 3908 5818 -490 611 -426 N
ATOM 1397 CA TYR A 179 -18.949 7.294 23.331 1.00 35.84 C
ANISOU 1397 CA TYR A 179 4098 3876 5642 -444 681 -361 C
ATOM 1398 C TYR A 179 -17.818 8.077 22.707 1.00 37.43 C
ANISOU 1398 C TYR A 179 4371 4164 5685 -381 584 -332 C
ATOM 1399 O TYR A 179 -17.755 9.282 22.909 1.00 37.67 O
ANISOU 1399 O TYR A 179 4378 4246 5691 -351 565 -311 O
ATOM 1400 CB TYR A 179 -18.525 6.627 24.649 1.00 37.33 C
ANISOU 1400 CB TYR A 179 4370 4025 5787 -445 846 -307 C
ATOM 1401 CG TYR A 179 -19.692 6.084 25.449 1.00 38.66 C
ANISOU 1401 CG TYR A 179 4472 4104 6115 -507 978 -327 C
ATOM 1402 CD1 TYR A 179 -19.729 4.753 25.849 1.00 40.40 C
ANISOU 1402 CD1 TYR A 179 4748 4240 6360 -544 1080 -321 C
ATOM 1403 CD2 TYR A 179 -20.734 6.916 25.851 1.00 40.16 C
ANISOU 1403 CD2 TYR A 179 4545 4283 6433 -527 1016 -350 C
ATOM 1404 CE1 TYR A 179 -20.803 4.245 26.586 1.00 41.80 C
ANISOU 1404 CE1 TYR A 179 4868 4323 6691 -608 1222 -338 C
ATOM 1405 CE2 TYR A 179 -21.815 6.419 26.583 1.00 41.54 C
ANISOU 1405 CE2 TYR A 179 4649 4366 6768 -588 1159 -371 C
ATOM 1406 CZ TYR A 179 -21.839 5.085 26.957 1.00 48.37 C
ANISOU 1406 CZ TYR A 179 5575 5146 7657 -631 1267 -364 C
ATOM 1407 OH TYR A 179 -22.886 4.599 27.703 1.00 54.43 O
ANISOU 1407 OH TYR A 179 6281 5814 8587 -696 1429 -383 O
ATOM 1408 N SER A 180 -16.959 7.422 21.902 1.00 32.66 N
ANISOU 1408 N SER A 180 3853 3571 4985 -365 529 -333 N
ATOM 1409 CA SER A 180 -15.870 8.121 21.197 1.00 31.24 C
ANISOU 1409 CA SER A 180 3740 3465 4665 -311 450 -310 C
ATOM 1410 C SER A 180 -16.401 9.198 20.239 1.00 33.97 C
ANISOU 1410 C SER A 180 4033 3844 5031 -303 323 -341 C
ATOM 1411 O SER A 180 -15.771 10.241 20.127 1.00 32.34 O
ANISOU 1411 O SER A 180 3853 3695 4740 -262 296 -308 O
ATOM 1412 CB SER A 180 -15.004 7.139 20.423 1.00 33.62 C
ANISOU 1412 CB SER A 180 4135 3757 4883 -300 426 -318 C
ATOM 1413 OG SER A 180 -14.266 6.312 21.300 1.00 45.65 O
ANISOU 1413 OG SER A 180 5722 5258 6364 -288 531 -278 O
ATOM 1414 N LEU A 181 -17.543 8.946 19.550 1.00 33.30 N
ANISOU 1414 N LEU A 181 3876 3717 5061 -340 240 -403 N
ATOM 1415 CA LEU A 181 -18.158 9.898 18.605 1.00 34.20 C
ANISOU 1415 CA LEU A 181 3943 3849 5201 -326 98 -436 C
ATOM 1416 C LEU A 181 -18.739 11.103 19.332 1.00 37.49 C
ANISOU 1416 C LEU A 181 4268 4286 5691 -313 121 -418 C
ATOM 1417 O LEU A 181 -18.545 12.228 18.878 1.00 37.18 O
ANISOU 1417 O LEU A 181 4243 4291 5595 -273 46 -402 O
ATOM 1418 CB LEU A 181 -19.241 9.218 17.730 1.00 34.39 C
ANISOU 1418 CB LEU A 181 3909 3815 5342 -367 -13 -517 C
ATOM 1419 CG LEU A 181 -19.866 10.032 16.565 1.00 38.40 C
ANISOU 1419 CG LEU A 181 4392 4332 5865 -345 -197 -559 C
ATOM 1420 CD1 LEU A 181 -18.797 10.497 15.526 1.00 37.28 C
ANISOU 1420 CD1 LEU A 181 4401 4239 5526 -293 -273 -531 C
ATOM 1421 CD2 LEU A 181 -20.941 9.212 15.849 1.00 41.54 C
ANISOU 1421 CD2 LEU A 181 4726 4662 6394 -389 -310 -647 C
ATOM 1422 N ILE A 182 -19.426 10.874 20.467 1.00 33.82 N
ANISOU 1422 N ILE A 182 3720 3783 5348 -346 236 -419 N
ATOM 1423 CA ILE A 182 -20.017 11.955 21.266 1.00 33.49 C
ANISOU 1423 CA ILE A 182 3592 3749 5383 -335 283 -406 C
ATOM 1424 C ILE A 182 -18.886 12.863 21.728 1.00 34.81 C
ANISOU 1424 C ILE A 182 3846 3982 5399 -285 323 -341 C
ATOM 1425 O ILE A 182 -18.974 14.079 21.591 1.00 35.06 O
ANISOU 1425 O ILE A 182 3853 4046 5422 -253 271 -331 O
ATOM 1426 CB ILE A 182 -20.854 11.397 22.458 1.00 37.17 C
ANISOU 1426 CB ILE A 182 3979 4152 5992 -383 435 -417 C
ATOM 1427 CG1 ILE A 182 -22.131 10.672 21.961 1.00 37.99 C
ANISOU 1427 CG1 ILE A 182 3961 4184 6290 -438 387 -494 C
ATOM 1428 CG2 ILE A 182 -21.202 12.502 23.484 1.00 38.10 C
ANISOU 1428 CG2 ILE A 182 4045 4281 6153 -364 523 -393 C
ATOM 1429 CD1 ILE A 182 -22.821 9.697 23.036 1.00 44.40 C
ANISOU 1429 CD1 ILE A 182 4718 4913 7241 -502 565 -506 C
ATOM 1430 N TYR A 183 -17.821 12.259 22.257 1.00 30.01 N
ANISOU 1430 N TYR A 183 3337 3388 4678 -278 406 -299 N
ATOM 1431 CA TYR A 183 -16.662 12.980 22.755 1.00 29.47 C
ANISOU 1431 CA TYR A 183 3346 3375 4477 -235 441 -244 C
ATOM 1432 C TYR A 183 -15.939 13.727 21.623 1.00 31.66 C
ANISOU 1432 C TYR A 183 3671 3704 4657 -200 328 -236 C
ATOM 1433 O TYR A 183 -15.674 14.909 21.764 1.00 30.60 O
ANISOU 1433 O TYR A 183 3535 3604 4486 -171 315 -213 O
ATOM 1434 CB TYR A 183 -15.715 12.009 23.496 1.00 30.01 C
ANISOU 1434 CB TYR A 183 3504 3436 4464 -232 535 -209 C
ATOM 1435 CG TYR A 183 -14.419 12.659 23.937 1.00 30.35 C
ANISOU 1435 CG TYR A 183 3620 3533 4377 -186 550 -160 C
ATOM 1436 CD1 TYR A 183 -14.418 13.737 24.825 1.00 31.11 C
ANISOU 1436 CD1 TYR A 183 3704 3651 4465 -168 588 -138 C
ATOM 1437 CD2 TYR A 183 -13.197 12.191 23.478 1.00 31.17 C
ANISOU 1437 CD2 TYR A 183 3800 3661 4381 -162 527 -143 C
ATOM 1438 CE1 TYR A 183 -13.226 14.333 25.235 1.00 27.75 C
ANISOU 1438 CE1 TYR A 183 3339 3270 3934 -131 590 -102 C
ATOM 1439 CE2 TYR A 183 -12.002 12.773 23.884 1.00 32.16 C
ANISOU 1439 CE2 TYR A 183 3975 3832 4414 -123 536 -106 C
ATOM 1440 CZ TYR A 183 -12.019 13.848 24.757 1.00 33.71 C
ANISOU 1440 CZ TYR A 183 4156 4050 4604 -109 561 -87 C
ATOM 1441 OH TYR A 183 -10.822 14.400 25.135 1.00 29.08 O
ANISOU 1441 OH TYR A 183 3611 3503 3936 -75 557 -59 O
ATOM 1442 N SER A 184 -15.666 13.037 20.490 1.00 28.33 N
ANISOU 1442 N SER A 184 3296 3276 4192 -203 255 -258 N
ATOM 1443 CA SER A 184 -14.979 13.615 19.341 1.00 27.82 C
ANISOU 1443 CA SER A 184 3299 3248 4025 -172 166 -252 C
ATOM 1444 C SER A 184 -15.754 14.787 18.735 1.00 34.17 C
ANISOU 1444 C SER A 184 4057 4056 4868 -158 64 -266 C
ATOM 1445 O SER A 184 -15.144 15.808 18.436 1.00 34.26 O
ANISOU 1445 O SER A 184 4113 4103 4800 -126 41 -235 O
ATOM 1446 CB SER A 184 -14.689 12.552 18.296 1.00 25.49 C
ANISOU 1446 CB SER A 184 3072 2932 3682 -181 119 -280 C
ATOM 1447 OG SER A 184 -14.022 13.073 17.163 1.00 32.56 O
ANISOU 1447 OG SER A 184 4051 3852 4467 -152 50 -274 O
ATOM 1448 N LEU A 185 -17.089 14.658 18.600 1.00 32.24 N
ANISOU 1448 N LEU A 185 3721 3772 4757 -180 6 -313 N
ATOM 1449 CA LEU A 185 -17.936 15.730 18.048 1.00 32.69 C
ANISOU 1449 CA LEU A 185 3723 3825 4872 -159 -106 -331 C
ATOM 1450 C LEU A 185 -18.029 16.927 19.004 1.00 38.06 C
ANISOU 1450 C LEU A 185 4350 4525 5586 -138 -43 -298 C
ATOM 1451 O LEU A 185 -17.999 18.060 18.530 1.00 37.51 O
ANISOU 1451 O LEU A 185 4297 4471 5482 -102 -113 -283 O
ATOM 1452 CB LEU A 185 -19.338 15.233 17.652 1.00 32.02 C
ANISOU 1452 CB LEU A 185 3535 3686 4945 -186 -195 -398 C
ATOM 1453 CG LEU A 185 -19.429 14.274 16.458 1.00 35.71 C
ANISOU 1453 CG LEU A 185 4059 4126 5382 -200 -306 -445 C
ATOM 1454 CD1 LEU A 185 -20.780 13.579 16.437 1.00 35.21 C
ANISOU 1454 CD1 LEU A 185 3867 4002 5508 -243 -360 -518 C
ATOM 1455 CD2 LEU A 185 -19.209 15.000 15.140 1.00 38.83 C
ANISOU 1455 CD2 LEU A 185 4551 4537 5667 -155 -455 -444 C
ATOM 1456 N CYS A 186 -18.143 16.689 20.338 1.00 34.99 N
ANISOU 1456 N CYS A 186 3912 4128 5255 -159 91 -287 N
ATOM 1457 CA CYS A 186 -18.191 17.786 21.316 1.00 35.46 C
ANISOU 1457 CA CYS A 186 3938 4201 5335 -140 161 -261 C
ATOM 1458 C CYS A 186 -16.859 18.534 21.360 1.00 36.55 C
ANISOU 1458 C CYS A 186 4175 4390 5322 -108 176 -210 C
ATOM 1459 O CYS A 186 -16.848 19.755 21.495 1.00 35.18 O
ANISOU 1459 O CYS A 186 3994 4230 5143 -82 163 -194 O
ATOM 1460 CB CYS A 186 -18.605 17.292 22.700 1.00 37.35 C
ANISOU 1460 CB CYS A 186 4128 4411 5652 -169 306 -263 C
ATOM 1461 SG CYS A 186 -20.324 16.717 22.795 1.00 42.72 S
ANISOU 1461 SG CYS A 186 4657 5020 6556 -210 315 -327 S
ATOM 1462 N LEU A 187 -15.743 17.793 21.232 1.00 32.02 N
ANISOU 1462 N LEU A 187 3688 3838 4639 -112 205 -189 N
ATOM 1463 CA LEU A 187 -14.391 18.326 21.201 1.00 32.23 C
ANISOU 1463 CA LEU A 187 3797 3907 4541 -88 221 -149 C
ATOM 1464 C LEU A 187 -14.149 19.086 19.886 1.00 33.92 C
ANISOU 1464 C LEU A 187 4058 4133 4697 -65 122 -144 C
ATOM 1465 O LEU A 187 -13.462 20.105 19.892 1.00 32.66 O
ANISOU 1465 O LEU A 187 3933 3996 4479 -45 129 -114 O
ATOM 1466 CB LEU A 187 -13.400 17.172 21.382 1.00 33.32 C
ANISOU 1466 CB LEU A 187 3998 4054 4610 -96 276 -137 C
ATOM 1467 CG LEU A 187 -11.932 17.478 21.602 1.00 38.75 C
ANISOU 1467 CG LEU A 187 4749 4779 5196 -75 312 -102 C
ATOM 1468 CD1 LEU A 187 -11.729 18.417 22.790 1.00 39.14 C
ANISOU 1468 CD1 LEU A 187 4780 4843 5248 -63 362 -81 C
ATOM 1469 CD2 LEU A 187 -11.177 16.177 21.852 1.00 41.87 C
ANISOU 1469 CD2 LEU A 187 5186 5169 5553 -78 361 -97 C
ATOM 1470 N THR A 188 -14.754 18.630 18.775 1.00 30.19 N
ANISOU 1470 N THR A 188 3594 3638 4240 -69 28 -174 N
ATOM 1471 CA THR A 188 -14.683 19.352 17.494 1.00 30.15 C
ANISOU 1471 CA THR A 188 3655 3632 4171 -43 -74 -169 C
ATOM 1472 C THR A 188 -15.408 20.699 17.646 1.00 33.12 C
ANISOU 1472 C THR A 188 3978 3999 4607 -18 -121 -163 C
ATOM 1473 O THR A 188 -14.910 21.727 17.186 1.00 31.84 O
ANISOU 1473 O THR A 188 3878 3846 4375 8 -144 -131 O
ATOM 1474 CB THR A 188 -15.326 18.528 16.358 1.00 33.10 C
ANISOU 1474 CB THR A 188 4053 3974 4551 -49 -181 -212 C
ATOM 1475 OG1 THR A 188 -14.609 17.294 16.248 1.00 29.74 O
ANISOU 1475 OG1 THR A 188 3681 3551 4069 -70 -128 -219 O
ATOM 1476 CG2 THR A 188 -15.314 19.282 14.989 1.00 29.35 C
ANISOU 1476 CG2 THR A 188 3673 3488 3990 -15 -299 -206 C
ATOM 1477 N LEU A 189 -16.584 20.675 18.290 1.00 29.58 N
ANISOU 1477 N LEU A 189 3415 3527 4298 -27 -124 -193 N
ATOM 1478 CA LEU A 189 -17.382 21.863 18.519 1.00 30.88 C
ANISOU 1478 CA LEU A 189 3512 3676 4546 -1 -160 -194 C
ATOM 1479 C LEU A 189 -16.666 22.861 19.460 1.00 35.34 C
ANISOU 1479 C LEU A 189 4092 4265 5071 10 -63 -154 C
ATOM 1480 O LEU A 189 -16.364 23.975 19.046 1.00 33.39 O
ANISOU 1480 O LEU A 189 3892 4019 4775 39 -102 -128 O
ATOM 1481 CB LEU A 189 -18.786 21.486 19.047 1.00 31.31 C
ANISOU 1481 CB LEU A 189 3426 3692 4778 -17 -164 -243 C
ATOM 1482 CG LEU A 189 -19.761 22.653 19.285 1.00 37.75 C
ANISOU 1482 CG LEU A 189 4149 4481 5711 15 -201 -254 C
ATOM 1483 CD1 LEU A 189 -20.025 23.457 17.987 1.00 38.12 C
ANISOU 1483 CD1 LEU A 189 4241 4513 5730 62 -368 -251 C
ATOM 1484 CD2 LEU A 189 -21.092 22.152 19.891 1.00 40.73 C
ANISOU 1484 CD2 LEU A 189 4373 4816 6286 -8 -173 -307 C
ATOM 1485 N LEU A 190 -16.350 22.436 20.690 1.00 32.82 N
ANISOU 1485 N LEU A 190 3749 3958 4763 -13 58 -150 N
ATOM 1486 CA LEU A 190 -15.748 23.290 21.711 1.00 32.70 C
ANISOU 1486 CA LEU A 190 3747 3960 4716 -5 143 -123 C
ATOM 1487 C LEU A 190 -14.283 23.624 21.474 1.00 31.91 C
ANISOU 1487 C LEU A 190 3743 3894 4486 0 157 -87 C
ATOM 1488 O LEU A 190 -13.836 24.728 21.799 1.00 27.36 O
ANISOU 1488 O LEU A 190 3186 3325 3886 14 175 -67 O
ATOM 1489 CB LEU A 190 -15.952 22.623 23.091 1.00 33.89 C
ANISOU 1489 CB LEU A 190 3859 4104 4912 -29 259 -134 C
ATOM 1490 CG LEU A 190 -15.569 23.407 24.366 1.00 40.66 C
ANISOU 1490 CG LEU A 190 4731 4969 5749 -21 349 -119 C
ATOM 1491 CD1 LEU A 190 -16.352 24.733 24.482 1.00 41.82 C
ANISOU 1491 CD1 LEU A 190 4826 5092 5972 4 332 -129 C
ATOM 1492 CD2 LEU A 190 -15.787 22.546 25.617 1.00 40.30 C
ANISOU 1492 CD2 LEU A 190 4679 4908 5727 -42 462 -127 C
ATOM 1493 N GLY A 191 -13.536 22.658 20.953 1.00 28.17 N
ANISOU 1493 N GLY A 191 3323 3437 3943 -13 157 -82 N
ATOM 1494 CA GLY A 191 -12.110 22.842 20.757 1.00 26.99 C
ANISOU 1494 CA GLY A 191 3247 3315 3691 -11 185 -53 C
ATOM 1495 C GLY A 191 -11.744 23.507 19.463 1.00 29.81 C
ANISOU 1495 C GLY A 191 3672 3668 3987 4 125 -36 C
ATOM 1496 O GLY A 191 -10.721 24.175 19.394 1.00 29.54 O
ANISOU 1496 O GLY A 191 3682 3646 3897 6 158 -11 O
ATOM 1497 N PHE A 192 -12.532 23.285 18.418 1.00 27.23 N
ANISOU 1497 N PHE A 192 3361 3318 3667 13 38 -51 N
ATOM 1498 CA PHE A 192 -12.207 23.807 17.103 1.00 27.43 C
ANISOU 1498 CA PHE A 192 3482 3329 3611 31 -20 -32 C
ATOM 1499 C PHE A 192 -13.211 24.830 16.537 1.00 31.42 C
ANISOU 1499 C PHE A 192 3988 3801 4150 62 -120 -31 C
ATOM 1500 O PHE A 192 -12.818 25.965 16.271 1.00 30.78 O
ANISOU 1500 O PHE A 192 3959 3709 4028 79 -118 2 O
ATOM 1501 CB PHE A 192 -11.993 22.632 16.104 1.00 28.81 C
ANISOU 1501 CB PHE A 192 3725 3500 3722 24 -49 -48 C
ATOM 1502 CG PHE A 192 -11.826 23.000 14.647 1.00 30.57 C
ANISOU 1502 CG PHE A 192 4072 3697 3846 45 -114 -35 C
ATOM 1503 CD1 PHE A 192 -11.051 24.099 14.268 1.00 32.40 C
ANISOU 1503 CD1 PHE A 192 4380 3923 4010 57 -80 6 C
ATOM 1504 CD2 PHE A 192 -12.388 22.212 13.646 1.00 32.49 C
ANISOU 1504 CD2 PHE A 192 4369 3916 4058 51 -204 -64 C
ATOM 1505 CE1 PHE A 192 -10.911 24.445 12.921 1.00 33.54 C
ANISOU 1505 CE1 PHE A 192 4662 4033 4050 78 -128 24 C
ATOM 1506 CE2 PHE A 192 -12.228 22.548 12.299 1.00 34.36 C
ANISOU 1506 CE2 PHE A 192 4748 4125 4184 75 -266 -51 C
ATOM 1507 CZ PHE A 192 -11.480 23.650 11.944 1.00 32.38 C
ANISOU 1507 CZ PHE A 192 4582 3864 3857 89 -221 -4 C
ATOM 1508 N LEU A 193 -14.453 24.404 16.264 1.00 28.55 N
ANISOU 1508 N LEU A 193 3571 3414 3862 71 -213 -66 N
ATOM 1509 CA LEU A 193 -15.438 25.238 15.588 1.00 28.73 C
ANISOU 1509 CA LEU A 193 3594 3399 3922 110 -335 -70 C
ATOM 1510 C LEU A 193 -15.810 26.504 16.325 1.00 33.63 C
ANISOU 1510 C LEU A 193 4153 4008 4617 131 -316 -55 C
ATOM 1511 O LEU A 193 -16.018 27.526 15.667 1.00 33.85 O
ANISOU 1511 O LEU A 193 4235 4006 4622 170 -390 -33 O
ATOM 1512 CB LEU A 193 -16.700 24.439 15.226 1.00 29.22 C
ANISOU 1512 CB LEU A 193 3587 3436 4079 112 -445 -122 C
ATOM 1513 CG LEU A 193 -16.535 23.277 14.221 1.00 34.09 C
ANISOU 1513 CG LEU A 193 4284 4049 4620 98 -503 -146 C
ATOM 1514 CD1 LEU A 193 -17.854 22.534 14.044 1.00 34.08 C
ANISOU 1514 CD1 LEU A 193 4187 4018 4745 93 -612 -208 C
ATOM 1515 CD2 LEU A 193 -16.033 23.777 12.843 1.00 37.43 C
ANISOU 1515 CD2 LEU A 193 4878 4453 4893 132 -580 -117 C
ATOM 1516 N ILE A 194 -15.893 26.451 17.668 1.00 30.44 N
ANISOU 1516 N ILE A 194 3652 3622 4293 110 -218 -67 N
ATOM 1517 CA ILE A 194 -16.258 27.608 18.486 1.00 29.71 C
ANISOU 1517 CA ILE A 194 3501 3514 4273 129 -185 -61 C
ATOM 1518 C ILE A 194 -15.108 28.633 18.481 1.00 32.64 C
ANISOU 1518 C ILE A 194 3963 3893 4548 132 -134 -16 C
ATOM 1519 O ILE A 194 -15.372 29.733 18.022 1.00 33.40 O
ANISOU 1519 O ILE A 194 4089 3954 4646 167 -188 3 O
ATOM 1520 CB ILE A 194 -16.804 27.254 19.901 1.00 32.13 C
ANISOU 1520 CB ILE A 194 3693 3826 4689 108 -92 -91 C
ATOM 1521 CG1 ILE A 194 -18.241 26.674 19.765 1.00 31.73 C
ANISOU 1521 CG1 ILE A 194 3533 3745 4779 112 -156 -138 C
ATOM 1522 CG2 ILE A 194 -16.771 28.508 20.835 1.00 31.90 C
ANISOU 1522 CG2 ILE A 194 3643 3786 4692 123 -27 -80 C
ATOM 1523 CD1 ILE A 194 -18.953 26.143 21.131 1.00 32.41 C
ANISOU 1523 CD1 ILE A 194 3502 3822 4991 85 -42 -173 C
ATOM 1524 N PRO A 195 -13.841 28.306 18.865 1.00 28.45 N
ANISOU 1524 N PRO A 195 3475 3397 3937 100 -41 0 N
ATOM 1525 CA PRO A 195 -12.765 29.312 18.757 1.00 27.42 C
ANISOU 1525 CA PRO A 195 3418 3263 3735 98 1 36 C
ATOM 1526 C PRO A 195 -12.612 29.879 17.328 1.00 33.93 C
ANISOU 1526 C PRO A 195 4353 4055 4484 122 -67 68 C
ATOM 1527 O PRO A 195 -12.340 31.063 17.198 1.00 33.10 O
ANISOU 1527 O PRO A 195 4293 3921 4364 135 -58 96 O
ATOM 1528 CB PRO A 195 -11.507 28.535 19.196 1.00 27.75 C
ANISOU 1528 CB PRO A 195 3476 3347 3722 62 88 38 C
ATOM 1529 CG PRO A 195 -12.035 27.463 20.127 1.00 31.73 C
ANISOU 1529 CG PRO A 195 3901 3872 4283 48 114 5 C
ATOM 1530 CD PRO A 195 -13.322 27.038 19.448 1.00 28.25 C
ANISOU 1530 CD PRO A 195 3430 3408 3895 65 27 -15 C
ATOM 1531 N LEU A 196 -12.808 29.052 16.263 1.00 31.27 N
ANISOU 1531 N LEU A 196 4072 3715 4096 128 -133 64 N
ATOM 1532 CA LEU A 196 -12.712 29.514 14.878 1.00 31.31 C
ANISOU 1532 CA LEU A 196 4208 3681 4008 155 -200 94 C
ATOM 1533 C LEU A 196 -13.797 30.551 14.587 1.00 36.32 C
ANISOU 1533 C LEU A 196 4839 4266 4693 206 -307 101 C
ATOM 1534 O LEU A 196 -13.495 31.598 13.986 1.00 36.26 O
ANISOU 1534 O LEU A 196 4933 4217 4626 229 -317 143 O
ATOM 1535 CB LEU A 196 -12.764 28.328 13.862 1.00 31.79 C
ANISOU 1535 CB LEU A 196 4336 3744 3997 154 -256 78 C
ATOM 1536 CG LEU A 196 -12.597 28.699 12.361 1.00 36.72 C
ANISOU 1536 CG LEU A 196 5133 4323 4494 184 -321 109 C
ATOM 1537 CD1 LEU A 196 -11.204 29.267 12.072 1.00 36.55 C
ANISOU 1537 CD1 LEU A 196 5218 4294 4378 164 -198 154 C
ATOM 1538 CD2 LEU A 196 -12.884 27.494 11.452 1.00 39.22 C
ANISOU 1538 CD2 LEU A 196 5511 4638 4751 187 -397 79 C
ATOM 1539 N SER A 197 -15.042 30.280 15.066 1.00 32.23 N
ANISOU 1539 N SER A 197 4201 3747 4298 223 -376 61 N
ATOM 1540 CA SER A 197 -16.225 31.152 14.934 1.00 31.57 C
ANISOU 1540 CA SER A 197 4076 3616 4304 276 -484 55 C
ATOM 1541 C SER A 197 -16.027 32.468 15.668 1.00 34.54 C
ANISOU 1541 C SER A 197 4434 3972 4717 287 -417 79 C
ATOM 1542 O SER A 197 -16.447 33.499 15.167 1.00 35.24 O
ANISOU 1542 O SER A 197 4569 4008 4811 336 -490 103 O
ATOM 1543 CB SER A 197 -17.471 30.456 15.479 1.00 33.25 C
ANISOU 1543 CB SER A 197 4133 3833 4666 279 -534 -2 C
ATOM 1544 OG SER A 197 -17.798 29.377 14.622 1.00 45.56 O
ANISOU 1544 OG SER A 197 5716 5394 6199 275 -627 -28 O
ATOM 1545 N VAL A 198 -15.414 32.427 16.858 1.00 30.75 N
ANISOU 1545 N VAL A 198 3893 3528 4262 245 -286 71 N
ATOM 1546 CA VAL A 198 -15.127 33.610 17.660 1.00 30.31 C
ANISOU 1546 CA VAL A 198 3825 3454 4237 247 -215 85 C
ATOM 1547 C VAL A 198 -14.112 34.506 16.889 1.00 33.43 C
ANISOU 1547 C VAL A 198 4360 3820 4523 247 -196 137 C
ATOM 1548 O VAL A 198 -14.350 35.710 16.776 1.00 33.19 O
ANISOU 1548 O VAL A 198 4362 3737 4513 280 -218 159 O
ATOM 1549 CB VAL A 198 -14.690 33.252 19.105 1.00 33.21 C
ANISOU 1549 CB VAL A 198 4111 3865 4642 203 -93 58 C
ATOM 1550 CG1 VAL A 198 -14.080 34.471 19.820 1.00 32.88 C
ANISOU 1550 CG1 VAL A 198 4089 3803 4600 197 -20 71 C
ATOM 1551 CG2 VAL A 198 -15.876 32.694 19.909 1.00 32.00 C
ANISOU 1551 CG2 VAL A 198 3830 3717 4613 211 -95 11 C
ATOM 1552 N MET A 199 -13.048 33.918 16.297 1.00 28.99 N
ANISOU 1552 N MET A 199 3883 3281 3852 213 -153 157 N
ATOM 1553 CA MET A 199 -12.081 34.692 15.480 1.00 29.70 C
ANISOU 1553 CA MET A 199 4110 3333 3843 207 -115 206 C
ATOM 1554 C MET A 199 -12.773 35.309 14.249 1.00 35.28 C
ANISOU 1554 C MET A 199 4929 3975 4503 265 -230 240 C
ATOM 1555 O MET A 199 -12.514 36.461 13.928 1.00 35.01 O
ANISOU 1555 O MET A 199 4978 3882 4440 281 -215 281 O
ATOM 1556 CB MET A 199 -10.875 33.844 15.048 1.00 32.02 C
ANISOU 1556 CB MET A 199 4463 3660 4045 162 -38 214 C
ATOM 1557 CG MET A 199 -9.944 33.536 16.191 1.00 36.17 C
ANISOU 1557 CG MET A 199 4902 4233 4607 111 73 192 C
ATOM 1558 SD MET A 199 -8.395 32.716 15.718 1.00 41.25 S
ANISOU 1558 SD MET A 199 5600 4904 5168 64 174 200 S
ATOM 1559 CE MET A 199 -9.003 31.073 15.349 1.00 36.99 C
ANISOU 1559 CE MET A 199 5044 4406 4606 75 111 171 C
ATOM 1560 N CYS A 200 -13.693 34.563 13.612 1.00 34.01 N
ANISOU 1560 N CYS A 200 4767 3815 4340 299 -351 221 N
ATOM 1561 CA CYS A 200 -14.486 35.044 12.484 1.00 34.92 C
ANISOU 1561 CA CYS A 200 4984 3867 4415 365 -495 245 C
ATOM 1562 C CYS A 200 -15.337 36.224 12.904 1.00 38.73 C
ANISOU 1562 C CYS A 200 5412 4301 5002 415 -550 250 C
ATOM 1563 O CYS A 200 -15.432 37.178 12.142 1.00 38.48 O
ANISOU 1563 O CYS A 200 5504 4201 4917 461 -607 295 O
ATOM 1564 CB CYS A 200 -15.338 33.929 11.885 1.00 36.16 C
ANISOU 1564 CB CYS A 200 5123 4039 4576 386 -625 207 C
ATOM 1565 SG CYS A 200 -14.393 32.714 10.934 1.00 41.06 S
ANISOU 1565 SG CYS A 200 5877 4688 5037 348 -587 211 S
ATOM 1566 N PHE A 201 -15.954 36.157 14.108 1.00 35.72 N
ANISOU 1566 N PHE A 201 4856 3948 4766 408 -526 204 N
ATOM 1567 CA PHE A 201 -16.799 37.216 14.662 1.00 35.22 C
ANISOU 1567 CA PHE A 201 4719 3840 4824 455 -560 197 C
ATOM 1568 C PHE A 201 -15.971 38.476 14.922 1.00 38.03 C
ANISOU 1568 C PHE A 201 5151 4157 5143 445 -463 240 C
ATOM 1569 O PHE A 201 -16.421 39.583 14.611 1.00 37.59 O
ANISOU 1569 O PHE A 201 5143 4029 5109 500 -521 267 O
ATOM 1570 CB PHE A 201 -17.514 36.747 15.953 1.00 37.43 C
ANISOU 1570 CB PHE A 201 4805 4159 5257 440 -517 136 C
ATOM 1571 CG PHE A 201 -18.320 37.820 16.660 1.00 40.52 C
ANISOU 1571 CG PHE A 201 5112 4503 5781 484 -520 122 C
ATOM 1572 CD1 PHE A 201 -19.535 38.255 16.142 1.00 44.02 C
ANISOU 1572 CD1 PHE A 201 5519 4889 6317 561 -662 114 C
ATOM 1573 CD2 PHE A 201 -17.854 38.405 17.833 1.00 44.60 C
ANISOU 1573 CD2 PHE A 201 5589 5026 6331 453 -386 113 C
ATOM 1574 CE1 PHE A 201 -20.272 39.257 16.785 1.00 45.65 C
ANISOU 1574 CE1 PHE A 201 5644 5046 6657 608 -658 99 C
ATOM 1575 CE2 PHE A 201 -18.595 39.399 18.481 1.00 47.97 C
ANISOU 1575 CE2 PHE A 201 5947 5402 6877 497 -379 97 C
ATOM 1576 CZ PHE A 201 -19.803 39.814 17.954 1.00 46.06 C
ANISOU 1576 CZ PHE A 201 5662 5104 6735 574 -508 90 C
ATOM 1577 N PHE A 202 -14.772 38.313 15.494 1.00 32.90 N
ANISOU 1577 N PHE A 202 4508 3548 4446 375 -322 242 N
ATOM 1578 CA PHE A 202 -13.925 39.460 15.790 1.00 31.53 C
ANISOU 1578 CA PHE A 202 4394 3335 4252 354 -227 272 C
ATOM 1579 C PHE A 202 -13.271 40.019 14.524 1.00 38.48 C
ANISOU 1579 C PHE A 202 5458 4156 5007 362 -231 337 C
ATOM 1580 O PHE A 202 -13.025 41.215 14.472 1.00 36.29 O
ANISOU 1580 O PHE A 202 5248 3811 4729 372 -199 370 O
ATOM 1581 CB PHE A 202 -12.937 39.152 16.920 1.00 31.43 C
ANISOU 1581 CB PHE A 202 4310 3379 4253 281 -92 243 C
ATOM 1582 CG PHE A 202 -13.621 39.280 18.265 1.00 31.86 C
ANISOU 1582 CG PHE A 202 4229 3450 4427 287 -71 193 C
ATOM 1583 CD1 PHE A 202 -13.851 40.531 18.831 1.00 34.07 C
ANISOU 1583 CD1 PHE A 202 4500 3674 4770 308 -49 192 C
ATOM 1584 CD2 PHE A 202 -14.111 38.156 18.927 1.00 32.71 C
ANISOU 1584 CD2 PHE A 202 4227 3618 4585 276 -70 148 C
ATOM 1585 CE1 PHE A 202 -14.527 40.654 20.053 1.00 34.67 C
ANISOU 1585 CE1 PHE A 202 4464 3759 4951 317 -19 142 C
ATOM 1586 CE2 PHE A 202 -14.771 38.277 20.152 1.00 35.62 C
ANISOU 1586 CE2 PHE A 202 4486 3992 5056 283 -33 103 C
ATOM 1587 CZ PHE A 202 -14.979 39.528 20.706 1.00 34.28 C
ANISOU 1587 CZ PHE A 202 4313 3770 4943 304 -6 100 C
ATOM 1588 N TYR A 203 -13.079 39.201 13.466 1.00 38.22 N
ANISOU 1588 N TYR A 203 5518 4134 4868 363 -272 354 N
ATOM 1589 CA TYR A 203 -12.583 39.752 12.203 1.00 39.12 C
ANISOU 1589 CA TYR A 203 5832 4179 4852 379 -275 418 C
ATOM 1590 C TYR A 203 -13.678 40.709 11.683 1.00 44.53 C
ANISOU 1590 C TYR A 203 6579 4782 5557 467 -413 446 C
ATOM 1591 O TYR A 203 -13.383 41.850 11.338 1.00 44.10 O
ANISOU 1591 O TYR A 203 6641 4649 5468 483 -383 497 O
ATOM 1592 CB TYR A 203 -12.285 38.642 11.174 1.00 41.37 C
ANISOU 1592 CB TYR A 203 6216 4489 5014 371 -298 425 C
ATOM 1593 CG TYR A 203 -12.195 39.163 9.752 1.00 46.31 C
ANISOU 1593 CG TYR A 203 7070 5030 5496 413 -343 488 C
ATOM 1594 CD1 TYR A 203 -11.041 39.789 9.289 1.00 48.65 C
ANISOU 1594 CD1 TYR A 203 7507 5275 5702 376 -204 541 C
ATOM 1595 CD2 TYR A 203 -13.285 39.082 8.888 1.00 48.98 C
ANISOU 1595 CD2 TYR A 203 7487 5331 5793 493 -526 495 C
ATOM 1596 CE1 TYR A 203 -10.967 40.305 7.992 1.00 51.88 C
ANISOU 1596 CE1 TYR A 203 8150 5594 5967 416 -231 605 C
ATOM 1597 CE2 TYR A 203 -13.223 39.590 7.587 1.00 51.25 C
ANISOU 1597 CE2 TYR A 203 8010 5531 5931 539 -577 557 C
ATOM 1598 CZ TYR A 203 -12.052 40.183 7.138 1.00 62.39 C
ANISOU 1598 CZ TYR A 203 9578 6891 7237 500 -420 615 C
ATOM 1599 OH TYR A 203 -11.993 40.719 5.874 1.00 68.62 O
ANISOU 1599 OH TYR A 203 10621 7583 7868 547 -455 681 O
ATOM 1600 N TYR A 204 -14.945 40.238 11.669 1.00 42.88 N
ANISOU 1600 N TYR A 204 6283 4588 5420 523 -563 410 N
ATOM 1601 CA TYR A 204 -16.123 40.992 11.249 1.00 43.99 C
ANISOU 1601 CA TYR A 204 6446 4658 5612 617 -721 423 C
ATOM 1602 C TYR A 204 -16.292 42.293 12.060 1.00 47.43 C
ANISOU 1602 C TYR A 204 6827 5042 6153 635 -672 430 C
ATOM 1603 O TYR A 204 -16.619 43.329 11.478 1.00 46.53 O
ANISOU 1603 O TYR A 204 6823 4837 6019 700 -741 477 O
ATOM 1604 CB TYR A 204 -17.386 40.105 11.341 1.00 46.29 C
ANISOU 1604 CB TYR A 204 6595 4986 6007 656 -869 362 C
ATOM 1605 CG TYR A 204 -18.680 40.891 11.368 1.00 50.24 C
ANISOU 1605 CG TYR A 204 7032 5423 6635 747 -1013 352 C
ATOM 1606 CD1 TYR A 204 -19.232 41.409 10.198 1.00 52.96 C
ANISOU 1606 CD1 TYR A 204 7520 5686 6916 835 -1182 392 C
ATOM 1607 CD2 TYR A 204 -19.346 41.133 12.566 1.00 52.16 C
ANISOU 1607 CD2 TYR A 204 7077 5681 7061 751 -978 302 C
ATOM 1608 CE1 TYR A 204 -20.414 42.151 10.221 1.00 55.12 C
ANISOU 1608 CE1 TYR A 204 7727 5896 7320 927 -1325 382 C
ATOM 1609 CE2 TYR A 204 -20.515 41.892 12.605 1.00 54.07 C
ANISOU 1609 CE2 TYR A 204 7249 5858 7437 839 -1098 291 C
ATOM 1610 CZ TYR A 204 -21.049 42.393 11.430 1.00 64.31 C
ANISOU 1610 CZ TYR A 204 8675 7076 8683 928 -1278 329 C
ATOM 1611 OH TYR A 204 -22.216 43.118 11.478 1.00 70.45 O
ANISOU 1611 OH TYR A 204 9371 7787 9609 1022 -1408 314 O
ATOM 1612 N LYS A 205 -16.095 42.232 13.402 1.00 42.31 N
ANISOU 1612 N LYS A 205 6019 4446 5612 583 -558 384 N
ATOM 1613 CA LYS A 205 -16.208 43.408 14.275 1.00 41.30 C
ANISOU 1613 CA LYS A 205 5839 4272 5582 594 -498 380 C
ATOM 1614 C LYS A 205 -15.130 44.434 13.919 1.00 45.42 C
ANISOU 1614 C LYS A 205 6517 4727 6012 566 -403 440 C
ATOM 1615 O LYS A 205 -15.391 45.641 13.938 1.00 43.69 O
ANISOU 1615 O LYS A 205 6344 4423 5831 609 -414 466 O
ATOM 1616 CB LYS A 205 -16.100 43.021 15.760 1.00 42.77 C
ANISOU 1616 CB LYS A 205 5852 4528 5871 538 -389 316 C
ATOM 1617 CG LYS A 205 -17.295 42.249 16.336 1.00 50.23 C
ANISOU 1617 CG LYS A 205 6627 5516 6943 567 -454 254 C
ATOM 1618 CD LYS A 205 -18.618 43.020 16.342 1.00 58.50 C
ANISOU 1618 CD LYS A 205 7611 6494 8120 657 -560 242 C
ATOM 1619 CE LYS A 205 -18.732 44.036 17.457 1.00 68.15 C
ANISOU 1619 CE LYS A 205 8769 7680 9443 662 -467 220 C
ATOM 1620 NZ LYS A 205 -20.055 44.716 17.436 1.00 69.82 N
ANISOU 1620 NZ LYS A 205 8908 7822 9798 756 -568 204 N
ATOM 1621 N MET A 206 -13.928 43.940 13.569 1.00 43.24 N
ANISOU 1621 N MET A 206 6320 4483 5624 495 -304 460 N
ATOM 1622 CA MET A 206 -12.780 44.751 13.161 1.00 43.94 C
ANISOU 1622 CA MET A 206 6553 4511 5632 452 -190 513 C
ATOM 1623 C MET A 206 -13.076 45.470 11.845 1.00 49.05 C
ANISOU 1623 C MET A 206 7402 5055 6182 520 -271 587 C
ATOM 1624 O MET A 206 -12.856 46.670 11.766 1.00 48.07 O
ANISOU 1624 O MET A 206 7365 4839 6060 530 -228 628 O
ATOM 1625 CB MET A 206 -11.528 43.881 13.023 1.00 46.43 C
ANISOU 1625 CB MET A 206 6888 4888 5867 367 -73 510 C
ATOM 1626 CG MET A 206 -10.878 43.501 14.331 1.00 51.11 C
ANISOU 1626 CG MET A 206 7323 5556 6541 294 32 451 C
ATOM 1627 SD MET A 206 -9.510 42.366 13.967 1.00 57.34 S
ANISOU 1627 SD MET A 206 8135 6409 7242 213 141 450 S
ATOM 1628 CE MET A 206 -8.393 42.882 15.110 1.00 54.28 C
ANISOU 1628 CE MET A 206 7659 6030 6933 134 276 417 C
ATOM 1629 N VAL A 207 -13.582 44.740 10.824 1.00 47.88 N
ANISOU 1629 N VAL A 207 7335 4913 5943 568 -393 603 N
ATOM 1630 CA VAL A 207 -13.955 45.273 9.507 1.00 48.91 C
ANISOU 1630 CA VAL A 207 7679 4946 5960 645 -500 671 C
ATOM 1631 C VAL A 207 -14.984 46.400 9.653 1.00 55.21 C
ANISOU 1631 C VAL A 207 8467 5661 6850 735 -612 685 C
ATOM 1632 O VAL A 207 -14.806 47.463 9.061 1.00 57.03 O
ANISOU 1632 O VAL A 207 8868 5782 7017 769 -604 752 O
ATOM 1633 CB VAL A 207 -14.432 44.147 8.534 1.00 52.47 C
ANISOU 1633 CB VAL A 207 8196 5431 6311 683 -636 665 C
ATOM 1634 CG1 VAL A 207 -15.214 44.716 7.347 1.00 52.05 C
ANISOU 1634 CG1 VAL A 207 8334 5276 6168 790 -810 720 C
ATOM 1635 CG2 VAL A 207 -13.255 43.308 8.048 1.00 51.80 C
ANISOU 1635 CG2 VAL A 207 8201 5387 6094 605 -507 675 C
ATOM 1636 N VAL A 208 -16.034 46.173 10.461 1.00 51.26 N
ANISOU 1636 N VAL A 208 7767 5205 6505 773 -704 622 N
ATOM 1637 CA VAL A 208 -17.092 47.148 10.732 1.00 50.69 C
ANISOU 1637 CA VAL A 208 7645 5060 6555 862 -808 620 C
ATOM 1638 C VAL A 208 -16.515 48.420 11.404 1.00 54.57 C
ANISOU 1638 C VAL A 208 8155 5486 7094 834 -668 641 C
ATOM 1639 O VAL A 208 -16.826 49.534 10.961 1.00 54.62 O
ANISOU 1639 O VAL A 208 8277 5380 7095 902 -720 692 O
ATOM 1640 CB VAL A 208 -18.269 46.500 11.518 1.00 53.96 C
ANISOU 1640 CB VAL A 208 7822 5540 7142 895 -902 538 C
ATOM 1641 CG1 VAL A 208 -19.198 47.548 12.127 1.00 53.68 C
ANISOU 1641 CG1 VAL A 208 7691 5436 7267 969 -950 522 C
ATOM 1642 CG2 VAL A 208 -19.055 45.562 10.620 1.00 53.80 C
ANISOU 1642 CG2 VAL A 208 7813 5541 7087 949 -1087 525 C
ATOM 1643 N PHE A 209 -15.656 48.249 12.439 1.00 49.15 N
ANISOU 1643 N PHE A 209 7363 4863 6448 734 -499 601 N
ATOM 1644 CA PHE A 209 -15.040 49.370 13.153 1.00 47.53 C
ANISOU 1644 CA PHE A 209 7164 4601 6293 694 -367 607 C
ATOM 1645 C PHE A 209 -14.232 50.263 12.212 1.00 54.97 C
ANISOU 1645 C PHE A 209 8333 5437 7118 685 -307 692 C
ATOM 1646 O PHE A 209 -14.373 51.488 12.268 1.00 54.15 O
ANISOU 1646 O PHE A 209 8294 5227 7052 720 -297 722 O
ATOM 1647 CB PHE A 209 -14.180 48.879 14.326 1.00 47.25 C
ANISOU 1647 CB PHE A 209 6993 4657 6304 588 -219 546 C
ATOM 1648 CG PHE A 209 -13.515 49.974 15.132 1.00 46.44 C
ANISOU 1648 CG PHE A 209 6887 4499 6258 540 -92 538 C
ATOM 1649 CD1 PHE A 209 -14.173 50.573 16.198 1.00 47.00 C
ANISOU 1649 CD1 PHE A 209 6844 4554 6461 568 -94 487 C
ATOM 1650 CD2 PHE A 209 -12.220 50.392 14.833 1.00 46.72 C
ANISOU 1650 CD2 PHE A 209 7033 4495 6222 462 34 574 C
ATOM 1651 CE1 PHE A 209 -13.552 51.573 16.948 1.00 47.60 C
ANISOU 1651 CE1 PHE A 209 6925 4575 6585 522 16 472 C
ATOM 1652 CE2 PHE A 209 -11.601 51.391 15.578 1.00 48.59 C
ANISOU 1652 CE2 PHE A 209 7261 4677 6524 412 142 557 C
ATOM 1653 CZ PHE A 209 -12.266 51.968 16.640 1.00 46.63 C
ANISOU 1653 CZ PHE A 209 6907 4415 6396 442 127 505 C
ATOM 1654 N LEU A 210 -13.419 49.645 11.337 1.00 54.54 N
ANISOU 1654 N LEU A 210 8404 5400 6919 640 -261 730 N
ATOM 1655 CA LEU A 210 -12.576 50.349 10.380 1.00 56.39 C
ANISOU 1655 CA LEU A 210 8865 5532 7029 621 -176 811 C
ATOM 1656 C LEU A 210 -13.364 51.068 9.273 1.00 67.13 C
ANISOU 1656 C LEU A 210 10422 6773 8311 734 -315 887 C
ATOM 1657 O LEU A 210 -12.912 52.111 8.790 1.00 67.20 O
ANISOU 1657 O LEU A 210 10606 6661 8264 735 -244 955 O
ATOM 1658 CB LEU A 210 -11.508 49.424 9.794 1.00 56.17 C
ANISOU 1658 CB LEU A 210 8907 5556 6878 542 -73 824 C
ATOM 1659 CG LEU A 210 -10.441 48.943 10.772 1.00 60.92 C
ANISOU 1659 CG LEU A 210 9355 6245 7548 427 87 765 C
ATOM 1660 CD1 LEU A 210 -9.585 47.866 10.150 1.00 61.07 C
ANISOU 1660 CD1 LEU A 210 9424 6321 7459 370 161 770 C
ATOM 1661 CD2 LEU A 210 -9.567 50.090 11.260 1.00 63.31 C
ANISOU 1661 CD2 LEU A 210 9673 6470 7910 362 237 776 C
ATOM 1662 N LYS A 211 -14.542 50.531 8.894 1.00 67.02 N
ANISOU 1662 N LYS A 211 10380 6785 8301 829 -515 872 N
ATOM 1663 CA LYS A 211 -15.419 51.120 7.882 1.00 68.03 C
ANISOU 1663 CA LYS A 211 10678 6804 8364 952 -689 934 C
ATOM 1664 C LYS A 211 -16.038 52.409 8.414 1.00 75.60 C
ANISOU 1664 C LYS A 211 11601 7670 9453 1016 -723 942 C
ATOM 1665 O LYS A 211 -16.166 53.386 7.671 1.00 76.85 O
ANISOU 1665 O LYS A 211 11960 7697 9544 1085 -767 1018 O
ATOM 1666 CB LYS A 211 -16.504 50.119 7.453 1.00 70.49 C
ANISOU 1666 CB LYS A 211 10930 7177 8675 1028 -904 898 C
ATOM 1667 CG LYS A 211 -16.027 49.165 6.366 1.00 82.30 C
ANISOU 1667 CG LYS A 211 12588 8701 9980 1007 -919 924 C
ATOM 1668 CD LYS A 211 -17.098 48.163 5.969 1.00 91.43 C
ANISOU 1668 CD LYS A 211 13679 9914 11146 1077 -1140 878 C
ATOM 1669 CE LYS A 211 -16.605 47.240 4.881 1.00 99.31 C
ANISOU 1669 CE LYS A 211 14858 10932 11945 1056 -1151 901 C
ATOM 1670 NZ LYS A 211 -17.379 45.970 4.843 1.00108.59 N
ANISOU 1670 NZ LYS A 211 15899 12200 13161 1075 -1308 827 N
ATOM 1671 N LYS A 212 -16.385 52.413 9.711 1.00 73.31 N
ANISOU 1671 N LYS A 212 11068 7442 9343 995 -691 863 N
ATOM 1672 CA LYS A 212 -16.957 53.546 10.438 1.00 73.56 C
ANISOU 1672 CA LYS A 212 11029 7399 9522 1046 -698 850 C
ATOM 1673 C LYS A 212 -15.894 54.661 10.545 1.00 79.26 C
ANISOU 1673 C LYS A 212 11881 8025 10209 981 -521 898 C
ATOM 1674 O LYS A 212 -16.175 55.814 10.213 1.00 78.92 O
ANISOU 1674 O LYS A 212 11965 7850 10173 1049 -553 952 O
ATOM 1675 CB LYS A 212 -17.406 53.073 11.832 1.00 75.75 C
ANISOU 1675 CB LYS A 212 11027 7780 9976 1016 -669 747 C
ATOM 1676 CG LYS A 212 -18.274 54.051 12.607 1.00 93.45 C
ANISOU 1676 CG LYS A 212 13166 9954 12387 1087 -701 716 C
ATOM 1677 CD LYS A 212 -18.532 53.545 14.023 1.00104.17 C
ANISOU 1677 CD LYS A 212 14275 11413 13893 1040 -629 616 C
ATOM 1678 CE LYS A 212 -19.464 54.444 14.797 1.00117.25 C
ANISOU 1678 CE LYS A 212 15825 13002 15724 1116 -651 577 C
ATOM 1679 NZ LYS A 212 -19.613 53.997 16.207 1.00127.03 N
ANISOU 1679 NZ LYS A 212 16853 14328 17085 1063 -552 482 N
ATOM 1680 N ARG A 213 -14.662 54.289 10.955 1.00 77.08 N
ANISOU 1680 N ARG A 213 11577 7810 9898 851 -339 878 N
ATOM 1681 CA ARG A 213 -13.522 55.192 11.133 1.00 77.27 C
ANISOU 1681 CA ARG A 213 11692 7758 9909 766 -155 907 C
ATOM 1682 C ARG A 213 -12.975 55.768 9.810 1.00 82.66 C
ANISOU 1682 C ARG A 213 12658 8315 10434 776 -117 1015 C
ATOM 1683 O ARG A 213 -12.291 56.799 9.842 1.00 83.31 O
ANISOU 1683 O ARG A 213 12840 8290 10524 732 13 1051 O
ATOM 1684 CB ARG A 213 -12.404 54.511 11.960 1.00 76.36 C
ANISOU 1684 CB ARG A 213 11442 7751 9821 629 5 845 C
ATOM 1685 CG ARG A 213 -12.775 54.229 13.427 1.00 83.35 C
ANISOU 1685 CG ARG A 213 12082 8729 10857 608 7 744 C
ATOM 1686 CD ARG A 213 -12.575 55.436 14.335 1.00 92.60 C
ANISOU 1686 CD ARG A 213 13222 9823 12139 584 93 717 C
ATOM 1687 NE ARG A 213 -13.296 55.313 15.605 1.00 97.26 N
ANISOU 1687 NE ARG A 213 13615 10475 12863 604 62 630 N
ATOM 1688 CZ ARG A 213 -12.719 55.339 16.804 1.00107.75 C
ANISOU 1688 CZ ARG A 213 14827 11849 14264 523 165 557 C
ATOM 1689 NH1 ARG A 213 -11.401 55.456 16.912 1.00 91.68 N
ANISOU 1689 NH1 ARG A 213 12828 9811 12197 414 294 556 N
ATOM 1690 NH2 ARG A 213 -13.453 55.223 17.903 1.00 92.19 N
ANISOU 1690 NH2 ARG A 213 12704 9925 12399 550 140 482 N
ATOM 1691 N SER A 214 -13.289 55.124 8.660 1.00 78.54 N
ANISOU 1691 N SER A 214 12275 7797 9769 834 -227 1063 N
ATOM 1692 CA SER A 214 -12.845 55.557 7.331 1.00103.45 C
ANISOU 1692 CA SER A 214 15728 10832 12747 854 -197 1168 C
ATOM 1693 C SER A 214 -13.694 56.712 6.795 1.00129.97 C
ANISOU 1693 C SER A 214 19250 14040 16095 980 -324 1237 C
ATOM 1694 O SER A 214 -14.923 56.645 6.808 1.00 90.93 O
ANISOU 1694 O SER A 214 14238 9103 11208 1095 -530 1218 O
ATOM 1695 CB SER A 214 -12.853 54.389 6.349 1.00106.55 C
ANISOU 1695 CB SER A 214 16217 11287 12980 869 -270 1185 C
ATOM 1696 N ASN A 224 -4.953 46.102 6.328 1.00 66.36 N
ANISOU 1696 N ASN A 224 10677 6894 7643 134 781 916 N
ATOM 1697 CA ASN A 224 -4.530 46.562 7.652 1.00 65.72 C
ANISOU 1697 CA ASN A 224 10378 6847 7747 70 840 863 C
ATOM 1698 C ASN A 224 -3.940 45.420 8.482 1.00 67.58 C
ANISOU 1698 C ASN A 224 10395 7213 8070 9 878 782 C
ATOM 1699 O ASN A 224 -4.324 44.264 8.288 1.00 65.62 O
ANISOU 1699 O ASN A 224 10120 7046 7765 39 796 758 O
ATOM 1700 CB ASN A 224 -5.694 47.225 8.394 1.00 68.14 C
ANISOU 1700 CB ASN A 224 10602 7153 8134 135 677 849 C
ATOM 1701 CG ASN A 224 -6.360 48.332 7.620 1.00 97.30 C
ANISOU 1701 CG ASN A 224 14501 10716 11751 210 615 926 C
ATOM 1702 OD1 ASN A 224 -5.847 49.456 7.510 1.00 94.04 O
ANISOU 1702 OD1 ASN A 224 14181 10193 11356 179 728 969 O
ATOM 1703 ND2 ASN A 224 -7.524 48.029 7.068 1.00 89.51 N
ANISOU 1703 ND2 ASN A 224 13591 9735 10683 311 428 944 N
ATOM 1704 N LYS A 225 -3.013 45.751 9.412 1.00 64.05 N
ANISOU 1704 N LYS A 225 9795 6777 7762 -74 995 740 N
ATOM 1705 CA LYS A 225 -2.302 44.799 10.284 1.00 63.16 C
ANISOU 1705 CA LYS A 225 9478 6774 7746 -134 1037 664 C
ATOM 1706 C LYS A 225 -3.207 44.009 11.226 1.00 67.63 C
ANISOU 1706 C LYS A 225 9882 7457 8357 -91 876 605 C
ATOM 1707 O LYS A 225 -3.016 42.787 11.312 1.00 67.30 O
ANISOU 1707 O LYS A 225 9765 7503 8302 -99 866 569 O
ATOM 1708 CB LYS A 225 -1.165 45.469 11.089 1.00 65.86 C
ANISOU 1708 CB LYS A 225 9700 7090 8236 -226 1171 628 C
ATOM 1709 CG LYS A 225 -0.219 46.382 10.280 1.00 70.55 C
ANISOU 1709 CG LYS A 225 10432 7553 8821 -284 1354 681 C
ATOM 1710 CD LYS A 225 0.805 47.069 11.187 1.00 72.24 C
ANISOU 1710 CD LYS A 225 10500 7741 9208 -376 1461 631 C
ATOM 1711 CE LYS A 225 1.558 48.148 10.454 1.00 82.33 C
ANISOU 1711 CE LYS A 225 11914 8872 10496 -432 1637 685 C
ATOM 1712 NZ LYS A 225 2.239 49.088 11.384 1.00 90.38 N
ANISOU 1712 NZ LYS A 225 12805 9845 11690 -511 1699 637 N
ATOM 1713 N PRO A 226 -4.185 44.638 11.952 1.00 63.47 N
ANISOU 1713 N PRO A 226 9300 6929 7889 -47 760 592 N
ATOM 1714 CA PRO A 226 -5.027 43.846 12.865 1.00 62.22 C
ANISOU 1714 CA PRO A 226 8988 6874 7780 -12 632 534 C
ATOM 1715 C PRO A 226 -5.788 42.779 12.110 1.00 64.83 C
ANISOU 1715 C PRO A 226 9372 7250 8010 46 531 545 C
ATOM 1716 O PRO A 226 -5.944 41.649 12.599 1.00 65.88 O
ANISOU 1716 O PRO A 226 9389 7478 8164 43 488 497 O
ATOM 1717 CB PRO A 226 -5.976 44.878 13.468 1.00 64.41 C
ANISOU 1717 CB PRO A 226 9242 7109 8121 34 548 532 C
ATOM 1718 CG PRO A 226 -5.361 46.194 13.221 1.00 68.92 C
ANISOU 1718 CG PRO A 226 9909 7568 8710 1 646 571 C
ATOM 1719 CD PRO A 226 -4.578 46.065 11.971 1.00 64.82 C
ANISOU 1719 CD PRO A 226 9546 6996 8087 -25 749 627 C
ATOM 1720 N LEU A 227 -6.200 43.121 10.882 1.00 58.02 N
ANISOU 1720 N LEU A 227 8699 6312 7034 96 494 608 N
ATOM 1721 CA LEU A 227 -6.915 42.207 10.012 1.00 56.69 C
ANISOU 1721 CA LEU A 227 8613 6170 6758 153 385 619 C
ATOM 1722 C LEU A 227 -6.016 41.084 9.541 1.00 58.79 C
ANISOU 1722 C LEU A 227 8899 6481 6957 108 478 608 C
ATOM 1723 O LEU A 227 -6.502 39.973 9.402 1.00 58.70 O
ANISOU 1723 O LEU A 227 8856 6536 6912 133 393 579 O
ATOM 1724 CB LEU A 227 -7.518 42.959 8.821 1.00 56.66 C
ANISOU 1724 CB LEU A 227 8830 6060 6638 223 314 691 C
ATOM 1725 CG LEU A 227 -8.998 43.342 8.925 1.00 61.75 C
ANISOU 1725 CG LEU A 227 9457 6689 7316 314 120 690 C
ATOM 1726 CD1 LEU A 227 -9.304 44.091 10.204 1.00 62.61 C
ANISOU 1726 CD1 LEU A 227 9401 6807 7583 307 118 656 C
ATOM 1727 CD2 LEU A 227 -9.411 44.198 7.771 1.00 63.03 C
ANISOU 1727 CD2 LEU A 227 9851 6733 7364 383 58 766 C
ATOM 1728 N ARG A 228 -4.705 41.351 9.357 1.00 53.22 N
ANISOU 1728 N ARG A 228 8230 5739 6251 38 657 623 N
ATOM 1729 CA ARG A 228 -3.734 40.389 8.844 1.00 51.87 C
ANISOU 1729 CA ARG A 228 8084 5596 6027 -5 773 614 C
ATOM 1730 C ARG A 228 -3.539 39.185 9.771 1.00 51.15 C
ANISOU 1730 C ARG A 228 7793 5623 6020 -31 754 542 C
ATOM 1731 O ARG A 228 -3.650 38.055 9.302 1.00 50.80 O
ANISOU 1731 O ARG A 228 7773 5622 5905 -14 726 528 O
ATOM 1732 CB ARG A 228 -2.402 41.071 8.490 1.00 54.67 C
ANISOU 1732 CB ARG A 228 8505 5873 6395 -75 979 643 C
ATOM 1733 CG ARG A 228 -1.692 40.443 7.290 1.00 72.47 C
ANISOU 1733 CG ARG A 228 10914 8094 8526 -89 1101 670 C
ATOM 1734 CD ARG A 228 -0.521 41.276 6.788 1.00 87.49 C
ANISOU 1734 CD ARG A 228 12912 9894 10438 -153 1316 710 C
ATOM 1735 NE ARG A 228 -0.960 42.450 6.026 1.00100.34 N
ANISOU 1735 NE ARG A 228 14753 11401 11972 -119 1314 786 N
ATOM 1736 CZ ARG A 228 -0.663 43.710 6.336 1.00113.12 C
ANISOU 1736 CZ ARG A 228 16372 12938 13669 -153 1385 811 C
ATOM 1737 NH1 ARG A 228 -1.113 44.708 5.586 1.00 99.63 N
ANISOU 1737 NH1 ARG A 228 14877 11115 11863 -113 1376 886 N
ATOM 1738 NH2 ARG A 228 0.090 43.983 7.395 1.00 97.43 N
ANISOU 1738 NH2 ARG A 228 14179 10979 11860 -226 1461 760 N
ATOM 1739 N LEU A 229 -3.312 39.417 11.076 1.00 43.99 N
ANISOU 1739 N LEU A 229 6702 4759 5251 -65 761 497 N
ATOM 1740 CA LEU A 229 -3.140 38.355 12.060 1.00 43.18 C
ANISOU 1740 CA LEU A 229 6423 4760 5225 -84 738 433 C
ATOM 1741 C LEU A 229 -4.377 37.437 12.115 1.00 44.91 C
ANISOU 1741 C LEU A 229 6616 5039 5407 -26 586 414 C
ATOM 1742 O LEU A 229 -4.225 36.217 12.093 1.00 43.37 O
ANISOU 1742 O LEU A 229 6380 4905 5194 -30 583 386 O
ATOM 1743 CB LEU A 229 -2.844 38.926 13.466 1.00 43.33 C
ANISOU 1743 CB LEU A 229 6281 4801 5380 -120 748 391 C
ATOM 1744 CG LEU A 229 -2.450 37.903 14.541 1.00 48.89 C
ANISOU 1744 CG LEU A 229 6818 5599 6159 -143 739 329 C
ATOM 1745 CD1 LEU A 229 -1.425 38.470 15.488 1.00 49.46 C
ANISOU 1745 CD1 LEU A 229 6782 5667 6344 -202 811 294 C
ATOM 1746 CD2 LEU A 229 -3.660 37.370 15.294 1.00 50.77 C
ANISOU 1746 CD2 LEU A 229 6982 5899 6409 -97 607 301 C
ATOM 1747 N VAL A 230 -5.571 38.029 12.250 1.00 41.35 N
ANISOU 1747 N VAL A 230 6178 4569 4966 26 466 424 N
ATOM 1748 CA VAL A 230 -6.840 37.304 12.399 1.00 41.86 C
ANISOU 1748 CA VAL A 230 6193 4680 5031 79 320 399 C
ATOM 1749 C VAL A 230 -7.161 36.511 11.139 1.00 43.75 C
ANISOU 1749 C VAL A 230 6564 4911 5148 112 265 418 C
ATOM 1750 O VAL A 230 -7.528 35.352 11.246 1.00 42.11 O
ANISOU 1750 O VAL A 230 6296 4763 4941 119 209 381 O
ATOM 1751 CB VAL A 230 -8.013 38.211 12.865 1.00 45.69 C
ANISOU 1751 CB VAL A 230 6644 5136 5580 128 214 401 C
ATOM 1752 CG1 VAL A 230 -9.205 37.368 13.318 1.00 45.46 C
ANISOU 1752 CG1 VAL A 230 6508 5164 5599 166 91 358 C
ATOM 1753 CG2 VAL A 230 -7.563 39.109 14.003 1.00 46.18 C
ANISOU 1753 CG2 VAL A 230 6612 5192 5744 92 284 384 C
ATOM 1754 N VAL A 231 -6.965 37.113 9.960 1.00 40.64 N
ANISOU 1754 N VAL A 231 6360 4438 4646 130 288 473 N
ATOM 1755 CA VAL A 231 -7.182 36.451 8.658 1.00 40.38 C
ANISOU 1755 CA VAL A 231 6492 4382 4469 163 240 492 C
ATOM 1756 C VAL A 231 -6.251 35.253 8.524 1.00 41.43 C
ANISOU 1756 C VAL A 231 6605 4565 4573 118 344 464 C
ATOM 1757 O VAL A 231 -6.705 34.178 8.149 1.00 41.48 O
ANISOU 1757 O VAL A 231 6625 4606 4529 139 267 437 O
ATOM 1758 CB VAL A 231 -7.053 37.450 7.466 1.00 44.25 C
ANISOU 1758 CB VAL A 231 7218 4763 4835 191 265 564 C
ATOM 1759 CG1 VAL A 231 -6.986 36.732 6.120 1.00 43.90 C
ANISOU 1759 CG1 VAL A 231 7371 4689 4620 215 253 582 C
ATOM 1760 CG2 VAL A 231 -8.212 38.436 7.475 1.00 44.02 C
ANISOU 1760 CG2 VAL A 231 7217 4683 4827 258 117 588 C
ATOM 1761 N LEU A 232 -4.963 35.431 8.859 1.00 36.44 N
ANISOU 1761 N LEU A 232 5929 3932 3984 56 514 464 N
ATOM 1762 CA LEU A 232 -3.998 34.350 8.796 1.00 36.25 C
ANISOU 1762 CA LEU A 232 5868 3950 3954 16 622 435 C
ATOM 1763 C LEU A 232 -4.391 33.229 9.773 1.00 36.88 C
ANISOU 1763 C LEU A 232 5770 4125 4116 16 545 376 C
ATOM 1764 O LEU A 232 -4.341 32.063 9.401 1.00 35.55 O
ANISOU 1764 O LEU A 232 5618 3989 3901 20 539 352 O
ATOM 1765 CB LEU A 232 -2.556 34.836 9.024 1.00 37.28 C
ANISOU 1765 CB LEU A 232 5962 4056 4148 -49 810 442 C
ATOM 1766 CG LEU A 232 -1.461 33.747 8.838 1.00 44.71 C
ANISOU 1766 CG LEU A 232 6869 5027 5091 -85 935 413 C
ATOM 1767 CD1 LEU A 232 -1.387 33.235 7.361 1.00 46.01 C
ANISOU 1767 CD1 LEU A 232 7246 5143 5093 -62 981 439 C
ATOM 1768 CD2 LEU A 232 -0.109 34.235 9.304 1.00 46.44 C
ANISOU 1768 CD2 LEU A 232 6995 5229 5422 -149 1099 404 C
ATOM 1769 N ALA A 233 -4.864 33.587 10.966 1.00 33.33 N
ANISOU 1769 N ALA A 233 5171 3712 3780 15 485 353 N
ATOM 1770 CA ALA A 233 -5.288 32.599 11.953 1.00 32.72 C
ANISOU 1770 CA ALA A 233 4940 3714 3777 15 423 302 C
ATOM 1771 C ALA A 233 -6.494 31.800 11.423 1.00 36.17 C
ANISOU 1771 C ALA A 233 5417 4163 4162 61 286 288 C
ATOM 1772 O ALA A 233 -6.458 30.574 11.435 1.00 34.25 O
ANISOU 1772 O ALA A 233 5139 3963 3910 55 280 256 O
ATOM 1773 CB ALA A 233 -5.614 33.276 13.273 1.00 32.63 C
ANISOU 1773 CB ALA A 233 4794 3724 3881 9 395 284 C
ATOM 1774 N VAL A 234 -7.529 32.494 10.913 1.00 33.78 N
ANISOU 1774 N VAL A 234 5190 3816 3829 107 175 311 N
ATOM 1775 CA VAL A 234 -8.724 31.837 10.375 1.00 33.86 C
ANISOU 1775 CA VAL A 234 5230 3829 3806 153 25 293 C
ATOM 1776 C VAL A 234 -8.357 30.886 9.233 1.00 37.73 C
ANISOU 1776 C VAL A 234 5855 4310 4171 154 36 291 C
ATOM 1777 O VAL A 234 -8.815 29.755 9.246 1.00 37.16 O
ANISOU 1777 O VAL A 234 5739 4275 4107 157 -27 249 O
ATOM 1778 CB VAL A 234 -9.833 32.856 9.996 1.00 37.84 C
ANISOU 1778 CB VAL A 234 5791 4277 4309 210 -106 317 C
ATOM 1779 CG1 VAL A 234 -10.976 32.195 9.217 1.00 36.85 C
ANISOU 1779 CG1 VAL A 234 5716 4142 4144 259 -276 296 C
ATOM 1780 CG2 VAL A 234 -10.366 33.545 11.252 1.00 38.13 C
ANISOU 1780 CG2 VAL A 234 5668 4330 4489 212 -123 302 C
ATOM 1781 N VAL A 235 -7.474 31.325 8.309 1.00 34.12 N
ANISOU 1781 N VAL A 235 5562 3800 3604 146 135 333 N
ATOM 1782 CA VAL A 235 -7.013 30.543 7.153 1.00 34.35 C
ANISOU 1782 CA VAL A 235 5749 3806 3496 148 174 335 C
ATOM 1783 C VAL A 235 -6.195 29.318 7.597 1.00 37.74 C
ANISOU 1783 C VAL A 235 6080 4294 3965 106 275 293 C
ATOM 1784 O VAL A 235 -6.499 28.207 7.177 1.00 35.93 O
ANISOU 1784 O VAL A 235 5881 4081 3688 117 222 259 O
ATOM 1785 CB VAL A 235 -6.269 31.430 6.102 1.00 38.48 C
ANISOU 1785 CB VAL A 235 6481 4244 3894 150 280 395 C
ATOM 1786 CG1 VAL A 235 -5.584 30.589 5.023 1.00 38.34 C
ANISOU 1786 CG1 VAL A 235 6625 4203 3740 143 368 393 C
ATOM 1787 CG2 VAL A 235 -7.225 32.428 5.455 1.00 38.70 C
ANISOU 1787 CG2 VAL A 235 6648 4204 3852 208 147 437 C
ATOM 1788 N ILE A 236 -5.187 29.515 8.461 1.00 36.37 N
ANISOU 1788 N ILE A 236 5786 4148 3884 61 409 291 N
ATOM 1789 CA ILE A 236 -4.320 28.420 8.920 1.00 36.40 C
ANISOU 1789 CA ILE A 236 5693 4202 3936 28 503 254 C
ATOM 1790 C ILE A 236 -5.136 27.312 9.603 1.00 38.11 C
ANISOU 1790 C ILE A 236 5791 4478 4211 39 395 207 C
ATOM 1791 O ILE A 236 -5.020 26.158 9.209 1.00 37.22 O
ANISOU 1791 O ILE A 236 5707 4377 4057 40 400 179 O
ATOM 1792 CB ILE A 236 -3.128 28.945 9.777 1.00 40.09 C
ANISOU 1792 CB ILE A 236 6043 4682 4508 -17 640 258 C
ATOM 1793 CG1 ILE A 236 -2.093 29.667 8.855 1.00 41.06 C
ANISOU 1793 CG1 ILE A 236 6296 4734 4569 -38 791 297 C
ATOM 1794 CG2 ILE A 236 -2.461 27.814 10.572 1.00 41.26 C
ANISOU 1794 CG2 ILE A 236 6051 4889 4735 -38 689 214 C
ATOM 1795 CD1 ILE A 236 -0.817 30.234 9.577 1.00 52.49 C
ANISOU 1795 CD1 ILE A 236 7626 6182 6136 -89 932 294 C
ATOM 1796 N PHE A 237 -5.992 27.672 10.575 1.00 33.85 N
ANISOU 1796 N PHE A 237 5130 3967 3765 46 304 197 N
ATOM 1797 CA PHE A 237 -6.815 26.706 11.302 1.00 32.52 C
ANISOU 1797 CA PHE A 237 4846 3845 3666 51 218 154 C
ATOM 1798 C PHE A 237 -7.921 26.089 10.432 1.00 36.28 C
ANISOU 1798 C PHE A 237 5400 4302 4083 82 86 134 C
ATOM 1799 O PHE A 237 -8.111 24.885 10.523 1.00 36.52 O
ANISOU 1799 O PHE A 237 5393 4357 4126 75 65 96 O
ATOM 1800 CB PHE A 237 -7.351 27.314 12.607 1.00 33.50 C
ANISOU 1800 CB PHE A 237 4827 3995 3906 48 186 148 C
ATOM 1801 CG PHE A 237 -6.248 27.540 13.627 1.00 33.87 C
ANISOU 1801 CG PHE A 237 4782 4070 4018 15 297 148 C
ATOM 1802 CD1 PHE A 237 -5.657 26.471 14.286 1.00 36.37 C
ANISOU 1802 CD1 PHE A 237 5020 4429 4371 -3 346 120 C
ATOM 1803 CD2 PHE A 237 -5.800 28.818 13.918 1.00 36.79 C
ANISOU 1803 CD2 PHE A 237 5147 4418 4414 4 343 173 C
ATOM 1804 CE1 PHE A 237 -4.609 26.674 15.191 1.00 37.34 C
ANISOU 1804 CE1 PHE A 237 5062 4573 4552 -27 428 116 C
ATOM 1805 CE2 PHE A 237 -4.750 29.022 14.827 1.00 39.77 C
ANISOU 1805 CE2 PHE A 237 5440 4817 4856 -28 431 165 C
ATOM 1806 CZ PHE A 237 -4.165 27.946 15.459 1.00 36.91 C
ANISOU 1806 CZ PHE A 237 4999 4498 4526 -41 465 135 C
ATOM 1807 N SER A 238 -8.598 26.863 9.554 1.00 32.31 N
ANISOU 1807 N SER A 238 5013 3750 3513 117 -7 158 N
ATOM 1808 CA SER A 238 -9.607 26.301 8.635 1.00 32.78 C
ANISOU 1808 CA SER A 238 5158 3784 3512 151 -154 134 C
ATOM 1809 C SER A 238 -8.967 25.261 7.711 1.00 38.70 C
ANISOU 1809 C SER A 238 6034 4523 4147 143 -104 118 C
ATOM 1810 O SER A 238 -9.546 24.204 7.480 1.00 38.94 O
ANISOU 1810 O SER A 238 6058 4561 4176 146 -186 72 O
ATOM 1811 CB SER A 238 -10.210 27.388 7.741 1.00 35.37 C
ANISOU 1811 CB SER A 238 5623 4050 3766 198 -257 169 C
ATOM 1812 OG SER A 238 -10.959 28.329 8.481 1.00 42.83 O
ANISOU 1812 OG SER A 238 6460 4995 4820 216 -320 179 O
ATOM 1813 N VAL A 239 -7.791 25.573 7.153 1.00 35.90 N
ANISOU 1813 N VAL A 239 5796 4144 3702 131 35 152 N
ATOM 1814 CA VAL A 239 -7.118 24.677 6.207 1.00 35.38 C
ANISOU 1814 CA VAL A 239 5866 4056 3519 127 104 138 C
ATOM 1815 C VAL A 239 -6.534 23.459 6.899 1.00 38.91 C
ANISOU 1815 C VAL A 239 6189 4554 4041 95 187 97 C
ATOM 1816 O VAL A 239 -6.771 22.348 6.430 1.00 38.59 O
ANISOU 1816 O VAL A 239 6195 4510 3956 99 146 57 O
ATOM 1817 CB VAL A 239 -6.060 25.406 5.317 1.00 39.28 C
ANISOU 1817 CB VAL A 239 6536 4495 3895 125 247 187 C
ATOM 1818 CG1 VAL A 239 -5.262 24.417 4.449 1.00 38.85 C
ANISOU 1818 CG1 VAL A 239 6608 4418 3733 118 353 166 C
ATOM 1819 CG2 VAL A 239 -6.707 26.490 4.447 1.00 38.56 C
ANISOU 1819 CG2 VAL A 239 6615 4338 3698 166 152 230 C
ATOM 1820 N LEU A 240 -5.785 23.661 8.009 1.00 32.54 N
ANISOU 1820 N LEU A 240 5230 3787 3345 65 293 106 N
ATOM 1821 CA LEU A 240 -5.050 22.580 8.665 1.00 31.16 C
ANISOU 1821 CA LEU A 240 4950 3652 3236 42 379 75 C
ATOM 1822 C LEU A 240 -5.868 21.719 9.617 1.00 34.43 C
ANISOU 1822 C LEU A 240 5225 4109 3748 39 290 37 C
ATOM 1823 O LEU A 240 -5.620 20.511 9.668 1.00 35.00 O
ANISOU 1823 O LEU A 240 5279 4193 3827 33 317 4 O
ATOM 1824 CB LEU A 240 -3.776 23.108 9.374 1.00 31.12 C
ANISOU 1824 CB LEU A 240 4855 3663 3304 16 525 96 C
ATOM 1825 CG LEU A 240 -2.757 23.877 8.474 1.00 35.20 C
ANISOU 1825 CG LEU A 240 5496 4129 3748 8 659 131 C
ATOM 1826 CD1 LEU A 240 -1.531 24.295 9.257 1.00 35.16 C
ANISOU 1826 CD1 LEU A 240 5370 4140 3849 -23 790 138 C
ATOM 1827 CD2 LEU A 240 -2.367 23.077 7.233 1.00 33.38 C
ANISOU 1827 CD2 LEU A 240 5426 3859 3397 19 722 119 C
ATOM 1828 N PHE A 241 -6.842 22.301 10.344 1.00 28.73 N
ANISOU 1828 N PHE A 241 4411 3404 3103 43 195 40 N
ATOM 1829 CA PHE A 241 -7.639 21.526 11.292 1.00 28.22 C
ANISOU 1829 CA PHE A 241 4214 3370 3136 35 132 6 C
ATOM 1830 C PHE A 241 -8.848 20.841 10.697 1.00 33.39 C
ANISOU 1830 C PHE A 241 4903 4004 3779 47 0 -32 C
ATOM 1831 O PHE A 241 -9.326 19.895 11.295 1.00 34.07 O
ANISOU 1831 O PHE A 241 4900 4105 3938 33 -23 -66 O
ATOM 1832 CB PHE A 241 -8.071 22.383 12.499 1.00 28.63 C
ANISOU 1832 CB PHE A 241 4138 3447 3293 31 117 19 C
ATOM 1833 CG PHE A 241 -7.055 22.642 13.592 1.00 29.27 C
ANISOU 1833 CG PHE A 241 4131 3560 3430 13 224 33 C
ATOM 1834 CD1 PHE A 241 -5.684 22.588 13.328 1.00 31.26 C
ANISOU 1834 CD1 PHE A 241 4420 3811 3645 3 334 46 C
ATOM 1835 CD2 PHE A 241 -7.468 22.996 14.878 1.00 31.00 C
ANISOU 1835 CD2 PHE A 241 4233 3802 3742 7 214 31 C
ATOM 1836 CE1 PHE A 241 -4.748 22.855 14.335 1.00 32.00 C
ANISOU 1836 CE1 PHE A 241 4424 3931 3804 -12 412 52 C
ATOM 1837 CE2 PHE A 241 -6.533 23.211 15.898 1.00 33.42 C
ANISOU 1837 CE2 PHE A 241 4471 4135 4091 -6 294 38 C
ATOM 1838 CZ PHE A 241 -5.180 23.161 15.616 1.00 31.23 C
ANISOU 1838 CZ PHE A 241 4222 3859 3785 -15 382 48 C
ATOM 1839 N THR A 242 -9.398 21.339 9.585 1.00 30.91 N
ANISOU 1839 N THR A 242 4712 3650 3382 73 -95 -27 N
ATOM 1840 CA THR A 242 -10.636 20.770 9.025 1.00 31.00 C
ANISOU 1840 CA THR A 242 4744 3637 3396 86 -251 -71 C
ATOM 1841 C THR A 242 -10.459 19.336 8.535 1.00 34.73 C
ANISOU 1841 C THR A 242 5269 4101 3826 72 -244 -116 C
ATOM 1842 O THR A 242 -11.281 18.511 8.942 1.00 33.97 O
ANISOU 1842 O THR A 242 5079 4008 3819 57 -312 -161 O
ATOM 1843 CB THR A 242 -11.250 21.694 7.947 1.00 36.47 C
ANISOU 1843 CB THR A 242 5569 4283 4004 127 -375 -54 C
ATOM 1844 OG1 THR A 242 -11.550 22.940 8.560 1.00 31.90 O
ANISOU 1844 OG1 THR A 242 4915 3710 3494 139 -387 -18 O
ATOM 1845 CG2 THR A 242 -12.514 21.116 7.294 1.00 31.23 C
ANISOU 1845 CG2 THR A 242 4929 3589 3348 145 -562 -108 C
ATOM 1846 N PRO A 243 -9.439 18.970 7.695 1.00 32.20 N
ANISOU 1846 N PRO A 243 5093 3762 3381 75 -156 -110 N
ATOM 1847 CA PRO A 243 -9.353 17.561 7.245 1.00 31.44 C
ANISOU 1847 CA PRO A 243 5047 3651 3250 64 -154 -160 C
ATOM 1848 C PRO A 243 -9.244 16.589 8.410 1.00 33.82 C
ANISOU 1848 C PRO A 243 5189 3986 3676 35 -93 -182 C
ATOM 1849 O PRO A 243 -9.936 15.574 8.412 1.00 33.32 O
ANISOU 1849 O PRO A 243 5097 3908 3654 21 -162 -232 O
ATOM 1850 CB PRO A 243 -8.111 17.541 6.340 1.00 32.31 C
ANISOU 1850 CB PRO A 243 5320 3736 3220 74 -27 -141 C
ATOM 1851 CG PRO A 243 -7.941 18.948 5.901 1.00 35.70 C
ANISOU 1851 CG PRO A 243 5835 4148 3580 94 -20 -87 C
ATOM 1852 CD PRO A 243 -8.368 19.784 7.072 1.00 32.39 C
ANISOU 1852 CD PRO A 243 5244 3768 3294 86 -46 -62 C
ATOM 1853 N TYR A 244 -8.433 16.936 9.428 1.00 30.15 N
ANISOU 1853 N TYR A 244 4623 3559 3273 25 26 -146 N
ATOM 1854 CA TYR A 244 -8.247 16.105 10.620 1.00 29.69 C
ANISOU 1854 CA TYR A 244 4431 3530 3321 5 85 -157 C
ATOM 1855 C TYR A 244 -9.532 15.930 11.435 1.00 32.99 C
ANISOU 1855 C TYR A 244 4726 3953 3855 -10 -5 -179 C
ATOM 1856 O TYR A 244 -9.817 14.823 11.880 1.00 32.41 O
ANISOU 1856 O TYR A 244 4600 3873 3841 -29 -1 -211 O
ATOM 1857 CB TYR A 244 -7.105 16.636 11.497 1.00 29.98 C
ANISOU 1857 CB TYR A 244 4399 3601 3391 4 209 -116 C
ATOM 1858 CG TYR A 244 -7.092 16.042 12.891 1.00 29.44 C
ANISOU 1858 CG TYR A 244 4196 3560 3428 -8 243 -120 C
ATOM 1859 CD1 TYR A 244 -6.660 14.731 13.112 1.00 30.53 C
ANISOU 1859 CD1 TYR A 244 4327 3692 3582 -11 292 -142 C
ATOM 1860 CD2 TYR A 244 -7.527 16.781 13.986 1.00 29.38 C
ANISOU 1860 CD2 TYR A 244 4085 3578 3499 -14 227 -101 C
ATOM 1861 CE1 TYR A 244 -6.652 14.181 14.394 1.00 29.23 C
ANISOU 1861 CE1 TYR A 244 4062 3542 3501 -17 322 -140 C
ATOM 1862 CE2 TYR A 244 -7.570 16.225 15.262 1.00 29.39 C
ANISOU 1862 CE2 TYR A 244 3991 3596 3580 -23 259 -103 C
ATOM 1863 CZ TYR A 244 -7.104 14.937 15.467 1.00 33.94 C
ANISOU 1863 CZ TYR A 244 4570 4164 4163 -24 306 -119 C
ATOM 1864 OH TYR A 244 -7.092 14.447 16.742 1.00 30.10 O
ANISOU 1864 OH TYR A 244 4009 3687 3741 -27 339 -113 O
ATOM 1865 N HIS A 245 -10.289 17.018 11.647 1.00 29.65 N
ANISOU 1865 N HIS A 245 4257 3536 3472 -3 -76 -163 N
ATOM 1866 CA HIS A 245 -11.526 16.926 12.415 1.00 27.58 C
ANISOU 1866 CA HIS A 245 3870 3273 3336 -17 -146 -187 C
ATOM 1867 C HIS A 245 -12.595 16.167 11.635 1.00 32.37 C
ANISOU 1867 C HIS A 245 4499 3840 3960 -24 -272 -244 C
ATOM 1868 O HIS A 245 -13.333 15.400 12.237 1.00 31.79 O
ANISOU 1868 O HIS A 245 4327 3756 3995 -50 -287 -278 O
ATOM 1869 CB HIS A 245 -11.988 18.295 12.910 1.00 27.09 C
ANISOU 1869 CB HIS A 245 3744 3223 3324 -3 -174 -158 C
ATOM 1870 CG HIS A 245 -11.210 18.749 14.102 1.00 29.20 C
ANISOU 1870 CG HIS A 245 3944 3527 3624 -10 -57 -121 C
ATOM 1871 ND1 HIS A 245 -10.020 19.446 13.964 1.00 29.48 N
ANISOU 1871 ND1 HIS A 245 4036 3578 3586 0 19 -82 N
ATOM 1872 CD2 HIS A 245 -11.443 18.534 15.419 1.00 29.70 C
ANISOU 1872 CD2 HIS A 245 3896 3607 3782 -26 -6 -123 C
ATOM 1873 CE1 HIS A 245 -9.585 19.650 15.196 1.00 28.46 C
ANISOU 1873 CE1 HIS A 245 3823 3478 3513 -9 94 -66 C
ATOM 1874 NE2 HIS A 245 -10.408 19.124 16.104 1.00 28.69 N
ANISOU 1874 NE2 HIS A 245 3760 3508 3632 -22 83 -87 N
ATOM 1875 N ILE A 246 -12.642 16.313 10.297 1.00 29.79 N
ANISOU 1875 N ILE A 246 4310 3484 3524 -2 -358 -256 N
ATOM 1876 CA ILE A 246 -13.587 15.509 9.519 1.00 30.10 C
ANISOU 1876 CA ILE A 246 4382 3481 3574 -8 -493 -319 C
ATOM 1877 C ILE A 246 -13.217 14.021 9.665 1.00 34.29 C
ANISOU 1877 C ILE A 246 4914 4001 4114 -39 -424 -355 C
ATOM 1878 O ILE A 246 -14.062 13.222 10.066 1.00 34.99 O
ANISOU 1878 O ILE A 246 4908 4070 4318 -70 -467 -401 O
ATOM 1879 CB ILE A 246 -13.685 15.904 8.021 1.00 32.74 C
ANISOU 1879 CB ILE A 246 4894 3779 3765 27 -610 -328 C
ATOM 1880 CG1 ILE A 246 -14.222 17.342 7.831 1.00 32.52 C
ANISOU 1880 CG1 ILE A 246 4871 3748 3737 64 -702 -295 C
ATOM 1881 CG2 ILE A 246 -14.534 14.869 7.237 1.00 33.44 C
ANISOU 1881 CG2 ILE A 246 5026 3821 3859 17 -751 -406 C
ATOM 1882 CD1 ILE A 246 -14.067 17.908 6.356 1.00 36.29 C
ANISOU 1882 CD1 ILE A 246 5568 4185 4035 109 -793 -283 C
ATOM 1883 N MET A 247 -11.947 13.671 9.397 1.00 30.75 N
ANISOU 1883 N MET A 247 4563 3561 3560 -32 -306 -334 N
ATOM 1884 CA MET A 247 -11.475 12.273 9.391 1.00 30.03 C
ANISOU 1884 CA MET A 247 4497 3452 3462 -51 -239 -366 C
ATOM 1885 C MET A 247 -11.481 11.593 10.763 1.00 33.52 C
ANISOU 1885 C MET A 247 4796 3909 4032 -79 -154 -362 C
ATOM 1886 O MET A 247 -11.774 10.409 10.816 1.00 33.55 O
ANISOU 1886 O MET A 247 4789 3881 4080 -103 -157 -404 O
ATOM 1887 CB MET A 247 -10.111 12.151 8.708 1.00 32.45 C
ANISOU 1887 CB MET A 247 4941 3757 3633 -29 -130 -346 C
ATOM 1888 CG MET A 247 -10.199 12.374 7.176 1.00 36.55 C
ANISOU 1888 CG MET A 247 5648 4237 4003 -6 -211 -368 C
ATOM 1889 SD MET A 247 -11.450 11.295 6.387 1.00 42.91 S
ANISOU 1889 SD MET A 247 6504 4984 4816 -23 -385 -459 S
ATOM 1890 CE MET A 247 -12.421 12.408 5.784 1.00 40.24 C
ANISOU 1890 CE MET A 247 6202 4636 4453 0 -556 -457 C
ATOM 1891 N ARG A 248 -11.221 12.318 11.859 1.00 29.67 N
ANISOU 1891 N ARG A 248 4210 3463 3601 -76 -85 -313 N
ATOM 1892 CA ARG A 248 -11.283 11.692 13.186 1.00 30.46 C
ANISOU 1892 CA ARG A 248 4197 3569 3806 -97 -9 -306 C
ATOM 1893 C ARG A 248 -12.734 11.229 13.438 1.00 34.83 C
ANISOU 1893 C ARG A 248 4664 4088 4481 -132 -90 -352 C
ATOM 1894 O ARG A 248 -12.946 10.108 13.849 1.00 33.91 O
ANISOU 1894 O ARG A 248 4518 3941 4425 -159 -55 -377 O
ATOM 1895 CB ARG A 248 -10.834 12.662 14.297 1.00 27.19 C
ANISOU 1895 CB ARG A 248 3709 3200 3420 -86 62 -251 C
ATOM 1896 CG ARG A 248 -10.774 11.967 15.662 1.00 30.05 C
ANISOU 1896 CG ARG A 248 3991 3564 3863 -101 145 -240 C
ATOM 1897 CD ARG A 248 -10.279 12.888 16.752 1.00 30.57 C
ANISOU 1897 CD ARG A 248 4004 3671 3943 -86 206 -193 C
ATOM 1898 NE ARG A 248 -11.311 13.850 17.139 1.00 31.74 N
ANISOU 1898 NE ARG A 248 4079 3824 4157 -95 159 -192 N
ATOM 1899 CZ ARG A 248 -11.066 15.037 17.681 1.00 36.99 C
ANISOU 1899 CZ ARG A 248 4715 4520 4818 -80 177 -158 C
ATOM 1900 NH1 ARG A 248 -9.819 15.432 17.895 1.00 26.48 N
ANISOU 1900 NH1 ARG A 248 3416 3219 3427 -60 234 -126 N
ATOM 1901 NH2 ARG A 248 -12.063 15.840 18.002 1.00 25.32 N
ANISOU 1901 NH2 ARG A 248 3172 3038 3409 -84 137 -163 N
ATOM 1902 N ASN A 249 -13.707 12.091 13.135 1.00 32.85 N
ANISOU 1902 N ASN A 249 4375 3835 4271 -129 -197 -365 N
ATOM 1903 CA ASN A 249 -15.121 11.817 13.282 1.00 34.01 C
ANISOU 1903 CA ASN A 249 4421 3946 4556 -159 -283 -414 C
ATOM 1904 C ASN A 249 -15.612 10.732 12.306 1.00 38.35 C
ANISOU 1904 C ASN A 249 5023 4442 5104 -181 -377 -484 C
ATOM 1905 O ASN A 249 -16.407 9.888 12.709 1.00 36.42 O
ANISOU 1905 O ASN A 249 4693 4158 4985 -223 -383 -527 O
ATOM 1906 CB ASN A 249 -15.921 13.118 13.162 1.00 31.19 C
ANISOU 1906 CB ASN A 249 4009 3599 4243 -139 -380 -408 C
ATOM 1907 CG ASN A 249 -15.761 13.968 14.399 1.00 41.19 C
ANISOU 1907 CG ASN A 249 5188 4902 5560 -133 -281 -357 C
ATOM 1908 OD1 ASN A 249 -16.120 13.557 15.502 1.00 34.35 O
ANISOU 1908 OD1 ASN A 249 4224 4028 4798 -160 -201 -359 O
ATOM 1909 ND2 ASN A 249 -15.218 15.171 14.245 1.00 28.65 N
ANISOU 1909 ND2 ASN A 249 3644 3346 3894 -97 -281 -312 N
ATOM 1910 N VAL A 250 -15.111 10.737 11.046 1.00 35.09 N
ANISOU 1910 N VAL A 250 4759 4022 4549 -155 -441 -496 N
ATOM 1911 CA VAL A 250 -15.480 9.739 10.041 1.00 34.87 C
ANISOU 1911 CA VAL A 250 4811 3942 4496 -171 -536 -567 C
ATOM 1912 C VAL A 250 -14.897 8.359 10.427 1.00 39.65 C
ANISOU 1912 C VAL A 250 5432 4525 5111 -199 -419 -580 C
ATOM 1913 O VAL A 250 -15.589 7.339 10.298 1.00 39.53 O
ANISOU 1913 O VAL A 250 5389 4455 5174 -238 -467 -643 O
ATOM 1914 CB VAL A 250 -15.124 10.185 8.599 1.00 38.79 C
ANISOU 1914 CB VAL A 250 5488 4431 4821 -130 -630 -574 C
ATOM 1915 CG1 VAL A 250 -15.268 9.024 7.597 1.00 38.57 C
ANISOU 1915 CG1 VAL A 250 5572 4345 4737 -145 -704 -649 C
ATOM 1916 CG2 VAL A 250 -15.986 11.372 8.166 1.00 37.99 C
ANISOU 1916 CG2 VAL A 250 5371 4331 4733 -103 -782 -574 C
ATOM 1917 N ARG A 251 -13.654 8.347 10.967 1.00 34.56 N
ANISOU 1917 N ARG A 251 4817 3914 4399 -179 -270 -522 N
ATOM 1918 CA ARG A 251 -12.990 7.136 11.441 1.00 33.88 C
ANISOU 1918 CA ARG A 251 4744 3808 4323 -192 -154 -523 C
ATOM 1919 C ARG A 251 -13.844 6.465 12.532 1.00 37.87 C
ANISOU 1919 C ARG A 251 5118 4283 4990 -238 -125 -537 C
ATOM 1920 O ARG A 251 -14.076 5.253 12.474 1.00 36.86 O
ANISOU 1920 O ARG A 251 5000 4098 4906 -269 -115 -581 O
ATOM 1921 CB ARG A 251 -11.567 7.466 11.956 1.00 32.79 C
ANISOU 1921 CB ARG A 251 4632 3716 4111 -155 -17 -455 C
ATOM 1922 CG ARG A 251 -10.859 6.349 12.730 1.00 38.78 C
ANISOU 1922 CG ARG A 251 5380 4456 4898 -157 103 -442 C
ATOM 1923 CD ARG A 251 -10.572 5.161 11.846 1.00 41.59 C
ANISOU 1923 CD ARG A 251 5840 4758 5202 -159 103 -493 C
ATOM 1924 NE ARG A 251 -9.562 4.274 12.415 1.00 47.95 N
ANISOU 1924 NE ARG A 251 6661 5551 6008 -140 225 -471 N
ATOM 1925 CZ ARG A 251 -9.625 2.950 12.377 1.00 55.58 C
ANISOU 1925 CZ ARG A 251 7658 6454 7004 -155 250 -508 C
ATOM 1926 NH1 ARG A 251 -10.670 2.346 11.838 1.00 39.96 N
ANISOU 1926 NH1 ARG A 251 5693 4423 5069 -199 164 -573 N
ATOM 1927 NH2 ARG A 251 -8.651 2.219 12.897 1.00 49.76 N
ANISOU 1927 NH2 ARG A 251 6936 5704 6266 -127 355 -483 N
ATOM 1928 N ILE A 252 -14.326 7.260 13.512 1.00 33.10 N
ANISOU 1928 N ILE A 252 4397 3707 4472 -244 -104 -502 N
ATOM 1929 CA ILE A 252 -15.159 6.728 14.599 1.00 31.58 C
ANISOU 1929 CA ILE A 252 4086 3481 4432 -288 -53 -511 C
ATOM 1930 C ILE A 252 -16.512 6.232 14.069 1.00 37.45 C
ANISOU 1930 C ILE A 252 4769 4163 5296 -336 -166 -592 C
ATOM 1931 O ILE A 252 -16.911 5.127 14.410 1.00 37.07 O
ANISOU 1931 O ILE A 252 4690 4057 5339 -380 -123 -624 O
ATOM 1932 CB ILE A 252 -15.328 7.764 15.747 1.00 32.42 C
ANISOU 1932 CB ILE A 252 4097 3629 4592 -279 6 -458 C
ATOM 1933 CG1 ILE A 252 -13.951 8.152 16.337 1.00 31.20 C
ANISOU 1933 CG1 ILE A 252 3997 3528 4330 -235 109 -388 C
ATOM 1934 CG2 ILE A 252 -16.268 7.214 16.834 1.00 31.91 C
ANISOU 1934 CG2 ILE A 252 3922 3517 4684 -327 75 -470 C
ATOM 1935 CD1 ILE A 252 -13.909 9.467 17.119 1.00 31.11 C
ANISOU 1935 CD1 ILE A 252 3928 3566 4325 -214 136 -340 C
ATOM 1936 N ALA A 253 -17.213 7.066 13.278 1.00 36.73 N
ANISOU 1936 N ALA A 253 4660 4082 5215 -325 -311 -623 N
ATOM 1937 CA ALA A 253 -18.532 6.777 12.699 1.00 38.81 C
ANISOU 1937 CA ALA A 253 4854 4290 5604 -362 -453 -706 C
ATOM 1938 C ALA A 253 -18.530 5.480 11.865 1.00 45.30 C
ANISOU 1938 C ALA A 253 5759 5050 6402 -391 -504 -774 C
ATOM 1939 O ALA A 253 -19.443 4.674 12.016 1.00 45.57 O
ANISOU 1939 O ALA A 253 5706 5020 6588 -448 -530 -836 O
ATOM 1940 CB ALA A 253 -19.019 7.962 11.861 1.00 39.43 C
ANISOU 1940 CB ALA A 253 4937 4392 5653 -325 -616 -718 C
ATOM 1941 N SER A 254 -17.461 5.237 11.070 1.00 42.59 N
ANISOU 1941 N SER A 254 5583 4721 5880 -356 -497 -763 N
ATOM 1942 CA SER A 254 -17.293 4.004 10.289 1.00 42.31 C
ANISOU 1942 CA SER A 254 5651 4626 5800 -376 -526 -826 C
ATOM 1943 C SER A 254 -17.213 2.739 11.174 1.00 47.34 C
ANISOU 1943 C SER A 254 6241 5212 6533 -422 -390 -829 C
ATOM 1944 O SER A 254 -17.425 1.632 10.679 1.00 47.59 O
ANISOU 1944 O SER A 254 6318 5176 6587 -456 -422 -895 O
ATOM 1945 CB SER A 254 -16.070 4.108 9.377 1.00 44.89 C
ANISOU 1945 CB SER A 254 6164 4977 5914 -323 -508 -804 C
ATOM 1946 OG SER A 254 -14.860 3.941 10.092 1.00 49.98 O
ANISOU 1946 OG SER A 254 6833 5655 6501 -299 -332 -734 O
ATOM 1947 N ARG A 255 -16.890 2.896 12.471 1.00 43.49 N
ANISOU 1947 N ARG A 255 5678 4752 6093 -421 -242 -758 N
ATOM 1948 CA ARG A 255 -16.800 1.767 13.401 1.00 42.54 C
ANISOU 1948 CA ARG A 255 5529 4580 6053 -456 -107 -749 C
ATOM 1949 C ARG A 255 -18.143 1.453 14.071 1.00 46.42 C
ANISOU 1949 C ARG A 255 5871 5012 6753 -526 -105 -787 C
ATOM 1950 O ARG A 255 -18.226 0.479 14.812 1.00 46.45 O
ANISOU 1950 O ARG A 255 5857 4957 6837 -564 7 -784 O
ATOM 1951 CB ARG A 255 -15.713 1.997 14.467 1.00 40.64 C
ANISOU 1951 CB ARG A 255 5308 4387 5746 -415 48 -654 C
ATOM 1952 CG ARG A 255 -14.293 2.078 13.912 1.00 41.62 C
ANISOU 1952 CG ARG A 255 5563 4553 5696 -353 76 -621 C
ATOM 1953 CD ARG A 255 -13.267 1.888 15.010 1.00 40.18 C
ANISOU 1953 CD ARG A 255 5392 4391 5484 -319 221 -546 C
ATOM 1954 NE ARG A 255 -13.300 2.989 15.969 1.00 46.70 N
ANISOU 1954 NE ARG A 255 6139 5276 6329 -304 256 -486 N
ATOM 1955 CZ ARG A 255 -13.543 2.857 17.269 1.00 50.88 C
ANISOU 1955 CZ ARG A 255 6608 5792 6934 -318 347 -447 C
ATOM 1956 NH1 ARG A 255 -13.761 1.657 17.792 1.00 32.51 N
ANISOU 1956 NH1 ARG A 255 4290 3392 4672 -349 419 -456 N
ATOM 1957 NH2 ARG A 255 -13.537 3.921 18.061 1.00 40.42 N
ANISOU 1957 NH2 ARG A 255 5228 4520 5611 -301 373 -399 N
ATOM 1958 N LEU A 256 -19.193 2.258 13.819 1.00 44.05 N
ANISOU 1958 N LEU A 256 5465 4721 6550 -541 -221 -824 N
ATOM 1959 CA LEU A 256 -20.513 2.030 14.441 1.00 53.48 C
ANISOU 1959 CA LEU A 256 6495 5856 7968 -608 -211 -867 C
ATOM 1960 C LEU A 256 -21.191 0.779 13.909 1.00 91.22 C
ANISOU 1960 C LEU A 256 11262 10539 12860 -675 -268 -961 C
ATOM 1961 O LEU A 256 -21.386 0.666 12.707 1.00 62.22 O
ANISOU 1961 O LEU A 256 7641 6851 9147 -672 -434 -1030 O
ATOM 1962 CB LEU A 256 -21.446 3.242 14.294 1.00 52.75 C
ANISOU 1962 CB LEU A 256 6280 5795 7968 -599 -327 -886 C
ATOM 1963 CG LEU A 256 -21.178 4.431 15.202 1.00 56.57 C
ANISOU 1963 CG LEU A 256 6720 6349 8425 -558 -239 -803 C
ATOM 1964 CD1 LEU A 256 -21.900 5.652 14.700 1.00 56.25 C
ANISOU 1964 CD1 LEU A 256 6602 6341 8431 -530 -388 -826 C
ATOM 1965 CD2 LEU A 256 -21.578 4.133 16.644 1.00 58.29 C
ANISOU 1965 CD2 LEU A 256 6838 6531 8779 -600 -58 -773 C
ATOM 1966 N GLY A 262 -13.786 -4.592 7.228 1.00 75.91 N
ANISOU 1966 N GLY A 262 10679 8444 9720 -424 -211 -1120 N
ATOM 1967 CA GLY A 262 -14.032 -4.205 5.842 1.00 75.18 C
ANISOU 1967 CA GLY A 262 10713 8349 9504 -412 -362 -1188 C
ATOM 1968 C GLY A 262 -12.957 -3.305 5.263 1.00 76.21 C
ANISOU 1968 C GLY A 262 10963 8548 9445 -336 -316 -1134 C
ATOM 1969 O GLY A 262 -12.233 -2.642 6.016 1.00 75.91 O
ANISOU 1969 O GLY A 262 10862 8581 9401 -300 -201 -1042 O
ATOM 1970 N CYS A 263 -12.839 -3.278 3.911 1.00 69.73 N
ANISOU 1970 N CYS A 263 10324 7701 8468 -314 -403 -1195 N
ATOM 1971 CA CYS A 263 -11.833 -2.451 3.225 1.00 67.73 C
ANISOU 1971 CA CYS A 263 10209 7498 8027 -246 -346 -1150 C
ATOM 1972 C CYS A 263 -12.105 -0.941 3.368 1.00 65.54 C
ANISOU 1972 C CYS A 263 9866 7303 7732 -227 -411 -1087 C
ATOM 1973 O CYS A 263 -11.157 -0.164 3.459 1.00 64.44 O
ANISOU 1973 O CYS A 263 9753 7222 7509 -180 -301 -1012 O
ATOM 1974 CB CYS A 263 -11.653 -2.869 1.767 1.00 68.09 C
ANISOU 1974 CB CYS A 263 10490 7482 7900 -227 -406 -1231 C
ATOM 1975 SG CYS A 263 -10.791 -4.459 1.533 1.00 72.14 S
ANISOU 1975 SG CYS A 263 11119 7907 8386 -220 -260 -1283 S
ATOM 1976 N SER A 264 -13.394 -0.548 3.442 1.00 57.81 N
ANISOU 1976 N SER A 264 8790 6324 6851 -265 -583 -1119 N
ATOM 1977 CA SER A 264 -13.849 0.830 3.617 1.00 55.82 C
ANISOU 1977 CA SER A 264 8460 6138 6610 -250 -664 -1069 C
ATOM 1978 C SER A 264 -13.262 1.410 4.906 1.00 55.18 C
ANISOU 1978 C SER A 264 8232 6130 6604 -238 -508 -966 C
ATOM 1979 O SER A 264 -12.752 2.531 4.875 1.00 54.03 O
ANISOU 1979 O SER A 264 8106 6045 6378 -197 -475 -900 O
ATOM 1980 CB SER A 264 -15.375 0.886 3.653 1.00 59.36 C
ANISOU 1980 CB SER A 264 8790 6559 7203 -297 -861 -1132 C
ATOM 1981 OG SER A 264 -15.857 2.178 3.982 1.00 71.03 O
ANISOU 1981 OG SER A 264 10168 8098 8723 -281 -928 -1081 O
ATOM 1982 N GLN A 265 -13.283 0.616 6.011 1.00 48.98 N
ANISOU 1982 N GLN A 265 7317 5331 5964 -272 -408 -954 N
ATOM 1983 CA GLN A 265 -12.747 0.983 7.325 1.00 47.95 C
ANISOU 1983 CA GLN A 265 7058 5257 5906 -262 -265 -864 C
ATOM 1984 C GLN A 265 -11.244 1.236 7.263 1.00 47.14 C
ANISOU 1984 C GLN A 265 7040 5192 5678 -204 -119 -803 C
ATOM 1985 O GLN A 265 -10.804 2.268 7.746 1.00 45.17 O
ANISOU 1985 O GLN A 265 6738 5011 5415 -177 -71 -733 O
ATOM 1986 CB GLN A 265 -13.099 -0.071 8.389 1.00 49.76 C
ANISOU 1986 CB GLN A 265 7173 5441 6293 -307 -194 -871 C
ATOM 1987 CG GLN A 265 -14.042 0.466 9.475 1.00 73.47 C
ANISOU 1987 CG GLN A 265 9994 8467 9452 -343 -213 -842 C
ATOM 1988 CD GLN A 265 -13.908 -0.225 10.823 1.00 98.18 C
ANISOU 1988 CD GLN A 265 13032 11578 12695 -365 -73 -801 C
ATOM 1989 OE1 GLN A 265 -14.877 -0.776 11.358 1.00 95.22 O
ANISOU 1989 OE1 GLN A 265 12562 11150 12467 -423 -84 -832 O
ATOM 1990 NE2 GLN A 265 -12.715 -0.196 11.421 1.00 88.45 N
ANISOU 1990 NE2 GLN A 265 11826 10381 11399 -318 60 -730 N
ATOM 1991 N LYS A 266 -10.473 0.344 6.600 1.00 42.19 N
ANISOU 1991 N LYS A 266 6547 4520 4965 -184 -53 -837 N
ATOM 1992 CA LYS A 266 -9.022 0.508 6.433 1.00 41.97 C
ANISOU 1992 CA LYS A 266 6595 4516 4834 -129 92 -791 C
ATOM 1993 C LYS A 266 -8.691 1.671 5.513 1.00 44.93 C
ANISOU 1993 C LYS A 266 7075 4928 5067 -96 66 -772 C
ATOM 1994 O LYS A 266 -7.704 2.374 5.757 1.00 44.21 O
ANISOU 1994 O LYS A 266 6971 4886 4940 -60 177 -708 O
ATOM 1995 CB LYS A 266 -8.337 -0.787 5.951 1.00 44.57 C
ANISOU 1995 CB LYS A 266 7036 4776 5122 -114 177 -838 C
ATOM 1996 CG LYS A 266 -8.144 -1.782 7.078 1.00 53.89 C
ANISOU 1996 CG LYS A 266 8115 5930 6432 -124 265 -821 C
ATOM 1997 CD LYS A 266 -7.084 -2.827 6.759 1.00 62.49 C
ANISOU 1997 CD LYS A 266 9299 6965 7480 -86 388 -841 C
ATOM 1998 CE LYS A 266 -6.831 -3.745 7.935 1.00 65.48 C
ANISOU 1998 CE LYS A 266 9584 7314 7981 -84 472 -812 C
ATOM 1999 NZ LYS A 266 -6.203 -3.027 9.087 1.00 69.51 N
ANISOU 1999 NZ LYS A 266 9971 7897 8543 -52 543 -720 N
ATOM 2000 N ALA A 267 -9.548 1.923 4.500 1.00 41.27 N
ANISOU 2000 N ALA A 267 6712 4438 4530 -108 -87 -826 N
ATOM 2001 CA ALA A 267 -9.354 3.049 3.577 1.00 41.27 C
ANISOU 2001 CA ALA A 267 6837 4461 4382 -75 -126 -806 C
ATOM 2002 C ALA A 267 -9.573 4.383 4.309 1.00 43.50 C
ANISOU 2002 C ALA A 267 6989 4817 4722 -71 -146 -732 C
ATOM 2003 O ALA A 267 -8.789 5.316 4.133 1.00 43.16 O
ANISOU 2003 O ALA A 267 6991 4810 4597 -38 -67 -676 O
ATOM 2004 CB ALA A 267 -10.287 2.928 2.391 1.00 41.90 C
ANISOU 2004 CB ALA A 267 7059 4487 4372 -84 -308 -885 C
ATOM 2005 N ILE A 268 -10.598 4.451 5.180 1.00 38.06 N
ANISOU 2005 N ILE A 268 6133 4143 4184 -107 -233 -733 N
ATOM 2006 CA ILE A 268 -10.886 5.638 5.978 1.00 36.15 C
ANISOU 2006 CA ILE A 268 5758 3964 4013 -105 -248 -670 C
ATOM 2007 C ILE A 268 -9.731 5.895 6.984 1.00 36.70 C
ANISOU 2007 C ILE A 268 5746 4084 4114 -86 -70 -595 C
ATOM 2008 O ILE A 268 -9.322 7.042 7.176 1.00 34.54 O
ANISOU 2008 O ILE A 268 5453 3860 3813 -65 -36 -537 O
ATOM 2009 CB ILE A 268 -12.298 5.535 6.631 1.00 39.34 C
ANISOU 2009 CB ILE A 268 6006 4359 4581 -149 -370 -701 C
ATOM 2010 CG1 ILE A 268 -13.397 5.807 5.568 1.00 39.78 C
ANISOU 2010 CG1 ILE A 268 6132 4379 4603 -152 -577 -764 C
ATOM 2011 CG2 ILE A 268 -12.448 6.502 7.838 1.00 37.66 C
ANISOU 2011 CG2 ILE A 268 5628 4207 4472 -150 -329 -633 C
ATOM 2012 CD1 ILE A 268 -14.762 5.152 5.880 1.00 47.08 C
ANISOU 2012 CD1 ILE A 268 6929 5261 5697 -205 -702 -834 C
ATOM 2013 N ASN A 269 -9.186 4.818 7.580 1.00 32.53 N
ANISOU 2013 N ASN A 269 5181 3538 3642 -92 35 -600 N
ATOM 2014 CA ASN A 269 -8.068 4.930 8.499 1.00 32.36 C
ANISOU 2014 CA ASN A 269 5088 3554 3651 -68 183 -538 C
ATOM 2015 C ASN A 269 -6.825 5.532 7.816 1.00 36.94 C
ANISOU 2015 C ASN A 269 5768 4154 4115 -26 279 -509 C
ATOM 2016 O ASN A 269 -6.099 6.309 8.441 1.00 36.28 O
ANISOU 2016 O ASN A 269 5614 4118 4052 -8 356 -451 O
ATOM 2017 CB ASN A 269 -7.748 3.594 9.146 1.00 31.98 C
ANISOU 2017 CB ASN A 269 5004 3470 3677 -74 260 -552 C
ATOM 2018 CG ASN A 269 -6.751 3.723 10.265 1.00 47.90 C
ANISOU 2018 CG ASN A 269 6930 5524 5744 -46 379 -488 C
ATOM 2019 OD1 ASN A 269 -6.818 4.639 11.091 1.00 38.29 O
ANISOU 2019 OD1 ASN A 269 5616 4360 4571 -46 377 -439 O
ATOM 2020 ND2 ASN A 269 -5.797 2.820 10.305 1.00 37.65 N
ANISOU 2020 ND2 ASN A 269 5665 4197 4442 -17 478 -493 N
ATOM 2021 N CYS A 270 -6.594 5.167 6.538 1.00 35.51 N
ANISOU 2021 N CYS A 270 5753 3926 3812 -14 279 -553 N
ATOM 2022 CA CYS A 270 -5.507 5.690 5.709 1.00 36.14 C
ANISOU 2022 CA CYS A 270 5954 4007 3773 21 383 -534 C
ATOM 2023 C CYS A 270 -5.699 7.174 5.463 1.00 39.47 C
ANISOU 2023 C CYS A 270 6391 4466 4140 26 338 -489 C
ATOM 2024 O CYS A 270 -4.757 7.932 5.665 1.00 39.64 O
ANISOU 2024 O CYS A 270 6389 4518 4156 44 448 -438 O
ATOM 2025 CB CYS A 270 -5.382 4.904 4.407 1.00 36.43 C
ANISOU 2025 CB CYS A 270 6184 3974 3683 32 389 -598 C
ATOM 2026 SG CYS A 270 -4.729 3.230 4.640 1.00 40.85 S
ANISOU 2026 SG CYS A 270 6740 4483 4300 40 497 -642 S
ATOM 2027 N LEU A 271 -6.933 7.608 5.131 1.00 36.76 N
ANISOU 2027 N LEU A 271 6070 4118 3779 10 172 -508 N
ATOM 2028 CA LEU A 271 -7.247 9.031 4.961 1.00 37.48 C
ANISOU 2028 CA LEU A 271 6171 4239 3832 19 111 -464 C
ATOM 2029 C LEU A 271 -7.006 9.763 6.278 1.00 37.29 C
ANISOU 2029 C LEU A 271 5964 4277 3929 12 166 -403 C
ATOM 2030 O LEU A 271 -6.441 10.855 6.269 1.00 36.14 O
ANISOU 2030 O LEU A 271 5826 4157 3749 27 223 -352 O
ATOM 2031 CB LEU A 271 -8.720 9.254 4.555 1.00 38.95 C
ANISOU 2031 CB LEU A 271 6375 4406 4016 6 -96 -501 C
ATOM 2032 CG LEU A 271 -9.161 8.942 3.129 1.00 45.83 C
ANISOU 2032 CG LEU A 271 7453 5216 4743 19 -207 -559 C
ATOM 2033 CD1 LEU A 271 -10.660 9.249 2.974 1.00 47.03 C
ANISOU 2033 CD1 LEU A 271 7570 5357 4942 9 -432 -595 C
ATOM 2034 CD2 LEU A 271 -8.366 9.760 2.105 1.00 47.98 C
ANISOU 2034 CD2 LEU A 271 7922 5473 4836 56 -137 -524 C
ATOM 2035 N TYR A 272 -7.422 9.140 7.409 1.00 31.04 N
ANISOU 2035 N TYR A 272 5018 3501 3274 -10 153 -410 N
ATOM 2036 CA TYR A 272 -7.266 9.706 8.742 1.00 30.04 C
ANISOU 2036 CA TYR A 272 4730 3427 3258 -15 198 -360 C
ATOM 2037 C TYR A 272 -5.785 9.909 9.099 1.00 33.31 C
ANISOU 2037 C TYR A 272 5125 3864 3665 7 353 -318 C
ATOM 2038 O TYR A 272 -5.427 10.978 9.590 1.00 32.38 O
ANISOU 2038 O TYR A 272 4948 3786 3568 13 384 -271 O
ATOM 2039 CB TYR A 272 -8.050 8.857 9.764 1.00 30.55 C
ANISOU 2039 CB TYR A 272 4671 3487 3452 -44 161 -380 C
ATOM 2040 CG TYR A 272 -7.767 9.104 11.230 1.00 31.51 C
ANISOU 2040 CG TYR A 272 4650 3649 3674 -46 228 -334 C
ATOM 2041 CD1 TYR A 272 -7.909 10.378 11.788 1.00 33.17 C
ANISOU 2041 CD1 TYR A 272 4790 3903 3910 -43 214 -291 C
ATOM 2042 CD2 TYR A 272 -7.482 8.044 12.089 1.00 32.32 C
ANISOU 2042 CD2 TYR A 272 4697 3738 3844 -49 292 -336 C
ATOM 2043 CE1 TYR A 272 -7.723 10.593 13.158 1.00 33.97 C
ANISOU 2043 CE1 TYR A 272 4777 4037 4095 -44 264 -255 C
ATOM 2044 CE2 TYR A 272 -7.280 8.249 13.454 1.00 32.94 C
ANISOU 2044 CE2 TYR A 272 4668 3848 4001 -47 340 -294 C
ATOM 2045 CZ TYR A 272 -7.395 9.526 13.983 1.00 38.69 C
ANISOU 2045 CZ TYR A 272 5333 4621 4745 -45 326 -256 C
ATOM 2046 OH TYR A 272 -7.173 9.718 15.321 1.00 33.18 O
ANISOU 2046 OH TYR A 272 4548 3949 4110 -41 370 -220 O
ATOM 2047 N ILE A 273 -4.930 8.908 8.808 1.00 30.93 N
ANISOU 2047 N ILE A 273 4875 3535 3341 22 446 -340 N
ATOM 2048 CA ILE A 273 -3.480 8.973 9.036 1.00 30.72 C
ANISOU 2048 CA ILE A 273 4825 3520 3325 47 592 -313 C
ATOM 2049 C ILE A 273 -2.887 10.184 8.307 1.00 34.81 C
ANISOU 2049 C ILE A 273 5414 4047 3765 57 646 -283 C
ATOM 2050 O ILE A 273 -2.062 10.901 8.878 1.00 34.03 O
ANISOU 2050 O ILE A 273 5234 3980 3717 63 722 -244 O
ATOM 2051 CB ILE A 273 -2.774 7.648 8.609 1.00 32.34 C
ANISOU 2051 CB ILE A 273 5093 3679 3515 67 677 -352 C
ATOM 2052 CG1 ILE A 273 -3.030 6.524 9.648 1.00 31.32 C
ANISOU 2052 CG1 ILE A 273 4867 3542 3490 63 660 -363 C
ATOM 2053 CG2 ILE A 273 -1.261 7.856 8.365 1.00 30.80 C
ANISOU 2053 CG2 ILE A 273 4907 3482 3313 97 833 -335 C
ATOM 2054 CD1 ILE A 273 -2.758 5.119 9.125 1.00 32.43 C
ANISOU 2054 CD1 ILE A 273 5087 3621 3612 76 704 -413 C
ATOM 2055 N LEU A 274 -3.311 10.400 7.063 1.00 32.17 N
ANISOU 2055 N LEU A 274 5239 3678 3308 57 604 -303 N
ATOM 2056 CA LEU A 274 -2.834 11.517 6.231 1.00 32.63 C
ANISOU 2056 CA LEU A 274 5403 3727 3269 66 659 -272 C
ATOM 2057 C LEU A 274 -3.074 12.903 6.844 1.00 36.02 C
ANISOU 2057 C LEU A 274 5745 4199 3742 56 620 -220 C
ATOM 2058 O LEU A 274 -2.190 13.766 6.786 1.00 34.70 O
ANISOU 2058 O LEU A 274 5577 4037 3570 59 725 -183 O
ATOM 2059 CB LEU A 274 -3.421 11.439 4.802 1.00 32.98 C
ANISOU 2059 CB LEU A 274 5658 3718 3154 73 592 -304 C
ATOM 2060 CG LEU A 274 -2.962 10.249 3.914 1.00 38.56 C
ANISOU 2060 CG LEU A 274 6503 4368 3779 86 663 -357 C
ATOM 2061 CD1 LEU A 274 -3.644 10.303 2.547 1.00 39.43 C
ANISOU 2061 CD1 LEU A 274 6838 4425 3719 95 570 -389 C
ATOM 2062 CD2 LEU A 274 -1.441 10.260 3.689 1.00 40.13 C
ANISOU 2062 CD2 LEU A 274 6723 4552 3972 104 877 -342 C
ATOM 2063 N THR A 275 -4.246 13.090 7.483 1.00 32.45 N
ANISOU 2063 N THR A 275 5210 3772 3349 43 480 -220 N
ATOM 2064 CA THR A 275 -4.664 14.368 8.060 1.00 30.98 C
ANISOU 2064 CA THR A 275 4947 3620 3206 36 428 -178 C
ATOM 2065 C THR A 275 -3.956 14.782 9.347 1.00 34.68 C
ANISOU 2065 C THR A 275 5256 4133 3788 30 504 -145 C
ATOM 2066 O THR A 275 -3.955 15.971 9.686 1.00 34.21 O
ANISOU 2066 O THR A 275 5157 4094 3749 26 499 -108 O
ATOM 2067 CB THR A 275 -6.187 14.356 8.293 1.00 31.20 C
ANISOU 2067 CB THR A 275 4932 3651 3272 26 260 -199 C
ATOM 2068 OG1 THR A 275 -6.495 13.468 9.367 1.00 31.15 O
ANISOU 2068 OG1 THR A 275 4793 3663 3381 10 251 -218 O
ATOM 2069 CG2 THR A 275 -6.987 14.006 7.042 1.00 30.88 C
ANISOU 2069 CG2 THR A 275 5042 3562 3128 34 148 -239 C
ATOM 2070 N ARG A 276 -3.430 13.813 10.104 1.00 31.49 N
ANISOU 2070 N ARG A 276 4765 3741 3458 31 559 -159 N
ATOM 2071 CA ARG A 276 -2.839 14.079 11.428 1.00 31.12 C
ANISOU 2071 CA ARG A 276 4572 3734 3517 31 603 -134 C
ATOM 2072 C ARG A 276 -1.623 15.001 11.370 1.00 32.71 C
ANISOU 2072 C ARG A 276 4758 3943 3726 35 709 -105 C
ATOM 2073 O ARG A 276 -1.711 16.047 11.997 1.00 32.01 O
ANISOU 2073 O ARG A 276 4604 3881 3677 25 687 -78 O
ATOM 2074 CB ARG A 276 -2.543 12.787 12.211 1.00 28.46 C
ANISOU 2074 CB ARG A 276 4166 3398 3248 40 628 -154 C
ATOM 2075 CG ARG A 276 -3.798 11.973 12.488 1.00 33.51 C
ANISOU 2075 CG ARG A 276 4798 4027 3909 26 533 -179 C
ATOM 2076 CD ARG A 276 -3.632 11.102 13.713 1.00 34.49 C
ANISOU 2076 CD ARG A 276 4829 4157 4117 32 552 -177 C
ATOM 2077 NE ARG A 276 -2.619 10.047 13.555 1.00 30.09 N
ANISOU 2077 NE ARG A 276 4293 3575 3563 58 633 -193 N
ATOM 2078 CZ ARG A 276 -2.872 8.823 13.103 1.00 36.75 C
ANISOU 2078 CZ ARG A 276 5195 4376 4391 58 631 -229 C
ATOM 2079 NH1 ARG A 276 -4.074 8.513 12.638 1.00 28.31 N
ANISOU 2079 NH1 ARG A 276 4175 3284 3299 31 549 -258 N
ATOM 2080 NH2 ARG A 276 -1.918 7.910 13.087 1.00 29.48 N
ANISOU 2080 NH2 ARG A 276 4284 3431 3486 88 708 -240 N
ATOM 2081 N PRO A 277 -0.520 14.713 10.628 1.00 29.13 N
ANISOU 2081 N PRO A 277 4362 3463 3243 46 827 -114 N
ATOM 2082 CA PRO A 277 0.585 15.688 10.570 1.00 29.66 C
ANISOU 2082 CA PRO A 277 4402 3530 3338 41 934 -89 C
ATOM 2083 C PRO A 277 0.195 17.018 9.889 1.00 34.31 C
ANISOU 2083 C PRO A 277 5081 4105 3853 26 920 -58 C
ATOM 2084 O PRO A 277 0.789 18.046 10.202 1.00 31.36 O
ANISOU 2084 O PRO A 277 4651 3737 3526 12 973 -33 O
ATOM 2085 CB PRO A 277 1.693 14.937 9.829 1.00 31.11 C
ANISOU 2085 CB PRO A 277 4634 3676 3510 57 1069 -113 C
ATOM 2086 CG PRO A 277 0.984 13.935 8.997 1.00 34.45 C
ANISOU 2086 CG PRO A 277 5185 4067 3835 67 1028 -144 C
ATOM 2087 CD PRO A 277 -0.222 13.526 9.801 1.00 30.41 C
ANISOU 2087 CD PRO A 277 4616 3586 3354 62 879 -150 C
ATOM 2088 N LEU A 278 -0.852 17.018 9.021 1.00 32.15 N
ANISOU 2088 N LEU A 278 4940 3808 3469 29 835 -62 N
ATOM 2089 CA LEU A 278 -1.342 18.256 8.412 1.00 32.76 C
ANISOU 2089 CA LEU A 278 5110 3865 3471 24 798 -30 C
ATOM 2090 C LEU A 278 -1.904 19.206 9.494 1.00 35.53 C
ANISOU 2090 C LEU A 278 5338 4254 3907 13 716 -5 C
ATOM 2091 O LEU A 278 -1.549 20.381 9.489 1.00 33.39 O
ANISOU 2091 O LEU A 278 5070 3976 3642 3 758 29 O
ATOM 2092 CB LEU A 278 -2.373 17.965 7.310 1.00 33.78 C
ANISOU 2092 CB LEU A 278 5405 3958 3471 38 696 -46 C
ATOM 2093 CG LEU A 278 -2.906 19.175 6.499 1.00 38.52 C
ANISOU 2093 CG LEU A 278 6140 4525 3971 46 643 -11 C
ATOM 2094 CD1 LEU A 278 -1.786 19.844 5.672 1.00 38.11 C
ANISOU 2094 CD1 LEU A 278 6208 4427 3845 42 807 21 C
ATOM 2095 CD2 LEU A 278 -4.040 18.732 5.560 1.00 41.12 C
ANISOU 2095 CD2 LEU A 278 6613 4822 4188 67 499 -37 C
ATOM 2096 N ALA A 279 -2.689 18.684 10.483 1.00 31.59 N
ANISOU 2096 N ALA A 279 4729 3793 3482 13 618 -22 N
ATOM 2097 CA ALA A 279 -3.169 19.541 11.587 1.00 30.86 C
ANISOU 2097 CA ALA A 279 4522 3733 3471 4 559 -3 C
ATOM 2098 C ALA A 279 -1.983 20.091 12.420 1.00 34.80 C
ANISOU 2098 C ALA A 279 4920 4253 4051 -7 654 12 C
ATOM 2099 O ALA A 279 -1.972 21.268 12.738 1.00 33.00 O
ANISOU 2099 O ALA A 279 4665 4027 3847 -17 652 37 O
ATOM 2100 CB ALA A 279 -4.134 18.772 12.489 1.00 31.30 C
ANISOU 2100 CB ALA A 279 4489 3815 3589 4 469 -27 C
ATOM 2101 N PHE A 280 -0.958 19.264 12.694 1.00 32.09 N
ANISOU 2101 N PHE A 280 4526 3916 3750 -3 735 -5 N
ATOM 2102 CA PHE A 280 0.206 19.645 13.511 1.00 31.69 C
ANISOU 2102 CA PHE A 280 4366 3882 3794 -10 806 -1 C
ATOM 2103 C PHE A 280 1.247 20.494 12.782 1.00 37.80 C
ANISOU 2103 C PHE A 280 5175 4624 4564 -25 923 13 C
ATOM 2104 O PHE A 280 2.194 20.970 13.428 1.00 37.03 O
ANISOU 2104 O PHE A 280 4975 4534 4560 -37 975 12 O
ATOM 2105 CB PHE A 280 0.851 18.408 14.164 1.00 32.62 C
ANISOU 2105 CB PHE A 280 4405 4015 3974 9 829 -27 C
ATOM 2106 CG PHE A 280 -0.014 17.930 15.304 1.00 31.93 C
ANISOU 2106 CG PHE A 280 4256 3958 3918 16 729 -32 C
ATOM 2107 CD1 PHE A 280 -1.047 17.028 15.080 1.00 32.72 C
ANISOU 2107 CD1 PHE A 280 4406 4051 3975 21 670 -45 C
ATOM 2108 CD2 PHE A 280 0.116 18.482 16.575 1.00 32.82 C
ANISOU 2108 CD2 PHE A 280 4271 4098 4099 14 696 -24 C
ATOM 2109 CE1 PHE A 280 -1.924 16.679 16.106 1.00 32.82 C
ANISOU 2109 CE1 PHE A 280 4366 4082 4022 21 597 -47 C
ATOM 2110 CE2 PHE A 280 -0.754 18.117 17.607 1.00 34.46 C
ANISOU 2110 CE2 PHE A 280 4445 4326 4324 20 621 -25 C
ATOM 2111 CZ PHE A 280 -1.763 17.213 17.365 1.00 31.96 C
ANISOU 2111 CZ PHE A 280 4172 3999 3972 22 580 -35 C
ATOM 2112 N LEU A 281 1.032 20.767 11.469 1.00 35.47 N
ANISOU 2112 N LEU A 281 5028 4287 4163 -27 960 27 N
ATOM 2113 CA LEU A 281 1.895 21.659 10.704 1.00 36.36 C
ANISOU 2113 CA LEU A 281 5200 4356 4260 -46 1085 48 C
ATOM 2114 C LEU A 281 1.735 23.047 11.321 1.00 39.66 C
ANISOU 2114 C LEU A 281 5563 4779 4726 -67 1052 75 C
ATOM 2115 O LEU A 281 2.681 23.828 11.336 1.00 39.24 O
ANISOU 2115 O LEU A 281 5473 4703 4734 -92 1152 84 O
ATOM 2116 CB LEU A 281 1.562 21.634 9.191 1.00 37.14 C
ANISOU 2116 CB LEU A 281 5503 4401 4209 -37 1119 61 C
ATOM 2117 CG LEU A 281 2.396 22.551 8.239 1.00 44.17 C
ANISOU 2117 CG LEU A 281 6497 5228 5057 -57 1272 89 C
ATOM 2118 CD1 LEU A 281 3.926 22.377 8.439 1.00 44.42 C
ANISOU 2118 CD1 LEU A 281 6422 5248 5206 -76 1440 70 C
ATOM 2119 CD2 LEU A 281 2.022 22.306 6.765 1.00 47.60 C
ANISOU 2119 CD2 LEU A 281 7162 5607 5318 -39 1296 98 C
ATOM 2120 N ASN A 282 0.561 23.298 11.932 1.00 37.20 N
ANISOU 2120 N ASN A 282 5229 4496 4408 -59 915 81 N
ATOM 2121 CA ASN A 282 0.232 24.501 12.706 1.00 36.82 C
ANISOU 2121 CA ASN A 282 5120 4458 4412 -72 864 99 C
ATOM 2122 C ASN A 282 1.358 24.836 13.727 1.00 39.24 C
ANISOU 2122 C ASN A 282 5283 4782 4845 -94 922 85 C
ATOM 2123 O ASN A 282 1.796 25.975 13.795 1.00 37.04 O
ANISOU 2123 O ASN A 282 4990 4478 4604 -119 966 100 O
ATOM 2124 CB ASN A 282 -1.085 24.260 13.475 1.00 37.72 C
ANISOU 2124 CB ASN A 282 5191 4608 4531 -54 723 91 C
ATOM 2125 CG ASN A 282 -1.302 25.192 14.660 1.00 64.19 C
ANISOU 2125 CG ASN A 282 8446 7982 7962 -64 679 95 C
ATOM 2126 OD1 ASN A 282 -1.338 26.428 14.523 1.00 58.12 O
ANISOU 2126 OD1 ASN A 282 7703 7185 7194 -76 688 118 O
ATOM 2127 ND2 ASN A 282 -1.432 24.616 15.852 1.00 48.27 N
ANISOU 2127 ND2 ASN A 282 6326 6006 6007 -59 635 72 N
ATOM 2128 N SER A 283 1.811 23.835 14.506 1.00 36.27 N
ANISOU 2128 N SER A 283 4806 4441 4532 -83 912 54 N
ATOM 2129 CA SER A 283 2.836 23.997 15.543 1.00 36.87 C
ANISOU 2129 CA SER A 283 4744 4535 4729 -93 934 32 C
ATOM 2130 C SER A 283 4.195 24.346 15.006 1.00 42.63 C
ANISOU 2130 C SER A 283 5446 5227 5523 -117 1067 25 C
ATOM 2131 O SER A 283 5.002 24.927 15.737 1.00 42.92 O
ANISOU 2131 O SER A 283 5373 5265 5669 -137 1081 9 O
ATOM 2132 CB SER A 283 2.903 22.768 16.442 1.00 40.07 C
ANISOU 2132 CB SER A 283 5072 4980 5172 -64 879 5 C
ATOM 2133 OG SER A 283 1.622 22.540 17.009 1.00 42.06 O
ANISOU 2133 OG SER A 283 5345 5258 5379 -50 773 12 O
ATOM 2134 N ALA A 284 4.436 24.055 13.712 1.00 38.94 N
ANISOU 2134 N ALA A 284 5084 4721 4990 -118 1169 36 N
ATOM 2135 CA ALA A 284 5.683 24.400 13.054 1.00 38.81 C
ANISOU 2135 CA ALA A 284 5057 4656 5032 -144 1326 31 C
ATOM 2136 C ALA A 284 5.590 25.781 12.405 1.00 43.77 C
ANISOU 2136 C ALA A 284 5774 5232 5622 -179 1388 68 C
ATOM 2137 O ALA A 284 6.613 26.439 12.264 1.00 45.57 O
ANISOU 2137 O ALA A 284 5954 5420 5942 -215 1506 63 O
ATOM 2138 CB ALA A 284 6.041 23.347 12.006 1.00 39.35 C
ANISOU 2138 CB ALA A 284 5208 4699 5045 -125 1425 22 C
ATOM 2139 N VAL A 285 4.383 26.229 11.995 1.00 38.25 N
ANISOU 2139 N VAL A 285 5206 4528 4800 -169 1309 103 N
ATOM 2140 CA VAL A 285 4.274 27.518 11.300 1.00 37.78 C
ANISOU 2140 CA VAL A 285 5255 4408 4692 -194 1366 144 C
ATOM 2141 C VAL A 285 3.722 28.670 12.168 1.00 39.86 C
ANISOU 2141 C VAL A 285 5464 4680 4999 -207 1272 157 C
ATOM 2142 O VAL A 285 3.931 29.820 11.807 1.00 38.91 O
ANISOU 2142 O VAL A 285 5397 4505 4882 -235 1337 185 O
ATOM 2143 CB VAL A 285 3.488 27.420 9.962 1.00 42.86 C
ANISOU 2143 CB VAL A 285 6114 5011 5160 -170 1367 179 C
ATOM 2144 CG1 VAL A 285 4.122 26.396 9.013 1.00 43.09 C
ANISOU 2144 CG1 VAL A 285 6220 5016 5137 -160 1485 164 C
ATOM 2145 CG2 VAL A 285 1.998 27.142 10.180 1.00 42.87 C
ANISOU 2145 CG2 VAL A 285 6155 5052 5082 -131 1184 184 C
ATOM 2146 N ASN A 286 3.053 28.387 13.303 1.00 35.29 N
ANISOU 2146 N ASN A 286 4790 4164 4455 -187 1134 136 N
ATOM 2147 CA ASN A 286 2.435 29.447 14.098 1.00 34.09 C
ANISOU 2147 CA ASN A 286 4603 4017 4334 -194 1049 145 C
ATOM 2148 C ASN A 286 3.485 30.415 14.769 1.00 40.05 C
ANISOU 2148 C ASN A 286 5250 4749 5218 -240 1111 128 C
ATOM 2149 O ASN A 286 3.069 31.526 15.092 1.00 39.38 O
ANISOU 2149 O ASN A 286 5176 4641 5144 -252 1076 142 O
ATOM 2150 CB ASN A 286 1.370 28.916 15.071 1.00 30.05 C
ANISOU 2150 CB ASN A 286 4037 3564 3815 -162 904 128 C
ATOM 2151 CG ASN A 286 1.913 28.113 16.204 1.00 43.24 C
ANISOU 2151 CG ASN A 286 5573 5287 5570 -159 877 87 C
ATOM 2152 OD1 ASN A 286 3.025 28.353 16.683 1.00 38.43 O
ANISOU 2152 OD1 ASN A 286 4871 4672 5057 -183 928 64 O
ATOM 2153 ND2 ASN A 286 1.138 27.152 16.666 1.00 30.75 N
ANISOU 2153 ND2 ASN A 286 3979 3748 3958 -128 793 75 N
ATOM 2154 N PRO A 287 4.831 30.160 14.848 1.00 38.04 N
ANISOU 2154 N PRO A 287 4901 4485 5068 -268 1210 98 N
ATOM 2155 CA PRO A 287 5.743 31.234 15.296 1.00 36.75 C
ANISOU 2155 CA PRO A 287 4648 4283 5032 -318 1268 81 C
ATOM 2156 C PRO A 287 5.684 32.479 14.383 1.00 39.58 C
ANISOU 2156 C PRO A 287 5126 4560 5351 -351 1362 126 C
ATOM 2157 O PRO A 287 6.151 33.543 14.794 1.00 38.06 O
ANISOU 2157 O PRO A 287 4879 4330 5253 -394 1391 116 O
ATOM 2158 CB PRO A 287 7.130 30.574 15.211 1.00 38.21 C
ANISOU 2158 CB PRO A 287 4725 4462 5330 -336 1371 42 C
ATOM 2159 CG PRO A 287 6.859 29.129 15.414 1.00 43.05 C
ANISOU 2159 CG PRO A 287 5321 5137 5900 -285 1304 26 C
ATOM 2160 CD PRO A 287 5.597 28.916 14.604 1.00 39.41 C
ANISOU 2160 CD PRO A 287 5028 4676 5269 -255 1269 71 C
ATOM 2161 N ILE A 288 5.073 32.371 13.172 1.00 36.17 N
ANISOU 2161 N ILE A 288 4869 4097 4778 -329 1401 174 N
ATOM 2162 CA ILE A 288 4.908 33.515 12.240 1.00 36.27 C
ANISOU 2162 CA ILE A 288 5031 4023 4726 -349 1482 227 C
ATOM 2163 C ILE A 288 4.080 34.637 12.912 1.00 36.18 C
ANISOU 2163 C ILE A 288 5020 4005 4721 -347 1373 241 C
ATOM 2164 O ILE A 288 4.270 35.807 12.610 1.00 33.29 O
ANISOU 2164 O ILE A 288 4713 3565 4372 -379 1442 269 O
ATOM 2165 CB ILE A 288 4.289 33.094 10.862 1.00 40.17 C
ANISOU 2165 CB ILE A 288 5733 4486 5042 -312 1508 274 C
ATOM 2166 CG1 ILE A 288 4.465 34.168 9.775 1.00 41.99 C
ANISOU 2166 CG1 ILE A 288 6137 4612 5206 -335 1633 330 C
ATOM 2167 CG2 ILE A 288 2.815 32.685 10.959 1.00 41.07 C
ANISOU 2167 CG2 ILE A 288 5908 4650 5047 -252 1328 285 C
ATOM 2168 CD1 ILE A 288 5.857 34.178 9.087 1.00 56.45 C
ANISOU 2168 CD1 ILE A 288 7976 6376 7094 -386 1859 327 C
ATOM 2169 N PHE A 289 3.165 34.256 13.822 1.00 31.94 N
ANISOU 2169 N PHE A 289 4422 3538 4175 -309 1216 221 N
ATOM 2170 CA PHE A 289 2.309 35.206 14.504 1.00 31.83 C
ANISOU 2170 CA PHE A 289 4404 3519 4169 -299 1116 227 C
ATOM 2171 C PHE A 289 3.084 36.231 15.347 1.00 35.08 C
ANISOU 2171 C PHE A 289 4713 3902 4715 -351 1152 199 C
ATOM 2172 O PHE A 289 2.584 37.337 15.521 1.00 33.99 O
ANISOU 2172 O PHE A 289 4615 3721 4578 -354 1123 217 O
ATOM 2173 CB PHE A 289 1.227 34.495 15.303 1.00 33.16 C
ANISOU 2173 CB PHE A 289 4524 3764 4310 -251 966 207 C
ATOM 2174 CG PHE A 289 0.223 33.865 14.366 1.00 34.56 C
ANISOU 2174 CG PHE A 289 4823 3947 4360 -203 914 239 C
ATOM 2175 CD1 PHE A 289 -0.649 34.657 13.617 1.00 36.67 C
ANISOU 2175 CD1 PHE A 289 5225 4161 4548 -177 878 285 C
ATOM 2176 CD2 PHE A 289 0.134 32.481 14.242 1.00 35.18 C
ANISOU 2176 CD2 PHE A 289 4885 4079 4403 -180 889 219 C
ATOM 2177 CE1 PHE A 289 -1.579 34.072 12.755 1.00 36.84 C
ANISOU 2177 CE1 PHE A 289 5357 4185 4457 -129 807 307 C
ATOM 2178 CE2 PHE A 289 -0.797 31.904 13.388 1.00 37.78 C
ANISOU 2178 CE2 PHE A 289 5325 4409 4622 -140 829 240 C
ATOM 2179 CZ PHE A 289 -1.637 32.705 12.639 1.00 35.69 C
ANISOU 2179 CZ PHE A 289 5190 4093 4280 -115 784 281 C
ATOM 2180 N TYR A 290 4.318 35.895 15.792 1.00 31.29 N
ANISOU 2180 N TYR A 290 4104 3434 4350 -391 1214 153 N
ATOM 2181 CA TYR A 290 5.196 36.809 16.546 1.00 31.36 C
ANISOU 2181 CA TYR A 290 4003 3409 4502 -447 1245 115 C
ATOM 2182 C TYR A 290 5.523 38.055 15.745 1.00 36.15 C
ANISOU 2182 C TYR A 290 4699 3913 5125 -493 1368 152 C
ATOM 2183 O TYR A 290 5.881 39.083 16.319 1.00 36.10 O
ANISOU 2183 O TYR A 290 4637 3862 5217 -537 1375 130 O
ATOM 2184 CB TYR A 290 6.525 36.105 16.861 1.00 31.10 C
ANISOU 2184 CB TYR A 290 3824 3398 4595 -476 1300 61 C
ATOM 2185 CG TYR A 290 6.507 35.301 18.137 1.00 30.71 C
ANISOU 2185 CG TYR A 290 3651 3432 4587 -447 1165 7 C
ATOM 2186 CD1 TYR A 290 5.869 34.061 18.199 1.00 31.70 C
ANISOU 2186 CD1 TYR A 290 3797 3626 4620 -389 1094 14 C
ATOM 2187 CD2 TYR A 290 7.171 35.754 19.274 1.00 30.70 C
ANISOU 2187 CD2 TYR A 290 3520 3433 4714 -476 1110 -52 C
ATOM 2188 CE1 TYR A 290 5.858 33.315 19.378 1.00 33.43 C
ANISOU 2188 CE1 TYR A 290 3921 3911 4868 -360 980 -30 C
ATOM 2189 CE2 TYR A 290 7.195 35.001 20.446 1.00 30.76 C
ANISOU 2189 CE2 TYR A 290 3436 3509 4744 -443 984 -99 C
ATOM 2190 CZ TYR A 290 6.549 33.780 20.489 1.00 38.05 C
ANISOU 2190 CZ TYR A 290 4392 4497 5569 -385 926 -84 C
ATOM 2191 OH TYR A 290 6.661 33.036 21.623 1.00 37.78 O
ANISOU 2191 OH TYR A 290 4280 4518 5555 -353 816 -125 O
ATOM 2192 N PHE A 291 5.444 37.946 14.415 1.00 34.79 N
ANISOU 2192 N PHE A 291 4672 3693 4853 -485 1469 208 N
ATOM 2193 CA PHE A 291 5.794 39.022 13.488 1.00 36.01 C
ANISOU 2193 CA PHE A 291 4944 3736 5001 -526 1611 255 C
ATOM 2194 C PHE A 291 4.564 39.777 12.999 1.00 39.13 C
ANISOU 2194 C PHE A 291 5514 4090 5263 -484 1547 318 C
ATOM 2195 O PHE A 291 4.678 40.614 12.116 1.00 38.21 O
ANISOU 2195 O PHE A 291 5537 3876 5105 -503 1653 371 O
ATOM 2196 CB PHE A 291 6.620 38.453 12.316 1.00 38.57 C
ANISOU 2196 CB PHE A 291 5335 4021 5300 -546 1785 275 C
ATOM 2197 CG PHE A 291 7.832 37.696 12.793 1.00 41.66 C
ANISOU 2197 CG PHE A 291 5538 4448 5841 -580 1844 209 C
ATOM 2198 CD1 PHE A 291 8.959 38.370 13.238 1.00 46.06 C
ANISOU 2198 CD1 PHE A 291 5958 4957 6586 -653 1934 166 C
ATOM 2199 CD2 PHE A 291 7.823 36.311 12.864 1.00 45.25 C
ANISOU 2199 CD2 PHE A 291 5943 4984 6265 -538 1796 184 C
ATOM 2200 CE1 PHE A 291 10.079 37.667 13.701 1.00 47.77 C
ANISOU 2200 CE1 PHE A 291 5986 5205 6958 -678 1970 99 C
ATOM 2201 CE2 PHE A 291 8.926 35.614 13.359 1.00 49.00 C
ANISOU 2201 CE2 PHE A 291 6240 5490 6888 -559 1834 122 C
ATOM 2202 CZ PHE A 291 10.060 36.297 13.746 1.00 47.01 C
ANISOU 2202 CZ PHE A 291 5849 5188 6824 -627 1920 80 C
ATOM 2203 N LEU A 292 3.386 39.492 13.578 1.00 36.40 N
ANISOU 2203 N LEU A 292 5162 3812 4858 -424 1377 313 N
ATOM 2204 CA LEU A 292 2.165 40.167 13.129 1.00 36.12 C
ANISOU 2204 CA LEU A 292 5275 3736 4713 -374 1300 368 C
ATOM 2205 C LEU A 292 1.496 40.997 14.219 1.00 41.48 C
ANISOU 2205 C LEU A 292 5886 4422 5454 -363 1190 346 C
ATOM 2206 O LEU A 292 0.315 41.325 14.082 1.00 42.72 O
ANISOU 2206 O LEU A 292 6124 4569 5537 -306 1091 377 O
ATOM 2207 CB LEU A 292 1.177 39.165 12.488 1.00 35.35 C
ANISOU 2207 CB LEU A 292 5270 3688 4474 -303 1207 392 C
ATOM 2208 CG LEU A 292 1.719 38.393 11.260 1.00 38.73 C
ANISOU 2208 CG LEU A 292 5809 4097 4811 -305 1315 417 C
ATOM 2209 CD1 LEU A 292 0.771 37.285 10.853 1.00 38.27 C
ANISOU 2209 CD1 LEU A 292 5809 4098 4635 -241 1200 420 C
ATOM 2210 CD2 LEU A 292 2.048 39.331 10.090 1.00 38.60 C
ANISOU 2210 CD2 LEU A 292 5980 3960 4724 -323 1447 482 C
ATOM 2211 N VAL A 293 2.256 41.385 15.268 1.00 36.57 N
ANISOU 2211 N VAL A 293 5120 3806 4969 -416 1208 290 N
ATOM 2212 CA VAL A 293 1.685 42.152 16.385 1.00 35.59 C
ANISOU 2212 CA VAL A 293 4936 3686 4902 -408 1112 260 C
ATOM 2213 C VAL A 293 2.237 43.614 16.434 1.00 41.83 C
ANISOU 2213 C VAL A 293 5747 4370 5777 -464 1193 264 C
ATOM 2214 O VAL A 293 2.186 44.268 17.482 1.00 42.12 O
ANISOU 2214 O VAL A 293 5708 4402 5894 -480 1141 219 O
ATOM 2215 CB VAL A 293 1.746 41.422 17.754 1.00 37.59 C
ANISOU 2215 CB VAL A 293 5030 4035 5219 -404 1018 187 C
ATOM 2216 CG1 VAL A 293 0.737 40.283 17.805 1.00 36.84 C
ANISOU 2216 CG1 VAL A 293 4942 4023 5032 -337 917 193 C
ATOM 2217 CG2 VAL A 293 3.152 40.925 18.094 1.00 37.14 C
ANISOU 2217 CG2 VAL A 293 4847 3999 5264 -461 1083 136 C
ATOM 2218 N GLY A 294 2.692 44.104 15.274 1.00 37.47 N
ANISOU 2218 N GLY A 294 5315 3727 5195 -492 1323 319 N
ATOM 2219 CA GLY A 294 3.101 45.488 15.033 1.00 37.14 C
ANISOU 2219 CA GLY A 294 5336 3564 5212 -542 1421 342 C
ATOM 2220 C GLY A 294 4.224 46.120 15.830 1.00 41.36 C
ANISOU 2220 C GLY A 294 5734 4062 5920 -630 1485 278 C
ATOM 2221 O GLY A 294 4.391 47.342 15.787 1.00 41.73 O
ANISOU 2221 O GLY A 294 5829 4006 6022 -669 1545 291 O
ATOM 2222 N ASP A 295 5.035 45.311 16.496 1.00 37.55 N
ANISOU 2222 N ASP A 295 5086 3653 5528 -661 1475 209 N
ATOM 2223 CA ASP A 295 6.123 45.783 17.357 1.00 36.83 C
ANISOU 2223 CA ASP A 295 4841 3538 5616 -740 1504 133 C
ATOM 2224 C ASP A 295 7.484 45.814 16.677 1.00 41.00 C
ANISOU 2224 C ASP A 295 5324 4001 6254 -820 1682 127 C
ATOM 2225 O ASP A 295 8.465 46.179 17.330 1.00 39.32 O
ANISOU 2225 O ASP A 295 4967 3761 6211 -891 1706 57 O
ATOM 2226 CB ASP A 295 6.189 44.877 18.609 1.00 37.58 C
ANISOU 2226 CB ASP A 295 4777 3749 5751 -718 1363 54 C
ATOM 2227 CG ASP A 295 6.324 43.393 18.296 1.00 42.69 C
ANISOU 2227 CG ASP A 295 5389 4488 6344 -681 1355 58 C
ATOM 2228 OD1 ASP A 295 6.469 43.046 17.111 1.00 42.95 O
ANISOU 2228 OD1 ASP A 295 5509 4495 6316 -679 1465 112 O
ATOM 2229 OD2 ASP A 295 6.304 42.584 19.236 1.00 44.00 O
ANISOU 2229 OD2 ASP A 295 5451 4744 6525 -655 1242 5 O
ATOM 2230 N HIS A 296 7.568 45.374 15.387 1.00 40.00 N
ANISOU 2230 N HIS A 296 5316 3847 6036 -809 1807 194 N
ATOM 2231 CA HIS A 296 8.821 45.277 14.622 1.00 39.34 C
ANISOU 2231 CA HIS A 296 5203 3699 6047 -879 2005 193 C
ATOM 2232 C HIS A 296 9.801 44.324 15.339 1.00 40.94 C
ANISOU 2232 C HIS A 296 5183 3981 6393 -904 1981 106 C
ATOM 2233 O HIS A 296 10.998 44.593 15.447 1.00 40.08 O
ANISOU 2233 O HIS A 296 4943 3818 6466 -983 2088 56 O
ATOM 2234 CB HIS A 296 9.449 46.663 14.360 1.00 41.11 C
ANISOU 2234 CB HIS A 296 5458 3779 6384 -966 2152 203 C
ATOM 2235 CG HIS A 296 8.674 47.510 13.404 1.00 45.71 C
ANISOU 2235 CG HIS A 296 6283 4264 6823 -941 2214 301 C
ATOM 2236 ND1 HIS A 296 9.066 47.648 12.087 1.00 48.36 N
ANISOU 2236 ND1 HIS A 296 6773 4503 7100 -964 2414 371 N
ATOM 2237 CD2 HIS A 296 7.564 48.257 13.612 1.00 48.87 C
ANISOU 2237 CD2 HIS A 296 6793 4644 7130 -890 2100 337 C
ATOM 2238 CE1 HIS A 296 8.202 48.490 11.538 1.00 48.68 C
ANISOU 2238 CE1 HIS A 296 7022 4464 7009 -927 2406 450 C
ATOM 2239 NE2 HIS A 296 7.271 48.875 12.413 1.00 49.13 N
ANISOU 2239 NE2 HIS A 296 7053 4566 7049 -880 2216 433 N
ATOM 2240 N PHE A 297 9.274 43.208 15.841 1.00 37.75 N
ANISOU 2240 N PHE A 297 4733 3698 5912 -834 1835 87 N
ATOM 2241 CA PHE A 297 10.073 42.165 16.504 1.00 37.67 C
ANISOU 2241 CA PHE A 297 4535 3768 6011 -837 1789 13 C
ATOM 2242 C PHE A 297 11.114 41.572 15.556 1.00 44.23 C
ANISOU 2242 C PHE A 297 5336 4565 6905 -870 1972 17 C
ATOM 2243 O PHE A 297 12.218 41.274 16.003 1.00 43.18 O
ANISOU 2243 O PHE A 297 5018 4438 6951 -911 1998 -53 O
ATOM 2244 CB PHE A 297 9.169 41.055 17.071 1.00 37.98 C
ANISOU 2244 CB PHE A 297 4574 3931 5927 -749 1615 9 C
ATOM 2245 CG PHE A 297 9.866 39.867 17.711 1.00 37.83 C
ANISOU 2245 CG PHE A 297 4390 3994 5990 -735 1555 -55 C
ATOM 2246 CD1 PHE A 297 10.715 40.040 18.803 1.00 39.14 C
ANISOU 2246 CD1 PHE A 297 4377 4168 6327 -771 1487 -140 C
ATOM 2247 CD2 PHE A 297 9.616 38.571 17.267 1.00 36.35 C
ANISOU 2247 CD2 PHE A 297 4234 3873 5705 -678 1549 -34 C
ATOM 2248 CE1 PHE A 297 11.304 38.938 19.427 1.00 39.10 C
ANISOU 2248 CE1 PHE A 297 4232 4235 6390 -745 1410 -196 C
ATOM 2249 CE2 PHE A 297 10.200 37.470 17.900 1.00 37.73 C
ANISOU 2249 CE2 PHE A 297 4266 4118 5950 -655 1484 -89 C
ATOM 2250 CZ PHE A 297 11.037 37.658 18.972 1.00 36.25 C
ANISOU 2250 CZ PHE A 297 3908 3938 5929 -686 1413 -167 C
ATOM 2251 N ARG A 298 10.776 41.414 14.253 1.00 45.16 N
ANISOU 2251 N ARG A 298 5636 4642 6881 -850 2098 95 N
ATOM 2252 CA ARG A 298 11.713 40.880 13.245 1.00 47.73 C
ANISOU 2252 CA ARG A 298 5965 4924 7246 -879 2300 104 C
ATOM 2253 C ARG A 298 12.953 41.746 13.214 1.00 55.82 C
ANISOU 2253 C ARG A 298 6879 5843 8487 -980 2466 67 C
ATOM 2254 O ARG A 298 14.063 41.221 13.243 1.00 56.55 O
ANISOU 2254 O ARG A 298 6811 5934 8743 -1016 2557 12 O
ATOM 2255 CB ARG A 298 11.081 40.842 11.847 1.00 49.50 C
ANISOU 2255 CB ARG A 298 6447 5098 7263 -845 2409 198 C
ATOM 2256 CG ARG A 298 11.994 40.208 10.782 1.00 63.49 C
ANISOU 2256 CG ARG A 298 8247 6823 9052 -868 2628 207 C
ATOM 2257 CD ARG A 298 11.914 40.921 9.445 1.00 78.42 C
ANISOU 2257 CD ARG A 298 10383 8590 10825 -889 2822 291 C
ATOM 2258 NE ARG A 298 10.528 41.038 8.987 1.00 94.53 N
ANISOU 2258 NE ARG A 298 12653 10644 12622 -814 2701 365 N
ATOM 2259 CZ ARG A 298 10.124 41.813 7.984 1.00108.36 C
ANISOU 2259 CZ ARG A 298 14648 12291 14232 -811 2796 448 C
ATOM 2260 NH1 ARG A 298 10.998 42.552 7.314 1.00 94.57 N
ANISOU 2260 NH1 ARG A 298 12963 10415 12554 -885 3035 472 N
ATOM 2261 NH2 ARG A 298 8.842 41.862 7.651 1.00 96.77 N
ANISOU 2261 NH2 ARG A 298 13367 10842 12560 -734 2652 506 N
ATOM 2262 N ASP A 299 12.748 43.078 13.205 1.00 54.57 N
ANISOU 2262 N ASP A 299 6796 5595 8344 -1025 2499 94 N
ATOM 2263 CA ASP A 299 13.807 44.076 13.195 1.00 55.56 C
ANISOU 2263 CA ASP A 299 6830 5603 8676 -1130 2655 61 C
ATOM 2264 C ASP A 299 14.548 44.016 14.542 1.00 62.28 C
ANISOU 2264 C ASP A 299 7409 6503 9752 -1166 2527 -52 C
ATOM 2265 O ASP A 299 15.767 44.038 14.556 1.00 62.14 O
ANISOU 2265 O ASP A 299 7224 6436 9951 -1237 2644 -112 O
ATOM 2266 CB ASP A 299 13.220 45.480 12.899 1.00 57.68 C
ANISOU 2266 CB ASP A 299 7272 5765 8877 -1156 2694 123 C
ATOM 2267 CG ASP A 299 12.317 45.592 11.654 1.00 69.35 C
ANISOU 2267 CG ASP A 299 9044 7197 10108 -1103 2770 238 C
ATOM 2268 OD1 ASP A 299 12.562 46.488 10.830 1.00 71.55 O
ANISOU 2268 OD1 ASP A 299 9462 7341 10383 -1153 2953 293 O
ATOM 2269 OD2 ASP A 299 11.337 44.795 11.533 1.00 70.50 O
ANISOU 2269 OD2 ASP A 299 9285 7437 10066 -1009 2634 271 O
ATOM 2270 N MET A 300 13.822 43.852 15.660 1.00 62.31 N
ANISOU 2270 N MET A 300 7368 6603 9702 -1111 2285 -85 N
ATOM 2271 CA MET A 300 14.418 43.729 16.999 1.00 64.10 C
ANISOU 2271 CA MET A 300 7367 6882 10105 -1130 2130 -191 C
ATOM 2272 C MET A 300 15.322 42.477 17.117 1.00 71.92 C
ANISOU 2272 C MET A 300 8183 7936 11207 -1115 2133 -248 C
ATOM 2273 O MET A 300 16.345 42.530 17.801 1.00 72.50 O
ANISOU 2273 O MET A 300 8046 7998 11502 -1162 2102 -338 O
ATOM 2274 CB MET A 300 13.327 43.680 18.070 1.00 66.84 C
ANISOU 2274 CB MET A 300 7750 7320 10327 -1060 1888 -201 C
ATOM 2275 CG MET A 300 12.768 45.035 18.467 1.00 71.19 C
ANISOU 2275 CG MET A 300 8378 7806 10865 -1089 1845 -195 C
ATOM 2276 SD MET A 300 11.267 44.905 19.499 1.00 76.19 S
ANISOU 2276 SD MET A 300 9095 8539 11314 -994 1601 -188 S
ATOM 2277 CE MET A 300 11.817 43.775 20.734 1.00 72.66 C
ANISOU 2277 CE MET A 300 8454 8206 10949 -964 1430 -284 C
ATOM 2278 N LEU A 301 14.942 41.366 16.452 1.00 70.04 N
ANISOU 2278 N LEU A 301 8032 7760 10822 -1046 2162 -198 N
ATOM 2279 CA LEU A 301 15.677 40.097 16.441 1.00 71.01 C
ANISOU 2279 CA LEU A 301 8018 7939 11023 -1018 2174 -240 C
ATOM 2280 C LEU A 301 17.047 40.252 15.771 1.00 78.70 C
ANISOU 2280 C LEU A 301 8872 8818 12214 -1098 2401 -272 C
ATOM 2281 O LEU A 301 18.041 39.730 16.279 1.00 78.09 O
ANISOU 2281 O LEU A 301 8575 8758 12336 -1109 2375 -354 O
ATOM 2282 CB LEU A 301 14.865 39.018 15.694 1.00 70.87 C
ANISOU 2282 CB LEU A 301 8160 7986 10781 -935 2182 -170 C
ATOM 2283 CG LEU A 301 14.314 37.835 16.496 1.00 74.64 C
ANISOU 2283 CG LEU A 301 8598 8591 11172 -847 1976 -191 C
ATOM 2284 CD1 LEU A 301 13.416 36.995 15.634 1.00 74.58 C
ANISOU 2284 CD1 LEU A 301 8772 8623 10941 -780 1999 -119 C
ATOM 2285 CD2 LEU A 301 15.425 36.949 17.037 1.00 76.24 C
ANISOU 2285 CD2 LEU A 301 8581 8828 11558 -841 1946 -271 C
ATOM 2286 N PHE A 302 17.089 40.989 14.642 1.00 78.37 N
ANISOU 2286 N PHE A 302 8974 8667 12137 -1150 2626 -209 N
ATOM 2287 CA PHE A 302 18.290 41.248 13.834 1.00 79.15 C
ANISOU 2287 CA PHE A 302 8998 8652 12422 -1233 2893 -225 C
ATOM 2288 C PHE A 302 19.292 42.144 14.540 1.00 85.25 C
ANISOU 2288 C PHE A 302 9552 9354 13486 -1329 2903 -313 C
ATOM 2289 O PHE A 302 20.495 41.937 14.383 1.00 85.65 O
ANISOU 2289 O PHE A 302 9416 9354 13773 -1383 3039 -374 O
ATOM 2290 CB PHE A 302 17.914 41.817 12.455 1.00 81.06 C
ANISOU 2290 CB PHE A 302 9501 8793 12506 -1255 3122 -122 C
ATOM 2291 CG PHE A 302 17.126 40.903 11.537 1.00 83.33 C
ANISOU 2291 CG PHE A 302 10004 9128 12529 -1170 3150 -43 C
ATOM 2292 CD1 PHE A 302 16.633 39.679 11.990 1.00 86.67 C
ANISOU 2292 CD1 PHE A 302 10394 9684 12854 -1079 2966 -60 C
ATOM 2293 CD2 PHE A 302 16.869 41.268 10.220 1.00 86.28 C
ANISOU 2293 CD2 PHE A 302 10627 9406 12747 -1180 3357 46 C
ATOM 2294 CE1 PHE A 302 15.889 38.849 11.145 1.00 87.97 C
ANISOU 2294 CE1 PHE A 302 10756 9886 12782 -1006 2983 5 C
ATOM 2295 CE2 PHE A 302 16.138 40.426 9.370 1.00 89.13 C
ANISOU 2295 CE2 PHE A 302 11197 9808 12860 -1101 3365 111 C
ATOM 2296 CZ PHE A 302 15.657 39.223 9.838 1.00 87.17 C
ANISOU 2296 CZ PHE A 302 10897 9693 12531 -1017 3177 87 C
ATOM 2297 N SER A 303 18.804 43.127 15.325 1.00 83.26 N
ANISOU 2297 N SER A 303 9316 9092 13226 -1352 2758 -325 N
ATOM 2298 CA SER A 303 19.631 44.047 16.111 1.00 84.01 C
ANISOU 2298 CA SER A 303 9217 9120 13584 -1442 2728 -416 C
ATOM 2299 C SER A 303 20.499 43.290 17.125 1.00 90.20 C
ANISOU 2299 C SER A 303 9721 9974 14577 -1430 2569 -532 C
ATOM 2300 O SER A 303 21.684 43.608 17.261 1.00 90.42 O
ANISOU 2300 O SER A 303 9537 9929 14891 -1511 2649 -615 O
ATOM 2301 CB SER A 303 18.763 45.077 16.825 1.00 87.19 C
ANISOU 2301 CB SER A 303 9718 9517 13893 -1445 2570 -407 C
ATOM 2302 OG SER A 303 18.178 45.969 15.892 1.00 96.00 O
ANISOU 2302 OG SER A 303 11063 10537 14875 -1472 2731 -310 O
ATOM 2303 N LYS A 304 19.918 42.266 17.794 1.00 87.43 N
ANISOU 2303 N LYS A 304 9373 9759 14089 -1327 2350 -538 N
ATOM 2304 CA LYS A 304 20.600 41.424 18.779 1.00 87.38 C
ANISOU 2304 CA LYS A 304 9139 9828 14235 -1291 2171 -636 C
ATOM 2305 C LYS A 304 21.594 40.441 18.156 1.00 92.16 C
ANISOU 2305 C LYS A 304 9602 10426 14989 -1284 2316 -661 C
ATOM 2306 O LYS A 304 22.636 40.184 18.762 1.00 92.38 O
ANISOU 2306 O LYS A 304 9382 10450 15268 -1302 2249 -761 O
ATOM 2307 CB LYS A 304 19.587 40.682 19.668 1.00 89.46 C
ANISOU 2307 CB LYS A 304 9482 10224 14285 -1182 1908 -623 C
ATOM 2308 CG LYS A 304 19.086 41.513 20.841 1.00 99.95 C
ANISOU 2308 CG LYS A 304 10824 11566 15586 -1190 1699 -662 C
ATOM 2309 CD LYS A 304 19.900 41.299 22.117 1.00107.33 C
ANISOU 2309 CD LYS A 304 11537 12531 16712 -1187 1489 -782 C
ATOM 2310 CE LYS A 304 19.491 42.273 23.198 1.00113.95 C
ANISOU 2310 CE LYS A 304 12405 13360 17531 -1208 1311 -827 C
ATOM 2311 NZ LYS A 304 20.329 42.132 24.415 1.00119.91 N
ANISOU 2311 NZ LYS A 304 12959 14132 18471 -1207 1098 -950 N
ATOM 2312 N LEU A 305 21.277 39.891 16.960 1.00 88.44 N
ANISOU 2312 N LEU A 305 9288 9948 14365 -1256 2508 -575 N
ATOM 2313 CA LEU A 305 22.125 38.926 16.247 1.00114.59 C
ANISOU 2313 CA LEU A 305 12500 13248 17789 -1243 2675 -590 C
ATOM 2314 C LEU A 305 23.460 39.520 15.792 1.00154.62 C
ANISOU 2314 C LEU A 305 17388 18190 23171 -1351 2906 -648 C
ATOM 2315 O LEU A 305 23.503 40.634 15.275 1.00120.97 O
ANISOU 2315 O LEU A 305 13204 13821 18937 -1438 3073 -619 O
ATOM 2316 CB LEU A 305 21.381 38.303 15.049 1.00114.56 C
ANISOU 2316 CB LEU A 305 12746 13260 17523 -1190 2825 -484 C
ATOM 2317 CG LEU A 305 20.256 37.306 15.363 1.00119.11 C
ANISOU 2317 CG LEU A 305 13455 13965 17835 -1076 2625 -440 C
ATOM 2318 CD1 LEU A 305 19.339 37.130 14.171 1.00119.11 C
ANISOU 2318 CD1 LEU A 305 13738 13956 17563 -1044 2759 -333 C
ATOM 2319 CD2 LEU A 305 20.804 35.957 15.802 1.00121.63 C
ANISOU 2319 CD2 LEU A 305 13609 14360 18246 -1007 2532 -498 C
TER 2320 LEU A 305
ATOM 2321 N GLU B 9 18.669 60.004 14.612 1.00 78.68 N
ANISOU 2321 N GLU B 9 9262 8028 12603 -1692 4881 -1659 N
ATOM 2322 CA GLU B 9 19.287 60.520 15.834 1.00 78.22 C
ANISOU 2322 CA GLU B 9 8740 8001 12979 -1639 4654 -1716 C
ATOM 2323 C GLU B 9 18.634 61.842 16.267 1.00 79.54 C
ANISOU 2323 C GLU B 9 9103 8215 12903 -1704 4472 -1505 C
ATOM 2324 O GLU B 9 18.925 62.889 15.681 1.00 81.03 O
ANISOU 2324 O GLU B 9 9456 8302 13029 -1907 4821 -1507 O
ATOM 2325 CB GLU B 9 20.806 60.697 15.639 1.00 79.61 C
ANISOU 2325 CB GLU B 9 8499 8045 13704 -1763 5077 -2027 C
ATOM 2326 N VAL B 10 17.731 61.794 17.260 1.00 71.73 N
ANISOU 2326 N VAL B 10 8124 7359 11770 -1540 3959 -1322 N
ATOM 2327 CA VAL B 10 17.058 63.008 17.748 1.00 69.87 C
ANISOU 2327 CA VAL B 10 8055 7165 11328 -1580 3767 -1138 C
ATOM 2328 C VAL B 10 17.128 63.145 19.280 1.00 67.99 C
ANISOU 2328 C VAL B 10 7468 7026 11340 -1443 3328 -1139 C
ATOM 2329 O VAL B 10 17.246 62.144 19.992 1.00 67.57 O
ANISOU 2329 O VAL B 10 7176 7039 11460 -1270 3054 -1187 O
ATOM 2330 CB VAL B 10 15.599 63.212 17.223 1.00 74.03 C
ANISOU 2330 CB VAL B 10 9099 7736 11291 -1564 3633 -879 C
ATOM 2331 CG1 VAL B 10 15.549 63.306 15.696 1.00 74.14 C
ANISOU 2331 CG1 VAL B 10 9532 7638 10999 -1714 4048 -868 C
ATOM 2332 CG2 VAL B 10 14.640 62.145 17.743 1.00 73.77 C
ANISOU 2332 CG2 VAL B 10 9086 7831 11111 -1366 3230 -779 C
ATOM 2333 N GLN B 11 17.061 64.403 19.765 1.00 59.51 N
ANISOU 2333 N GLN B 11 6400 5944 10267 -1524 3271 -1086 N
ATOM 2334 CA GLN B 11 17.030 64.796 21.181 1.00 56.91 C
ANISOU 2334 CA GLN B 11 5828 5701 10093 -1426 2875 -1081 C
ATOM 2335 C GLN B 11 15.728 65.588 21.360 1.00 55.37 C
ANISOU 2335 C GLN B 11 5990 5556 9493 -1421 2693 -842 C
ATOM 2336 O GLN B 11 15.384 66.371 20.471 1.00 56.45 O
ANISOU 2336 O GLN B 11 6440 5604 9405 -1552 2941 -749 O
ATOM 2337 CB GLN B 11 18.231 65.689 21.551 1.00 58.13 C
ANISOU 2337 CB GLN B 11 5635 5774 10679 -1554 3015 -1291 C
ATOM 2338 CG GLN B 11 19.590 65.175 21.081 1.00 87.22 C
ANISOU 2338 CG GLN B 11 8963 9361 14815 -1617 3325 -1565 C
ATOM 2339 CD GLN B 11 20.329 64.409 22.147 1.00111.18 C
ANISOU 2339 CD GLN B 11 11525 12457 18260 -1438 2979 -1739 C
ATOM 2340 OE1 GLN B 11 19.993 63.265 22.474 1.00106.92 O
ANISOU 2340 OE1 GLN B 11 10983 11994 17649 -1240 2710 -1678 O
ATOM 2341 NE2 GLN B 11 21.370 65.023 22.700 1.00103.09 N
ANISOU 2341 NE2 GLN B 11 10096 11384 17688 -1504 2971 -1965 N
ATOM 2342 N LEU B 12 14.998 65.370 22.473 1.00 44.62 N
ANISOU 2342 N LEU B 12 4600 4319 8035 -1266 2275 -744 N
ATOM 2343 CA LEU B 12 13.719 66.018 22.745 1.00 42.49 C
ANISOU 2343 CA LEU B 12 4614 4098 7431 -1238 2090 -546 C
ATOM 2344 C LEU B 12 13.753 66.875 23.980 1.00 45.78 C
ANISOU 2344 C LEU B 12 4882 4554 7959 -1222 1858 -572 C
ATOM 2345 O LEU B 12 14.378 66.506 24.971 1.00 46.17 O
ANISOU 2345 O LEU B 12 4641 4660 8240 -1144 1649 -689 O
ATOM 2346 CB LEU B 12 12.578 64.982 22.920 1.00 41.72 C
ANISOU 2346 CB LEU B 12 4671 4106 7073 -1084 1842 -405 C
ATOM 2347 CG LEU B 12 12.389 63.936 21.822 1.00 44.60 C
ANISOU 2347 CG LEU B 12 5191 4450 7307 -1074 1997 -389 C
ATOM 2348 CD1 LEU B 12 11.377 62.881 22.251 1.00 43.71 C
ANISOU 2348 CD1 LEU B 12 5149 4430 7028 -928 1724 -287 C
ATOM 2349 CD2 LEU B 12 12.005 64.581 20.482 1.00 44.60 C
ANISOU 2349 CD2 LEU B 12 5539 4359 7047 -1199 2263 -312 C
ATOM 2350 N VAL B 13 13.037 68.003 23.936 1.00 41.29 N
ANISOU 2350 N VAL B 13 4532 3947 7209 -1282 1868 -464 N
ATOM 2351 CA VAL B 13 12.878 68.907 25.065 1.00 40.94 C
ANISOU 2351 CA VAL B 13 4406 3930 7218 -1272 1662 -484 C
ATOM 2352 C VAL B 13 11.407 69.292 25.122 1.00 42.72 C
ANISOU 2352 C VAL B 13 4927 4186 7118 -1209 1527 -294 C
ATOM 2353 O VAL B 13 10.894 69.856 24.154 1.00 42.58 O
ANISOU 2353 O VAL B 13 5175 4073 6930 -1270 1693 -185 O
ATOM 2354 CB VAL B 13 13.795 70.175 24.987 1.00 45.50 C
ANISOU 2354 CB VAL B 13 4870 4373 8044 -1445 1873 -616 C
ATOM 2355 CG1 VAL B 13 13.498 71.145 26.131 1.00 45.64 C
ANISOU 2355 CG1 VAL B 13 4846 4412 8083 -1435 1651 -642 C
ATOM 2356 CG2 VAL B 13 15.276 69.810 24.976 1.00 45.53 C
ANISOU 2356 CG2 VAL B 13 4512 4341 8445 -1511 2005 -847 C
ATOM 2357 N GLU B 14 10.736 69.005 26.246 1.00 37.40 N
ANISOU 2357 N GLU B 14 4217 3630 6363 -1087 1232 -262 N
ATOM 2358 CA GLU B 14 9.348 69.415 26.456 1.00 36.70 C
ANISOU 2358 CA GLU B 14 4343 3566 6035 -1028 1110 -125 C
ATOM 2359 C GLU B 14 9.369 70.806 27.071 1.00 40.45 C
ANISOU 2359 C GLU B 14 4808 3979 6583 -1087 1094 -175 C
ATOM 2360 O GLU B 14 10.263 71.123 27.868 1.00 40.72 O
ANISOU 2360 O GLU B 14 4634 4020 6817 -1127 1041 -324 O
ATOM 2361 CB GLU B 14 8.586 68.487 27.433 1.00 37.88 C
ANISOU 2361 CB GLU B 14 4469 3852 6070 -893 858 -83 C
ATOM 2362 CG GLU B 14 8.521 67.026 27.030 1.00 40.54 C
ANISOU 2362 CG GLU B 14 4805 4242 6356 -824 843 -42 C
ATOM 2363 CD GLU B 14 9.693 66.202 27.515 1.00 47.88 C
ANISOU 2363 CD GLU B 14 5507 5201 7485 -790 784 -154 C
ATOM 2364 OE1 GLU B 14 9.604 64.960 27.438 1.00 46.85 O
ANISOU 2364 OE1 GLU B 14 5370 5105 7327 -712 732 -123 O
ATOM 2365 OE2 GLU B 14 10.707 66.786 27.959 1.00 40.11 O
ANISOU 2365 OE2 GLU B 14 4340 4192 6709 -837 779 -285 O
ATOM 2366 N SER B 15 8.376 71.627 26.717 1.00 35.78 N
ANISOU 2366 N SER B 15 4435 3316 5844 -1084 1115 -66 N
ATOM 2367 CA SER B 15 8.213 72.959 27.279 1.00 35.13 C
ANISOU 2367 CA SER B 15 4374 3152 5823 -1125 1100 -105 C
ATOM 2368 C SER B 15 6.724 73.318 27.398 1.00 36.29 C
ANISOU 2368 C SER B 15 4698 3298 5793 -1025 982 9 C
ATOM 2369 O SER B 15 5.877 72.641 26.811 1.00 35.13 O
ANISOU 2369 O SER B 15 4669 3191 5488 -946 938 122 O
ATOM 2370 CB SER B 15 9.022 74.007 26.503 1.00 39.03 C
ANISOU 2370 CB SER B 15 4919 3458 6454 -1277 1353 -137 C
ATOM 2371 OG SER B 15 8.378 74.430 25.315 1.00 50.20 O
ANISOU 2371 OG SER B 15 6632 4741 7700 -1286 1482 25 O
ATOM 2372 N GLY B 16 6.428 74.341 28.187 1.00 32.07 N
ANISOU 2372 N GLY B 16 4155 2716 5314 -1027 927 -49 N
ATOM 2373 CA GLY B 16 5.070 74.834 28.386 1.00 31.36 C
ANISOU 2373 CA GLY B 16 4188 2600 5127 -932 834 19 C
ATOM 2374 C GLY B 16 4.453 74.525 29.728 1.00 33.87 C
ANISOU 2374 C GLY B 16 4409 3051 5407 -857 680 -57 C
ATOM 2375 O GLY B 16 3.326 74.938 29.985 1.00 34.72 O
ANISOU 2375 O GLY B 16 4579 3136 5477 -784 630 -36 O
ATOM 2376 N GLY B 17 5.167 73.788 30.577 1.00 30.24 N
ANISOU 2376 N GLY B 17 3810 2720 4960 -871 608 -147 N
ATOM 2377 CA GLY B 17 4.680 73.433 31.913 1.00 30.23 C
ANISOU 2377 CA GLY B 17 3774 2839 4873 -812 477 -213 C
ATOM 2378 C GLY B 17 4.386 74.662 32.759 1.00 34.69 C
ANISOU 2378 C GLY B 17 4359 3341 5480 -832 471 -326 C
ATOM 2379 O GLY B 17 5.061 75.673 32.614 1.00 34.56 O
ANISOU 2379 O GLY B 17 4318 3209 5602 -913 531 -401 O
ATOM 2380 N GLY B 18 3.362 74.610 33.595 1.00 32.09 N
ANISOU 2380 N GLY B 18 4078 3066 5049 -770 432 -349 N
ATOM 2381 CA GLY B 18 2.977 75.779 34.378 1.00 31.89 C
ANISOU 2381 CA GLY B 18 4081 2969 5064 -782 453 -474 C
ATOM 2382 C GLY B 18 1.861 75.494 35.352 1.00 35.75 C
ANISOU 2382 C GLY B 18 4621 3535 5428 -722 451 -514 C
ATOM 2383 O GLY B 18 1.577 74.336 35.631 1.00 34.11 O
ANISOU 2383 O GLY B 18 4428 3445 5086 -688 420 -455 O
ATOM 2384 N LEU B 19 1.285 76.564 35.927 1.00 34.34 N
ANISOU 2384 N LEU B 19 4472 3272 5302 -719 507 -631 N
ATOM 2385 CA LEU B 19 0.199 76.509 36.901 1.00 34.33 C
ANISOU 2385 CA LEU B 19 4517 3315 5213 -679 567 -712 C
ATOM 2386 C LEU B 19 -1.093 76.885 36.211 1.00 39.37 C
ANISOU 2386 C LEU B 19 5121 3849 5988 -597 647 -663 C
ATOM 2387 O LEU B 19 -1.178 77.932 35.571 1.00 38.59 O
ANISOU 2387 O LEU B 19 5015 3591 6055 -574 658 -661 O
ATOM 2388 CB LEU B 19 0.461 77.450 38.100 1.00 34.14 C
ANISOU 2388 CB LEU B 19 4546 3263 5163 -731 582 -921 C
ATOM 2389 CG LEU B 19 -0.619 77.434 39.211 1.00 37.79 C
ANISOU 2389 CG LEU B 19 5085 3762 5510 -709 697 -1036 C
ATOM 2390 CD1 LEU B 19 -0.779 76.036 39.830 1.00 37.08 C
ANISOU 2390 CD1 LEU B 19 5080 3833 5176 -709 690 -970 C
ATOM 2391 CD2 LEU B 19 -0.325 78.468 40.280 1.00 38.65 C
ANISOU 2391 CD2 LEU B 19 5269 3825 5589 -764 717 -1260 C
ATOM 2392 N VAL B 20 -2.097 76.018 36.339 1.00 37.38 N
ANISOU 2392 N VAL B 20 4847 3672 5683 -550 693 -626 N
ATOM 2393 CA VAL B 20 -3.414 76.156 35.703 1.00 37.61 C
ANISOU 2393 CA VAL B 20 4797 3622 5872 -458 732 -598 C
ATOM 2394 C VAL B 20 -4.503 76.095 36.789 1.00 40.71 C
ANISOU 2394 C VAL B 20 5159 4041 6268 -450 883 -744 C
ATOM 2395 O VAL B 20 -4.404 75.300 37.725 1.00 40.04 O
ANISOU 2395 O VAL B 20 5144 4075 5993 -513 954 -777 O
ATOM 2396 CB VAL B 20 -3.582 74.986 34.674 1.00 42.85 C
ANISOU 2396 CB VAL B 20 5427 4349 6505 -429 657 -432 C
ATOM 2397 CG1 VAL B 20 -4.917 75.038 33.950 1.00 42.74 C
ANISOU 2397 CG1 VAL B 20 5313 4260 6666 -328 639 -416 C
ATOM 2398 CG2 VAL B 20 -2.432 74.945 33.663 1.00 42.85 C
ANISOU 2398 CG2 VAL B 20 5480 4330 6472 -457 561 -306 C
ATOM 2399 N GLN B 21 -5.541 76.911 36.662 1.00 38.04 N
ANISOU 2399 N GLN B 21 4726 3577 6149 -372 943 -833 N
ATOM 2400 CA GLN B 21 -6.679 76.826 37.583 1.00 38.85 C
ANISOU 2400 CA GLN B 21 4762 3689 6311 -368 1133 -993 C
ATOM 2401 C GLN B 21 -7.601 75.687 37.065 1.00 41.64 C
ANISOU 2401 C GLN B 21 4990 4099 6732 -338 1144 -921 C
ATOM 2402 O GLN B 21 -7.602 75.454 35.852 1.00 39.96 O
ANISOU 2402 O GLN B 21 4722 3861 6601 -274 973 -783 O
ATOM 2403 CB GLN B 21 -7.427 78.179 37.640 1.00 40.65 C
ANISOU 2403 CB GLN B 21 4898 3738 6811 -282 1193 -1147 C
ATOM 2404 CG GLN B 21 -7.074 79.049 38.862 1.00 67.18 C
ANISOU 2404 CG GLN B 21 8365 7066 10094 -348 1331 -1342 C
ATOM 2405 CD GLN B 21 -5.622 79.474 38.910 1.00 96.57 C
ANISOU 2405 CD GLN B 21 12236 10797 13658 -421 1207 -1300 C
ATOM 2406 OE1 GLN B 21 -4.789 78.860 39.591 1.00 92.04 O
ANISOU 2406 OE1 GLN B 21 11788 10365 12817 -519 1190 -1296 O
ATOM 2407 NE2 GLN B 21 -5.289 80.540 38.192 1.00 93.88 N
ANISOU 2407 NE2 GLN B 21 11883 10290 13496 -375 1113 -1276 N
ATOM 2408 N PRO B 22 -8.348 74.934 37.924 1.00 38.94 N
ANISOU 2408 N PRO B 22 4622 3827 6348 -397 1349 -1012 N
ATOM 2409 CA PRO B 22 -9.222 73.867 37.399 1.00 37.96 C
ANISOU 2409 CA PRO B 22 4355 3736 6334 -387 1368 -964 C
ATOM 2410 C PRO B 22 -10.157 74.396 36.327 1.00 40.79 C
ANISOU 2410 C PRO B 22 4486 3975 7038 -251 1237 -990 C
ATOM 2411 O PRO B 22 -10.744 75.454 36.487 1.00 41.22 O
ANISOU 2411 O PRO B 22 4438 3909 7315 -173 1278 -1130 O
ATOM 2412 CB PRO B 22 -9.976 73.386 38.639 1.00 39.92 C
ANISOU 2412 CB PRO B 22 4611 4017 6538 -482 1681 -1111 C
ATOM 2413 CG PRO B 22 -9.062 73.689 39.766 1.00 45.24 C
ANISOU 2413 CG PRO B 22 5543 4742 6904 -562 1757 -1146 C
ATOM 2414 CD PRO B 22 -8.480 75.034 39.390 1.00 41.19 C
ANISOU 2414 CD PRO B 22 5023 4145 6484 -486 1594 -1174 C
ATOM 2415 N GLY B 23 -10.206 73.698 35.209 1.00 37.56 N
ANISOU 2415 N GLY B 23 4023 3589 6660 -211 1050 -855 N
ATOM 2416 CA GLY B 23 -11.004 74.109 34.069 1.00 37.62 C
ANISOU 2416 CA GLY B 23 3860 3487 6948 -67 847 -855 C
ATOM 2417 C GLY B 23 -10.207 74.896 33.048 1.00 40.12 C
ANISOU 2417 C GLY B 23 4319 3722 7202 17 604 -705 C
ATOM 2418 O GLY B 23 -10.705 75.177 31.960 1.00 38.37 O
ANISOU 2418 O GLY B 23 4039 3405 7134 144 384 -656 O
ATOM 2419 N GLY B 24 -8.979 75.253 33.403 1.00 38.46 N
ANISOU 2419 N GLY B 24 4306 3537 6769 -58 644 -638 N
ATOM 2420 CA GLY B 24 -8.076 76.013 32.543 1.00 38.41 C
ANISOU 2420 CA GLY B 24 4457 3441 6697 -22 487 -505 C
ATOM 2421 C GLY B 24 -7.418 75.163 31.469 1.00 44.00 C
ANISOU 2421 C GLY B 24 5269 4215 7234 -48 352 -322 C
ATOM 2422 O GLY B 24 -7.506 73.934 31.494 1.00 42.88 O
ANISOU 2422 O GLY B 24 5087 4201 7005 -101 374 -298 O
ATOM 2423 N SER B 25 -6.732 75.831 30.529 1.00 42.55 N
ANISOU 2423 N SER B 25 5240 3926 7001 -18 237 -199 N
ATOM 2424 CA SER B 25 -6.044 75.265 29.367 1.00 41.71 C
ANISOU 2424 CA SER B 25 5275 3842 6730 -41 134 -33 C
ATOM 2425 C SER B 25 -4.552 75.564 29.401 1.00 44.57 C
ANISOU 2425 C SER B 25 5785 4203 6948 -153 223 28 C
ATOM 2426 O SER B 25 -4.120 76.568 29.976 1.00 43.75 O
ANISOU 2426 O SER B 25 5707 4016 6899 -183 299 -33 O
ATOM 2427 CB SER B 25 -6.603 75.878 28.087 1.00 46.57 C
ANISOU 2427 CB SER B 25 5986 4296 7414 93 -66 60 C
ATOM 2428 OG SER B 25 -7.864 75.321 27.776 1.00 59.60 O
ANISOU 2428 OG SER B 25 7485 5968 9193 194 -207 9 O
ATOM 2429 N LEU B 26 -3.781 74.737 28.700 1.00 40.05 N
ANISOU 2429 N LEU B 26 5296 3701 6219 -214 213 132 N
ATOM 2430 CA LEU B 26 -2.336 74.857 28.608 1.00 39.90 C
ANISOU 2430 CA LEU B 26 5372 3683 6105 -326 306 172 C
ATOM 2431 C LEU B 26 -1.854 74.106 27.363 1.00 40.55 C
ANISOU 2431 C LEU B 26 5572 3781 6054 -349 280 297 C
ATOM 2432 O LEU B 26 -2.371 73.039 27.044 1.00 37.20 O
ANISOU 2432 O LEU B 26 5110 3450 5575 -318 214 317 O
ATOM 2433 CB LEU B 26 -1.692 74.249 29.885 1.00 40.55 C
ANISOU 2433 CB LEU B 26 5345 3916 6146 -413 392 74 C
ATOM 2434 CG LEU B 26 -0.228 74.577 30.182 1.00 46.14 C
ANISOU 2434 CG LEU B 26 6073 4622 6837 -520 465 43 C
ATOM 2435 CD1 LEU B 26 -0.036 76.070 30.489 1.00 46.29 C
ANISOU 2435 CD1 LEU B 26 6126 4491 6971 -541 510 -28 C
ATOM 2436 CD2 LEU B 26 0.266 73.757 31.349 1.00 48.58 C
ANISOU 2436 CD2 LEU B 26 6293 5086 7078 -566 470 -38 C
ATOM 2437 N ARG B 27 -0.869 74.670 26.662 1.00 37.67 N
ANISOU 2437 N ARG B 27 5356 3312 5645 -416 358 364 N
ATOM 2438 CA ARG B 27 -0.293 74.009 25.494 1.00 36.48 C
ANISOU 2438 CA ARG B 27 5343 3164 5354 -459 390 461 C
ATOM 2439 C ARG B 27 1.150 73.632 25.773 1.00 37.58 C
ANISOU 2439 C ARG B 27 5417 3364 5497 -591 551 415 C
ATOM 2440 O ARG B 27 1.957 74.494 26.140 1.00 37.49 O
ANISOU 2440 O ARG B 27 5391 3275 5578 -670 657 366 O
ATOM 2441 CB ARG B 27 -0.374 74.882 24.234 1.00 35.67 C
ANISOU 2441 CB ARG B 27 5513 2864 5175 -433 377 587 C
ATOM 2442 CG ARG B 27 -0.059 74.080 22.958 1.00 41.02 C
ANISOU 2442 CG ARG B 27 6377 3552 5657 -461 397 680 C
ATOM 2443 CD ARG B 27 -0.088 74.944 21.714 1.00 42.83 C
ANISOU 2443 CD ARG B 27 6952 3572 5750 -444 395 820 C
ATOM 2444 NE ARG B 27 1.013 75.898 21.694 1.00 52.21 N
ANISOU 2444 NE ARG B 27 8242 4612 6984 -572 630 837 N
ATOM 2445 CZ ARG B 27 1.242 76.762 20.707 1.00 76.14 C
ANISOU 2445 CZ ARG B 27 11610 7422 9898 -600 713 967 C
ATOM 2446 NH1 ARG B 27 0.456 76.782 19.636 1.00 63.99 N
ANISOU 2446 NH1 ARG B 27 10368 5792 8154 -489 539 1101 N
ATOM 2447 NH2 ARG B 27 2.260 77.608 20.781 1.00 60.94 N
ANISOU 2447 NH2 ARG B 27 9743 5352 8058 -743 963 960 N
ATOM 2448 N LEU B 28 1.478 72.353 25.585 1.00 32.82 N
ANISOU 2448 N LEU B 28 4760 2887 4825 -611 561 414 N
ATOM 2449 CA LEU B 28 2.856 71.889 25.729 1.00 31.96 C
ANISOU 2449 CA LEU B 28 4565 2824 4755 -713 693 360 C
ATOM 2450 C LEU B 28 3.481 71.734 24.356 1.00 36.81 C
ANISOU 2450 C LEU B 28 5346 3356 5282 -776 829 427 C
ATOM 2451 O LEU B 28 2.765 71.522 23.376 1.00 36.58 O
ANISOU 2451 O LEU B 28 5501 3291 5107 -725 774 518 O
ATOM 2452 CB LEU B 28 2.960 70.568 26.493 1.00 31.17 C
ANISOU 2452 CB LEU B 28 4298 2888 4657 -691 633 306 C
ATOM 2453 CG LEU B 28 2.248 70.479 27.855 1.00 33.88 C
ANISOU 2453 CG LEU B 28 4528 3319 5026 -637 525 249 C
ATOM 2454 CD1 LEU B 28 2.373 69.097 28.413 1.00 32.66 C
ANISOU 2454 CD1 LEU B 28 4284 3288 4837 -618 482 234 C
ATOM 2455 CD2 LEU B 28 2.774 71.519 28.843 1.00 34.52 C
ANISOU 2455 CD2 LEU B 28 4544 3371 5200 -678 541 156 C
ATOM 2456 N SER B 29 4.809 71.814 24.288 1.00 33.23 N
ANISOU 2456 N SER B 29 4830 2872 4924 -889 1008 365 N
ATOM 2457 CA SER B 29 5.557 71.611 23.048 1.00 33.58 C
ANISOU 2457 CA SER B 29 5022 2836 4903 -977 1211 397 C
ATOM 2458 C SER B 29 6.622 70.573 23.275 1.00 39.36 C
ANISOU 2458 C SER B 29 5541 3662 5753 -1024 1301 288 C
ATOM 2459 O SER B 29 7.216 70.516 24.348 1.00 39.75 O
ANISOU 2459 O SER B 29 5345 3777 5981 -1031 1251 179 O
ATOM 2460 CB SER B 29 6.218 72.902 22.582 1.00 34.55 C
ANISOU 2460 CB SER B 29 5280 2767 5080 -1094 1417 412 C
ATOM 2461 OG SER B 29 5.241 73.888 22.317 1.00 45.74 O
ANISOU 2461 OG SER B 29 6919 4063 6396 -1031 1320 526 O
ATOM 2462 N CYS B 30 6.861 69.757 22.269 1.00 37.11 N
ANISOU 2462 N CYS B 30 5358 3373 5369 -1046 1416 306 N
ATOM 2463 CA CYS B 30 7.905 68.746 22.278 1.00 38.23 C
ANISOU 2463 CA CYS B 30 5309 3571 5646 -1082 1529 195 C
ATOM 2464 C CYS B 30 8.753 69.129 21.087 1.00 43.47 C
ANISOU 2464 C CYS B 30 6127 4093 6296 -1220 1854 180 C
ATOM 2465 O CYS B 30 8.280 69.042 19.958 1.00 41.81 O
ANISOU 2465 O CYS B 30 6219 3823 5845 -1229 1928 273 O
ATOM 2466 CB CYS B 30 7.327 67.338 22.142 1.00 39.16 C
ANISOU 2466 CB CYS B 30 5425 3795 5657 -986 1403 214 C
ATOM 2467 SG CYS B 30 8.583 66.043 21.967 1.00 43.73 S
ANISOU 2467 SG CYS B 30 5801 4402 6413 -1010 1554 78 S
ATOM 2468 N GLU B 31 9.939 69.680 21.345 1.00 42.86 N
ANISOU 2468 N GLU B 31 5870 3947 6469 -1336 2046 60 N
ATOM 2469 CA GLU B 31 10.835 70.144 20.285 1.00 44.24 C
ANISOU 2469 CA GLU B 31 6174 3961 6674 -1502 2426 25 C
ATOM 2470 C GLU B 31 11.971 69.177 20.117 1.00 51.03 C
ANISOU 2470 C GLU B 31 6788 4849 7752 -1550 2614 -145 C
ATOM 2471 O GLU B 31 12.554 68.716 21.105 1.00 48.60 O
ANISOU 2471 O GLU B 31 6114 4633 7720 -1499 2478 -279 O
ATOM 2472 CB GLU B 31 11.391 71.549 20.570 1.00 45.84 C
ANISOU 2472 CB GLU B 31 6343 4021 7053 -1632 2572 -14 C
ATOM 2473 CG GLU B 31 10.335 72.619 20.772 1.00 60.55 C
ANISOU 2473 CG GLU B 31 8436 5822 8750 -1580 2400 137 C
ATOM 2474 CD GLU B 31 10.852 74.038 20.913 1.00 83.10 C
ANISOU 2474 CD GLU B 31 11313 8494 11768 -1719 2577 108 C
ATOM 2475 OE1 GLU B 31 11.725 74.452 20.113 1.00 79.57 O
ANISOU 2475 OE1 GLU B 31 10964 7880 11389 -1896 2945 73 O
ATOM 2476 OE2 GLU B 31 10.352 74.750 21.814 1.00 74.65 O
ANISOU 2476 OE2 GLU B 31 10176 7431 10757 -1660 2368 113 O
ATOM 2477 N ALA B 32 12.303 68.896 18.859 1.00 52.64 N
ANISOU 2477 N ALA B 32 7207 4961 7833 -1644 2927 -146 N
ATOM 2478 CA ALA B 32 13.357 67.965 18.513 1.00 55.05 C
ANISOU 2478 CA ALA B 32 7303 5266 8347 -1693 3164 -322 C
ATOM 2479 C ALA B 32 14.563 68.622 17.881 1.00 64.61 C
ANISOU 2479 C ALA B 32 8481 6305 9762 -1907 3631 -452 C
ATOM 2480 O ALA B 32 14.441 69.601 17.143 1.00 63.32 O
ANISOU 2480 O ALA B 32 8657 5989 9413 -2039 3865 -351 O
ATOM 2481 CB ALA B 32 12.817 66.880 17.605 1.00 55.79 C
ANISOU 2481 CB ALA B 32 7638 5399 8161 -1633 3180 -271 C
ATOM 2482 N SER B 33 15.736 68.065 18.192 1.00 67.06 N
ANISOU 2482 N SER B 33 8377 6625 10479 -1939 3765 -683 N
ATOM 2483 CA SER B 33 17.030 68.470 17.660 1.00 69.60 C
ANISOU 2483 CA SER B 33 8549 6788 11107 -2148 4243 -876 C
ATOM 2484 C SER B 33 17.610 67.243 16.970 1.00 78.05 C
ANISOU 2484 C SER B 33 9527 7861 12266 -2141 4477 -1023 C
ATOM 2485 O SER B 33 17.640 66.168 17.567 1.00 77.99 O
ANISOU 2485 O SER B 33 9245 7982 12408 -1969 4204 -1096 O
ATOM 2486 CB SER B 33 17.950 68.947 18.779 1.00 74.12 C
ANISOU 2486 CB SER B 33 8618 7364 12180 -2177 4149 -1073 C
ATOM 2487 OG SER B 33 18.071 70.359 18.749 1.00 86.71 O
ANISOU 2487 OG SER B 33 10327 8814 13805 -2348 4324 -1043 O
ATOM 2488 N GLY B 34 18.011 67.405 15.714 1.00 77.91 N
ANISOU 2488 N GLY B 34 9784 7691 12129 -2324 4983 -1057 N
ATOM 2489 CA GLY B 34 18.554 66.329 14.890 1.00 79.33 C
ANISOU 2489 CA GLY B 34 9941 7843 12357 -2348 5292 -1213 C
ATOM 2490 C GLY B 34 18.210 66.509 13.426 1.00 88.16 C
ANISOU 2490 C GLY B 34 11660 8837 13000 -2491 5684 -1101 C
ATOM 2491 O GLY B 34 17.569 67.498 13.066 1.00 88.37 O
ANISOU 2491 O GLY B 34 12117 8787 12673 -2562 5692 -890 O
ATOM 2492 N TYR B 35 18.633 65.555 12.569 1.00 88.16 N
ANISOU 2492 N TYR B 35 11716 8802 12979 -2527 6003 -1247 N
ATOM 2493 CA TYR B 35 18.434 65.589 11.108 1.00 88.94 C
ANISOU 2493 CA TYR B 35 12411 8775 12606 -2674 6419 -1183 C
ATOM 2494 C TYR B 35 16.968 65.847 10.679 1.00 92.51 C
ANISOU 2494 C TYR B 35 13464 9275 12410 -2582 6081 -870 C
ATOM 2495 O TYR B 35 16.711 66.884 10.056 1.00 92.68 O
ANISOU 2495 O TYR B 35 13950 9158 12107 -2712 6259 -705 O
ATOM 2496 CB TYR B 35 19.002 64.321 10.434 1.00 90.51 C
ANISOU 2496 CB TYR B 35 12528 8965 12895 -2678 6720 -1414 C
ATOM 2497 N THR B 36 16.020 64.928 11.018 1.00 87.24 N
ANISOU 2497 N THR B 36 12782 8783 11583 -2359 5595 -795 N
ATOM 2498 CA THR B 36 14.596 65.065 10.661 1.00 86.17 C
ANISOU 2498 CA THR B 36 13134 8702 10904 -2252 5226 -541 C
ATOM 2499 C THR B 36 13.655 64.328 11.636 1.00 86.71 C
ANISOU 2499 C THR B 36 12947 8971 11027 -2011 4631 -479 C
ATOM 2500 O THR B 36 14.018 63.293 12.193 1.00 87.23 O
ANISOU 2500 O THR B 36 12616 9126 11402 -1918 4546 -632 O
ATOM 2501 CB THR B 36 14.331 64.669 9.178 1.00 96.21 C
ANISOU 2501 CB THR B 36 14991 9892 11672 -2332 5484 -526 C
ATOM 2502 OG1 THR B 36 12.979 64.986 8.830 1.00 97.30 O
ANISOU 2502 OG1 THR B 36 15597 10063 11310 -2228 5093 -283 O
ATOM 2503 CG2 THR B 36 14.636 63.198 8.874 1.00 94.35 C
ANISOU 2503 CG2 THR B 36 14600 9720 11529 -2284 5581 -740 C
ATOM 2504 N LEU B 37 12.438 64.871 11.810 1.00 79.60 N
ANISOU 2504 N LEU B 37 12296 8120 9830 -1911 4238 -256 N
ATOM 2505 CA LEU B 37 11.373 64.338 12.670 1.00 77.08 C
ANISOU 2505 CA LEU B 37 11804 7968 9514 -1708 3706 -177 C
ATOM 2506 C LEU B 37 10.273 63.635 11.844 1.00 77.25 C
ANISOU 2506 C LEU B 37 12202 8033 9116 -1628 3498 -109 C
ATOM 2507 O LEU B 37 9.477 62.878 12.399 1.00 77.45 O
ANISOU 2507 O LEU B 37 12068 8186 9174 -1483 3134 -98 O
ATOM 2508 CB LEU B 37 10.769 65.486 13.516 1.00 76.56 C
ANISOU 2508 CB LEU B 37 11694 7917 9476 -1654 3420 -13 C
ATOM 2509 CG LEU B 37 9.902 65.098 14.739 1.00 80.35 C
ANISOU 2509 CG LEU B 37 11881 8561 10085 -1471 2942 34 C
ATOM 2510 CD1 LEU B 37 10.723 64.401 15.815 1.00 80.12 C
ANISOU 2510 CD1 LEU B 37 11342 8613 10485 -1429 2925 -122 C
ATOM 2511 CD2 LEU B 37 9.216 66.310 15.337 1.00 80.85 C
ANISOU 2511 CD2 LEU B 37 11994 8611 10112 -1431 2715 185 C
ATOM 2512 N ALA B 38 10.241 63.889 10.523 1.00 70.72 N
ANISOU 2512 N ALA B 38 11886 7091 7895 -1732 3735 -73 N
ATOM 2513 CA ALA B 38 9.261 63.361 9.566 1.00 68.76 C
ANISOU 2513 CA ALA B 38 12069 6859 7196 -1676 3546 -24 C
ATOM 2514 C ALA B 38 8.843 61.907 9.789 1.00 67.27 C
ANISOU 2514 C ALA B 38 11660 6801 7099 -1563 3324 -150 C
ATOM 2515 O ALA B 38 7.646 61.642 9.856 1.00 67.15 O
ANISOU 2515 O ALA B 38 11728 6867 6918 -1442 2907 -74 O
ATOM 2516 CB ALA B 38 9.758 63.542 8.138 1.00 69.10 C
ANISOU 2516 CB ALA B 38 12639 6750 6865 -1837 3969 -50 C
ATOM 2517 N ASN B 39 9.822 60.981 9.894 1.00 59.46 N
ANISOU 2517 N ASN B 39 10382 5813 6398 -1605 3605 -353 N
ATOM 2518 CA ASN B 39 9.586 59.541 10.029 1.00 57.77 C
ANISOU 2518 CA ASN B 39 9979 5677 6293 -1513 3465 -489 C
ATOM 2519 C ASN B 39 9.350 59.057 11.469 1.00 55.38 C
ANISOU 2519 C ASN B 39 9173 5487 6381 -1370 3139 -477 C
ATOM 2520 O ASN B 39 9.217 57.853 11.673 1.00 55.22 O
ANISOU 2520 O ASN B 39 8984 5505 6490 -1296 3040 -579 O
ATOM 2521 CB ASN B 39 10.726 58.740 9.362 1.00 62.66 C
ANISOU 2521 CB ASN B 39 10569 6212 7027 -1612 3931 -721 C
ATOM 2522 CG ASN B 39 12.022 58.740 10.139 1.00 96.62 C
ANISOU 2522 CG ASN B 39 14376 10482 11854 -1637 4189 -848 C
ATOM 2523 OD1 ASN B 39 12.275 57.859 10.978 1.00 86.25 O
ANISOU 2523 OD1 ASN B 39 12639 9220 10912 -1525 4052 -942 O
ATOM 2524 ND2 ASN B 39 12.869 59.733 9.874 1.00 93.52 N
ANISOU 2524 ND2 ASN B 39 14032 9990 11512 -1784 4556 -858 N
ATOM 2525 N TYR B 40 9.290 59.969 12.449 1.00 48.18 N
ANISOU 2525 N TYR B 40 8057 4613 5637 -1336 2983 -355 N
ATOM 2526 CA TYR B 40 9.068 59.614 13.854 1.00 46.54 C
ANISOU 2526 CA TYR B 40 7434 4504 5746 -1210 2687 -332 C
ATOM 2527 C TYR B 40 7.616 59.706 14.294 1.00 46.80 C
ANISOU 2527 C TYR B 40 7534 4625 5622 -1107 2265 -190 C
ATOM 2528 O TYR B 40 6.877 60.584 13.851 1.00 45.73 O
ANISOU 2528 O TYR B 40 7680 4477 5220 -1118 2151 -68 O
ATOM 2529 CB TYR B 40 9.912 60.501 14.794 1.00 47.60 C
ANISOU 2529 CB TYR B 40 7269 4630 6187 -1234 2762 -322 C
ATOM 2530 CG TYR B 40 11.375 60.126 14.871 1.00 50.76 C
ANISOU 2530 CG TYR B 40 7377 4968 6940 -1287 3082 -509 C
ATOM 2531 CD1 TYR B 40 12.288 60.604 13.934 1.00 54.56 C
ANISOU 2531 CD1 TYR B 40 7995 5332 7404 -1446 3523 -604 C
ATOM 2532 CD2 TYR B 40 11.865 59.363 15.925 1.00 50.88 C
ANISOU 2532 CD2 TYR B 40 6977 5029 7328 -1179 2945 -594 C
ATOM 2533 CE1 TYR B 40 13.644 60.283 14.014 1.00 58.24 C
ANISOU 2533 CE1 TYR B 40 8136 5731 8260 -1498 3833 -811 C
ATOM 2534 CE2 TYR B 40 13.218 59.041 16.021 1.00 51.95 C
ANISOU 2534 CE2 TYR B 40 6801 5097 7840 -1204 3196 -785 C
ATOM 2535 CZ TYR B 40 14.104 59.493 15.058 1.00 66.34 C
ANISOU 2535 CZ TYR B 40 8710 6809 9688 -1365 3647 -908 C
ATOM 2536 OH TYR B 40 15.437 59.162 15.141 1.00 73.00 O
ANISOU 2536 OH TYR B 40 9197 7577 10962 -1391 3911 -1131 O
ATOM 2537 N ALA B 41 7.221 58.806 15.192 1.00 41.09 N
ANISOU 2537 N ALA B 41 6549 3975 5088 -1005 2040 -207 N
ATOM 2538 CA ALA B 41 5.942 58.875 15.887 1.00 39.61 C
ANISOU 2538 CA ALA B 41 6324 3868 4858 -917 1681 -98 C
ATOM 2539 C ALA B 41 6.310 59.541 17.204 1.00 41.41 C
ANISOU 2539 C ALA B 41 6272 4135 5328 -883 1619 -39 C
ATOM 2540 O ALA B 41 7.399 59.298 17.756 1.00 39.50 O
ANISOU 2540 O ALA B 41 5787 3879 5343 -883 1751 -113 O
ATOM 2541 CB ALA B 41 5.367 57.484 16.156 1.00 39.91 C
ANISOU 2541 CB ALA B 41 6255 3937 4973 -851 1529 -159 C
ATOM 2542 N ILE B 42 5.421 60.407 17.691 1.00 37.19 N
ANISOU 2542 N ILE B 42 5768 3641 4721 -848 1410 77 N
ATOM 2543 CA ILE B 42 5.643 61.134 18.926 1.00 36.46 C
ANISOU 2543 CA ILE B 42 5455 3585 4812 -821 1338 124 C
ATOM 2544 C ILE B 42 4.466 60.873 19.846 1.00 37.42 C
ANISOU 2544 C ILE B 42 5483 3783 4954 -737 1065 183 C
ATOM 2545 O ILE B 42 3.315 61.085 19.474 1.00 37.16 O
ANISOU 2545 O ILE B 42 5590 3759 4769 -714 912 231 O
ATOM 2546 CB ILE B 42 5.901 62.661 18.681 1.00 39.59 C
ANISOU 2546 CB ILE B 42 5976 3924 5143 -886 1432 187 C
ATOM 2547 CG1 ILE B 42 7.076 62.919 17.684 1.00 40.39 C
ANISOU 2547 CG1 ILE B 42 6200 3924 5223 -1003 1775 121 C
ATOM 2548 CG2 ILE B 42 6.086 63.442 20.010 1.00 40.66 C
ANISOU 2548 CG2 ILE B 42 5884 4095 5470 -862 1341 210 C
ATOM 2549 CD1 ILE B 42 8.518 62.724 18.197 1.00 44.50 C
ANISOU 2549 CD1 ILE B 42 6422 4426 6060 -1048 1982 -7 C
ATOM 2550 N GLY B 43 4.771 60.396 21.032 1.00 31.69 N
ANISOU 2550 N GLY B 43 4524 3097 4417 -691 1008 168 N
ATOM 2551 CA GLY B 43 3.766 60.124 22.047 1.00 31.03 C
ANISOU 2551 CA GLY B 43 4357 3072 4360 -631 812 218 C
ATOM 2552 C GLY B 43 4.000 61.004 23.254 1.00 35.79 C
ANISOU 2552 C GLY B 43 4834 3710 5055 -615 757 251 C
ATOM 2553 O GLY B 43 5.140 61.351 23.570 1.00 34.06 O
ANISOU 2553 O GLY B 43 4511 3478 4953 -631 838 212 O
ATOM 2554 N TRP B 44 2.919 61.359 23.932 1.00 32.58 N
ANISOU 2554 N TRP B 44 4423 3342 4613 -587 625 299 N
ATOM 2555 CA TRP B 44 2.935 62.143 25.149 1.00 31.30 C
ANISOU 2555 CA TRP B 44 4170 3214 4508 -571 567 317 C
ATOM 2556 C TRP B 44 2.497 61.216 26.239 1.00 34.49 C
ANISOU 2556 C TRP B 44 4506 3654 4943 -532 491 331 C
ATOM 2557 O TRP B 44 1.519 60.466 26.094 1.00 33.14 O
ANISOU 2557 O TRP B 44 4367 3481 4742 -527 460 342 O
ATOM 2558 CB TRP B 44 1.993 63.361 25.051 1.00 29.72 C
ANISOU 2558 CB TRP B 44 4040 3007 4246 -572 512 349 C
ATOM 2559 CG TRP B 44 2.600 64.543 24.341 1.00 30.87 C
ANISOU 2559 CG TRP B 44 4273 3089 4368 -613 595 358 C
ATOM 2560 CD1 TRP B 44 2.411 64.906 23.040 1.00 33.84 C
ANISOU 2560 CD1 TRP B 44 4833 3398 4626 -633 632 390 C
ATOM 2561 CD2 TRP B 44 3.461 65.539 24.915 1.00 30.98 C
ANISOU 2561 CD2 TRP B 44 4221 3081 4468 -649 654 332 C
ATOM 2562 NE1 TRP B 44 3.061 66.093 22.779 1.00 33.89 N
ANISOU 2562 NE1 TRP B 44 4911 3328 4637 -683 735 406 N
ATOM 2563 CE2 TRP B 44 3.716 66.502 23.913 1.00 34.88 C
ANISOU 2563 CE2 TRP B 44 4863 3480 4910 -699 755 360 C
ATOM 2564 CE3 TRP B 44 3.996 65.743 26.199 1.00 32.66 C
ANISOU 2564 CE3 TRP B 44 4285 3336 4787 -644 617 284 C
ATOM 2565 CZ2 TRP B 44 4.489 67.643 24.150 1.00 34.05 C
ANISOU 2565 CZ2 TRP B 44 4734 3310 4893 -760 849 335 C
ATOM 2566 CZ3 TRP B 44 4.787 66.867 26.427 1.00 34.21 C
ANISOU 2566 CZ3 TRP B 44 4441 3486 5070 -698 678 240 C
ATOM 2567 CH2 TRP B 44 5.032 67.794 25.407 1.00 34.72 C
ANISOU 2567 CH2 TRP B 44 4627 3446 5119 -762 807 261 C
ATOM 2568 N PHE B 45 3.254 61.243 27.325 1.00 30.18 N
ANISOU 2568 N PHE B 45 3880 3128 4457 -508 460 324 N
ATOM 2569 CA PHE B 45 3.069 60.415 28.500 1.00 28.34 C
ANISOU 2569 CA PHE B 45 3638 2910 4219 -468 391 355 C
ATOM 2570 C PHE B 45 3.095 61.332 29.707 1.00 32.77 C
ANISOU 2570 C PHE B 45 4190 3513 4748 -463 330 351 C
ATOM 2571 O PHE B 45 3.559 62.462 29.605 1.00 33.62 O
ANISOU 2571 O PHE B 45 4258 3629 4887 -486 338 308 O
ATOM 2572 CB PHE B 45 4.207 59.381 28.580 1.00 29.36 C
ANISOU 2572 CB PHE B 45 3713 3002 4439 -418 372 342 C
ATOM 2573 CG PHE B 45 4.200 58.432 27.405 1.00 30.22 C
ANISOU 2573 CG PHE B 45 3841 3059 4584 -426 454 322 C
ATOM 2574 CD1 PHE B 45 4.811 58.779 26.205 1.00 32.21 C
ANISOU 2574 CD1 PHE B 45 4077 3290 4871 -463 562 260 C
ATOM 2575 CD2 PHE B 45 3.567 57.194 27.495 1.00 31.77 C
ANISOU 2575 CD2 PHE B 45 4092 3210 4767 -410 447 357 C
ATOM 2576 CE1 PHE B 45 4.783 57.907 25.107 1.00 33.62 C
ANISOU 2576 CE1 PHE B 45 4306 3419 5049 -477 649 223 C
ATOM 2577 CE2 PHE B 45 3.511 56.337 26.393 1.00 34.29 C
ANISOU 2577 CE2 PHE B 45 4438 3475 5116 -426 520 315 C
ATOM 2578 CZ PHE B 45 4.102 56.709 25.199 1.00 32.69 C
ANISOU 2578 CZ PHE B 45 4231 3267 4922 -456 614 244 C
ATOM 2579 N ARG B 46 2.571 60.869 30.831 1.00 27.92 N
ANISOU 2579 N ARG B 46 3636 2911 4061 -445 290 389 N
ATOM 2580 CA ARG B 46 2.575 61.663 32.044 1.00 28.53 C
ANISOU 2580 CA ARG B 46 3745 3027 4068 -443 239 370 C
ATOM 2581 C ARG B 46 2.784 60.758 33.240 1.00 34.29 C
ANISOU 2581 C ARG B 46 4578 3746 4703 -399 164 422 C
ATOM 2582 O ARG B 46 2.401 59.579 33.210 1.00 34.53 O
ANISOU 2582 O ARG B 46 4676 3729 4715 -389 197 488 O
ATOM 2583 CB ARG B 46 1.288 62.519 32.180 1.00 26.64 C
ANISOU 2583 CB ARG B 46 3531 2804 3788 -487 315 351 C
ATOM 2584 CG ARG B 46 0.013 61.731 32.443 1.00 30.92 C
ANISOU 2584 CG ARG B 46 4127 3328 4293 -511 396 383 C
ATOM 2585 CD ARG B 46 -1.172 62.669 32.568 1.00 39.95 C
ANISOU 2585 CD ARG B 46 5239 4479 5460 -541 467 327 C
ATOM 2586 NE ARG B 46 -2.433 61.939 32.736 1.00 37.96 N
ANISOU 2586 NE ARG B 46 4988 4201 5236 -580 571 324 N
ATOM 2587 CZ ARG B 46 -3.637 62.503 32.720 1.00 48.56 C
ANISOU 2587 CZ ARG B 46 6252 5533 6667 -602 642 254 C
ATOM 2588 NH1 ARG B 46 -3.765 63.816 32.531 1.00 29.33 N
ANISOU 2588 NH1 ARG B 46 3759 3104 4283 -574 606 197 N
ATOM 2589 NH2 ARG B 46 -4.724 61.764 32.896 1.00 35.21 N
ANISOU 2589 NH2 ARG B 46 4527 3808 5042 -653 755 227 N
ATOM 2590 N GLN B 47 3.405 61.296 34.282 1.00 31.38 N
ANISOU 2590 N GLN B 47 4245 3409 4269 -373 53 390 N
ATOM 2591 CA GLN B 47 3.607 60.545 35.504 1.00 32.70 C
ANISOU 2591 CA GLN B 47 4575 3559 4291 -320 -52 450 C
ATOM 2592 C GLN B 47 3.337 61.448 36.695 1.00 39.10 C
ANISOU 2592 C GLN B 47 5505 4415 4935 -346 -78 405 C
ATOM 2593 O GLN B 47 3.991 62.480 36.842 1.00 37.58 O
ANISOU 2593 O GLN B 47 5227 4264 4787 -348 -166 305 O
ATOM 2594 CB GLN B 47 5.009 59.903 35.556 1.00 34.40 C
ANISOU 2594 CB GLN B 47 4729 3742 4599 -219 -247 449 C
ATOM 2595 CG GLN B 47 5.236 59.073 36.835 1.00 43.54 C
ANISOU 2595 CG GLN B 47 6107 4857 5579 -136 -408 535 C
ATOM 2596 CD GLN B 47 6.382 58.102 36.712 1.00 65.71 C
ANISOU 2596 CD GLN B 47 8851 7594 8522 -10 -597 557 C
ATOM 2597 OE1 GLN B 47 7.498 58.453 36.315 1.00 61.51 O
ANISOU 2597 OE1 GLN B 47 8096 7079 8195 37 -717 450 O
ATOM 2598 NE2 GLN B 47 6.128 56.854 37.062 1.00 59.41 N
ANISOU 2598 NE2 GLN B 47 8240 6698 7637 47 -614 687 N
ATOM 2599 N ALA B 48 2.320 61.090 37.488 1.00 39.43 N
ANISOU 2599 N ALA B 48 5743 4439 4799 -384 36 460 N
ATOM 2600 CA ALA B 48 1.916 61.792 38.712 1.00 41.80 C
ANISOU 2600 CA ALA B 48 6214 4770 4896 -419 64 414 C
ATOM 2601 C ALA B 48 2.746 61.193 39.858 1.00 50.70 C
ANISOU 2601 C ALA B 48 7571 5879 5813 -342 -144 470 C
ATOM 2602 O ALA B 48 3.211 60.058 39.698 1.00 49.87 O
ANISOU 2602 O ALA B 48 7507 5713 5730 -271 -240 574 O
ATOM 2603 CB ALA B 48 0.431 61.587 38.967 1.00 42.67 C
ANISOU 2603 CB ALA B 48 6426 4850 4935 -506 329 435 C
ATOM 2604 N PRO B 49 3.043 61.927 40.965 1.00 52.56 N
ANISOU 2604 N PRO B 49 7958 6157 5856 -338 -254 397 N
ATOM 2605 CA PRO B 49 3.897 61.329 42.019 1.00 53.90 C
ANISOU 2605 CA PRO B 49 8370 6303 5807 -241 -521 453 C
ATOM 2606 C PRO B 49 3.261 60.107 42.682 1.00 57.94 C
ANISOU 2606 C PRO B 49 9222 6720 6073 -240 -420 625 C
ATOM 2607 O PRO B 49 2.082 60.138 43.044 1.00 56.88 O
ANISOU 2607 O PRO B 49 9245 6566 5802 -349 -128 642 O
ATOM 2608 CB PRO B 49 4.146 62.481 43.000 1.00 56.32 C
ANISOU 2608 CB PRO B 49 8783 6676 5940 -261 -629 311 C
ATOM 2609 CG PRO B 49 3.034 63.459 42.751 1.00 60.81 C
ANISOU 2609 CG PRO B 49 9269 7276 6561 -386 -321 218 C
ATOM 2610 CD PRO B 49 2.617 63.303 41.316 1.00 55.38 C
ANISOU 2610 CD PRO B 49 8291 6570 6180 -412 -159 252 C
ATOM 2611 N GLY B 50 4.030 59.022 42.728 1.00 55.56 N
ANISOU 2611 N GLY B 50 9001 6342 5768 -120 -636 742 N
ATOM 2612 CA GLY B 50 3.615 57.736 43.289 1.00 55.86 C
ANISOU 2612 CA GLY B 50 9381 6248 5596 -101 -573 931 C
ATOM 2613 C GLY B 50 2.820 56.852 42.340 1.00 59.13 C
ANISOU 2613 C GLY B 50 9685 6580 6203 -166 -302 1014 C
ATOM 2614 O GLY B 50 2.437 55.740 42.714 1.00 60.24 O
ANISOU 2614 O GLY B 50 10092 6584 6212 -169 -213 1169 O
ATOM 2615 N LYS B 51 2.561 57.333 41.111 1.00 52.42 N
ANISOU 2615 N LYS B 51 8465 5797 5654 -223 -176 911 N
ATOM 2616 CA LYS B 51 1.795 56.602 40.099 1.00 51.01 C
ANISOU 2616 CA LYS B 51 8152 5556 5673 -289 49 949 C
ATOM 2617 C LYS B 51 2.672 56.126 38.935 1.00 52.94 C
ANISOU 2617 C LYS B 51 8138 5783 6194 -199 -96 938 C
ATOM 2618 O LYS B 51 3.774 56.633 38.716 1.00 52.38 O
ANISOU 2618 O LYS B 51 7901 5771 6228 -113 -314 863 O
ATOM 2619 CB LYS B 51 0.642 57.470 39.552 1.00 52.91 C
ANISOU 2619 CB LYS B 51 8210 5871 6024 -424 311 836 C
ATOM 2620 CG LYS B 51 -0.422 57.818 40.581 1.00 67.64 C
ANISOU 2620 CG LYS B 51 10291 7730 7680 -533 543 821 C
ATOM 2621 CD LYS B 51 -1.778 57.227 40.233 1.00 80.77 C
ANISOU 2621 CD LYS B 51 11921 9317 9450 -659 862 829 C
ATOM 2622 CE LYS B 51 -2.705 58.219 39.568 1.00 93.54 C
ANISOU 2622 CE LYS B 51 13258 11012 11273 -734 1015 674 C
ATOM 2623 NZ LYS B 51 -4.113 57.731 39.556 1.00102.53 N
ANISOU 2623 NZ LYS B 51 14375 12072 12508 -866 1330 645 N
ATOM 2624 N GLU B 52 2.168 55.149 38.185 1.00 47.91 N
ANISOU 2624 N GLU B 52 7460 5056 5688 -232 49 991 N
ATOM 2625 CA GLU B 52 2.858 54.643 37.011 1.00 46.92 C
ANISOU 2625 CA GLU B 52 7110 4903 5815 -167 -27 961 C
ATOM 2626 C GLU B 52 2.718 55.649 35.838 1.00 45.16 C
ANISOU 2626 C GLU B 52 6595 4797 5768 -230 50 822 C
ATOM 2627 O GLU B 52 1.778 56.443 35.792 1.00 41.62 O
ANISOU 2627 O GLU B 52 6117 4415 5283 -328 193 770 O
ATOM 2628 CB GLU B 52 2.302 53.266 36.612 1.00 48.69 C
ANISOU 2628 CB GLU B 52 7414 4978 6107 -194 110 1047 C
ATOM 2629 CG GLU B 52 2.473 52.176 37.668 1.00 67.58 C
ANISOU 2629 CG GLU B 52 10133 7209 8335 -127 45 1211 C
ATOM 2630 CD GLU B 52 3.851 52.026 38.293 1.00104.73 C
ANISOU 2630 CD GLU B 52 14915 11882 12996 60 -289 1259 C
ATOM 2631 OE1 GLU B 52 4.835 51.836 37.542 1.00108.94 O
ANISOU 2631 OE1 GLU B 52 15217 12410 13765 168 -440 1193 O
ATOM 2632 OE2 GLU B 52 3.942 52.092 39.541 1.00102.80 O
ANISOU 2632 OE2 GLU B 52 14965 11612 12483 101 -401 1350 O
ATOM 2633 N ARG B 53 3.666 55.608 34.913 1.00 40.71 N
ANISOU 2633 N ARG B 53 5834 4240 5395 -167 -40 761 N
ATOM 2634 CA ARG B 53 3.641 56.437 33.722 1.00 39.85 C
ANISOU 2634 CA ARG B 53 5510 4208 5424 -224 41 652 C
ATOM 2635 C ARG B 53 2.460 55.981 32.853 1.00 41.22 C
ANISOU 2635 C ARG B 53 5676 4351 5634 -312 223 654 C
ATOM 2636 O ARG B 53 2.217 54.781 32.735 1.00 40.51 O
ANISOU 2636 O ARG B 53 5657 4162 5574 -307 267 707 O
ATOM 2637 CB ARG B 53 4.951 56.266 32.958 1.00 38.97 C
ANISOU 2637 CB ARG B 53 5224 4078 5504 -148 -47 586 C
ATOM 2638 CG ARG B 53 5.130 57.273 31.826 1.00 45.30 C
ANISOU 2638 CG ARG B 53 5854 4946 6410 -213 45 480 C
ATOM 2639 CD ARG B 53 6.300 56.871 30.961 1.00 49.81 C
ANISOU 2639 CD ARG B 53 6269 5472 7182 -164 43 406 C
ATOM 2640 NE ARG B 53 6.102 55.548 30.364 1.00 48.26 N
ANISOU 2640 NE ARG B 53 6112 5183 7041 -140 109 435 N
ATOM 2641 CZ ARG B 53 7.082 54.687 30.130 1.00 62.93 C
ANISOU 2641 CZ ARG B 53 7885 6956 9071 -50 66 398 C
ATOM 2642 NH1 ARG B 53 6.820 53.511 29.578 1.00 49.36 N
ANISOU 2642 NH1 ARG B 53 6215 5139 7402 -36 141 414 N
ATOM 2643 NH2 ARG B 53 8.337 54.996 30.443 1.00 49.93 N
ANISOU 2643 NH2 ARG B 53 6082 5311 7577 29 -55 324 N
ATOM 2644 N GLU B 54 1.720 56.931 32.272 1.00 35.63 N
ANISOU 2644 N GLU B 54 4886 3716 4937 -388 308 589 N
ATOM 2645 CA GLU B 54 0.599 56.583 31.406 1.00 34.39 C
ANISOU 2645 CA GLU B 54 4698 3537 4834 -460 424 563 C
ATOM 2646 C GLU B 54 0.603 57.430 30.145 1.00 34.94 C
ANISOU 2646 C GLU B 54 4653 3659 4965 -478 424 486 C
ATOM 2647 O GLU B 54 0.812 58.641 30.209 1.00 32.40 O
ANISOU 2647 O GLU B 54 4291 3397 4622 -477 396 457 O
ATOM 2648 CB GLU B 54 -0.753 56.687 32.147 1.00 35.62 C
ANISOU 2648 CB GLU B 54 4914 3689 4932 -535 534 571 C
ATOM 2649 CG GLU B 54 -1.150 58.101 32.538 1.00 41.03 C
ANISOU 2649 CG GLU B 54 5558 4457 5575 -555 543 519 C
ATOM 2650 CD GLU B 54 -2.565 58.349 33.026 1.00 64.57 C
ANISOU 2650 CD GLU B 54 8534 7433 8566 -632 683 478 C
ATOM 2651 OE1 GLU B 54 -3.508 57.657 32.576 1.00 68.22 O
ANISOU 2651 OE1 GLU B 54 8945 7844 9130 -689 770 450 O
ATOM 2652 OE2 GLU B 54 -2.731 59.277 33.847 1.00 56.30 O
ANISOU 2652 OE2 GLU B 54 7516 6428 7448 -639 712 449 O
ATOM 2653 N GLY B 55 0.353 56.782 29.009 1.00 31.86 N
ANISOU 2653 N GLY B 55 4240 3230 4634 -498 456 453 N
ATOM 2654 CA GLY B 55 0.241 57.476 27.732 1.00 30.41 C
ANISOU 2654 CA GLY B 55 4017 3077 4458 -517 452 392 C
ATOM 2655 C GLY B 55 -1.020 58.315 27.722 1.00 32.87 C
ANISOU 2655 C GLY B 55 4307 3425 4758 -550 439 368 C
ATOM 2656 O GLY B 55 -2.013 57.955 28.366 1.00 30.71 O
ANISOU 2656 O GLY B 55 4018 3137 4513 -583 475 365 O
ATOM 2657 N VAL B 56 -0.988 59.449 27.028 1.00 30.07 N
ANISOU 2657 N VAL B 56 3950 3099 4377 -542 401 346 N
ATOM 2658 CA VAL B 56 -2.173 60.312 26.938 1.00 30.55 C
ANISOU 2658 CA VAL B 56 3977 3173 4457 -545 356 316 C
ATOM 2659 C VAL B 56 -2.572 60.555 25.503 1.00 30.84 C
ANISOU 2659 C VAL B 56 4060 3189 4467 -535 273 285 C
ATOM 2660 O VAL B 56 -3.759 60.575 25.190 1.00 29.36 O
ANISOU 2660 O VAL B 56 3826 2992 4336 -530 192 235 O
ATOM 2661 CB VAL B 56 -2.093 61.642 27.750 1.00 36.66 C
ANISOU 2661 CB VAL B 56 4730 3974 5225 -528 358 323 C
ATOM 2662 CG1 VAL B 56 -2.114 61.373 29.254 1.00 37.30 C
ANISOU 2662 CG1 VAL B 56 4799 4074 5298 -543 422 334 C
ATOM 2663 CG2 VAL B 56 -0.902 62.493 27.368 1.00 35.92 C
ANISOU 2663 CG2 VAL B 56 4681 3878 5089 -517 357 344 C
ATOM 2664 N SER B 57 -1.582 60.672 24.615 1.00 27.14 N
ANISOU 2664 N SER B 57 3690 2706 3916 -533 293 303 N
ATOM 2665 CA SER B 57 -1.839 60.993 23.226 1.00 28.26 C
ANISOU 2665 CA SER B 57 3956 2818 3965 -525 221 289 C
ATOM 2666 C SER B 57 -0.644 60.640 22.404 1.00 33.58 C
ANISOU 2666 C SER B 57 4741 3466 4551 -553 327 290 C
ATOM 2667 O SER B 57 0.469 60.719 22.900 1.00 34.36 O
ANISOU 2667 O SER B 57 4794 3569 4694 -566 439 305 O
ATOM 2668 CB SER B 57 -2.154 62.485 23.084 1.00 32.39 C
ANISOU 2668 CB SER B 57 4528 3321 4457 -489 151 324 C
ATOM 2669 OG SER B 57 -2.569 62.706 21.752 1.00 48.32 O
ANISOU 2669 OG SER B 57 6709 5295 6357 -466 39 323 O
ATOM 2670 N CYS B 58 -0.862 60.294 21.140 1.00 31.94 N
ANISOU 2670 N CYS B 58 4680 3228 4228 -563 291 256 N
ATOM 2671 CA CYS B 58 0.200 59.855 20.247 1.00 34.60 C
ANISOU 2671 CA CYS B 58 5142 3529 4475 -603 434 229 C
ATOM 2672 C CYS B 58 -0.118 60.264 18.830 1.00 36.77 C
ANISOU 2672 C CYS B 58 5673 3762 4535 -610 378 225 C
ATOM 2673 O CYS B 58 -1.282 60.218 18.409 1.00 36.73 O
ANISOU 2673 O CYS B 58 5720 3760 4475 -575 175 203 O
ATOM 2674 CB CYS B 58 0.390 58.336 20.370 1.00 37.16 C
ANISOU 2674 CB CYS B 58 5387 3847 4884 -616 487 161 C
ATOM 2675 SG CYS B 58 1.751 57.658 19.386 1.00 43.05 S
ANISOU 2675 SG CYS B 58 6239 4537 5583 -657 703 88 S
ATOM 2676 N ILE B 59 0.918 60.647 18.091 1.00 32.53 N
ANISOU 2676 N ILE B 59 5302 3176 3880 -657 556 236 N
ATOM 2677 CA ILE B 59 0.801 61.023 16.688 1.00 33.13 C
ANISOU 2677 CA ILE B 59 5705 3192 3689 -677 548 245 C
ATOM 2678 C ILE B 59 1.788 60.214 15.856 1.00 38.64 C
ANISOU 2678 C ILE B 59 6527 3852 4300 -750 787 160 C
ATOM 2679 O ILE B 59 2.977 60.211 16.157 1.00 39.07 O
ANISOU 2679 O ILE B 59 6476 3889 4479 -798 1032 138 O
ATOM 2680 CB ILE B 59 0.866 62.568 16.412 1.00 36.18 C
ANISOU 2680 CB ILE B 59 6278 3514 3956 -672 549 358 C
ATOM 2681 CG1 ILE B 59 0.506 62.886 14.920 1.00 35.77 C
ANISOU 2681 CG1 ILE B 59 6641 3383 3568 -673 475 390 C
ATOM 2682 CG2 ILE B 59 2.219 63.212 16.860 1.00 36.55 C
ANISOU 2682 CG2 ILE B 59 6249 3525 4115 -745 830 381 C
ATOM 2683 CD1 ILE B 59 -0.012 64.303 14.653 1.00 38.99 C
ANISOU 2683 CD1 ILE B 59 7257 3706 3851 -616 328 520 C
ATOM 2684 N SER B 60 1.291 59.505 14.840 1.00 35.20 N
ANISOU 2684 N SER B 60 6294 3402 3679 -757 711 88 N
ATOM 2685 CA SER B 60 2.127 58.711 13.954 1.00 36.98 C
ANISOU 2685 CA SER B 60 6670 3581 3799 -828 948 -19 C
ATOM 2686 C SER B 60 2.853 59.626 12.934 1.00 44.11 C
ANISOU 2686 C SER B 60 7918 4401 4442 -901 1170 25 C
ATOM 2687 O SER B 60 2.492 60.797 12.776 1.00 42.49 O
ANISOU 2687 O SER B 60 7884 4163 4096 -883 1070 149 O
ATOM 2688 CB SER B 60 1.264 57.690 13.208 1.00 39.68 C
ANISOU 2688 CB SER B 60 7140 3930 4008 -817 773 -128 C
ATOM 2689 OG SER B 60 0.483 58.341 12.215 1.00 46.62 O
ANISOU 2689 OG SER B 60 8359 4785 4570 -798 569 -89 O
ATOM 2690 N SER B 61 3.833 59.069 12.192 1.00 44.04 N
ANISOU 2690 N SER B 61 8034 4337 4363 -987 1484 -82 N
ATOM 2691 CA SER B 61 4.541 59.820 11.144 1.00 44.55 C
ANISOU 2691 CA SER B 61 8468 4300 4159 -1087 1765 -58 C
ATOM 2692 C SER B 61 3.598 60.156 9.958 1.00 52.70 C
ANISOU 2692 C SER B 61 9989 5294 4742 -1071 1555 -3 C
ATOM 2693 O SER B 61 3.835 61.136 9.249 1.00 53.61 O
ANISOU 2693 O SER B 61 10470 5314 4587 -1124 1678 97 O
ATOM 2694 CB SER B 61 5.760 59.049 10.659 1.00 44.96 C
ANISOU 2694 CB SER B 61 8511 4298 4275 -1185 2177 -221 C
ATOM 2695 OG SER B 61 5.351 57.770 10.213 1.00 55.58 O
ANISOU 2695 OG SER B 61 9896 5665 5556 -1162 2093 -359 O
ATOM 2696 N GLY B 62 2.543 59.349 9.779 1.00 49.89 N
ANISOU 2696 N GLY B 62 9639 4998 4320 -998 1230 -70 N
ATOM 2697 CA GLY B 62 1.507 59.562 8.771 1.00 49.91 C
ANISOU 2697 CA GLY B 62 10045 4978 3941 -952 919 -44 C
ATOM 2698 C GLY B 62 0.465 60.602 9.172 1.00 54.82 C
ANISOU 2698 C GLY B 62 10648 5610 4571 -835 538 111 C
ATOM 2699 O GLY B 62 -0.374 60.981 8.352 1.00 56.21 O
ANISOU 2699 O GLY B 62 11166 5748 4442 -771 237 154 O
ATOM 2700 N GLY B 63 0.503 61.049 10.432 1.00 50.33 N
ANISOU 2700 N GLY B 63 9685 5085 4353 -797 533 182 N
ATOM 2701 CA GLY B 63 -0.403 62.061 10.970 1.00 49.52 C
ANISOU 2701 CA GLY B 63 9502 4983 4329 -688 226 309 C
ATOM 2702 C GLY B 63 -1.621 61.570 11.733 1.00 52.02 C
ANISOU 2702 C GLY B 63 9471 5394 4901 -589 -122 245 C
ATOM 2703 O GLY B 63 -2.423 62.392 12.178 1.00 53.17 O
ANISOU 2703 O GLY B 63 9524 5534 5143 -492 -367 323 O
ATOM 2704 N SER B 64 -1.799 60.246 11.868 1.00 46.22 N
ANISOU 2704 N SER B 64 8545 4726 4292 -616 -131 93 N
ATOM 2705 CA SER B 64 -2.911 59.660 12.630 1.00 45.20 C
ANISOU 2705 CA SER B 64 8070 4668 4437 -556 -392 14 C
ATOM 2706 C SER B 64 -2.729 59.955 14.121 1.00 45.18 C
ANISOU 2706 C SER B 64 7687 4709 4769 -547 -280 77 C
ATOM 2707 O SER B 64 -1.603 59.908 14.629 1.00 44.62 O
ANISOU 2707 O SER B 64 7532 4640 4781 -606 16 109 O
ATOM 2708 CB SER B 64 -2.987 58.153 12.413 1.00 49.32 C
ANISOU 2708 CB SER B 64 8509 5215 5014 -613 -364 -158 C
ATOM 2709 OG SER B 64 -3.401 57.892 11.081 1.00 65.23 O
ANISOU 2709 OG SER B 64 10869 7198 6719 -611 -544 -245 O
ATOM 2710 N THR B 65 -3.832 60.264 14.812 1.00 38.46 N
ANISOU 2710 N THR B 65 6610 3889 4115 -473 -519 78 N
ATOM 2711 CA THR B 65 -3.783 60.607 16.227 1.00 37.94 C
ANISOU 2711 CA THR B 65 6230 3862 4325 -464 -424 129 C
ATOM 2712 C THR B 65 -4.598 59.655 17.074 1.00 40.23 C
ANISOU 2712 C THR B 65 6204 4200 4880 -473 -487 27 C
ATOM 2713 O THR B 65 -5.676 59.219 16.663 1.00 40.13 O
ANISOU 2713 O THR B 65 6149 4187 4911 -449 -716 -77 O
ATOM 2714 CB THR B 65 -4.244 62.064 16.460 1.00 43.04 C
ANISOU 2714 CB THR B 65 6896 4472 4984 -379 -562 230 C
ATOM 2715 OG1 THR B 65 -5.636 62.163 16.152 1.00 46.18 O
ANISOU 2715 OG1 THR B 65 7248 4862 5437 -289 -901 166 O
ATOM 2716 CG2 THR B 65 -3.448 63.092 15.637 1.00 38.03 C
ANISOU 2716 CG2 THR B 65 6610 3753 4086 -383 -473 350 C
ATOM 2717 N VAL B 66 -4.100 59.361 18.273 1.00 34.63 N
ANISOU 2717 N VAL B 66 5283 3522 4352 -510 -290 54 N
ATOM 2718 CA VAL B 66 -4.791 58.507 19.232 1.00 33.44 C
ANISOU 2718 CA VAL B 66 4870 3394 4441 -535 -287 -14 C
ATOM 2719 C VAL B 66 -4.772 59.180 20.577 1.00 33.89 C
ANISOU 2719 C VAL B 66 4755 3478 4642 -519 -200 58 C
ATOM 2720 O VAL B 66 -3.800 59.855 20.913 1.00 33.05 O
ANISOU 2720 O VAL B 66 4703 3379 4476 -514 -77 147 O
ATOM 2721 CB VAL B 66 -4.355 57.016 19.275 1.00 37.19 C
ANISOU 2721 CB VAL B 66 5313 3850 4966 -604 -148 -79 C
ATOM 2722 CG1 VAL B 66 -4.667 56.308 17.959 1.00 37.32 C
ANISOU 2722 CG1 VAL B 66 5485 3836 4859 -626 -264 -197 C
ATOM 2723 CG2 VAL B 66 -2.882 56.858 19.643 1.00 36.84 C
ANISOU 2723 CG2 VAL B 66 5308 3801 4889 -621 86 -7 C
ATOM 2724 N TYR B 67 -5.816 58.950 21.364 1.00 30.10 N
ANISOU 2724 N TYR B 67 4069 3007 4362 -525 -242 1 N
ATOM 2725 CA TYR B 67 -6.009 59.577 22.666 1.00 30.21 C
ANISOU 2725 CA TYR B 67 3934 3042 4502 -517 -156 41 C
ATOM 2726 C TYR B 67 -6.457 58.582 23.690 1.00 33.46 C
ANISOU 2726 C TYR B 67 4190 3447 5077 -586 -29 -3 C
ATOM 2727 O TYR B 67 -7.293 57.745 23.375 1.00 34.00 O
ANISOU 2727 O TYR B 67 4174 3485 5258 -627 -80 -105 O
ATOM 2728 CB TYR B 67 -7.092 60.692 22.542 1.00 30.35 C
ANISOU 2728 CB TYR B 67 3873 3048 4611 -443 -335 2 C
ATOM 2729 CG TYR B 67 -6.685 61.804 21.607 1.00 29.84 C
ANISOU 2729 CG TYR B 67 4010 2957 4371 -367 -460 76 C
ATOM 2730 CD1 TYR B 67 -7.105 61.815 20.279 1.00 30.50 C
ANISOU 2730 CD1 TYR B 67 4241 3007 4342 -319 -683 43 C
ATOM 2731 CD2 TYR B 67 -5.820 62.814 22.029 1.00 29.68 C
ANISOU 2731 CD2 TYR B 67 4069 2931 4278 -353 -350 178 C
ATOM 2732 CE1 TYR B 67 -6.690 62.817 19.397 1.00 30.79 C
ANISOU 2732 CE1 TYR B 67 4536 2993 4172 -258 -776 135 C
ATOM 2733 CE2 TYR B 67 -5.400 63.822 21.158 1.00 29.87 C
ANISOU 2733 CE2 TYR B 67 4309 2899 4140 -305 -422 256 C
ATOM 2734 CZ TYR B 67 -5.843 63.824 19.846 1.00 35.10 C
ANISOU 2734 CZ TYR B 67 5153 3516 4667 -256 -626 247 C
ATOM 2735 OH TYR B 67 -5.437 64.831 19.002 1.00 35.95 O
ANISOU 2735 OH TYR B 67 5534 3544 4581 -213 -678 347 O
ATOM 2736 N SER B 68 -5.972 58.700 24.941 1.00 29.15 N
ANISOU 2736 N SER B 68 3617 2917 4543 -603 133 67 N
ATOM 2737 CA SER B 68 -6.469 57.808 25.985 1.00 29.23 C
ANISOU 2737 CA SER B 68 3534 2899 4674 -675 276 45 C
ATOM 2738 C SER B 68 -7.887 58.257 26.315 1.00 36.05 C
ANISOU 2738 C SER B 68 4217 3754 5726 -689 258 -60 C
ATOM 2739 O SER B 68 -8.270 59.396 26.013 1.00 36.59 O
ANISOU 2739 O SER B 68 4238 3843 5821 -619 134 -87 O
ATOM 2740 CB SER B 68 -5.589 57.845 27.229 1.00 30.62 C
ANISOU 2740 CB SER B 68 3780 3088 4769 -679 421 149 C
ATOM 2741 OG SER B 68 -5.660 59.111 27.858 1.00 37.65 O
ANISOU 2741 OG SER B 68 4643 4020 5643 -644 424 161 O
ATOM 2742 N GLU B 69 -8.675 57.359 26.876 1.00 34.67 N
ANISOU 2742 N GLU B 69 3937 3529 5707 -779 385 -129 N
ATOM 2743 CA GLU B 69 -10.062 57.617 27.243 1.00 35.37 C
ANISOU 2743 CA GLU B 69 3806 3592 6039 -816 420 -266 C
ATOM 2744 C GLU B 69 -10.209 58.802 28.192 1.00 39.42 C
ANISOU 2744 C GLU B 69 4279 4137 6562 -779 506 -252 C
ATOM 2745 O GLU B 69 -11.163 59.558 28.056 1.00 39.36 O
ANISOU 2745 O GLU B 69 4090 4123 6743 -739 430 -368 O
ATOM 2746 CB GLU B 69 -10.706 56.353 27.831 1.00 37.04 C
ANISOU 2746 CB GLU B 69 3943 3721 6409 -955 628 -330 C
ATOM 2747 CG GLU B 69 -10.858 55.224 26.815 1.00 53.22 C
ANISOU 2747 CG GLU B 69 5978 5718 8524 -1001 527 -404 C
ATOM 2748 CD GLU B 69 -11.782 55.516 25.647 1.00 75.92 C
ANISOU 2748 CD GLU B 69 8676 8605 11565 -959 260 -575 C
ATOM 2749 OE1 GLU B 69 -11.295 55.493 24.494 1.00 60.73 O
ANISOU 2749 OE1 GLU B 69 6873 6709 9493 -893 42 -564 O
ATOM 2750 OE2 GLU B 69 -12.982 55.787 25.881 1.00 76.14 O
ANISOU 2750 OE2 GLU B 69 8452 8608 11869 -989 263 -729 O
ATOM 2751 N SER B 70 -9.258 58.991 29.116 1.00 35.67 N
ANISOU 2751 N SER B 70 3969 3688 5896 -782 639 -126 N
ATOM 2752 CA SER B 70 -9.332 60.094 30.082 1.00 36.26 C
ANISOU 2752 CA SER B 70 4035 3788 5955 -758 732 -129 C
ATOM 2753 C SER B 70 -9.105 61.496 29.479 1.00 37.75 C
ANISOU 2753 C SER B 70 4211 4010 6122 -640 543 -127 C
ATOM 2754 O SER B 70 -9.481 62.487 30.100 1.00 36.43 O
ANISOU 2754 O SER B 70 3981 3841 6020 -613 597 -178 O
ATOM 2755 CB SER B 70 -8.372 59.854 31.242 1.00 40.94 C
ANISOU 2755 CB SER B 70 4828 4394 6332 -792 886 -11 C
ATOM 2756 OG SER B 70 -7.054 59.667 30.761 1.00 55.58 O
ANISOU 2756 OG SER B 70 6828 6279 8012 -739 760 105 O
ATOM 2757 N VAL B 71 -8.503 61.590 28.274 1.00 32.29 N
ANISOU 2757 N VAL B 71 3602 3331 5337 -577 344 -70 N
ATOM 2758 CA VAL B 71 -8.204 62.903 27.695 1.00 30.54 C
ANISOU 2758 CA VAL B 71 3428 3109 5066 -477 192 -40 C
ATOM 2759 C VAL B 71 -8.866 63.128 26.334 1.00 36.71 C
ANISOU 2759 C VAL B 71 4173 3855 5919 -402 -53 -89 C
ATOM 2760 O VAL B 71 -8.744 64.218 25.779 1.00 36.43 O
ANISOU 2760 O VAL B 71 4209 3790 5843 -312 -192 -53 O
ATOM 2761 CB VAL B 71 -6.666 63.173 27.638 1.00 31.85 C
ANISOU 2761 CB VAL B 71 3788 3304 5011 -471 208 87 C
ATOM 2762 CG1 VAL B 71 -5.965 62.819 28.952 1.00 30.96 C
ANISOU 2762 CG1 VAL B 71 3724 3225 4815 -529 382 129 C
ATOM 2763 CG2 VAL B 71 -6.000 62.489 26.446 1.00 30.89 C
ANISOU 2763 CG2 VAL B 71 3782 3181 4774 -472 122 138 C
ATOM 2764 N LYS B 72 -9.557 62.103 25.801 1.00 35.79 N
ANISOU 2764 N LYS B 72 3969 3729 5902 -438 -118 -171 N
ATOM 2765 CA LYS B 72 -10.175 62.097 24.471 1.00 37.59 C
ANISOU 2765 CA LYS B 72 4186 3927 6168 -370 -393 -235 C
ATOM 2766 C LYS B 72 -11.048 63.341 24.146 1.00 43.74 C
ANISOU 2766 C LYS B 72 4868 4657 7095 -239 -607 -294 C
ATOM 2767 O LYS B 72 -10.925 63.902 23.054 1.00 42.01 O
ANISOU 2767 O LYS B 72 4808 4405 6750 -142 -848 -244 O
ATOM 2768 CB LYS B 72 -10.964 60.798 24.280 1.00 41.47 C
ANISOU 2768 CB LYS B 72 4529 4407 6820 -451 -399 -365 C
ATOM 2769 CG LYS B 72 -11.199 60.399 22.841 1.00 62.57 C
ANISOU 2769 CG LYS B 72 7277 7065 9433 -412 -675 -420 C
ATOM 2770 CD LYS B 72 -11.988 59.089 22.797 1.00 74.82 C
ANISOU 2770 CD LYS B 72 8649 8593 11186 -515 -655 -577 C
ATOM 2771 CE LYS B 72 -12.060 58.482 21.416 1.00 90.74 C
ANISOU 2771 CE LYS B 72 10777 10598 13101 -500 -907 -646 C
ATOM 2772 NZ LYS B 72 -10.721 58.072 20.918 1.00102.12 N
ANISOU 2772 NZ LYS B 72 12524 12060 14217 -524 -822 -512 N
ATOM 2773 N ASP B 73 -11.892 63.787 25.077 1.00 43.42 N
ANISOU 2773 N ASP B 73 4594 4595 7309 -232 -513 -397 N
ATOM 2774 CA ASP B 73 -12.755 64.950 24.792 1.00 45.05 C
ANISOU 2774 CA ASP B 73 4676 4733 7710 -87 -726 -471 C
ATOM 2775 C ASP B 73 -12.117 66.307 25.106 1.00 49.18 C
ANISOU 2775 C ASP B 73 5343 5220 8122 -10 -692 -359 C
ATOM 2776 O ASP B 73 -12.809 67.332 25.055 1.00 51.27 O
ANISOU 2776 O ASP B 73 5503 5404 8572 116 -832 -419 O
ATOM 2777 CB ASP B 73 -14.110 64.811 25.522 1.00 47.46 C
ANISOU 2777 CB ASP B 73 4611 5008 8416 -106 -645 -684 C
ATOM 2778 CG ASP B 73 -14.851 63.504 25.259 1.00 69.10 C
ANISOU 2778 CG ASP B 73 7165 7758 11333 -202 -660 -828 C
ATOM 2779 OD1 ASP B 73 -15.617 63.072 26.142 1.00 73.71 O
ANISOU 2779 OD1 ASP B 73 7492 8326 12188 -301 -426 -976 O
ATOM 2780 OD2 ASP B 73 -14.664 62.915 24.161 1.00 75.02 O
ANISOU 2780 OD2 ASP B 73 8036 8519 11947 -189 -886 -804 O
ATOM 2781 N ARG B 74 -10.812 66.325 25.439 1.00 41.27 N
ANISOU 2781 N ARG B 74 4563 4264 6855 -81 -515 -215 N
ATOM 2782 CA ARG B 74 -10.146 67.534 25.919 1.00 38.03 C
ANISOU 2782 CA ARG B 74 4264 3818 6367 -46 -435 -136 C
ATOM 2783 C ARG B 74 -8.809 67.880 25.284 1.00 38.12 C
ANISOU 2783 C ARG B 74 4566 3822 6095 -55 -448 28 C
ATOM 2784 O ARG B 74 -8.447 69.045 25.316 1.00 37.53 O
ANISOU 2784 O ARG B 74 4589 3675 5995 -4 -456 82 O
ATOM 2785 CB ARG B 74 -9.901 67.392 27.433 1.00 35.18 C
ANISOU 2785 CB ARG B 74 3823 3512 6032 -148 -136 -177 C
ATOM 2786 CG ARG B 74 -11.122 67.137 28.299 1.00 42.56 C
ANISOU 2786 CG ARG B 74 4491 4441 7238 -175 -9 -347 C
ATOM 2787 CD ARG B 74 -10.733 66.260 29.476 1.00 48.09 C
ANISOU 2787 CD ARG B 74 5220 5212 7840 -320 281 -343 C
ATOM 2788 NE ARG B 74 -9.847 66.989 30.357 1.00 46.86 N
ANISOU 2788 NE ARG B 74 5205 5074 7524 -337 411 -287 N
ATOM 2789 CZ ARG B 74 -8.948 66.455 31.168 1.00 49.18 C
ANISOU 2789 CZ ARG B 74 5643 5429 7612 -427 564 -217 C
ATOM 2790 NH1 ARG B 74 -8.806 65.134 31.245 1.00 28.59 N
ANISOU 2790 NH1 ARG B 74 3073 2859 4932 -508 632 -176 N
ATOM 2791 NH2 ARG B 74 -8.168 67.233 31.894 1.00 38.10 N
ANISOU 2791 NH2 ARG B 74 4355 4038 6083 -430 626 -192 N
ATOM 2792 N PHE B 75 -8.001 66.890 24.877 1.00 34.22 N
ANISOU 2792 N PHE B 75 4195 3391 5417 -138 -394 92 N
ATOM 2793 CA PHE B 75 -6.659 67.173 24.341 1.00 33.64 C
ANISOU 2793 CA PHE B 75 4364 3306 5111 -169 -344 219 C
ATOM 2794 C PHE B 75 -6.616 67.061 22.828 1.00 38.14 C
ANISOU 2794 C PHE B 75 5141 3828 5524 -127 -520 276 C
ATOM 2795 O PHE B 75 -7.400 66.311 22.242 1.00 39.61 O
ANISOU 2795 O PHE B 75 5280 4029 5742 -103 -673 212 O
ATOM 2796 CB PHE B 75 -5.573 66.239 24.962 1.00 34.38 C
ANISOU 2796 CB PHE B 75 4466 3486 5111 -282 -139 245 C
ATOM 2797 CG PHE B 75 -5.259 66.328 26.451 1.00 34.44 C
ANISOU 2797 CG PHE B 75 4370 3542 5176 -331 32 217 C
ATOM 2798 CD1 PHE B 75 -6.081 67.047 27.320 1.00 35.64 C
ANISOU 2798 CD1 PHE B 75 4396 3673 5472 -300 56 143 C
ATOM 2799 CD2 PHE B 75 -4.153 65.679 26.982 1.00 34.88 C
ANISOU 2799 CD2 PHE B 75 4462 3652 5137 -401 157 253 C
ATOM 2800 CE1 PHE B 75 -5.802 67.110 28.693 1.00 36.15 C
ANISOU 2800 CE1 PHE B 75 4416 3780 5538 -352 216 108 C
ATOM 2801 CE2 PHE B 75 -3.883 65.729 28.360 1.00 36.80 C
ANISOU 2801 CE2 PHE B 75 4653 3936 5392 -436 269 228 C
ATOM 2802 CZ PHE B 75 -4.706 66.447 29.204 1.00 34.80 C
ANISOU 2802 CZ PHE B 75 4318 3669 5235 -418 305 158 C
ATOM 2803 N THR B 76 -5.678 67.784 22.207 1.00 33.05 N
ANISOU 2803 N THR B 76 4737 3118 4703 -132 -484 386 N
ATOM 2804 CA THR B 76 -5.403 67.718 20.778 1.00 33.29 C
ANISOU 2804 CA THR B 76 5049 3092 4509 -118 -586 458 C
ATOM 2805 C THR B 76 -3.886 67.638 20.594 1.00 38.45 C
ANISOU 2805 C THR B 76 5863 3747 4999 -230 -339 529 C
ATOM 2806 O THR B 76 -3.152 68.485 21.108 1.00 38.33 O
ANISOU 2806 O THR B 76 5857 3692 5016 -265 -192 570 O
ATOM 2807 CB THR B 76 -6.036 68.895 19.991 1.00 39.37 C
ANISOU 2807 CB THR B 76 6004 3720 5235 11 -817 524 C
ATOM 2808 OG1 THR B 76 -7.416 68.983 20.321 1.00 47.61 O
ANISOU 2808 OG1 THR B 76 6818 4760 6513 123 -1039 424 O
ATOM 2809 CG2 THR B 76 -5.915 68.722 18.484 1.00 34.22 C
ANISOU 2809 CG2 THR B 76 5697 3006 4300 32 -956 596 C
ATOM 2810 N ILE B 77 -3.427 66.616 19.867 1.00 34.71 N
ANISOU 2810 N ILE B 77 5493 3313 4382 -289 -287 517 N
ATOM 2811 CA ILE B 77 -2.021 66.457 19.531 1.00 34.02 C
ANISOU 2811 CA ILE B 77 5540 3215 4171 -391 -44 554 C
ATOM 2812 C ILE B 77 -1.867 66.892 18.073 1.00 38.23 C
ANISOU 2812 C ILE B 77 6446 3639 4441 -388 -75 630 C
ATOM 2813 O ILE B 77 -2.731 66.584 17.256 1.00 36.60 O
ANISOU 2813 O ILE B 77 6371 3420 4114 -321 -298 619 O
ATOM 2814 CB ILE B 77 -1.490 65.024 19.809 1.00 36.86 C
ANISOU 2814 CB ILE B 77 5761 3672 4572 -459 82 477 C
ATOM 2815 CG1 ILE B 77 0.062 64.968 19.765 1.00 36.77 C
ANISOU 2815 CG1 ILE B 77 5788 3646 4537 -554 352 484 C
ATOM 2816 CG2 ILE B 77 -2.141 63.951 18.895 1.00 36.63 C
ANISOU 2816 CG2 ILE B 77 5817 3662 4439 -445 -49 419 C
ATOM 2817 CD1 ILE B 77 0.684 63.639 20.231 1.00 37.72 C
ANISOU 2817 CD1 ILE B 77 5737 3840 4756 -594 462 408 C
ATOM 2818 N SER B 78 -0.817 67.650 17.758 1.00 37.64 N
ANISOU 2818 N SER B 78 6553 3474 4275 -461 140 702 N
ATOM 2819 CA SER B 78 -0.551 68.081 16.376 1.00 39.51 C
ANISOU 2819 CA SER B 78 7209 3584 4220 -484 178 789 C
ATOM 2820 C SER B 78 0.943 68.192 16.153 1.00 47.18 C
ANISOU 2820 C SER B 78 8271 4504 5151 -634 556 793 C
ATOM 2821 O SER B 78 1.701 68.207 17.126 1.00 45.90 O
ANISOU 2821 O SER B 78 7831 4392 5219 -695 725 737 O
ATOM 2822 CB SER B 78 -1.280 69.380 16.014 1.00 42.98 C
ANISOU 2822 CB SER B 78 7874 3878 4579 -381 -23 908 C
ATOM 2823 OG SER B 78 -1.026 70.429 16.931 1.00 46.42 O
ANISOU 2823 OG SER B 78 8165 4256 5215 -386 65 939 O
ATOM 2824 N ARG B 79 1.372 68.214 14.884 1.00 47.51 N
ANISOU 2824 N ARG B 79 8695 4449 4909 -698 690 840 N
ATOM 2825 CA ARG B 79 2.792 68.277 14.551 1.00 49.10 C
ANISOU 2825 CA ARG B 79 8982 4585 5091 -859 1101 817 C
ATOM 2826 C ARG B 79 3.102 69.215 13.430 1.00 57.79 C
ANISOU 2826 C ARG B 79 10564 5489 5903 -926 1261 941 C
ATOM 2827 O ARG B 79 2.303 69.351 12.504 1.00 58.88 O
ANISOU 2827 O ARG B 79 11074 5560 5736 -848 1048 1031 O
ATOM 2828 CB ARG B 79 3.386 66.878 14.266 1.00 45.47 C
ANISOU 2828 CB ARG B 79 8426 4220 4629 -924 1265 681 C
ATOM 2829 CG ARG B 79 3.019 66.235 12.931 1.00 49.65 C
ANISOU 2829 CG ARG B 79 9331 4725 4810 -923 1221 674 C
ATOM 2830 CD ARG B 79 3.421 64.753 12.897 1.00 55.72 C
ANISOU 2830 CD ARG B 79 9919 5597 5653 -959 1331 513 C
ATOM 2831 NE ARG B 79 4.877 64.599 12.917 1.00 56.03 N
ANISOU 2831 NE ARG B 79 9856 5599 5833 -1095 1757 427 N
ATOM 2832 CZ ARG B 79 5.517 63.490 13.266 1.00 65.66 C
ANISOU 2832 CZ ARG B 79 10794 6891 7264 -1118 1894 281 C
ATOM 2833 NH1 ARG B 79 4.836 62.407 13.626 1.00 45.40 N
ANISOU 2833 NH1 ARG B 79 8051 4430 4767 -1029 1660 219 N
ATOM 2834 NH2 ARG B 79 6.847 63.450 13.247 1.00 50.92 N
ANISOU 2834 NH2 ARG B 79 8813 4972 5564 -1230 2271 187 N
ATOM 2835 N ASP B 80 4.290 69.832 13.497 1.00 57.33 N
ANISOU 2835 N ASP B 80 10510 5328 5944 -1076 1638 938 N
ATOM 2836 CA ASP B 80 4.808 70.732 12.469 1.00 58.72 C
ANISOU 2836 CA ASP B 80 11158 5284 5867 -1189 1906 1052 C
ATOM 2837 C ASP B 80 6.228 70.249 12.158 1.00 64.59 C
ANISOU 2837 C ASP B 80 11846 6011 6686 -1386 2396 922 C
ATOM 2838 O ASP B 80 7.170 70.626 12.856 1.00 65.45 O
ANISOU 2838 O ASP B 80 11658 6097 7114 -1493 2644 842 O
ATOM 2839 CB ASP B 80 4.792 72.193 12.963 1.00 60.74 C
ANISOU 2839 CB ASP B 80 11440 5385 6252 -1190 1906 1165 C
ATOM 2840 CG ASP B 80 4.997 73.247 11.880 1.00 80.43 C
ANISOU 2840 CG ASP B 80 14509 7610 8442 -1270 2099 1337 C
ATOM 2841 OD1 ASP B 80 4.588 74.408 12.099 1.00 82.83 O
ANISOU 2841 OD1 ASP B 80 14934 7761 8777 -1212 1977 1467 O
ATOM 2842 OD2 ASP B 80 5.569 72.911 10.811 1.00 88.01 O
ANISOU 2842 OD2 ASP B 80 15820 8493 9125 -1393 2389 1342 O
ATOM 2843 N ASN B 81 6.369 69.364 11.162 1.00 60.60 N
ANISOU 2843 N ASN B 81 11586 5520 5919 -1429 2520 870 N
ATOM 2844 CA ASN B 81 7.666 68.813 10.763 1.00 61.47 C
ANISOU 2844 CA ASN B 81 11647 5603 6106 -1608 3005 719 C
ATOM 2845 C ASN B 81 8.684 69.884 10.317 1.00 69.05 C
ANISOU 2845 C ASN B 81 12835 6340 7061 -1810 3481 760 C
ATOM 2846 O ASN B 81 9.886 69.650 10.460 1.00 69.21 O
ANISOU 2846 O ASN B 81 12599 6343 7356 -1962 3886 595 O
ATOM 2847 CB ASN B 81 7.506 67.742 9.675 1.00 58.64 C
ANISOU 2847 CB ASN B 81 11586 5279 5417 -1613 3050 655 C
ATOM 2848 CG ASN B 81 6.975 66.407 10.151 1.00 69.96 C
ANISOU 2848 CG ASN B 81 12684 6918 6981 -1485 2757 530 C
ATOM 2849 OD1 ASN B 81 6.902 66.109 11.351 1.00 63.47 O
ANISOU 2849 OD1 ASN B 81 11370 6223 6523 -1406 2580 473 O
ATOM 2850 ND2 ASN B 81 6.606 65.557 9.204 1.00 59.80 N
ANISOU 2850 ND2 ASN B 81 11687 5652 5383 -1470 2712 480 N
ATOM 2851 N ALA B 82 8.215 71.048 9.796 1.00 67.13 N
ANISOU 2851 N ALA B 82 13057 5910 6539 -1810 3433 969 N
ATOM 2852 CA ALA B 82 9.112 72.136 9.365 1.00 68.31 C
ANISOU 2852 CA ALA B 82 13472 5809 6675 -2016 3901 1029 C
ATOM 2853 C ALA B 82 9.782 72.799 10.582 1.00 73.77 C
ANISOU 2853 C ALA B 82 13648 6494 7888 -2081 4001 942 C
ATOM 2854 O ALA B 82 10.967 73.121 10.533 1.00 75.41 O
ANISOU 2854 O ALA B 82 13753 6583 8318 -2293 4481 833 O
ATOM 2855 CB ALA B 82 8.355 73.168 8.536 1.00 68.99 C
ANISOU 2855 CB ALA B 82 14217 5678 6320 -1971 3769 1295 C
ATOM 2856 N LYS B 83 9.032 72.956 11.674 1.00 69.27 N
ANISOU 2856 N LYS B 83 12744 6053 7523 -1907 3559 965 N
ATOM 2857 CA LYS B 83 9.520 73.503 12.944 1.00 68.50 C
ANISOU 2857 CA LYS B 83 12155 5982 7890 -1938 3561 866 C
ATOM 2858 C LYS B 83 10.023 72.350 13.855 1.00 69.71 C
ANISOU 2858 C LYS B 83 11719 6375 8393 -1905 3506 640 C
ATOM 2859 O LYS B 83 10.569 72.613 14.929 1.00 70.40 O
ANISOU 2859 O LYS B 83 11374 6509 8868 -1933 3502 521 O
ATOM 2860 CB LYS B 83 8.400 74.296 13.653 1.00 70.54 C
ANISOU 2860 CB LYS B 83 12404 6240 8158 -1762 3124 1002 C
ATOM 2861 CG LYS B 83 8.005 75.580 12.930 1.00 84.95 C
ANISOU 2861 CG LYS B 83 14762 7788 9726 -1779 3162 1223 C
ATOM 2862 CD LYS B 83 6.867 76.296 13.642 1.00 95.54 C
ANISOU 2862 CD LYS B 83 16051 9125 11123 -1581 2719 1328 C
ATOM 2863 CE LYS B 83 6.295 77.411 12.802 1.00104.35 C
ANISOU 2863 CE LYS B 83 17745 9960 11942 -1539 2666 1569 C
ATOM 2864 NZ LYS B 83 5.168 78.093 13.490 1.00112.00 N
ANISOU 2864 NZ LYS B 83 18627 10914 13014 -1328 2233 1647 N
ATOM 2865 N LYS B 84 9.833 71.080 13.416 1.00 62.82 N
ANISOU 2865 N LYS B 84 10855 5640 7374 -1842 3445 582 N
ATOM 2866 CA LYS B 84 10.181 69.846 14.142 1.00 61.21 C
ANISOU 2866 CA LYS B 84 10173 5639 7446 -1781 3359 398 C
ATOM 2867 C LYS B 84 9.604 69.889 15.572 1.00 59.07 C
ANISOU 2867 C LYS B 84 9517 5517 7409 -1630 2953 395 C
ATOM 2868 O LYS B 84 10.314 69.604 16.545 1.00 58.95 O
ANISOU 2868 O LYS B 84 9062 5586 7749 -1638 2958 247 O
ATOM 2869 CB LYS B 84 11.707 69.620 14.146 1.00 64.91 C
ANISOU 2869 CB LYS B 84 10361 6058 8245 -1955 3802 190 C
ATOM 2870 CG LYS B 84 12.264 68.987 12.873 1.00 80.24 C
ANISOU 2870 CG LYS B 84 12569 7921 9998 -2075 4198 118 C
ATOM 2871 CD LYS B 84 13.798 69.081 12.807 1.00 91.57 C
ANISOU 2871 CD LYS B 84 13738 9250 11804 -2277 4708 -95 C
ATOM 2872 CE LYS B 84 14.540 68.321 13.888 1.00104.67 C
ANISOU 2872 CE LYS B 84 14752 11048 13971 -2215 4614 -317 C
ATOM 2873 NZ LYS B 84 14.389 66.848 13.746 1.00117.66 N
ANISOU 2873 NZ LYS B 84 16293 12827 15584 -2092 4499 -405 N
ATOM 2874 N ILE B 85 8.325 70.308 15.686 1.00 50.23 N
ANISOU 2874 N ILE B 85 8582 4414 6090 -1493 2605 552 N
ATOM 2875 CA ILE B 85 7.615 70.452 16.957 1.00 47.83 C
ANISOU 2875 CA ILE B 85 7987 4229 5957 -1358 2252 558 C
ATOM 2876 C ILE B 85 6.323 69.644 16.979 1.00 45.12 C
ANISOU 2876 C ILE B 85 7679 4020 5446 -1188 1892 611 C
ATOM 2877 O ILE B 85 5.582 69.614 16.001 1.00 44.43 O
ANISOU 2877 O ILE B 85 7940 3881 5059 -1143 1799 711 O
ATOM 2878 CB ILE B 85 7.362 71.966 17.290 1.00 51.49 C
ANISOU 2878 CB ILE B 85 8553 4550 6460 -1370 2216 654 C
ATOM 2879 CG1 ILE B 85 8.670 72.673 17.675 1.00 53.58 C
ANISOU 2879 CG1 ILE B 85 8632 4713 7014 -1543 2532 544 C
ATOM 2880 CG2 ILE B 85 6.333 72.167 18.408 1.00 52.13 C
ANISOU 2880 CG2 ILE B 85 8436 4736 6635 -1213 1844 675 C
ATOM 2881 CD1 ILE B 85 8.583 74.257 17.765 1.00 65.20 C
ANISOU 2881 CD1 ILE B 85 10277 5978 8517 -1600 2588 636 C
ATOM 2882 N VAL B 86 6.017 69.069 18.132 1.00 38.73 N
ANISOU 2882 N VAL B 86 6520 3366 4831 -1097 1680 542 N
ATOM 2883 CA VAL B 86 4.763 68.386 18.367 1.00 37.14 C
ANISOU 2883 CA VAL B 86 6289 3280 4544 -955 1360 573 C
ATOM 2884 C VAL B 86 4.093 69.135 19.513 1.00 41.63 C
ANISOU 2884 C VAL B 86 6688 3876 5255 -876 1155 596 C
ATOM 2885 O VAL B 86 4.720 69.349 20.548 1.00 41.96 O
ANISOU 2885 O VAL B 86 6475 3956 5514 -909 1206 523 O
ATOM 2886 CB VAL B 86 4.939 66.860 18.635 1.00 39.82 C
ANISOU 2886 CB VAL B 86 6414 3755 4961 -930 1338 469 C
ATOM 2887 CG1 VAL B 86 3.651 66.230 19.176 1.00 38.65 C
ANISOU 2887 CG1 VAL B 86 6167 3716 4802 -805 1032 483 C
ATOM 2888 CG2 VAL B 86 5.398 66.137 17.369 1.00 39.40 C
ANISOU 2888 CG2 VAL B 86 6574 3659 4736 -995 1531 434 C
ATOM 2889 N TYR B 87 2.831 69.540 19.334 1.00 37.92 N
ANISOU 2889 N TYR B 87 6354 3382 4673 -769 918 680 N
ATOM 2890 CA TYR B 87 2.081 70.245 20.375 1.00 36.63 C
ANISOU 2890 CA TYR B 87 6033 3232 4652 -688 742 683 C
ATOM 2891 C TYR B 87 1.063 69.369 21.019 1.00 38.44 C
ANISOU 2891 C TYR B 87 6067 3600 4938 -590 529 634 C
ATOM 2892 O TYR B 87 0.465 68.517 20.364 1.00 37.67 O
ANISOU 2892 O TYR B 87 6041 3544 4727 -549 421 637 O
ATOM 2893 CB TYR B 87 1.322 71.454 19.794 1.00 38.59 C
ANISOU 2893 CB TYR B 87 6539 3321 4801 -620 625 796 C
ATOM 2894 CG TYR B 87 2.190 72.460 19.083 1.00 41.55 C
ANISOU 2894 CG TYR B 87 7181 3510 5097 -723 850 873 C
ATOM 2895 CD1 TYR B 87 2.295 72.459 17.696 1.00 43.75 C
ANISOU 2895 CD1 TYR B 87 7843 3676 5105 -753 920 971 C
ATOM 2896 CD2 TYR B 87 2.883 73.440 19.793 1.00 42.52 C
ANISOU 2896 CD2 TYR B 87 7199 3551 5405 -801 1002 842 C
ATOM 2897 CE1 TYR B 87 3.067 73.410 17.028 1.00 46.09 C
ANISOU 2897 CE1 TYR B 87 8429 3771 5311 -865 1171 1054 C
ATOM 2898 CE2 TYR B 87 3.649 74.409 19.133 1.00 43.14 C
ANISOU 2898 CE2 TYR B 87 7530 3427 5437 -916 1240 910 C
ATOM 2899 CZ TYR B 87 3.757 74.370 17.750 1.00 54.24 C
ANISOU 2899 CZ TYR B 87 9329 4713 6568 -954 1345 1023 C
ATOM 2900 OH TYR B 87 4.551 75.269 17.082 1.00 60.70 O
ANISOU 2900 OH TYR B 87 10428 5313 7324 -1092 1635 1094 O
ATOM 2901 N LEU B 88 0.811 69.618 22.299 1.00 33.77 N
ANISOU 2901 N LEU B 88 5246 3067 4518 -562 476 581 N
ATOM 2902 CA LEU B 88 -0.276 68.989 23.027 1.00 31.44 C
ANISOU 2902 CA LEU B 88 4778 2873 4294 -483 314 534 C
ATOM 2903 C LEU B 88 -1.111 70.111 23.590 1.00 34.00 C
ANISOU 2903 C LEU B 88 5065 3137 4718 -411 214 532 C
ATOM 2904 O LEU B 88 -0.683 70.770 24.537 1.00 32.78 O
ANISOU 2904 O LEU B 88 4812 2976 4666 -443 292 491 O
ATOM 2905 CB LEU B 88 0.195 68.044 24.151 1.00 30.87 C
ANISOU 2905 CB LEU B 88 4487 2927 4315 -519 376 460 C
ATOM 2906 CG LEU B 88 -0.926 67.192 24.811 1.00 33.40 C
ANISOU 2906 CG LEU B 88 4670 3333 4687 -466 266 418 C
ATOM 2907 CD1 LEU B 88 -1.561 66.207 23.785 1.00 32.74 C
ANISOU 2907 CD1 LEU B 88 4655 3260 4526 -444 180 425 C
ATOM 2908 CD2 LEU B 88 -0.398 66.434 26.017 1.00 31.36 C
ANISOU 2908 CD2 LEU B 88 4266 3164 4485 -499 332 373 C
ATOM 2909 N GLN B 89 -2.271 70.371 22.983 1.00 31.95 N
ANISOU 2909 N GLN B 89 4882 2819 4439 -310 30 562 N
ATOM 2910 CA GLN B 89 -3.209 71.377 23.490 1.00 32.14 C
ANISOU 2910 CA GLN B 89 4836 2771 4606 -216 -82 539 C
ATOM 2911 C GLN B 89 -4.046 70.664 24.551 1.00 37.06 C
ANISOU 2911 C GLN B 89 5191 3515 5376 -195 -109 426 C
ATOM 2912 O GLN B 89 -4.733 69.704 24.219 1.00 37.83 O
ANISOU 2912 O GLN B 89 5228 3673 5472 -170 -205 396 O
ATOM 2913 CB GLN B 89 -4.113 71.922 22.359 1.00 33.38 C
ANISOU 2913 CB GLN B 89 5177 2798 4708 -93 -305 609 C
ATOM 2914 CG GLN B 89 -5.124 73.009 22.803 1.00 38.14 C
ANISOU 2914 CG GLN B 89 5693 3295 5506 35 -444 575 C
ATOM 2915 CD GLN B 89 -4.454 74.195 23.454 1.00 46.37 C
ANISOU 2915 CD GLN B 89 6761 4236 6620 -7 -287 584 C
ATOM 2916 OE1 GLN B 89 -3.535 74.799 22.913 1.00 46.03 O
ANISOU 2916 OE1 GLN B 89 6945 4084 6462 -70 -181 680 O
ATOM 2917 NE2 GLN B 89 -4.873 74.530 24.652 1.00 36.83 N
ANISOU 2917 NE2 GLN B 89 5328 3057 5608 10 -242 468 N
ATOM 2918 N MET B 90 -4.002 71.123 25.811 1.00 32.97 N
ANISOU 2918 N MET B 90 4532 3020 4977 -215 -11 353 N
ATOM 2919 CA MET B 90 -4.743 70.463 26.900 1.00 32.09 C
ANISOU 2919 CA MET B 90 4211 3008 4974 -219 23 248 C
ATOM 2920 C MET B 90 -5.832 71.382 27.405 1.00 36.38 C
ANISOU 2920 C MET B 90 4642 3477 5704 -133 -22 163 C
ATOM 2921 O MET B 90 -5.540 72.417 27.996 1.00 34.91 O
ANISOU 2921 O MET B 90 4469 3228 5566 -133 46 135 O
ATOM 2922 CB MET B 90 -3.815 70.061 28.056 1.00 33.99 C
ANISOU 2922 CB MET B 90 4406 3343 5165 -315 183 216 C
ATOM 2923 CG MET B 90 -2.668 69.169 27.635 1.00 38.39 C
ANISOU 2923 CG MET B 90 5036 3958 5593 -384 227 278 C
ATOM 2924 SD MET B 90 -1.604 68.649 29.014 1.00 43.39 S
ANISOU 2924 SD MET B 90 5610 4689 6187 -459 334 237 S
ATOM 2925 CE MET B 90 -1.057 70.218 29.633 1.00 39.37 C
ANISOU 2925 CE MET B 90 5114 4113 5731 -477 371 183 C
ATOM 2926 N ASN B 91 -7.085 71.011 27.183 1.00 33.92 N
ANISOU 2926 N ASN B 91 4197 3163 5527 -61 -133 99 N
ATOM 2927 CA ASN B 91 -8.178 71.869 27.618 1.00 34.31 C
ANISOU 2927 CA ASN B 91 4097 3128 5811 35 -174 -9 C
ATOM 2928 C ASN B 91 -8.870 71.241 28.802 1.00 39.47 C
ANISOU 2928 C ASN B 91 4536 3866 6595 -22 -8 -151 C
ATOM 2929 O ASN B 91 -8.731 70.032 29.019 1.00 38.09 O
ANISOU 2929 O ASN B 91 4338 3796 6337 -113 75 -147 O
ATOM 2930 CB ASN B 91 -9.161 72.112 26.465 1.00 35.12 C
ANISOU 2930 CB ASN B 91 4185 3131 6030 179 -447 -3 C
ATOM 2931 CG ASN B 91 -8.588 72.961 25.352 1.00 53.07 C
ANISOU 2931 CG ASN B 91 6734 5276 8156 247 -597 149 C
ATOM 2932 OD1 ASN B 91 -7.677 73.767 25.547 1.00 45.92 O
ANISOU 2932 OD1 ASN B 91 5977 4307 7162 205 -482 217 O
ATOM 2933 ND2 ASN B 91 -9.107 72.798 24.158 1.00 47.69 N
ANISOU 2933 ND2 ASN B 91 6144 4539 7435 345 -855 199 N
ATOM 2934 N SER B 92 -9.582 72.073 29.587 1.00 35.76 N
ANISOU 2934 N SER B 92 3931 3332 6326 25 68 -280 N
ATOM 2935 CA SER B 92 -10.362 71.660 30.753 1.00 34.92 C
ANISOU 2935 CA SER B 92 3635 3274 6359 -34 278 -439 C
ATOM 2936 C SER B 92 -9.575 70.782 31.718 1.00 37.17 C
ANISOU 2936 C SER B 92 4023 3684 6416 -185 491 -409 C
ATOM 2937 O SER B 92 -9.974 69.657 31.993 1.00 36.95 O
ANISOU 2937 O SER B 92 3928 3721 6391 -259 590 -436 O
ATOM 2938 CB SER B 92 -11.646 70.974 30.299 1.00 36.48 C
ANISOU 2938 CB SER B 92 3602 3464 6797 8 195 -539 C
ATOM 2939 OG SER B 92 -12.468 71.938 29.668 1.00 43.73 O
ANISOU 2939 OG SER B 92 4399 4249 7966 174 -13 -603 O
ATOM 2940 N LEU B 93 -8.422 71.275 32.168 1.00 32.85 N
ANISOU 2940 N LEU B 93 3648 3156 5679 -227 538 -348 N
ATOM 2941 CA LEU B 93 -7.542 70.538 33.076 1.00 32.11 C
ANISOU 2941 CA LEU B 93 3677 3168 5356 -341 673 -313 C
ATOM 2942 C LEU B 93 -8.101 70.523 34.489 1.00 36.79 C
ANISOU 2942 C LEU B 93 4244 3781 5955 -403 903 -447 C
ATOM 2943 O LEU B 93 -8.717 71.486 34.915 1.00 35.23 O
ANISOU 2943 O LEU B 93 3968 3513 5906 -365 979 -577 O
ATOM 2944 CB LEU B 93 -6.117 71.111 33.065 1.00 31.29 C
ANISOU 2944 CB LEU B 93 3732 3070 5087 -361 614 -235 C
ATOM 2945 CG LEU B 93 -5.305 70.847 31.790 1.00 35.08 C
ANISOU 2945 CG LEU B 93 4285 3544 5498 -346 465 -95 C
ATOM 2946 CD1 LEU B 93 -4.156 71.862 31.641 1.00 34.51 C
ANISOU 2946 CD1 LEU B 93 4316 3418 5377 -359 436 -64 C
ATOM 2947 CD2 LEU B 93 -4.779 69.428 31.756 1.00 36.02 C
ANISOU 2947 CD2 LEU B 93 4443 3762 5481 -405 476 -22 C
ATOM 2948 N GLN B 94 -7.913 69.418 35.193 1.00 35.08 N
ANISOU 2948 N GLN B 94 4112 3642 5575 -496 1027 -418 N
ATOM 2949 CA GLN B 94 -8.405 69.268 36.555 1.00 35.86 C
ANISOU 2949 CA GLN B 94 4259 3754 5613 -576 1280 -527 C
ATOM 2950 C GLN B 94 -7.244 68.874 37.458 1.00 40.57 C
ANISOU 2950 C GLN B 94 5108 4423 5884 -641 1294 -451 C
ATOM 2951 O GLN B 94 -6.235 68.411 36.920 1.00 39.76 O
ANISOU 2951 O GLN B 94 5075 4362 5672 -625 1121 -319 O
ATOM 2952 CB GLN B 94 -9.511 68.184 36.596 1.00 37.41 C
ANISOU 2952 CB GLN B 94 4340 3940 5934 -636 1442 -567 C
ATOM 2953 CG GLN B 94 -10.766 68.501 35.776 1.00 41.21 C
ANISOU 2953 CG GLN B 94 4528 4349 6783 -567 1402 -681 C
ATOM 2954 CD GLN B 94 -11.440 69.805 36.131 1.00 53.95 C
ANISOU 2954 CD GLN B 94 6010 5883 8606 -502 1475 -852 C
ATOM 2955 OE1 GLN B 94 -11.321 70.333 37.233 1.00 51.73 O
ANISOU 2955 OE1 GLN B 94 5835 5599 8221 -549 1668 -938 O
ATOM 2956 NE2 GLN B 94 -12.168 70.358 35.195 1.00 44.90 N
ANISOU 2956 NE2 GLN B 94 4640 4660 7759 -383 1305 -912 N
ATOM 2957 N PRO B 95 -7.339 69.027 38.809 1.00 38.30 N
ANISOU 2957 N PRO B 95 4971 4146 5435 -707 1485 -541 N
ATOM 2958 CA PRO B 95 -6.211 68.622 39.681 1.00 38.57 C
ANISOU 2958 CA PRO B 95 5274 4245 5137 -748 1433 -467 C
ATOM 2959 C PRO B 95 -5.628 67.234 39.395 1.00 41.46 C
ANISOU 2959 C PRO B 95 5730 4648 5373 -760 1336 -293 C
ATOM 2960 O PRO B 95 -4.424 67.066 39.513 1.00 41.05 O
ANISOU 2960 O PRO B 95 5800 4640 5156 -735 1152 -213 O
ATOM 2961 CB PRO B 95 -6.810 68.699 41.098 1.00 40.91 C
ANISOU 2961 CB PRO B 95 5742 4529 5272 -831 1706 -587 C
ATOM 2962 CG PRO B 95 -7.863 69.760 40.997 1.00 44.55 C
ANISOU 2962 CG PRO B 95 5996 4920 6010 -811 1858 -770 C
ATOM 2963 CD PRO B 95 -8.455 69.592 39.608 1.00 40.14 C
ANISOU 2963 CD PRO B 95 5149 4325 5778 -743 1751 -727 C
ATOM 2964 N GLU B 96 -6.467 66.259 38.982 1.00 37.62 N
ANISOU 2964 N GLU B 96 5160 4133 5000 -793 1448 -254 N
ATOM 2965 CA GLU B 96 -6.063 64.889 38.652 1.00 37.23 C
ANISOU 2965 CA GLU B 96 5186 4090 4871 -806 1384 -103 C
ATOM 2966 C GLU B 96 -5.132 64.813 37.420 1.00 38.23 C
ANISOU 2966 C GLU B 96 5212 4243 5069 -727 1119 -10 C
ATOM 2967 O GLU B 96 -4.487 63.791 37.220 1.00 36.38 O
ANISOU 2967 O GLU B 96 5059 4014 4751 -720 1036 105 O
ATOM 2968 CB GLU B 96 -7.288 63.944 38.502 1.00 38.76 C
ANISOU 2968 CB GLU B 96 5291 4224 5211 -882 1597 -120 C
ATOM 2969 CG GLU B 96 -8.094 63.719 39.782 1.00 45.86 C
ANISOU 2969 CG GLU B 96 6340 5078 6006 -994 1926 -191 C
ATOM 2970 CD GLU B 96 -9.064 64.820 40.181 1.00 70.14 C
ANISOU 2970 CD GLU B 96 9276 8130 9242 -1015 2124 -392 C
ATOM 2971 OE1 GLU B 96 -9.189 65.821 39.435 1.00 52.64 O
ANISOU 2971 OE1 GLU B 96 6833 5923 7245 -927 1979 -472 O
ATOM 2972 OE2 GLU B 96 -9.704 64.679 41.248 1.00 71.94 O
ANISOU 2972 OE2 GLU B 96 9640 8316 9378 -1120 2439 -470 O
ATOM 2973 N ASP B 97 -5.019 65.907 36.637 1.00 33.64 N
ANISOU 2973 N ASP B 97 4484 3662 4636 -669 1005 -61 N
ATOM 2974 CA ASP B 97 -4.118 66.009 35.488 1.00 33.60 C
ANISOU 2974 CA ASP B 97 4419 3667 4680 -612 807 12 C
ATOM 2975 C ASP B 97 -2.734 66.529 35.863 1.00 36.13 C
ANISOU 2975 C ASP B 97 4828 4020 4879 -596 683 25 C
ATOM 2976 O ASP B 97 -1.887 66.644 34.980 1.00 34.21 O
ANISOU 2976 O ASP B 97 4535 3775 4687 -567 562 70 O
ATOM 2977 CB ASP B 97 -4.708 66.885 34.374 1.00 35.70 C
ANISOU 2977 CB ASP B 97 4526 3886 5151 -563 750 -30 C
ATOM 2978 CG ASP B 97 -6.032 66.362 33.885 1.00 41.57 C
ANISOU 2978 CG ASP B 97 5138 4597 6058 -565 809 -67 C
ATOM 2979 OD1 ASP B 97 -6.044 65.299 33.210 1.00 40.43 O
ANISOU 2979 OD1 ASP B 97 4981 4459 5921 -577 766 -3 O
ATOM 2980 OD2 ASP B 97 -7.054 66.981 34.203 1.00 45.74 O
ANISOU 2980 OD2 ASP B 97 5563 5087 6730 -557 901 -180 O
ATOM 2981 N THR B 98 -2.507 66.841 37.160 1.00 33.54 N
ANISOU 2981 N THR B 98 4634 3715 4395 -621 721 -32 N
ATOM 2982 CA THR B 98 -1.212 67.285 37.688 1.00 33.07 C
ANISOU 2982 CA THR B 98 4651 3688 4227 -609 573 -55 C
ATOM 2983 C THR B 98 -0.221 66.129 37.517 1.00 36.20 C
ANISOU 2983 C THR B 98 5090 4109 4556 -578 435 56 C
ATOM 2984 O THR B 98 -0.490 65.009 37.969 1.00 35.60 O
ANISOU 2984 O THR B 98 5136 4030 4360 -582 475 134 O
ATOM 2985 CB THR B 98 -1.350 67.744 39.147 1.00 34.80 C
ANISOU 2985 CB THR B 98 5041 3925 4258 -642 634 -152 C
ATOM 2986 OG1 THR B 98 -2.218 68.876 39.165 1.00 36.66 O
ANISOU 2986 OG1 THR B 98 5196 4119 4614 -659 769 -275 O
ATOM 2987 CG2 THR B 98 -0.004 68.100 39.797 1.00 31.02 C
ANISOU 2987 CG2 THR B 98 4646 3483 3655 -627 431 -196 C
ATOM 2988 N ALA B 99 0.906 66.398 36.847 1.00 31.06 N
ANISOU 2988 N ALA B 99 4335 3462 4004 -551 293 56 N
ATOM 2989 CA ALA B 99 1.925 65.378 36.546 1.00 30.58 C
ANISOU 2989 CA ALA B 99 4259 3408 3950 -509 164 131 C
ATOM 2990 C ALA B 99 3.066 65.995 35.770 1.00 33.11 C
ANISOU 2990 C ALA B 99 4424 3720 4437 -505 77 80 C
ATOM 2991 O ALA B 99 2.939 67.087 35.229 1.00 32.44 O
ANISOU 2991 O ALA B 99 4264 3606 4456 -541 138 24 O
ATOM 2992 CB ALA B 99 1.307 64.267 35.680 1.00 31.24 C
ANISOU 2992 CB ALA B 99 4319 3464 4086 -503 248 232 C
ATOM 2993 N VAL B 100 4.156 65.252 35.648 1.00 29.74 N
ANISOU 2993 N VAL B 100 3947 3296 4057 -462 -47 100 N
ATOM 2994 CA VAL B 100 5.265 65.615 34.780 1.00 27.79 C
ANISOU 2994 CA VAL B 100 3525 3025 4010 -472 -76 44 C
ATOM 2995 C VAL B 100 4.851 64.980 33.454 1.00 31.98 C
ANISOU 2995 C VAL B 100 4024 3522 4607 -478 53 127 C
ATOM 2996 O VAL B 100 4.493 63.799 33.418 1.00 32.26 O
ANISOU 2996 O VAL B 100 4118 3555 4585 -439 54 209 O
ATOM 2997 CB VAL B 100 6.617 65.044 35.280 1.00 31.37 C
ANISOU 2997 CB VAL B 100 3903 3487 4528 -410 -275 -3 C
ATOM 2998 CG1 VAL B 100 7.754 65.453 34.339 1.00 30.95 C
ANISOU 2998 CG1 VAL B 100 3628 3397 4736 -443 -246 -94 C
ATOM 2999 CG2 VAL B 100 6.912 65.500 36.716 1.00 30.72 C
ANISOU 2999 CG2 VAL B 100 3910 3445 4317 -390 -458 -82 C
ATOM 3000 N TYR B 101 4.834 65.775 32.389 1.00 28.64 N
ANISOU 3000 N TYR B 101 3542 3059 4283 -529 163 108 N
ATOM 3001 CA TYR B 101 4.475 65.349 31.049 1.00 27.45 C
ANISOU 3001 CA TYR B 101 3399 2871 4161 -540 271 170 C
ATOM 3002 C TYR B 101 5.745 65.174 30.251 1.00 32.84 C
ANISOU 3002 C TYR B 101 3976 3516 4984 -560 314 127 C
ATOM 3003 O TYR B 101 6.614 66.053 30.255 1.00 32.65 O
ANISOU 3003 O TYR B 101 3865 3465 5076 -607 335 44 O
ATOM 3004 CB TYR B 101 3.544 66.377 30.382 1.00 27.29 C
ANISOU 3004 CB TYR B 101 3437 2809 4123 -574 353 187 C
ATOM 3005 CG TYR B 101 2.116 66.292 30.878 1.00 27.26 C
ANISOU 3005 CG TYR B 101 3495 2829 4035 -548 345 215 C
ATOM 3006 CD1 TYR B 101 1.093 65.819 30.053 1.00 28.02 C
ANISOU 3006 CD1 TYR B 101 3623 2909 4116 -534 371 266 C
ATOM 3007 CD2 TYR B 101 1.787 66.656 32.185 1.00 27.46 C
ANISOU 3007 CD2 TYR B 101 3541 2886 4005 -545 319 170 C
ATOM 3008 CE1 TYR B 101 -0.223 65.718 30.516 1.00 24.24 C
ANISOU 3008 CE1 TYR B 101 3149 2441 3621 -519 380 260 C
ATOM 3009 CE2 TYR B 101 0.486 66.525 32.668 1.00 27.93 C
ANISOU 3009 CE2 TYR B 101 3640 2956 4015 -536 364 173 C
ATOM 3010 CZ TYR B 101 -0.519 66.086 31.820 1.00 31.74 C
ANISOU 3010 CZ TYR B 101 4106 3417 4538 -525 400 212 C
ATOM 3011 OH TYR B 101 -1.786 65.970 32.313 1.00 32.98 O
ANISOU 3011 OH TYR B 101 4254 3574 4703 -527 462 184 O
ATOM 3012 N TYR B 102 5.863 64.028 29.581 1.00 29.31 N
ANISOU 3012 N TYR B 102 3527 3058 4550 -533 348 164 N
ATOM 3013 CA TYR B 102 7.032 63.696 28.768 1.00 29.57 C
ANISOU 3013 CA TYR B 102 3454 3047 4734 -550 431 105 C
ATOM 3014 C TYR B 102 6.603 63.359 27.365 1.00 34.67 C
ANISOU 3014 C TYR B 102 4199 3652 5324 -584 579 147 C
ATOM 3015 O TYR B 102 5.518 62.814 27.155 1.00 32.36 O
ANISOU 3015 O TYR B 102 4015 3375 4907 -561 553 217 O
ATOM 3016 CB TYR B 102 7.750 62.431 29.290 1.00 30.06 C
ANISOU 3016 CB TYR B 102 3423 3114 4884 -465 322 86 C
ATOM 3017 CG TYR B 102 8.187 62.447 30.730 1.00 30.55 C
ANISOU 3017 CG TYR B 102 3435 3213 4958 -399 113 57 C
ATOM 3018 CD1 TYR B 102 9.494 62.785 31.077 1.00 32.48 C
ANISOU 3018 CD1 TYR B 102 3492 3447 5401 -387 26 -68 C
ATOM 3019 CD2 TYR B 102 7.336 62.000 31.741 1.00 30.64 C
ANISOU 3019 CD2 TYR B 102 3595 3260 4787 -349 -2 145 C
ATOM 3020 CE1 TYR B 102 9.923 62.745 32.402 1.00 32.29 C
ANISOU 3020 CE1 TYR B 102 3445 3455 5367 -311 -223 -104 C
ATOM 3021 CE2 TYR B 102 7.749 61.969 33.071 1.00 31.21 C
ANISOU 3021 CE2 TYR B 102 3688 3358 4812 -285 -206 127 C
ATOM 3022 CZ TYR B 102 9.048 62.337 33.395 1.00 36.99 C
ANISOU 3022 CZ TYR B 102 4248 4088 5720 -257 -344 4 C
ATOM 3023 OH TYR B 102 9.460 62.326 34.700 1.00 37.28 O
ANISOU 3023 OH TYR B 102 4326 4150 5688 -183 -594 -25 O
ATOM 3024 N CYS B 103 7.490 63.610 26.414 1.00 34.29 N
ANISOU 3024 N CYS B 103 4111 3545 5374 -645 738 86 N
ATOM 3025 CA CYS B 103 7.288 63.178 25.044 1.00 36.55 C
ANISOU 3025 CA CYS B 103 4522 3784 5580 -680 889 106 C
ATOM 3026 C CYS B 103 8.375 62.168 24.703 1.00 38.05 C
ANISOU 3026 C CYS B 103 4583 3942 5932 -666 982 16 C
ATOM 3027 O CYS B 103 9.482 62.206 25.264 1.00 36.09 O
ANISOU 3027 O CYS B 103 4130 3685 5899 -655 970 -79 O
ATOM 3028 CB CYS B 103 7.226 64.337 24.051 1.00 38.46 C
ANISOU 3028 CB CYS B 103 4914 3957 5742 -772 1045 126 C
ATOM 3029 SG CYS B 103 8.781 65.234 23.845 1.00 43.68 S
ANISOU 3029 SG CYS B 103 5442 4534 6619 -884 1261 9 S
ATOM 3030 N ALA B 104 8.024 61.215 23.853 1.00 34.87 N
ANISOU 3030 N ALA B 104 4283 3518 5446 -656 1048 28 N
ATOM 3031 CA ALA B 104 8.924 60.158 23.429 1.00 34.34 C
ANISOU 3031 CA ALA B 104 4112 3403 5533 -634 1155 -67 C
ATOM 3032 C ALA B 104 8.837 60.035 21.926 1.00 38.94 C
ANISOU 3032 C ALA B 104 4879 3930 5988 -713 1379 -95 C
ATOM 3033 O ALA B 104 7.769 60.247 21.350 1.00 38.85 O
ANISOU 3033 O ALA B 104 5091 3931 5738 -736 1345 -14 O
ATOM 3034 CB ALA B 104 8.523 58.841 24.087 1.00 35.18 C
ANISOU 3034 CB ALA B 104 4186 3524 5657 -526 986 -32 C
ATOM 3035 N ALA B 105 9.943 59.659 21.288 1.00 36.58 N
ANISOU 3035 N ALA B 105 4488 3562 5849 -749 1600 -223 N
ATOM 3036 CA ALA B 105 9.996 59.536 19.837 1.00 37.05 C
ANISOU 3036 CA ALA B 105 4757 3556 5764 -839 1859 -271 C
ATOM 3037 C ALA B 105 10.316 58.113 19.403 1.00 40.95 C
ANISOU 3037 C ALA B 105 5205 4006 6347 -792 1938 -375 C
ATOM 3038 O ALA B 105 11.289 57.532 19.892 1.00 40.44 O
ANISOU 3038 O ALA B 105 4872 3908 6586 -732 1961 -482 O
ATOM 3039 CB ALA B 105 11.044 60.503 19.280 1.00 38.55 C
ANISOU 3039 CB ALA B 105 4924 3673 6052 -966 2158 -355 C
ATOM 3040 N ASP B 106 9.510 57.561 18.466 1.00 37.99 N
ANISOU 3040 N ASP B 106 5089 3621 5724 -813 1966 -358 N
ATOM 3041 CA ASP B 106 9.710 56.214 17.910 1.00 37.87 C
ANISOU 3041 CA ASP B 106 5078 3547 5764 -784 2061 -472 C
ATOM 3042 C ASP B 106 10.188 56.356 16.468 1.00 42.63 C
ANISOU 3042 C ASP B 106 5894 4076 6227 -904 2405 -583 C
ATOM 3043 O ASP B 106 9.432 56.894 15.658 1.00 41.45 O
ANISOU 3043 O ASP B 106 6069 3939 5742 -974 2410 -514 O
ATOM 3044 CB ASP B 106 8.392 55.380 17.962 1.00 38.74 C
ANISOU 3044 CB ASP B 106 5324 3689 5704 -729 1828 -402 C
ATOM 3045 CG ASP B 106 8.502 53.870 17.651 1.00 45.19 C
ANISOU 3045 CG ASP B 106 6117 4432 6622 -683 1874 -514 C
ATOM 3046 OD1 ASP B 106 9.581 53.423 17.180 1.00 45.79 O
ANISOU 3046 OD1 ASP B 106 6103 4425 6871 -690 2115 -664 O
ATOM 3047 OD2 ASP B 106 7.512 53.138 17.886 1.00 44.42 O
ANISOU 3047 OD2 ASP B 106 6076 4342 6458 -644 1687 -468 O
ATOM 3048 N PRO B 107 11.403 55.868 16.100 1.00 42.15 N
ANISOU 3048 N PRO B 107 5677 3928 6409 -927 2694 -763 N
ATOM 3049 CA PRO B 107 11.840 55.958 14.692 1.00 42.32 C
ANISOU 3049 CA PRO B 107 5944 3868 6267 -1061 3078 -883 C
ATOM 3050 C PRO B 107 10.979 55.120 13.725 1.00 48.42 C
ANISOU 3050 C PRO B 107 7046 4629 6722 -1070 3059 -908 C
ATOM 3051 O PRO B 107 11.015 55.351 12.515 1.00 50.13 O
ANISOU 3051 O PRO B 107 7593 4795 6658 -1186 3312 -963 O
ATOM 3052 CB PRO B 107 13.294 55.476 14.750 1.00 44.13 C
ANISOU 3052 CB PRO B 107 5842 4006 6921 -1057 3362 -1097 C
ATOM 3053 CG PRO B 107 13.317 54.528 15.907 1.00 48.44 C
ANISOU 3053 CG PRO B 107 6066 4570 7768 -878 3056 -1093 C
ATOM 3054 CD PRO B 107 12.420 55.176 16.923 1.00 44.37 C
ANISOU 3054 CD PRO B 107 5563 4167 7127 -824 2682 -877 C
ATOM 3055 N PHE B 108 10.209 54.158 14.247 1.00 43.95 N
ANISOU 3055 N PHE B 108 6412 4098 6190 -959 2768 -874 N
ATOM 3056 CA PHE B 108 9.267 53.374 13.445 1.00 43.53 C
ANISOU 3056 CA PHE B 108 6639 4038 5864 -970 2689 -908 C
ATOM 3057 C PHE B 108 7.945 54.140 13.563 1.00 45.10 C
ANISOU 3057 C PHE B 108 7034 4332 5771 -969 2377 -725 C
ATOM 3058 O PHE B 108 7.154 53.906 14.473 1.00 42.84 O
ANISOU 3058 O PHE B 108 6607 4104 5567 -888 2078 -629 O
ATOM 3059 CB PHE B 108 9.154 51.921 13.952 1.00 45.33 C
ANISOU 3059 CB PHE B 108 6673 4220 6331 -864 2566 -984 C
ATOM 3060 CG PHE B 108 10.368 51.047 13.721 1.00 47.60 C
ANISOU 3060 CG PHE B 108 6779 4387 6921 -840 2853 -1188 C
ATOM 3061 CD1 PHE B 108 10.751 50.680 12.432 1.00 52.98 C
ANISOU 3061 CD1 PHE B 108 7677 4988 7466 -933 3179 -1376 C
ATOM 3062 CD2 PHE B 108 11.096 50.542 14.792 1.00 49.38 C
ANISOU 3062 CD2 PHE B 108 6631 4566 7566 -714 2782 -1202 C
ATOM 3063 CE1 PHE B 108 11.851 49.835 12.219 1.00 53.95 C
ANISOU 3063 CE1 PHE B 108 7606 4983 7909 -903 3464 -1592 C
ATOM 3064 CE2 PHE B 108 12.202 49.706 14.579 1.00 52.69 C
ANISOU 3064 CE2 PHE B 108 6851 4854 8313 -666 3020 -1406 C
ATOM 3065 CZ PHE B 108 12.573 49.361 13.296 1.00 52.04 C
ANISOU 3065 CZ PHE B 108 6949 4691 8132 -763 3375 -1607 C
ATOM 3066 N GLY B 109 7.777 55.099 12.663 1.00 43.10 N
ANISOU 3066 N GLY B 109 7102 4077 5196 -1060 2470 -680 N
ATOM 3067 CA GLY B 109 6.675 56.053 12.613 1.00 42.93 C
ANISOU 3067 CA GLY B 109 7290 4118 4903 -1054 2204 -515 C
ATOM 3068 C GLY B 109 5.259 55.528 12.688 1.00 45.78 C
ANISOU 3068 C GLY B 109 7709 4536 5148 -989 1838 -482 C
ATOM 3069 O GLY B 109 4.370 56.252 13.131 1.00 44.09 O
ANISOU 3069 O GLY B 109 7494 4382 4877 -945 1573 -349 O
ATOM 3070 N GLU B 110 5.029 54.290 12.231 1.00 41.58 N
ANISOU 3070 N GLU B 110 7218 3975 4605 -987 1832 -621 N
ATOM 3071 CA GLU B 110 3.694 53.695 12.279 1.00 41.06 C
ANISOU 3071 CA GLU B 110 7174 3948 4480 -945 1501 -628 C
ATOM 3072 C GLU B 110 3.565 52.665 13.406 1.00 46.24 C
ANISOU 3072 C GLU B 110 7485 4600 5484 -883 1415 -647 C
ATOM 3073 O GLU B 110 2.543 51.976 13.484 1.00 48.23 O
ANISOU 3073 O GLU B 110 7717 4857 5750 -870 1202 -684 O
ATOM 3074 CB GLU B 110 3.294 53.110 10.903 1.00 42.00 C
ANISOU 3074 CB GLU B 110 7641 4026 4291 -1000 1498 -775 C
ATOM 3075 CG GLU B 110 3.125 54.157 9.802 1.00 51.63 C
ANISOU 3075 CG GLU B 110 9288 5241 5086 -1047 1493 -721 C
ATOM 3076 CD GLU B 110 2.122 55.267 10.076 1.00 76.84 C
ANISOU 3076 CD GLU B 110 12530 8495 8170 -988 1159 -548 C
ATOM 3077 OE1 GLU B 110 2.498 56.450 9.921 1.00 71.95 O
ANISOU 3077 OE1 GLU B 110 12070 7857 7412 -1005 1254 -419 O
ATOM 3078 OE2 GLU B 110 0.971 54.961 10.463 1.00 79.50 O
ANISOU 3078 OE2 GLU B 110 12732 8882 8591 -927 820 -551 O
ATOM 3079 N ARG B 111 4.569 52.590 14.312 1.00 40.74 N
ANISOU 3079 N ARG B 111 6522 3884 5074 -844 1564 -618 N
ATOM 3080 CA ARG B 111 4.552 51.626 15.418 1.00 39.25 C
ANISOU 3080 CA ARG B 111 6059 3665 5188 -772 1483 -610 C
ATOM 3081 C ARG B 111 3.928 52.141 16.721 1.00 40.25 C
ANISOU 3081 C ARG B 111 6012 3864 5417 -720 1265 -447 C
ATOM 3082 O ARG B 111 2.938 51.563 17.166 1.00 37.77 O
ANISOU 3082 O ARG B 111 5654 3550 5148 -709 1094 -427 O
ATOM 3083 CB ARG B 111 5.952 51.034 15.700 1.00 36.08 C
ANISOU 3083 CB ARG B 111 5471 3178 5061 -730 1713 -691 C
ATOM 3084 CG ARG B 111 5.990 50.093 16.928 1.00 37.32 C
ANISOU 3084 CG ARG B 111 5386 3280 5514 -631 1595 -646 C
ATOM 3085 CD ARG B 111 7.333 49.416 17.159 1.00 44.07 C
ANISOU 3085 CD ARG B 111 6051 4027 6667 -557 1765 -741 C
ATOM 3086 NE ARG B 111 8.390 50.365 17.532 1.00 43.20 N
ANISOU 3086 NE ARG B 111 5782 3957 6677 -538 1856 -718 N
ATOM 3087 CZ ARG B 111 9.589 50.011 17.980 1.00 52.39 C
ANISOU 3087 CZ ARG B 111 6704 5043 8158 -452 1940 -790 C
ATOM 3088 NH1 ARG B 111 9.904 48.727 18.118 1.00 40.04 N
ANISOU 3088 NH1 ARG B 111 5049 3347 6817 -361 1947 -871 N
ATOM 3089 NH2 ARG B 111 10.483 50.937 18.300 1.00 39.42 N
ANISOU 3089 NH2 ARG B 111 4898 3439 6640 -452 2006 -793 N
ATOM 3090 N LEU B 112 4.540 53.161 17.365 1.00 36.35 N
ANISOU 3090 N LEU B 112 5411 3418 4982 -699 1296 -350 N
ATOM 3091 CA LEU B 112 4.165 53.634 18.703 1.00 35.25 C
ANISOU 3091 CA LEU B 112 5107 3338 4948 -649 1129 -216 C
ATOM 3092 C LEU B 112 2.654 53.729 19.003 1.00 38.92 C
ANISOU 3092 C LEU B 112 5608 3852 5327 -655 910 -154 C
ATOM 3093 O LEU B 112 2.218 53.235 20.040 1.00 37.15 O
ANISOU 3093 O LEU B 112 5258 3623 5235 -623 821 -103 O
ATOM 3094 CB LEU B 112 4.836 54.998 19.018 1.00 34.55 C
ANISOU 3094 CB LEU B 112 4973 3300 4857 -655 1182 -149 C
ATOM 3095 CG LEU B 112 4.662 55.569 20.454 1.00 36.10 C
ANISOU 3095 CG LEU B 112 5004 3554 5158 -604 1034 -35 C
ATOM 3096 CD1 LEU B 112 5.154 54.576 21.539 1.00 34.49 C
ANISOU 3096 CD1 LEU B 112 4623 3310 5172 -525 991 -30 C
ATOM 3097 CD2 LEU B 112 5.369 56.920 20.580 1.00 36.04 C
ANISOU 3097 CD2 LEU B 112 4965 3576 5152 -630 1103 -6 C
ATOM 3098 N CYS B 113 1.885 54.404 18.134 1.00 37.13 N
ANISOU 3098 N CYS B 113 5554 3663 4891 -693 825 -160 N
ATOM 3099 CA CYS B 113 0.472 54.690 18.365 1.00 37.79 C
ANISOU 3099 CA CYS B 113 5630 3792 4938 -688 605 -125 C
ATOM 3100 C CYS B 113 -0.451 53.469 18.320 1.00 39.58 C
ANISOU 3100 C CYS B 113 5816 3979 5244 -710 514 -214 C
ATOM 3101 O CYS B 113 -1.604 53.574 18.755 1.00 38.56 O
ANISOU 3101 O CYS B 113 5602 3876 5174 -713 359 -204 O
ATOM 3102 CB CYS B 113 -0.003 55.797 17.436 1.00 39.23 C
ANISOU 3102 CB CYS B 113 6009 4003 4893 -695 503 -106 C
ATOM 3103 SG CYS B 113 1.039 57.281 17.471 1.00 43.25 S
ANISOU 3103 SG CYS B 113 6586 4521 5326 -696 644 -1 S
ATOM 3104 N ILE B 114 0.068 52.296 17.891 1.00 34.57 N
ANISOU 3104 N ILE B 114 5214 3266 4657 -729 630 -313 N
ATOM 3105 CA ILE B 114 -0.690 51.040 17.906 1.00 32.78 C
ANISOU 3105 CA ILE B 114 4943 2969 4543 -763 577 -407 C
ATOM 3106 C ILE B 114 -0.922 50.622 19.376 1.00 34.45 C
ANISOU 3106 C ILE B 114 4966 3150 4973 -745 583 -312 C
ATOM 3107 O ILE B 114 -2.004 50.153 19.724 1.00 33.41 O
ANISOU 3107 O ILE B 114 4765 2992 4939 -789 504 -340 O
ATOM 3108 CB ILE B 114 0.082 49.918 17.142 1.00 34.80 C
ANISOU 3108 CB ILE B 114 5286 3123 4813 -780 732 -538 C
ATOM 3109 CG1 ILE B 114 0.167 50.221 15.620 1.00 34.77 C
ANISOU 3109 CG1 ILE B 114 5532 3138 4541 -820 742 -654 C
ATOM 3110 CG2 ILE B 114 -0.524 48.531 17.408 1.00 33.27 C
ANISOU 3110 CG2 ILE B 114 5022 2820 4800 -814 713 -621 C
ATOM 3111 CD1 ILE B 114 1.087 49.220 14.786 1.00 34.58 C
ANISOU 3111 CD1 ILE B 114 5616 3010 4512 -842 958 -811 C
ATOM 3112 N ASP B 115 0.108 50.775 20.223 1.00 29.03 N
ANISOU 3112 N ASP B 115 4210 2458 4363 -685 682 -210 N
ATOM 3113 CA ASP B 115 0.072 50.303 21.611 1.00 27.89 C
ANISOU 3113 CA ASP B 115 3960 2266 4372 -657 691 -108 C
ATOM 3114 C ASP B 115 1.052 51.198 22.415 1.00 31.14 C
ANISOU 3114 C ASP B 115 4314 2739 4779 -585 706 3 C
ATOM 3115 O ASP B 115 2.127 50.731 22.807 1.00 30.93 O
ANISOU 3115 O ASP B 115 4246 2650 4854 -518 762 24 O
ATOM 3116 CB ASP B 115 0.529 48.839 21.602 1.00 28.48 C
ANISOU 3116 CB ASP B 115 4045 2187 4588 -641 779 -157 C
ATOM 3117 CG ASP B 115 0.206 48.015 22.835 1.00 33.75 C
ANISOU 3117 CG ASP B 115 4682 2749 5393 -633 786 -61 C
ATOM 3118 OD1 ASP B 115 0.146 48.594 23.934 1.00 32.94 O
ANISOU 3118 OD1 ASP B 115 4549 2696 5271 -606 750 68 O
ATOM 3119 OD2 ASP B 115 0.077 46.776 22.703 1.00 33.88 O
ANISOU 3119 OD2 ASP B 115 4732 2616 5526 -653 840 -114 O
ATOM 3120 N PRO B 116 0.694 52.486 22.656 1.00 28.07 N
ANISOU 3120 N PRO B 116 3909 2459 4296 -593 640 59 N
ATOM 3121 CA PRO B 116 1.669 53.424 23.262 1.00 27.27 C
ANISOU 3121 CA PRO B 116 3755 2413 4192 -541 654 129 C
ATOM 3122 C PRO B 116 2.248 53.022 24.605 1.00 31.29 C
ANISOU 3122 C PRO B 116 4197 2886 4805 -476 635 211 C
ATOM 3123 O PRO B 116 3.455 53.196 24.780 1.00 29.82 O
ANISOU 3123 O PRO B 116 3949 2695 4686 -418 653 208 O
ATOM 3124 CB PRO B 116 0.912 54.764 23.336 1.00 28.70 C
ANISOU 3124 CB PRO B 116 3945 2690 4270 -567 578 166 C
ATOM 3125 CG PRO B 116 -0.127 54.666 22.285 1.00 34.28 C
ANISOU 3125 CG PRO B 116 4728 3396 4900 -614 521 95 C
ATOM 3126 CD PRO B 116 -0.532 53.198 22.223 1.00 30.22 C
ANISOU 3126 CD PRO B 116 4206 2797 4478 -641 540 35 C
ATOM 3127 N ASN B 117 1.430 52.470 25.525 1.00 29.33 N
ANISOU 3127 N ASN B 117 3968 2600 4574 -488 602 276 N
ATOM 3128 CA ASN B 117 1.904 52.056 26.852 1.00 30.69 C
ANISOU 3128 CA ASN B 117 4152 2721 4786 -422 566 376 C
ATOM 3129 C ASN B 117 2.846 50.864 26.831 1.00 35.71 C
ANISOU 3129 C ASN B 117 4794 3227 5549 -342 574 373 C
ATOM 3130 O ASN B 117 3.642 50.699 27.754 1.00 36.23 O
ANISOU 3130 O ASN B 117 4859 3253 5654 -246 494 443 O
ATOM 3131 CB ASN B 117 0.747 51.806 27.820 1.00 31.26 C
ANISOU 3131 CB ASN B 117 4293 2768 4816 -476 580 450 C
ATOM 3132 CG ASN B 117 0.089 53.102 28.182 1.00 38.84 C
ANISOU 3132 CG ASN B 117 5221 3849 5686 -517 562 455 C
ATOM 3133 OD1 ASN B 117 0.760 54.084 28.469 1.00 27.50 O
ANISOU 3133 OD1 ASN B 117 3754 2492 4202 -474 507 470 O
ATOM 3134 ND2 ASN B 117 -1.224 53.145 28.149 1.00 29.64 N
ANISOU 3134 ND2 ASN B 117 4043 2689 4530 -601 608 423 N
ATOM 3135 N THR B 118 2.745 50.025 25.813 1.00 31.73 N
ANISOU 3135 N THR B 118 4300 2645 5112 -369 650 282 N
ATOM 3136 CA THR B 118 3.654 48.890 25.720 1.00 30.49 C
ANISOU 3136 CA THR B 118 4133 2341 5108 -283 670 256 C
ATOM 3137 C THR B 118 4.888 49.320 24.933 1.00 34.11 C
ANISOU 3137 C THR B 118 4481 2836 5644 -234 716 148 C
ATOM 3138 O THR B 118 6.007 49.068 25.374 1.00 34.14 O
ANISOU 3138 O THR B 118 4396 2779 5796 -120 671 150 O
ATOM 3139 CB THR B 118 2.996 47.712 24.990 1.00 35.49 C
ANISOU 3139 CB THR B 118 4833 2850 5800 -344 756 180 C
ATOM 3140 OG1 THR B 118 1.801 47.342 25.665 1.00 36.94 O
ANISOU 3140 OG1 THR B 118 5099 2990 5948 -419 754 257 O
ATOM 3141 CG2 THR B 118 3.925 46.501 24.877 1.00 33.29 C
ANISOU 3141 CG2 THR B 118 4549 2392 5709 -244 788 143 C
ATOM 3142 N PHE B 119 4.676 49.957 23.763 1.00 30.05 N
ANISOU 3142 N PHE B 119 3977 2405 5035 -321 808 48 N
ATOM 3143 CA PHE B 119 5.749 50.262 22.816 1.00 30.68 C
ANISOU 3143 CA PHE B 119 3994 2492 5172 -314 932 -74 C
ATOM 3144 C PHE B 119 6.683 51.373 23.304 1.00 37.72 C
ANISOU 3144 C PHE B 119 4759 3463 6111 -277 909 -54 C
ATOM 3145 O PHE B 119 7.824 51.440 22.831 1.00 37.22 O
ANISOU 3145 O PHE B 119 4584 3367 6190 -252 1023 -161 O
ATOM 3146 CB PHE B 119 5.184 50.516 21.399 1.00 31.42 C
ANISOU 3146 CB PHE B 119 4215 2624 5098 -423 1040 -175 C
ATOM 3147 CG PHE B 119 4.498 49.312 20.753 1.00 32.32 C
ANISOU 3147 CG PHE B 119 4430 2642 5208 -460 1069 -257 C
ATOM 3148 CD1 PHE B 119 4.559 48.048 21.339 1.00 35.83 C
ANISOU 3148 CD1 PHE B 119 4840 2946 5828 -400 1050 -245 C
ATOM 3149 CD2 PHE B 119 3.825 49.439 19.542 1.00 33.56 C
ANISOU 3149 CD2 PHE B 119 4734 2832 5186 -553 1103 -354 C
ATOM 3150 CE1 PHE B 119 3.955 46.936 20.726 1.00 36.61 C
ANISOU 3150 CE1 PHE B 119 5027 2935 5949 -448 1091 -341 C
ATOM 3151 CE2 PHE B 119 3.227 48.333 18.930 1.00 35.95 C
ANISOU 3151 CE2 PHE B 119 5122 3042 5495 -595 1114 -462 C
ATOM 3152 CZ PHE B 119 3.288 47.089 19.529 1.00 34.85 C
ANISOU 3152 CZ PHE B 119 4922 2761 5558 -550 1121 -461 C
ATOM 3153 N ALA B 120 6.253 52.164 24.323 1.00 35.51 N
ANISOU 3153 N ALA B 120 4478 3268 5745 -274 772 64 N
ATOM 3154 CA ALA B 120 7.084 53.221 24.932 1.00 35.43 C
ANISOU 3154 CA ALA B 120 4347 3326 5787 -245 720 73 C
ATOM 3155 C ALA B 120 8.305 52.586 25.564 1.00 38.24 C
ANISOU 3155 C ALA B 120 4550 3600 6380 -116 644 39 C
ATOM 3156 O ALA B 120 9.365 53.194 25.571 1.00 36.76 O
ANISOU 3156 O ALA B 120 4198 3430 6338 -95 660 -43 O
ATOM 3157 CB ALA B 120 6.302 53.979 25.998 1.00 35.96 C
ANISOU 3157 CB ALA B 120 4469 3480 5715 -258 583 191 C
ATOM 3158 N GLY B 121 8.138 51.356 26.047 1.00 36.73 N
ANISOU 3158 N GLY B 121 4411 3299 6245 -33 562 94 N
ATOM 3159 CA GLY B 121 9.187 50.541 26.655 1.00 37.81 C
ANISOU 3159 CA GLY B 121 4435 3318 6614 125 442 79 C
ATOM 3160 C GLY B 121 10.349 50.218 25.733 1.00 43.59 C
ANISOU 3160 C GLY B 121 4976 3975 7612 164 583 -102 C
ATOM 3161 O GLY B 121 11.427 49.859 26.215 1.00 44.33 O
ANISOU 3161 O GLY B 121 4895 3988 7961 306 466 -155 O
ATOM 3162 N TYR B 122 10.144 50.318 24.400 1.00 40.42 N
ANISOU 3162 N TYR B 122 4613 3589 7157 45 832 -212 N
ATOM 3163 CA TYR B 122 11.206 50.009 23.424 1.00 40.78 C
ANISOU 3163 CA TYR B 122 4504 3555 7436 56 1041 -408 C
ATOM 3164 C TYR B 122 12.003 51.250 23.027 1.00 44.16 C
ANISOU 3164 C TYR B 122 4786 4068 7926 -23 1181 -513 C
ATOM 3165 O TYR B 122 12.978 51.128 22.294 1.00 42.87 O
ANISOU 3165 O TYR B 122 4467 3838 7983 -30 1393 -692 O
ATOM 3166 CB TYR B 122 10.639 49.372 22.130 1.00 41.47 C
ANISOU 3166 CB TYR B 122 4757 3592 7410 -39 1264 -493 C
ATOM 3167 CG TYR B 122 9.563 48.315 22.261 1.00 42.48 C
ANISOU 3167 CG TYR B 122 5066 3646 7429 -31 1180 -409 C
ATOM 3168 CD1 TYR B 122 9.580 47.393 23.305 1.00 44.89 C
ANISOU 3168 CD1 TYR B 122 5355 3833 7866 103 994 -308 C
ATOM 3169 CD2 TYR B 122 8.599 48.157 21.272 1.00 42.77 C
ANISOU 3169 CD2 TYR B 122 5297 3703 7251 -157 1295 -449 C
ATOM 3170 CE1 TYR B 122 8.610 46.394 23.404 1.00 45.19 C
ANISOU 3170 CE1 TYR B 122 5565 3774 7832 87 962 -239 C
ATOM 3171 CE2 TYR B 122 7.665 47.129 21.328 1.00 42.92 C
ANISOU 3171 CE2 TYR B 122 5446 3634 7227 -166 1238 -413 C
ATOM 3172 CZ TYR B 122 7.652 46.270 22.411 1.00 51.61 C
ANISOU 3172 CZ TYR B 122 6524 4614 8471 -56 1092 -304 C
ATOM 3173 OH TYR B 122 6.687 45.293 22.462 1.00 51.85 O
ANISOU 3173 OH TYR B 122 6692 4539 8469 -93 1072 -270 O
ATOM 3174 N LEU B 123 11.570 52.440 23.484 1.00 41.67 N
ANISOU 3174 N LEU B 123 4522 3882 7429 -93 1095 -414 N
ATOM 3175 CA LEU B 123 12.156 53.722 23.096 1.00 41.45 C
ANISOU 3175 CA LEU B 123 4403 3919 7427 -198 1244 -493 C
ATOM 3176 C LEU B 123 13.288 54.193 23.969 1.00 48.45 C
ANISOU 3176 C LEU B 123 5003 4806 8598 -123 1118 -564 C
ATOM 3177 O LEU B 123 13.205 54.133 25.198 1.00 48.38 O
ANISOU 3177 O LEU B 123 4961 4824 8599 -16 821 -470 O
ATOM 3178 CB LEU B 123 11.072 54.822 23.000 1.00 40.19 C
ANISOU 3178 CB LEU B 123 4459 3875 6938 -316 1232 -366 C
ATOM 3179 CG LEU B 123 9.809 54.452 22.245 1.00 42.44 C
ANISOU 3179 CG LEU B 123 5013 4171 6942 -379 1277 -298 C
ATOM 3180 CD1 LEU B 123 8.836 55.608 22.200 1.00 41.59 C
ANISOU 3180 CD1 LEU B 123 5070 4160 6574 -465 1230 -191 C
ATOM 3181 CD2 LEU B 123 10.122 53.942 20.857 1.00 45.04 C
ANISOU 3181 CD2 LEU B 123 5420 4426 7266 -440 1541 -432 C
ATOM 3182 N GLU B 124 14.323 54.719 23.307 1.00 47.10 N
ANISOU 3182 N GLU B 124 4645 4604 8647 -196 1357 -741 N
ATOM 3183 CA GLU B 124 15.528 55.304 23.895 1.00 47.58 C
ANISOU 3183 CA GLU B 124 4377 4656 9046 -164 1294 -874 C
ATOM 3184 C GLU B 124 15.440 56.841 23.902 1.00 51.32 C
ANISOU 3184 C GLU B 124 4885 5213 9403 -318 1373 -857 C
ATOM 3185 O GLU B 124 16.215 57.472 24.612 1.00 53.31 O
ANISOU 3185 O GLU B 124 4893 5477 9885 -303 1252 -944 O
ATOM 3186 CB GLU B 124 16.763 54.902 23.073 1.00 49.43 C
ANISOU 3186 CB GLU B 124 4346 4774 9663 -173 1579 -1121 C
ATOM 3187 CG GLU B 124 17.195 53.447 23.204 1.00 66.63 C
ANISOU 3187 CG GLU B 124 6388 6834 12096 13 1480 -1192 C
ATOM 3188 CD GLU B 124 18.431 53.069 22.402 1.00 96.19 C
ANISOU 3188 CD GLU B 124 9830 10451 16265 9 1786 -1470 C
ATOM 3189 OE1 GLU B 124 18.500 51.910 21.931 1.00 98.27 O
ANISOU 3189 OE1 GLU B 124 10105 10604 16630 93 1875 -1536 O
ATOM 3190 OE2 GLU B 124 19.331 53.927 22.242 1.00 90.45 O
ANISOU 3190 OE2 GLU B 124 8851 9723 15795 -86 1959 -1640 O
ATOM 3191 N THR B 125 14.526 57.442 23.100 1.00 44.59 N
ANISOU 3191 N THR B 125 4331 4401 8212 -461 1558 -756 N
ATOM 3192 CA THR B 125 14.419 58.894 22.931 1.00 42.26 C
ANISOU 3192 CA THR B 125 4110 4144 7803 -609 1672 -732 C
ATOM 3193 C THR B 125 13.258 59.483 23.712 1.00 42.88 C
ANISOU 3193 C THR B 125 4381 4321 7591 -592 1418 -543 C
ATOM 3194 O THR B 125 12.101 59.366 23.317 1.00 42.48 O
ANISOU 3194 O THR B 125 4602 4302 7236 -610 1410 -410 O
ATOM 3195 CB THR B 125 14.398 59.259 21.432 1.00 50.58 C
ANISOU 3195 CB THR B 125 5364 5137 8715 -774 2074 -771 C
ATOM 3196 OG1 THR B 125 15.527 58.655 20.774 1.00 52.94 O
ANISOU 3196 OG1 THR B 125 5464 5336 9314 -794 2348 -977 O
ATOM 3197 CG2 THR B 125 14.393 60.752 21.195 1.00 43.74 C
ANISOU 3197 CG2 THR B 125 4596 4265 7756 -928 2220 -742 C
ATOM 3198 N TRP B 126 13.595 60.154 24.808 1.00 38.01 N
ANISOU 3198 N TRP B 126 3608 3746 7088 -563 1216 -558 N
ATOM 3199 CA TRP B 126 12.661 60.781 25.732 1.00 37.77 C
ANISOU 3199 CA TRP B 126 3717 3802 6834 -545 986 -419 C
ATOM 3200 C TRP B 126 13.142 62.164 26.068 1.00 41.87 C
ANISOU 3200 C TRP B 126 4134 4325 7451 -639 1009 -489 C
ATOM 3201 O TRP B 126 14.349 62.417 26.097 1.00 41.62 O
ANISOU 3201 O TRP B 126 3836 4245 7732 -671 1076 -660 O
ATOM 3202 CB TRP B 126 12.604 59.980 27.053 1.00 36.07 C
ANISOU 3202 CB TRP B 126 3439 3625 6642 -381 647 -373 C
ATOM 3203 CG TRP B 126 11.893 58.664 26.958 1.00 36.82 C
ANISOU 3203 CG TRP B 126 3680 3703 6607 -292 594 -269 C
ATOM 3204 CD1 TRP B 126 12.435 57.470 26.600 1.00 39.65 C
ANISOU 3204 CD1 TRP B 126 3948 3983 7137 -210 626 -328 C
ATOM 3205 CD2 TRP B 126 10.502 58.412 27.225 1.00 36.10 C
ANISOU 3205 CD2 TRP B 126 3836 3656 6222 -286 516 -106 C
ATOM 3206 NE1 TRP B 126 11.474 56.488 26.621 1.00 38.96 N
ANISOU 3206 NE1 TRP B 126 4054 3880 6867 -159 571 -205 N
ATOM 3207 CE2 TRP B 126 10.280 57.034 27.014 1.00 40.21 C
ANISOU 3207 CE2 TRP B 126 4412 4117 6749 -210 506 -72 C
ATOM 3208 CE3 TRP B 126 9.425 59.218 27.652 1.00 36.52 C
ANISOU 3208 CE3 TRP B 126 4050 3781 6043 -337 462 -4 C
ATOM 3209 CZ2 TRP B 126 9.016 56.440 27.181 1.00 39.37 C
ANISOU 3209 CZ2 TRP B 126 4510 4020 6429 -205 459 57 C
ATOM 3210 CZ3 TRP B 126 8.173 58.644 27.791 1.00 37.91 C
ANISOU 3210 CZ3 TRP B 126 4409 3973 6022 -323 421 114 C
ATOM 3211 CH2 TRP B 126 7.974 57.268 27.566 1.00 39.02 C
ANISOU 3211 CH2 TRP B 126 4595 4054 6177 -266 423 143 C
ATOM 3212 N GLY B 127 12.200 63.039 26.379 1.00 39.12 N
ANISOU 3212 N GLY B 127 3971 4023 6870 -680 945 -377 N
ATOM 3213 CA GLY B 127 12.535 64.361 26.880 1.00 38.55 C
ANISOU 3213 CA GLY B 127 3823 3947 6879 -759 929 -439 C
ATOM 3214 C GLY B 127 12.709 64.295 28.392 1.00 41.87 C
ANISOU 3214 C GLY B 127 4121 4437 7349 -655 596 -472 C
ATOM 3215 O GLY B 127 12.535 63.236 28.999 1.00 42.55 O
ANISOU 3215 O GLY B 127 4219 4564 7385 -522 395 -420 O
ATOM 3216 N GLN B 128 13.060 65.416 29.006 1.00 38.11 N
ANISOU 3216 N GLN B 128 3557 3961 6959 -717 536 -559 N
ATOM 3217 CA GLN B 128 13.310 65.562 30.442 1.00 37.20 C
ANISOU 3217 CA GLN B 128 3353 3909 6872 -637 214 -622 C
ATOM 3218 C GLN B 128 12.006 65.682 31.267 1.00 38.06 C
ANISOU 3218 C GLN B 128 3727 4094 6640 -587 65 -473 C
ATOM 3219 O GLN B 128 12.022 65.523 32.493 1.00 36.76 O
ANISOU 3219 O GLN B 128 3580 3987 6402 -502 -204 -488 O
ATOM 3220 CB GLN B 128 14.225 66.793 30.667 1.00 38.10 C
ANISOU 3220 CB GLN B 128 3262 3978 7238 -751 241 -812 C
ATOM 3221 CG GLN B 128 13.521 68.174 30.825 1.00 57.72 C
ANISOU 3221 CG GLN B 128 5912 6448 9573 -860 315 -779 C
ATOM 3222 CD GLN B 128 12.821 68.765 29.602 1.00 69.67 C
ANISOU 3222 CD GLN B 128 7627 7882 10961 -970 635 -660 C
ATOM 3223 OE1 GLN B 128 13.095 68.377 28.455 1.00 68.09 O
ANISOU 3223 OE1 GLN B 128 7430 7621 10820 -1017 873 -640 O
ATOM 3224 NE2 GLN B 128 11.907 69.747 29.823 1.00 37.89 N
ANISOU 3224 NE2 GLN B 128 3794 3844 6758 -1006 641 -586 N
ATOM 3225 N GLY B 129 10.925 66.036 30.584 1.00 33.14 N
ANISOU 3225 N GLY B 129 3309 3460 5824 -645 244 -349 N
ATOM 3226 CA GLY B 129 9.609 66.238 31.170 1.00 32.66 C
ANISOU 3226 CA GLY B 129 3465 3452 5494 -617 173 -232 C
ATOM 3227 C GLY B 129 9.352 67.672 31.566 1.00 37.07 C
ANISOU 3227 C GLY B 129 4059 3992 6032 -693 190 -284 C
ATOM 3228 O GLY B 129 10.292 68.408 31.872 1.00 37.32 O
ANISOU 3228 O GLY B 129 3940 3994 6244 -749 160 -428 O
ATOM 3229 N THR B 130 8.067 68.080 31.562 1.00 33.45 N
ANISOU 3229 N THR B 130 3783 3540 5385 -695 238 -187 N
ATOM 3230 CA THR B 130 7.650 69.403 32.013 1.00 32.14 C
ANISOU 3230 CA THR B 130 3673 3345 5196 -746 251 -234 C
ATOM 3231 C THR B 130 6.478 69.237 33.023 1.00 35.61 C
ANISOU 3231 C THR B 130 4252 3853 5426 -682 156 -186 C
ATOM 3232 O THR B 130 5.548 68.470 32.787 1.00 33.88 O
ANISOU 3232 O THR B 130 4124 3661 5088 -635 185 -77 O
ATOM 3233 CB THR B 130 7.413 70.364 30.823 1.00 34.24 C
ANISOU 3233 CB THR B 130 3999 3494 5515 -827 453 -196 C
ATOM 3234 OG1 THR B 130 7.486 71.705 31.305 1.00 29.08 O
ANISOU 3234 OG1 THR B 130 3343 2776 4929 -888 463 -286 O
ATOM 3235 CG2 THR B 130 6.078 70.106 30.072 1.00 31.41 C
ANISOU 3235 CG2 THR B 130 3811 3127 4997 -780 511 -48 C
ATOM 3236 N GLN B 131 6.556 69.935 34.149 1.00 32.37 N
ANISOU 3236 N GLN B 131 3855 3463 4983 -693 60 -289 N
ATOM 3237 CA GLN B 131 5.557 69.850 35.212 1.00 31.95 C
ANISOU 3237 CA GLN B 131 3948 3464 4728 -652 13 -275 C
ATOM 3238 C GLN B 131 4.293 70.641 34.892 1.00 34.96 C
ANISOU 3238 C GLN B 131 4405 3792 5085 -668 158 -246 C
ATOM 3239 O GLN B 131 4.357 71.843 34.658 1.00 33.01 O
ANISOU 3239 O GLN B 131 4134 3465 4944 -716 217 -312 O
ATOM 3240 CB GLN B 131 6.175 70.334 36.549 1.00 33.00 C
ANISOU 3240 CB GLN B 131 4094 3633 4810 -660 -150 -422 C
ATOM 3241 CG GLN B 131 5.190 70.352 37.747 1.00 38.29 C
ANISOU 3241 CG GLN B 131 4961 4350 5236 -638 -158 -432 C
ATOM 3242 CD GLN B 131 4.798 68.956 38.189 1.00 50.12 C
ANISOU 3242 CD GLN B 131 6594 5908 6542 -571 -202 -310 C
ATOM 3243 OE1 GLN B 131 5.650 68.097 38.408 1.00 45.05 O
ANISOU 3243 OE1 GLN B 131 5939 5294 5884 -518 -370 -284 O
ATOM 3244 NE2 GLN B 131 3.504 68.702 38.348 1.00 33.18 N
ANISOU 3244 NE2 GLN B 131 4571 3764 4273 -573 -47 -242 N
ATOM 3245 N VAL B 132 3.146 69.983 34.946 1.00 32.53 N
ANISOU 3245 N VAL B 132 4180 3516 4664 -626 210 -160 N
ATOM 3246 CA VAL B 132 1.852 70.652 34.779 1.00 32.19 C
ANISOU 3246 CA VAL B 132 4174 3423 4633 -619 320 -158 C
ATOM 3247 C VAL B 132 1.176 70.571 36.150 1.00 35.33 C
ANISOU 3247 C VAL B 132 4668 3871 4886 -615 340 -224 C
ATOM 3248 O VAL B 132 1.084 69.483 36.719 1.00 34.38 O
ANISOU 3248 O VAL B 132 4623 3816 4626 -600 319 -175 O
ATOM 3249 CB VAL B 132 1.004 70.030 33.632 1.00 35.97 C
ANISOU 3249 CB VAL B 132 4641 3881 5146 -585 375 -43 C
ATOM 3250 CG1 VAL B 132 -0.438 70.544 33.640 1.00 35.97 C
ANISOU 3250 CG1 VAL B 132 4643 3836 5186 -554 446 -64 C
ATOM 3251 CG2 VAL B 132 1.662 70.275 32.280 1.00 35.11 C
ANISOU 3251 CG2 VAL B 132 4501 3706 5133 -600 382 12 C
ATOM 3252 N THR B 133 0.799 71.729 36.725 1.00 32.08 N
ANISOU 3252 N THR B 133 4277 3414 4496 -633 393 -342 N
ATOM 3253 CA THR B 133 0.157 71.767 38.044 1.00 31.35 C
ANISOU 3253 CA THR B 133 4302 3359 4252 -644 457 -432 C
ATOM 3254 C THR B 133 -1.196 72.413 37.904 1.00 36.05 C
ANISOU 3254 C THR B 133 4857 3883 4956 -628 617 -481 C
ATOM 3255 O THR B 133 -1.298 73.538 37.411 1.00 34.83 O
ANISOU 3255 O THR B 133 4634 3633 4969 -615 630 -533 O
ATOM 3256 CB THR B 133 1.015 72.522 39.063 1.00 36.31 C
ANISOU 3256 CB THR B 133 4999 3998 4797 -682 366 -578 C
ATOM 3257 OG1 THR B 133 2.337 72.005 39.037 1.00 37.02 O
ANISOU 3257 OG1 THR B 133 5064 4138 4865 -682 180 -552 O
ATOM 3258 CG2 THR B 133 0.445 72.457 40.485 1.00 31.62 C
ANISOU 3258 CG2 THR B 133 4593 3447 3973 -701 437 -672 C
ATOM 3259 N VAL B 134 -2.235 71.674 38.285 1.00 34.08 N
ANISOU 3259 N VAL B 134 4642 3664 4645 -625 743 -465 N
ATOM 3260 CA VAL B 134 -3.612 72.156 38.255 1.00 34.53 C
ANISOU 3260 CA VAL B 134 4618 3654 4847 -605 905 -543 C
ATOM 3261 C VAL B 134 -4.077 72.230 39.710 1.00 43.51 C
ANISOU 3261 C VAL B 134 5892 4815 5825 -657 1075 -676 C
ATOM 3262 O VAL B 134 -4.239 71.215 40.382 1.00 44.13 O
ANISOU 3262 O VAL B 134 6101 4953 5714 -700 1156 -635 O
ATOM 3263 CB VAL B 134 -4.567 71.315 37.369 1.00 36.40 C
ANISOU 3263 CB VAL B 134 4735 3882 5214 -573 943 -455 C
ATOM 3264 CG1 VAL B 134 -5.893 72.048 37.159 1.00 34.98 C
ANISOU 3264 CG1 VAL B 134 4405 3611 5274 -525 1050 -564 C
ATOM 3265 CG2 VAL B 134 -3.920 70.958 36.031 1.00 35.87 C
ANISOU 3265 CG2 VAL B 134 4614 3814 5202 -537 775 -313 C
ATOM 3266 N SER B 135 -4.215 73.435 40.206 1.00 44.19 N
ANISOU 3266 N SER B 135 5983 4840 5967 -660 1136 -834 N
ATOM 3267 CA SER B 135 -4.613 73.679 41.584 1.00 45.79 C
ANISOU 3267 CA SER B 135 6343 5053 6002 -716 1317 -993 C
ATOM 3268 C SER B 135 -5.436 74.952 41.603 1.00 53.48 C
ANISOU 3268 C SER B 135 7196 5909 7214 -685 1455 -1169 C
ATOM 3269 O SER B 135 -5.167 75.858 40.818 1.00 52.60 O
ANISOU 3269 O SER B 135 6964 5711 7311 -629 1335 -1169 O
ATOM 3270 CB SER B 135 -3.362 73.853 42.446 1.00 48.91 C
ANISOU 3270 CB SER B 135 6943 5509 6132 -758 1167 -1036 C
ATOM 3271 OG SER B 135 -3.675 74.131 43.798 1.00 63.09 O
ANISOU 3271 OG SER B 135 8949 7315 7707 -816 1325 -1198 O
ATOM 3272 N SER B 136 -6.444 75.018 42.470 1.00 54.94 N
ANISOU 3272 N SER B 136 7419 6071 7385 -720 1724 -1320 N
ATOM 3273 CA SER B 136 -7.235 76.239 42.624 1.00 57.37 C
ANISOU 3273 CA SER B 136 7607 6252 7939 -682 1876 -1523 C
ATOM 3274 C SER B 136 -6.452 77.195 43.526 1.00 65.53 C
ANISOU 3274 C SER B 136 8824 7271 8803 -728 1851 -1677 C
ATOM 3275 O SER B 136 -5.631 76.735 44.332 1.00 65.61 O
ANISOU 3275 O SER B 136 9077 7386 8467 -801 1786 -1662 O
ATOM 3276 CB SER B 136 -8.616 75.934 43.201 1.00 62.02 C
ANISOU 3276 CB SER B 136 8134 6812 8618 -713 2212 -1659 C
ATOM 3277 OG SER B 136 -8.545 75.182 44.401 1.00 72.31 O
ANISOU 3277 OG SER B 136 9714 8202 9558 -831 2402 -1687 O
ATOM 3278 N LEU B 137 -6.690 78.519 43.356 1.00 64.24 N
ANISOU 3278 N LEU B 137 8548 6965 8896 -675 1875 -1826 N
ATOM 3279 CA LEU B 137 -6.096 79.677 44.056 1.00 97.85 C
ANISOU 3279 CA LEU B 137 12924 11155 13098 -710 1863 -2017 C
ATOM 3280 C LEU B 137 -4.856 80.201 43.350 1.00137.98 C
ANISOU 3280 C LEU B 137 17986 16206 18236 -703 1579 -1924 C
ATOM 3281 O LEU B 137 -4.959 81.137 42.561 1.00104.61 O
ANISOU 3281 O LEU B 137 13619 11821 14307 -636 1534 -1928 O
ATOM 3282 CB LEU B 137 -5.828 79.449 45.558 1.00 97.84 C
ANISOU 3282 CB LEU B 137 13220 11252 12701 -821 1984 -2168 C
TER 3283 LEU B 137
HETATM 3284 C1 KAZ A 401 1.123 8.360 22.376 1.00 26.05 C
ANISOU 3284 C1 KAZ A 401 3380 3111 3406 274 600 -48 C
HETATM 3285 C2 KAZ A 401 1.537 7.330 21.518 1.00 25.23 C
ANISOU 3285 C2 KAZ A 401 3301 2970 3314 294 646 -69 C
HETATM 3286 C3 KAZ A 401 1.154 7.356 20.166 1.00 28.35 C
ANISOU 3286 C3 KAZ A 401 3730 3361 3681 257 688 -94 C
HETATM 3287 C11 KAZ A 401 -1.858 11.818 18.073 1.00 28.28 C
ANISOU 3287 C11 KAZ A 401 3750 3459 3537 82 603 -92 C
HETATM 3288 C12 KAZ A 401 -1.433 12.513 16.918 1.00 28.94 C
ANISOU 3288 C12 KAZ A 401 3869 3545 3582 75 634 -97 C
HETATM 3289 C13 KAZ A 401 -2.308 13.428 16.294 1.00 28.93 C
ANISOU 3289 C13 KAZ A 401 3903 3549 3539 47 593 -94 C
HETATM 3290 C14 KAZ A 401 -3.606 13.633 16.784 1.00 27.84 C
ANISOU 3290 C14 KAZ A 401 3747 3416 3415 27 521 -92 C
HETATM 3291 C15 KAZ A 401 -4.021 12.948 17.931 1.00 31.05 C
ANISOU 3291 C15 KAZ A 401 4108 3820 3868 28 508 -90 C
HETATM 3292 C16 KAZ A 401 -3.155 12.037 18.568 1.00 30.12 C
ANISOU 3292 C16 KAZ A 401 3975 3694 3774 56 549 -87 C
HETATM 3293 C17 KAZ A 401 -0.032 12.310 16.307 1.00 27.68 C
ANISOU 3293 C17 KAZ A 401 3714 3374 3430 99 718 -107 C
HETATM 3294 C18 KAZ A 401 0.043 11.000 15.543 1.00 31.80 C
ANISOU 3294 C18 KAZ A 401 4304 3855 3925 113 753 -135 C
HETATM 3295 C20 KAZ A 401 2.151 6.475 18.038 1.00 32.01 C
ANISOU 3295 C20 KAZ A 401 4245 3779 4140 275 802 -148 C
HETATM 3296 C21 KAZ A 401 2.560 5.390 17.232 1.00 33.16 C
ANISOU 3296 C21 KAZ A 401 4440 3874 4285 299 862 -178 C
HETATM 3297 C22 KAZ A 401 2.329 4.064 17.633 1.00 32.75 C
ANISOU 3297 C22 KAZ A 401 4426 3772 4246 324 854 -181 C
HETATM 3298 C23 KAZ A 401 1.730 3.827 18.881 1.00 31.31 C
ANISOU 3298 C23 KAZ A 401 4235 3586 4073 325 794 -149 C
HETATM 3299 C24 KAZ A 401 1.337 4.905 19.690 1.00 28.07 C
ANISOU 3299 C24 KAZ A 401 3781 3227 3658 302 741 -120 C
HETATM 3300 C25 KAZ A 401 2.790 2.914 16.714 1.00 33.16 C
ANISOU 3300 C25 KAZ A 401 4536 3763 4299 351 924 -219 C
HETATM 3301 C27 KAZ A 401 2.228 1.007 15.274 1.00 40.07 C
ANISOU 3301 C27 KAZ A 401 5573 4531 5122 343 986 -285 C
HETATM 3302 C28 KAZ A 401 1.141 0.031 14.742 1.00 40.51 C
ANISOU 3302 C28 KAZ A 401 5730 4528 5133 304 967 -320 C
HETATM 3303 C30 KAZ A 401 -0.539 1.845 15.079 1.00 37.90 C
ANISOU 3303 C30 KAZ A 401 5358 4290 4753 210 846 -289 C
HETATM 3304 C4 KAZ A 401 0.397 8.444 19.685 1.00 28.28 C
ANISOU 3304 C4 KAZ A 401 3724 3385 3637 205 674 -95 C
HETATM 3305 C5 KAZ A 401 0.043 9.512 20.541 1.00 26.12 C
ANISOU 3305 C5 KAZ A 401 3411 3150 3365 189 630 -73 C
HETATM 3306 C6 KAZ A 401 0.427 9.464 21.886 1.00 25.24 C
ANISOU 3306 C6 KAZ A 401 3270 3043 3279 222 597 -52 C
HETATM 3307 C7 KAZ A 401 1.559 6.232 19.283 1.00 27.35 C
ANISOU 3307 C7 KAZ A 401 3645 3188 3557 278 742 -121 C
HETATM 3308 C8 KAZ A 401 -0.820 10.645 20.025 1.00 27.80 C
ANISOU 3308 C8 KAZ A 401 3627 3389 3546 141 612 -73 C
HETATM 3309 N9 KAZ A 401 -1.024 10.832 18.689 1.00 28.03 N
ANISOU 3309 N9 KAZ A 401 3698 3412 3539 118 632 -92 N
HETATM 3310 O10 KAZ A 401 -1.339 11.335 20.886 1.00 27.71 O
ANISOU 3310 O10 KAZ A 401 3591 3398 3539 128 577 -56 O
HETATM 3311 O19 KAZ A 401 0.248 9.946 16.313 1.00 31.66 O
ANISOU 3311 O19 KAZ A 401 4255 3823 3951 139 750 -138 O
HETATM 3312 N26 KAZ A 401 1.686 2.066 16.181 1.00 36.22 N
ANISOU 3312 N26 KAZ A 401 5021 4105 4636 314 913 -243 N
HETATM 3313 N29 KAZ A 401 -0.033 0.757 14.186 1.00 40.96 N
ANISOU 3313 N29 KAZ A 401 5824 4615 5126 235 908 -333 N
HETATM 3314 C31 KAZ A 401 0.599 2.812 15.494 1.00 37.37 C
ANISOU 3314 C31 KAZ A 401 5208 4277 4713 248 875 -256 C
HETATM 3315 C32 KAZ A 401 -1.108 -0.173 13.752 1.00 36.75 C
ANISOU 3315 C32 KAZ A 401 5371 4023 4572 194 873 -374 C
HETATM 3316 O33 KAZ A 401 -0.074 10.908 14.323 1.00 31.39 O
ANISOU 3316 O33 KAZ A 401 4339 3778 3808 104 780 -153 O
HETATM 3317 C10 OLC A 402 -12.698 30.614 29.490 1.00 62.88 C
ANISOU 3317 C10 OLC A 402 7764 7759 8369 52 555 -116 C
HETATM 3318 C9 OLC A 402 -13.940 31.124 29.563 1.00 66.26 C
ANISOU 3318 C9 OLC A 402 8140 8147 8887 71 584 -132 C
HETATM 3319 C11 OLC A 402 -11.579 31.094 28.600 1.00 60.14 C
ANISOU 3319 C11 OLC A 402 7439 7433 7979 43 486 -95 C
HETATM 3320 C8 OLC A 402 -14.512 32.269 28.756 1.00 65.92 C
ANISOU 3320 C8 OLC A 402 8056 8074 8916 94 535 -130 C
HETATM 3321 C24 OLC A 402 -6.675 40.430 25.864 1.00 50.98 C
ANISOU 3321 C24 OLC A 402 6485 6002 6882 -60 419 -45 C
HETATM 3322 C12 OLC A 402 -10.437 30.039 28.568 1.00 58.16 C
ANISOU 3322 C12 OLC A 402 7218 7224 7656 25 472 -82 C
HETATM 3323 C7 OLC A 402 -14.965 33.401 29.708 1.00 65.89 C
ANISOU 3323 C7 OLC A 402 8060 8024 8949 114 595 -158 C
HETATM 3324 C6 OLC A 402 -14.691 34.791 29.074 1.00 66.73 C
ANISOU 3324 C6 OLC A 402 8180 8105 9067 130 537 -147 C
HETATM 3325 C5 OLC A 402 -13.429 35.457 29.689 1.00 66.58 C
ANISOU 3325 C5 OLC A 402 8242 8092 8962 110 546 -153 C
HETATM 3326 C4 OLC A 402 -13.112 36.825 29.025 1.00 65.47 C
ANISOU 3326 C4 OLC A 402 8120 7916 8838 119 499 -140 C
HETATM 3327 C3 OLC A 402 -12.789 36.668 27.517 1.00 65.25 C
ANISOU 3327 C3 OLC A 402 8088 7904 8801 115 422 -95 C
HETATM 3328 C2 OLC A 402 -12.168 37.961 26.929 1.00 65.93 C
ANISOU 3328 C2 OLC A 402 8220 7951 8879 113 393 -76 C
HETATM 3329 C21 OLC A 402 -8.981 39.530 26.525 1.00 62.91 C
ANISOU 3329 C21 OLC A 402 7952 7543 8409 21 398 -58 C
HETATM 3330 C1 OLC A 402 -10.678 38.022 27.108 1.00 68.80 C
ANISOU 3330 C1 OLC A 402 8629 8336 9175 68 402 -75 C
HETATM 3331 C22 OLC A 402 -7.862 39.536 25.455 1.00 58.51 C
ANISOU 3331 C22 OLC A 402 7422 6987 7822 -14 393 -23 C
HETATM 3332 O19 OLC A 402 -10.154 37.579 28.115 1.00 73.51 O
ANISOU 3332 O19 OLC A 402 9232 8960 9738 48 431 -105 O
HETATM 3333 O25 OLC A 402 -7.062 41.757 25.480 1.00 42.61 O
ANISOU 3333 O25 OLC A 402 5467 4866 5858 -48 425 -29 O
HETATM 3334 O23 OLC A 402 -7.401 38.216 25.165 1.00 60.91 O
ANISOU 3334 O23 OLC A 402 7705 7352 8084 -28 388 -14 O
HETATM 3335 O20 OLC A 402 -9.994 38.590 26.101 1.00 66.78 O
ANISOU 3335 O20 OLC A 402 8408 8061 8905 54 376 -42 O
HETATM 3336 C10 OLC A 403 -13.666 31.342 23.982 1.00 47.07 C
ANISOU 3336 C10 OLC A 403 5694 5736 6453 93 250 -36 C
HETATM 3337 C9 OLC A 403 -14.421 32.448 23.841 1.00 48.43 C
ANISOU 3337 C9 OLC A 403 5846 5865 6689 125 222 -38 C
HETATM 3338 C11 OLC A 403 -13.892 30.049 23.228 1.00 45.22 C
ANISOU 3338 C11 OLC A 403 5449 5522 6210 84 211 -36 C
HETATM 3339 C8 OLC A 403 -14.282 33.786 24.530 1.00 48.24 C
ANISOU 3339 C8 OLC A 403 5838 5809 6682 136 259 -42 C
HETATM 3340 C24 OLC A 403 -18.845 42.705 21.729 1.00 83.83 C
ANISOU 3340 C24 OLC A 403 10393 9819 11641 526 -103 37 C
HETATM 3341 C12 OLC A 403 -13.776 28.808 24.160 1.00 45.42 C
ANISOU 3341 C12 OLC A 403 5452 5574 6231 58 279 -54 C
HETATM 3342 C7 OLC A 403 -15.447 34.731 24.126 1.00 50.66 C
ANISOU 3342 C7 OLC A 403 6105 6060 7082 184 209 -45 C
HETATM 3343 C6 OLC A 403 -14.938 36.180 23.918 1.00 55.73 C
ANISOU 3343 C6 OLC A 403 6810 6662 7701 198 200 -24 C
HETATM 3344 C5 OLC A 403 -15.789 37.273 24.624 1.00 59.62 C
ANISOU 3344 C5 OLC A 403 7264 7100 8289 234 227 -48 C
HETATM 3345 C4 OLC A 403 -14.899 38.307 25.372 1.00 61.75 C
ANISOU 3345 C4 OLC A 403 7594 7351 8518 216 288 -53 C
HETATM 3346 C3 OLC A 403 -15.475 39.748 25.361 1.00 64.68 C
ANISOU 3346 C3 OLC A 403 7970 7647 8958 260 278 -54 C
HETATM 3347 C2 OLC A 403 -14.603 40.728 24.522 1.00 68.06 C
ANISOU 3347 C2 OLC A 403 8491 8041 9329 254 242 -11 C
HETATM 3348 C21 OLC A 403 -16.819 43.384 23.181 1.00 79.47 C
ANISOU 3348 C21 OLC A 403 9942 9290 10963 419 96 27 C
HETATM 3349 C1 OLC A 403 -15.246 42.093 24.390 1.00 72.72 C
ANISOU 3349 C1 OLC A 403 9092 8548 9989 304 222 -7 C
HETATM 3350 C22 OLC A 403 -17.484 43.446 21.774 1.00 83.27 C
ANISOU 3350 C22 OLC A 403 10447 9736 11456 479 -37 70 C
HETATM 3351 O19 OLC A 403 -15.273 42.861 25.338 1.00 75.31 O
ANISOU 3351 O19 OLC A 403 9419 8843 10353 305 283 -39 O
HETATM 3352 O25 OLC A 403 -18.590 41.298 21.586 1.00 84.60 O
ANISOU 3352 O25 OLC A 403 10464 9995 11685 480 -105 30 O
HETATM 3353 O23 OLC A 403 -17.660 44.810 21.342 1.00 85.60 O
ANISOU 3353 O23 OLC A 403 10809 9939 11774 530 -74 101 O
HETATM 3354 O20 OLC A 403 -15.774 42.381 23.185 1.00 75.45 O
ANISOU 3354 O20 OLC A 403 9460 8856 10351 351 129 33 O
HETATM 3355 C18 OLC A 404 -5.531 36.250 42.846 1.00 76.00 C
ANISOU 3355 C18 OLC A 404 10563 9183 9131 116 344 -577 C
HETATM 3356 C10 OLC A 404 -6.415 41.681 37.162 1.00 65.11 C
ANISOU 3356 C10 OLC A 404 8616 7715 8408 -27 433 -515 C
HETATM 3357 C9 OLC A 404 -6.175 42.658 36.276 1.00 67.88 C
ANISOU 3357 C9 OLC A 404 8914 8033 8845 -53 423 -504 C
HETATM 3358 C17 OLC A 404 -7.053 36.091 42.579 1.00 75.38 C
ANISOU 3358 C17 OLC A 404 10462 9087 9090 127 517 -540 C
HETATM 3359 C11 OLC A 404 -6.394 40.205 36.847 1.00 65.13 C
ANISOU 3359 C11 OLC A 404 8583 7788 8377 -17 427 -469 C
HETATM 3360 C8 OLC A 404 -6.195 44.151 36.527 1.00 70.85 C
ANISOU 3360 C8 OLC A 404 9327 8329 9264 -65 433 -548 C
HETATM 3361 C24 OLC A 404 2.810 46.076 30.069 1.00 75.07 C
ANISOU 3361 C24 OLC A 404 9337 8752 10434 -523 371 -475 C
HETATM 3362 C16 OLC A 404 -7.382 36.251 41.066 1.00 73.87 C
ANISOU 3362 C16 OLC A 404 10087 8929 9051 100 538 -495 C
HETATM 3363 C12 OLC A 404 -5.636 39.409 37.938 1.00 67.44 C
ANISOU 3363 C12 OLC A 404 8950 8106 8569 -12 369 -502 C
HETATM 3364 C7 OLC A 404 -4.893 44.619 37.232 1.00 73.66 C
ANISOU 3364 C7 OLC A 404 9721 8666 9602 -108 350 -615 C
HETATM 3365 C15 OLC A 404 -7.834 37.701 40.748 1.00 73.14 C
ANISOU 3365 C15 OLC A 404 9952 8794 9044 87 572 -523 C
HETATM 3366 C13 OLC A 404 -6.560 38.345 38.597 1.00 70.52 C
ANISOU 3366 C13 OLC A 404 9402 8510 8882 28 440 -485 C
HETATM 3367 C6 OLC A 404 -3.838 45.156 36.225 1.00 74.62 C
ANISOU 3367 C6 OLC A 404 9762 8774 9816 -165 307 -601 C
HETATM 3368 C14 OLC A 404 -6.689 38.553 40.135 1.00 72.46 C
ANISOU 3368 C14 OLC A 404 9798 8714 9019 51 456 -543 C
HETATM 3369 C5 OLC A 404 -3.275 46.545 36.652 1.00 75.94 C
ANISOU 3369 C5 OLC A 404 9964 8859 10030 -204 281 -668 C
HETATM 3370 C4 OLC A 404 -2.559 47.292 35.486 1.00 76.39 C
ANISOU 3370 C4 OLC A 404 9948 8878 10199 -259 286 -640 C
HETATM 3371 C3 OLC A 404 -1.359 46.490 34.897 1.00 75.64 C
ANISOU 3371 C3 OLC A 404 9764 8838 10138 -300 237 -622 C
HETATM 3372 C2 OLC A 404 -0.965 46.938 33.458 1.00 74.38 C
ANISOU 3372 C2 OLC A 404 9540 8650 10073 -341 287 -564 C
HETATM 3373 C21 OLC A 404 0.286 45.457 30.276 1.00 70.12 C
ANISOU 3373 C21 OLC A 404 8840 8186 9618 -393 378 -402 C
HETATM 3374 C1 OLC A 404 -0.332 45.871 32.594 1.00 71.77 C
ANISOU 3374 C1 OLC A 404 9131 8385 9755 -355 287 -515 C
HETATM 3375 C22 OLC A 404 1.331 46.522 29.834 1.00 72.46 C
ANISOU 3375 C22 OLC A 404 9105 8400 10025 -469 411 -422 C
HETATM 3376 O19 OLC A 404 0.418 45.059 33.110 1.00 72.95 O
ANISOU 3376 O19 OLC A 404 9244 8584 9889 -362 223 -548 O
HETATM 3377 O25 OLC A 404 2.936 45.283 31.269 1.00 74.75 O
ANISOU 3377 O25 OLC A 404 9285 8775 10343 -493 268 -532 O
HETATM 3378 O23 OLC A 404 1.147 46.943 28.463 1.00 68.47 O
ANISOU 3378 O23 OLC A 404 8624 7850 9542 -479 501 -346 O
HETATM 3379 O20 OLC A 404 -0.657 45.941 31.274 1.00 68.17 O
ANISOU 3379 O20 OLC A 404 8661 7918 9323 -354 356 -437 O
HETATM 3380 C10 OLC A 405 -20.417 10.493 28.930 1.00 59.98 C
ANISOU 3380 C10 OLC A 405 7114 6895 8780 -411 1241 -233 C
HETATM 3381 C9 OLC A 405 -19.133 10.858 28.799 1.00 57.86 C
ANISOU 3381 C9 OLC A 405 6948 6700 8337 -356 1160 -192 C
HETATM 3382 C11 OLC A 405 -21.395 10.261 27.798 1.00 63.56 C
ANISOU 3382 C11 OLC A 405 7418 7326 9407 -454 1147 -301 C
HETATM 3383 C8 OLC A 405 -18.388 11.131 27.506 1.00 57.73 C
ANISOU 3383 C8 OLC A 405 6927 6755 8253 -327 985 -201 C
HETATM 3384 C24 OLC A 405 -15.547 1.922 26.581 1.00 79.26 C
ANISOU 3384 C24 OLC A 405 10167 9143 10807 -393 1146 -154 C
HETATM 3385 C12 OLC A 405 -22.772 10.911 28.104 1.00 64.01 C
ANISOU 3385 C12 OLC A 405 7322 7340 9660 -482 1210 -347 C
HETATM 3386 C7 OLC A 405 -17.629 9.849 27.072 1.00 55.80 C
ANISOU 3386 C7 OLC A 405 6764 6497 7939 -331 962 -189 C
HETATM 3387 C6 OLC A 405 -16.157 10.129 26.675 1.00 54.45 C
ANISOU 3387 C6 OLC A 405 6683 6400 7606 -275 874 -155 C
HETATM 3388 C5 OLC A 405 -15.633 8.963 25.798 1.00 57.01 C
ANISOU 3388 C5 OLC A 405 7050 6711 7902 -281 823 -166 C
HETATM 3389 C4 OLC A 405 -14.213 9.225 25.235 1.00 59.18 C
ANISOU 3389 C4 OLC A 405 7394 7052 8041 -228 743 -142 C
HETATM 3390 C3 OLC A 405 -13.299 8.003 25.470 1.00 62.24 C
ANISOU 3390 C3 OLC A 405 7877 7411 8359 -210 781 -117 C
HETATM 3391 C2 OLC A 405 -13.427 6.947 24.341 1.00 65.86 C
ANISOU 3391 C2 OLC A 405 8336 7836 8851 -235 736 -156 C
HETATM 3392 C21 OLC A 405 -14.482 4.257 26.385 1.00 75.70 C
ANISOU 3392 C21 OLC A 405 9680 8873 10209 -304 1006 -126 C
HETATM 3393 C1 OLC A 405 -14.378 5.804 24.610 1.00 68.86 C
ANISOU 3393 C1 OLC A 405 8704 8127 9332 -289 807 -179 C
HETATM 3394 C22 OLC A 405 -15.805 3.462 26.508 1.00 78.04 C
ANISOU 3394 C22 OLC A 405 9925 9074 10654 -381 1087 -162 C
HETATM 3395 O19 OLC A 405 -14.798 5.124 23.688 1.00 67.99 O
ANISOU 3395 O19 OLC A 405 8572 7984 9279 -322 762 -226 O
HETATM 3396 O25 OLC A 405 -14.597 1.478 25.585 1.00 77.07 O
ANISOU 3396 O25 OLC A 405 9932 8895 10457 -358 1049 -166 O
HETATM 3397 O23 OLC A 405 -16.513 3.902 27.687 1.00 78.09 O
ANISOU 3397 O23 OLC A 405 9917 9049 10704 -399 1205 -139 O
HETATM 3398 O20 OLC A 405 -14.723 5.593 25.895 1.00 73.19 O
ANISOU 3398 O20 OLC A 405 9276 8629 9903 -299 925 -147 O
HETATM 3399 C10 OLC A 406 1.296 28.868 31.668 1.00 85.98 C
ANISOU 3399 C10 OLC A 406 10717 10867 11083 -9 104 -225 C
HETATM 3400 C9 OLC A 406 0.684 29.951 32.176 1.00 83.71 C
ANISOU 3400 C9 OLC A 406 10473 10556 10776 -23 110 -242 C
HETATM 3401 C11 OLC A 406 1.290 27.465 32.242 1.00 86.45 C
ANISOU 3401 C11 OLC A 406 10820 10944 11083 37 75 -212 C
HETATM 3402 C8 OLC A 406 0.711 31.337 31.574 1.00 81.62 C
ANISOU 3402 C8 OLC A 406 10172 10265 10574 -67 140 -251 C
HETATM 3403 C24 OLC A 406 7.262 40.515 32.751 1.00 86.60 C
ANISOU 3403 C24 OLC A 406 10416 10516 11973 -463 -80 -675 C
HETATM 3404 C12 OLC A 406 2.231 26.551 31.412 1.00 85.76 C
ANISOU 3404 C12 OLC A 406 10657 10874 11054 45 74 -202 C
HETATM 3405 C7 OLC A 406 1.741 32.237 32.305 1.00 82.40 C
ANISOU 3405 C7 OLC A 406 10248 10340 10721 -87 67 -310 C
HETATM 3406 C13 OLC A 406 1.756 25.073 31.462 1.00 86.12 C
ANISOU 3406 C13 OLC A 406 10751 10931 11039 83 92 -167 C
HETATM 3407 C6 OLC A 406 3.197 31.686 32.225 1.00 83.82 C
ANISOU 3407 C6 OLC A 406 10343 10532 10973 -88 6 -336 C
HETATM 3408 C14 OLC A 406 2.233 24.285 30.212 1.00 87.32 C
ANISOU 3408 C14 OLC A 406 10837 11095 11244 80 136 -148 C
HETATM 3409 C5 OLC A 406 3.771 31.751 30.780 1.00 83.42 C
ANISOU 3409 C5 OLC A 406 10200 10479 11015 -125 79 -312 C
HETATM 3410 C4 OLC A 406 4.709 32.974 30.578 1.00 82.54 C
ANISOU 3410 C4 OLC A 406 10016 10328 11018 -179 76 -353 C
HETATM 3411 C3 OLC A 406 4.074 34.322 31.020 1.00 81.11 C
ANISOU 3411 C3 OLC A 406 9892 10109 10819 -204 78 -371 C
HETATM 3412 C2 OLC A 406 5.142 35.446 30.985 1.00 81.92 C
ANISOU 3412 C2 OLC A 406 9918 10164 11045 -261 62 -423 C
HETATM 3413 C21 OLC A 406 6.738 38.034 32.271 1.00 83.32 C
ANISOU 3413 C21 OLC A 406 10015 10224 11420 -363 -61 -579 C
HETATM 3414 C1 OLC A 406 5.034 36.444 32.109 1.00 83.59 C
ANISOU 3414 C1 OLC A 406 10176 10340 11244 -270 -10 -479 C
HETATM 3415 C22 OLC A 406 7.106 39.416 31.674 1.00 86.03 C
ANISOU 3415 C22 OLC A 406 10315 10495 11877 -438 8 -595 C
HETATM 3416 O19 OLC A 406 4.621 36.126 33.216 1.00 86.15 O
ANISOU 3416 O19 OLC A 406 10575 10679 11478 -229 -83 -501 O
HETATM 3417 O25 OLC A 406 7.372 41.765 32.054 1.00 86.95 O
ANISOU 3417 O25 OLC A 406 10440 10488 12109 -530 11 -672 O
HETATM 3418 O23 OLC A 406 8.318 39.334 30.911 1.00 87.91 O
ANISOU 3418 O23 OLC A 406 10421 10714 12265 -485 49 -608 O
HETATM 3419 O20 OLC A 406 5.431 37.686 31.785 1.00 81.96 O
ANISOU 3419 O20 OLC A 406 9933 10079 11131 -328 21 -504 O
HETATM 3420 C24 OLC A 407 5.733 14.169 26.628 1.00 82.14 C
ANISOU 3420 C24 OLC A 407 10096 10372 10740 350 283 -82 C
HETATM 3421 C7 OLC A 407 10.046 24.789 27.523 1.00 81.33 C
ANISOU 3421 C7 OLC A 407 9404 10276 11221 26 149 -330 C
HETATM 3422 C6 OLC A 407 8.917 23.833 27.047 1.00 80.75 C
ANISOU 3422 C6 OLC A 407 9448 10225 11008 52 206 -271 C
HETATM 3423 C5 OLC A 407 8.816 22.582 27.955 1.00 81.48 C
ANISOU 3423 C5 OLC A 407 9585 10332 11043 125 110 -266 C
HETATM 3424 C4 OLC A 407 8.726 21.278 27.118 1.00 82.55 C
ANISOU 3424 C4 OLC A 407 9739 10468 11158 156 185 -236 C
HETATM 3425 C3 OLC A 407 7.525 20.407 27.565 1.00 83.67 C
ANISOU 3425 C3 OLC A 407 10012 10624 11157 188 164 -195 C
HETATM 3426 C2 OLC A 407 7.929 19.386 28.662 1.00 85.22 C
ANISOU 3426 C2 OLC A 407 10225 10813 11341 261 54 -201 C
HETATM 3427 C21 OLC A 407 6.866 16.472 26.683 1.00 84.32 C
ANISOU 3427 C21 OLC A 407 10224 10680 11133 299 248 -130 C
HETATM 3428 C1 OLC A 407 7.993 17.965 28.151 1.00 87.09 C
ANISOU 3428 C1 OLC A 407 10478 11040 11573 304 96 -181 C
HETATM 3429 C22 OLC A 407 6.771 15.071 27.349 1.00 84.42 C
ANISOU 3429 C22 OLC A 407 10299 10672 11103 364 201 -112 C
HETATM 3430 O19 OLC A 407 9.054 17.344 28.162 1.00 89.07 O
ANISOU 3430 O19 OLC A 407 10652 11275 11915 349 65 -203 O
HETATM 3431 O25 OLC A 407 5.866 12.822 27.111 1.00 79.21 O
ANISOU 3431 O25 OLC A 407 9772 9971 10354 411 253 -69 O
HETATM 3432 O23 OLC A 407 8.062 14.428 27.436 1.00 85.12 O
ANISOU 3432 O23 OLC A 407 10307 10742 11293 422 162 -136 O
HETATM 3433 O20 OLC A 407 6.811 17.465 27.730 1.00 85.53 O
ANISOU 3433 O20 OLC A 407 10378 10845 11273 289 164 -141 O
HETATM 3434 C18 OLC A 408 -15.217 27.803 29.415 1.00 49.71 C
ANISOU 3434 C18 OLC A 408 5968 6064 6855 37 649 -133 C
HETATM 3435 C10 OLC A 408 -19.707 32.080 21.733 1.00 70.51 C
ANISOU 3435 C10 OLC A 408 8327 8531 9933 256 -84 -120 C
HETATM 3436 C9 OLC A 408 -19.700 31.203 20.706 1.00 74.79 C
ANISOU 3436 C9 OLC A 408 8893 9088 10436 248 -178 -118 C
HETATM 3437 C17 OLC A 408 -15.243 28.412 27.984 1.00 50.93 C
ANISOU 3437 C17 OLC A 408 6083 6227 7040 48 539 -121 C
HETATM 3438 C11 OLC A 408 -18.838 32.004 22.965 1.00 64.95 C
ANISOU 3438 C11 OLC A 408 7657 7857 9163 216 62 -116 C
HETATM 3439 C8 OLC A 408 -20.573 31.246 19.465 1.00 76.12 C
ANISOU 3439 C8 OLC A 408 9042 9221 10658 292 -347 -128 C
HETATM 3440 C24 OLC A 408 -21.353 37.723 12.734 1.00 88.91 C
ANISOU 3440 C24 OLC A 408 11370 10474 11936 723 -1180 130 C
HETATM 3441 C16 OLC A 408 -16.559 28.122 27.208 1.00 50.56 C
ANISOU 3441 C16 OLC A 408 5940 6153 7116 55 501 -137 C
HETATM 3442 C12 OLC A 408 -19.041 30.622 23.648 1.00 61.63 C
ANISOU 3442 C12 OLC A 408 7184 7462 8772 174 140 -144 C
HETATM 3443 C7 OLC A 408 -19.717 31.394 18.182 1.00 76.44 C
ANISOU 3443 C7 OLC A 408 9239 9269 10536 303 -438 -82 C
HETATM 3444 C15 OLC A 408 -17.391 29.414 26.991 1.00 52.18 C
ANISOU 3444 C15 OLC A 408 6091 6320 7414 89 472 -150 C
HETATM 3445 C13 OLC A 408 -17.889 30.296 24.639 1.00 59.54 C
ANISOU 3445 C13 OLC A 408 6993 7235 8396 136 253 -130 C
HETATM 3446 C6 OLC A 408 -19.040 32.790 18.092 1.00 78.15 C
ANISOU 3446 C6 OLC A 408 9554 9464 10677 330 -418 -33 C
HETATM 3447 C14 OLC A 408 -18.318 29.295 25.751 1.00 56.19 C
ANISOU 3447 C14 OLC A 408 6521 6810 8018 106 365 -159 C
HETATM 3448 C5 OLC A 408 -20.061 33.927 17.821 1.00 80.97 C
ANISOU 3448 C5 OLC A 408 9872 9756 11137 401 -516 -35 C
HETATM 3449 C4 OLC A 408 -20.783 33.737 16.457 1.00 84.82 C
ANISOU 3449 C4 OLC A 408 10391 10210 11627 450 -708 -38 C
HETATM 3450 C3 OLC A 408 -19.805 33.858 15.255 1.00 87.49 C
ANISOU 3450 C3 OLC A 408 10926 10545 11769 453 -758 17 C
HETATM 3451 C2 OLC A 408 -20.466 33.367 13.937 1.00 88.88 C
ANISOU 3451 C2 OLC A 408 11154 10695 11922 494 -949 5 C
HETATM 3452 C21 OLC A 408 -20.776 35.444 11.641 1.00 89.80 C
ANISOU 3452 C21 OLC A 408 11576 10669 11876 649 -1232 101 C
HETATM 3453 C1 OLC A 408 -19.647 33.703 12.714 1.00 89.60 C
ANISOU 3453 C1 OLC A 408 11462 10764 11819 512 -998 63 C
HETATM 3454 C22 OLC A 408 -20.794 36.990 11.486 1.00 89.24 C
ANISOU 3454 C22 OLC A 408 11588 10527 11794 712 -1253 155 C
HETATM 3455 O19 OLC A 408 -19.078 32.827 12.074 1.00 89.50 O
ANISOU 3455 O19 OLC A 408 11543 10777 11688 482 -1000 66 O
HETATM 3456 O25 OLC A 408 -22.079 38.894 12.307 1.00 88.99 O
ANISOU 3456 O25 OLC A 408 11411 10400 12000 816 -1305 153 O
HETATM 3457 O23 OLC A 408 -19.497 37.486 11.123 1.00 89.52 O
ANISOU 3457 O23 OLC A 408 11809 10553 11650 683 -1142 223 O
HETATM 3458 O20 OLC A 408 -19.620 35.013 12.397 1.00 89.49 O
ANISOU 3458 O20 OLC A 408 11536 10693 11775 565 -1031 110 O
HETATM 3459 C24 OLC A 409 11.236 37.340 29.697 1.00 83.75 C
ANISOU 3459 C24 OLC A 409 9552 10220 12049 -503 81 -644 C
HETATM 3460 C3 OLC A 409 8.442 31.314 32.909 1.00 86.89 C
ANISOU 3460 C3 OLC A 409 10354 10894 11766 -105 -291 -521 C
HETATM 3461 C2 OLC A 409 9.510 32.219 32.229 1.00 87.05 C
ANISOU 3461 C2 OLC A 409 10231 10877 11968 -173 -257 -563 C
HETATM 3462 C21 OLC A 409 10.052 35.226 30.567 1.00 85.12 C
ANISOU 3462 C21 OLC A 409 9866 10514 11962 -358 -40 -588 C
HETATM 3463 C1 OLC A 409 8.906 33.424 31.549 1.00 87.30 C
ANISOU 3463 C1 OLC A 409 10291 10877 12002 -236 -143 -541 C
HETATM 3464 C22 OLC A 409 10.874 36.486 30.947 1.00 84.59 C
ANISOU 3464 C22 OLC A 409 9720 10384 12037 -424 -83 -665 C
HETATM 3465 O19 OLC A 409 7.897 33.323 30.863 1.00 88.81 O
ANISOU 3465 O19 OLC A 409 10557 11082 12105 -233 -40 -476 O
HETATM 3466 O25 OLC A 409 11.726 38.640 30.081 1.00 82.40 O
ANISOU 3466 O25 OLC A 409 9337 9981 11990 -569 54 -709 O
HETATM 3467 O23 OLC A 409 10.149 37.262 31.915 1.00 85.60 O
ANISOU 3467 O23 OLC A 409 9957 10498 12071 -420 -159 -689 O
HETATM 3468 O20 OLC A 409 9.551 34.586 31.761 1.00 85.92 O
ANISOU 3468 O20 OLC A 409 10054 10654 11936 -291 -170 -599 O
HETATM 3469 C24 OLC A 410 -19.583 12.051 11.860 1.00 78.34 C
ANISOU 3469 C24 OLC A 410 9781 9430 10554 -199 -772 -613 C
HETATM 3470 C5 OLC A 410 -14.830 20.397 10.919 1.00 63.77 C
ANISOU 3470 C5 OLC A 410 8450 7784 7997 77 -580 -186 C
HETATM 3471 C4 OLC A 410 -16.203 19.729 10.634 1.00 64.96 C
ANISOU 3471 C4 OLC A 410 8529 7901 8250 73 -730 -252 C
HETATM 3472 C3 OLC A 410 -16.282 18.285 11.209 1.00 66.68 C
ANISOU 3472 C3 OLC A 410 8666 8125 8544 24 -669 -297 C
HETATM 3473 C2 OLC A 410 -17.116 17.341 10.288 1.00 70.06 C
ANISOU 3473 C2 OLC A 410 9121 8509 8990 16 -817 -367 C
HETATM 3474 C21 OLC A 410 -19.321 14.382 10.777 1.00 76.17 C
ANISOU 3474 C21 OLC A 410 9634 9198 10110 -96 -924 -548 C
HETATM 3475 C1 OLC A 410 -17.900 16.282 11.030 1.00 73.72 C
ANISOU 3475 C1 OLC A 410 9434 8958 9619 -32 -804 -422 C
HETATM 3476 C22 OLC A 410 -18.914 12.881 10.734 1.00 77.94 C
ANISOU 3476 C22 OLC A 410 9899 9402 10312 -141 -857 -582 C
HETATM 3477 O19 OLC A 410 -18.194 16.436 12.206 1.00 76.64 O
ANISOU 3477 O19 OLC A 410 9664 9343 10114 -52 -716 -411 O
HETATM 3478 O25 OLC A 410 -21.007 12.015 11.642 1.00 78.58 O
ANISOU 3478 O25 OLC A 410 9685 9413 10758 -217 -915 -684 O
HETATM 3479 O23 OLC A 410 -19.230 12.301 9.458 1.00 79.15 O
ANISOU 3479 O23 OLC A 410 10156 9512 10405 -138 -1013 -645 O
HETATM 3480 O20 OLC A 410 -18.221 15.190 10.299 1.00 74.86 O
ANISOU 3480 O20 OLC A 410 9622 9066 9756 -52 -886 -483 O
HETATM 3481 C24 OLC A 411 -24.208 12.032 19.288 1.00 82.11 C
ANISOU 3481 C24 OLC A 411 9320 9759 12119 -409 -70 -640 C
HETATM 3482 C4 OLC A 411 -22.921 19.585 18.087 1.00 88.12 C
ANISOU 3482 C4 OLC A 411 10244 10735 12502 -72 -413 -446 C
HETATM 3483 C3 OLC A 411 -22.643 18.128 17.633 1.00 87.57 C
ANISOU 3483 C3 OLC A 411 10224 10657 12389 -118 -423 -472 C
HETATM 3484 C2 OLC A 411 -23.659 17.138 18.274 1.00 86.49 C
ANISOU 3484 C2 OLC A 411 9942 10468 12453 -177 -356 -530 C
HETATM 3485 C21 OLC A 411 -22.986 14.306 19.592 1.00 82.77 C
ANISOU 3485 C21 OLC A 411 9520 9958 11973 -299 -67 -531 C
HETATM 3486 C1 OLC A 411 -23.244 16.649 19.643 1.00 85.15 C
ANISOU 3486 C1 OLC A 411 9774 10302 12278 -214 -138 -498 C
HETATM 3487 C22 OLC A 411 -23.819 13.390 18.646 1.00 83.81 C
ANISOU 3487 C22 OLC A 411 9588 10036 12221 -336 -196 -610 C
HETATM 3488 O19 OLC A 411 -22.510 17.311 20.372 1.00 84.58 O
ANISOU 3488 O19 OLC A 411 9762 10267 12107 -192 -39 -442 O
HETATM 3489 O25 OLC A 411 -24.300 11.033 18.258 1.00 81.15 O
ANISOU 3489 O25 OLC A 411 9229 9606 11998 -437 -189 -695 O
HETATM 3490 O23 OLC A 411 -24.985 14.053 18.126 1.00 86.04 O
ANISOU 3490 O23 OLC A 411 9738 10290 12663 -320 -337 -665 O
HETATM 3491 O20 OLC A 411 -23.765 15.454 19.984 1.00 83.25 O
ANISOU 3491 O20 OLC A 411 9469 10013 12149 -273 -71 -537 O
HETATM 3492 C18 OLC A 412 1.547 21.591 2.734 1.00 79.51 C
ANISOU 3492 C18 OLC A 412 11893 9465 8851 16 1409 107 C
HETATM 3493 C10 OLC A 412 -4.057 15.476 3.704 1.00 74.85 C
ANISOU 3493 C10 OLC A 412 11152 9016 8271 87 497 -170 C
HETATM 3494 C9 OLC A 412 -5.352 15.123 3.660 1.00 74.27 C
ANISOU 3494 C9 OLC A 412 11078 8942 8201 89 310 -204 C
HETATM 3495 C17 OLC A 412 0.704 20.295 2.602 1.00 79.59 C
ANISOU 3495 C17 OLC A 412 11934 9501 8807 44 1266 57 C
HETATM 3496 C11 OLC A 412 -3.031 15.313 2.605 1.00 74.78 C
ANISOU 3496 C11 OLC A 412 11328 8953 8133 100 655 -171 C
HETATM 3497 C8 OLC A 412 -6.078 14.479 2.503 1.00 74.49 C
ANISOU 3497 C8 OLC A 412 11288 8916 8098 105 190 -256 C
HETATM 3498 C24 OLC A 412 -14.540 8.978 3.055 1.00 95.25 C
ANISOU 3498 C24 OLC A 412 13440 11408 11341 -44 -978 -744 C
HETATM 3499 C16 OLC A 412 1.478 19.169 1.861 1.00 78.82 C
ANISOU 3499 C16 OLC A 412 11929 9365 8652 53 1408 16 C
HETATM 3500 C12 OLC A 412 -1.616 15.626 3.159 1.00 74.93 C
ANISOU 3500 C12 OLC A 412 11239 8989 8243 87 862 -140 C
HETATM 3501 C7 OLC A 412 -7.569 14.908 2.529 1.00 76.39 C
ANISOU 3501 C7 OLC A 412 11501 9159 8365 111 -38 -269 C
HETATM 3502 C15 OLC A 412 1.343 17.804 2.595 1.00 77.87 C
ANISOU 3502 C15 OLC A 412 11660 9297 8630 60 1342 -40 C
HETATM 3503 C13 OLC A 412 -1.100 17.006 2.668 1.00 76.07 C
ANISOU 3503 C13 OLC A 412 11475 9105 8325 85 956 -83 C
HETATM 3504 C6 OLC A 412 -8.400 14.022 3.500 1.00 78.40 C
ANISOU 3504 C6 OLC A 412 11561 9445 8783 84 -130 -314 C
HETATM 3505 C14 OLC A 412 0.268 16.892 1.938 1.00 77.45 C
ANISOU 3505 C14 OLC A 412 11749 9228 8450 85 1190 -81 C
HETATM 3506 C5 OLC A 412 -9.916 14.064 3.171 1.00 79.63 C
ANISOU 3506 C5 OLC A 412 11720 9579 8955 90 -364 -356 C
HETATM 3507 C4 OLC A 412 -10.688 15.047 4.099 1.00 81.60 C
ANISOU 3507 C4 OLC A 412 11796 9868 9341 88 -442 -323 C
HETATM 3508 C3 OLC A 412 -12.130 15.374 3.606 1.00 85.46 C
ANISOU 3508 C3 OLC A 412 12300 10326 9843 107 -677 -358 C
HETATM 3509 C2 OLC A 412 -12.695 14.367 2.555 1.00 89.76 C
ANISOU 3509 C2 OLC A 412 12979 10816 10309 110 -814 -436 C
HETATM 3510 C21 OLC A 412 -13.747 11.380 2.608 1.00 96.47 C
ANISOU 3510 C21 OLC A 412 13731 11613 11311 35 -934 -612 C
HETATM 3511 C1 OLC A 412 -13.992 13.695 2.949 1.00 93.25 C
ANISOU 3511 C1 OLC A 412 13269 11250 10911 85 -976 -507 C
HETATM 3512 C22 OLC A 412 -14.877 10.486 3.178 1.00 96.29 C
ANISOU 3512 C22 OLC A 412 13533 11575 11478 -10 -1042 -685 C
HETATM 3513 O19 OLC A 412 -14.683 14.090 3.876 1.00 94.38 O
ANISOU 3513 O19 OLC A 412 13220 11422 11220 72 -1013 -498 O
HETATM 3514 O25 OLC A 412 -15.775 8.245 3.033 1.00 94.67 O
ANISOU 3514 O25 OLC A 412 13278 11293 11399 -80 -1142 -830 O
HETATM 3515 O23 OLC A 412 -15.143 10.832 4.548 1.00 97.01 O
ANISOU 3515 O23 OLC A 412 13395 11714 11751 -34 -974 -647 O
HETATM 3516 O20 OLC A 412 -14.324 12.636 2.195 1.00 95.58 O
ANISOU 3516 O20 OLC A 412 13660 11498 11159 75 -1068 -583 O
HETATM 3517 C10 OLC A 413 -1.971 8.461 -0.472 1.00 61.66 C
ANISOU 3517 C10 OLC A 413 10191 7059 6177 148 859 -501 C
HETATM 3518 C9 OLC A 413 -2.985 7.608 -0.702 1.00 63.62 C
ANISOU 3518 C9 OLC A 413 10488 7284 6400 140 694 -563 C
HETATM 3519 C8 OLC A 413 -4.444 7.980 -0.866 1.00 66.01 C
ANISOU 3519 C8 OLC A 413 10819 7593 6670 128 445 -578 C
HETATM 3520 C24 OLC A 413 -12.237 0.080 -0.713 1.00 91.72 C
ANISOU 3520 C24 OLC A 413 13817 10538 10494 -139 -727 -1220 C
HETATM 3521 C7 OLC A 413 -5.351 6.731 -0.695 1.00 67.57 C
ANISOU 3521 C7 OLC A 413 10974 7770 6930 107 302 -655 C
HETATM 3522 C6 OLC A 413 -6.593 7.011 0.198 1.00 69.87 C
ANISOU 3522 C6 OLC A 413 11076 8108 7364 78 112 -650 C
HETATM 3523 C5 OLC A 413 -7.735 6.006 -0.113 1.00 73.01 C
ANISOU 3523 C5 OLC A 413 11504 8461 7777 56 -71 -738 C
HETATM 3524 C4 OLC A 413 -9.165 6.562 0.153 1.00 77.20 C
ANISOU 3524 C4 OLC A 413 11938 9011 8385 37 -299 -747 C
HETATM 3525 C3 OLC A 413 -10.236 5.490 -0.196 1.00 81.51 C
ANISOU 3525 C3 OLC A 413 12503 9502 8964 9 -473 -846 C
HETATM 3526 C2 OLC A 413 -11.696 5.999 -0.029 1.00 85.71 C
ANISOU 3526 C2 OLC A 413 12932 10043 9592 -8 -708 -868 C
HETATM 3527 C21 OLC A 413 -12.754 2.543 -0.211 1.00 90.87 C
ANISOU 3527 C21 OLC A 413 13569 10552 10408 -104 -828 -1093 C
HETATM 3528 C1 OLC A 413 -12.707 4.885 0.167 1.00 90.34 C
ANISOU 3528 C1 OLC A 413 13427 10587 10311 -55 -839 -957 C
HETATM 3529 C22 OLC A 413 -12.279 1.524 -1.280 1.00 91.51 C
ANISOU 3529 C22 OLC A 413 13879 10555 10336 -94 -802 -1168 C
HETATM 3530 O19 OLC A 413 -13.527 4.930 1.084 1.00 91.74 O
ANISOU 3530 O19 OLC A 413 13392 10788 10676 -90 -903 -957 O
HETATM 3531 O25 OLC A 413 -11.885 -0.839 -1.767 1.00 92.00 O
ANISOU 3531 O25 OLC A 413 14075 10494 10386 -128 -719 -1300 O
HETATM 3532 O23 OLC A 413 -13.127 1.583 -2.442 1.00 92.48 O
ANISOU 3532 O23 OLC A 413 14170 10623 10347 -87 -1029 -1248 O
HETATM 3533 O20 OLC A 413 -12.636 3.883 -0.742 1.00 90.86 O
ANISOU 3533 O20 OLC A 413 13665 10584 10275 -58 -871 -1038 O
HETATM 3534 C18 OLC A 414 -3.490 16.063 33.806 1.00 71.75 C
ANISOU 3534 C18 OLC A 414 9474 8952 8835 232 412 51 C
HETATM 3535 C10 OLC A 414 4.534 15.860 30.683 1.00 80.21 C
ANISOU 3535 C10 OLC A 414 10031 10138 10307 373 43 -67 C
HETATM 3536 C9 OLC A 414 5.159 15.785 31.871 1.00 80.29 C
ANISOU 3536 C9 OLC A 414 10072 10134 10301 427 -67 -77 C
HETATM 3537 C17 OLC A 414 -2.089 15.884 33.164 1.00 72.50 C
ANISOU 3537 C17 OLC A 414 9499 9078 8970 260 326 40 C
HETATM 3538 C11 OLC A 414 3.368 16.762 30.331 1.00 79.02 C
ANISOU 3538 C11 OLC A 414 9904 10005 10116 308 112 -58 C
HETATM 3539 C8 OLC A 414 6.318 14.880 32.214 1.00 79.36 C
ANISOU 3539 C8 OLC A 414 9926 9992 10233 503 -153 -87 C
HETATM 3540 C24 OLC A 414 6.348 3.563 31.928 1.00 60.81 C
ANISOU 3540 C24 OLC A 414 8095 7225 7785 912 9 137 C
HETATM 3541 C16 OLC A 414 -1.911 14.450 32.594 1.00 73.85 C
ANISOU 3541 C16 OLC A 414 9673 9227 9160 277 346 60 C
HETATM 3542 C12 OLC A 414 2.220 16.633 31.368 1.00 79.14 C
ANISOU 3542 C12 OLC A 414 10039 10002 10028 311 116 -34 C
HETATM 3543 C7 OLC A 414 5.819 13.415 32.317 1.00 77.78 C
ANISOU 3543 C7 OLC A 414 9828 9757 9969 544 -118 -44 C
HETATM 3544 C15 OLC A 414 -0.415 14.069 32.423 1.00 75.54 C
ANISOU 3544 C15 OLC A 414 9847 9452 9401 327 261 51 C
HETATM 3545 C13 OLC A 414 1.777 15.159 31.612 1.00 79.38 C
ANISOU 3545 C13 OLC A 414 10155 9998 10009 345 144 -2 C
HETATM 3546 C6 OLC A 414 6.797 12.428 31.627 1.00 76.44 C
ANISOU 3546 C6 OLC A 414 9579 9570 9895 590 -118 -53 C
HETATM 3547 C14 OLC A 414 0.260 14.963 31.352 1.00 77.65 C
ANISOU 3547 C14 OLC A 414 9988 9767 9749 300 240 21 C
HETATM 3548 C5 OLC A 414 7.461 11.480 32.665 1.00 75.48 C
ANISOU 3548 C5 OLC A 414 9520 9405 9756 687 -234 -42 C
HETATM 3549 C4 OLC A 414 8.788 10.887 32.116 1.00 74.48 C
ANISOU 3549 C4 OLC A 414 9266 9264 9768 743 -269 -70 C
HETATM 3550 C3 OLC A 414 8.972 9.417 32.575 1.00 74.56 C
ANISOU 3550 C3 OLC A 414 9363 9217 9748 831 -309 -38 C
HETATM 3551 C2 OLC A 414 9.879 8.642 31.586 1.00 75.17 C
ANISOU 3551 C2 OLC A 414 9323 9277 9960 866 -269 -60 C
HETATM 3552 C21 OLC A 414 8.087 5.471 32.144 1.00 66.14 C
ANISOU 3552 C21 OLC A 414 8546 7995 8590 939 -162 65 C
HETATM 3553 C1 OLC A 414 9.705 7.141 31.635 1.00 75.22 C
ANISOU 3553 C1 OLC A 414 9426 9224 9929 927 -247 -22 C
HETATM 3554 C22 OLC A 414 7.233 4.590 31.171 1.00 58.83 C
ANISOU 3554 C22 OLC A 414 7662 7043 7646 893 -14 82 C
HETATM 3555 O19 OLC A 414 10.678 6.395 31.721 1.00 76.59 O
ANISOU 3555 O19 OLC A 414 9552 9361 10188 1011 -311 -33 O
HETATM 3556 O25 OLC A 414 7.177 2.889 32.885 1.00 62.90 O
ANISOU 3556 O25 OLC A 414 8421 7435 8044 1022 -109 158 O
HETATM 3557 O23 OLC A 414 6.423 5.335 30.247 1.00 45.75 O
ANISOU 3557 O23 OLC A 414 5962 5438 5984 790 91 65 O
HETATM 3558 O20 OLC A 414 8.423 6.734 31.531 1.00 71.07 O
ANISOU 3558 O20 OLC A 414 9028 8687 9289 880 -150 19 O
HETATM 3559 C1 GOL A 415 -1.296 5.324 17.705 1.00 57.51 C
ANISOU 3559 C1 GOL A 415 7622 6950 7278 168 714 -170 C
HETATM 3560 O1 GOL A 415 -2.415 4.562 18.179 1.00 57.75 O
ANISOU 3560 O1 GOL A 415 7677 6943 7323 139 687 -172 O
HETATM 3561 C2 GOL A 415 -1.785 6.535 16.881 1.00 56.22 C
ANISOU 3561 C2 GOL A 415 7465 6825 7071 129 688 -178 C
HETATM 3562 O2 GOL A 415 -1.887 6.095 15.522 1.00 59.52 O
ANISOU 3562 O2 GOL A 415 7966 7212 7439 118 706 -217 O
HETATM 3563 C3 GOL A 415 -3.134 7.112 17.380 1.00 51.35 C
ANISOU 3563 C3 GOL A 415 6826 6225 6461 85 623 -167 C
HETATM 3564 O3 GOL A 415 -3.234 8.540 17.249 1.00 45.97 O
ANISOU 3564 O3 GOL A 415 6113 5591 5761 71 598 -152 O
HETATM 3565 S SO4 A 416 -12.888 46.132 31.641 0.50 30.38 S
ANISOU 3565 S SO4 A 416 3938 3025 4579 185 625 -300 S
HETATM 3566 O1 SO4 A 416 -12.031 45.231 30.862 0.50 30.56 O
ANISOU 3566 O1 SO4 A 416 3947 3117 4547 144 571 -257 O
HETATM 3567 O2 SO4 A 416 -13.807 46.841 30.732 0.50 30.67 O
ANISOU 3567 O2 SO4 A 416 3944 3003 4707 239 604 -265 O
HETATM 3568 O3 SO4 A 416 -13.640 45.367 32.635 0.50 29.93 O
ANISOU 3568 O3 SO4 A 416 3862 2993 4515 206 689 -338 O
HETATM 3569 O4 SO4 A 416 -12.063 47.130 32.343 0.50 28.41 O
ANISOU 3569 O4 SO4 A 416 3762 2727 4306 152 639 -345 O
HETATM 3570 O HOH A 501 5.099 43.330 21.406 1.00 34.07 O
ANISOU 3570 O HOH A 501 4155 3531 5259 -612 1006 -66 O
HETATM 3571 O HOH A 502 5.113 41.572 15.446 1.00 37.99 O
ANISOU 3571 O HOH A 502 5106 3928 5402 -566 1455 219 O
HETATM 3572 O HOH A 503 -7.260 53.629 24.730 1.00 34.65 O
ANISOU 3572 O HOH A 503 4936 2997 5234 -53 615 14 O
HETATM 3573 O HOH A 504 -11.661 25.041 23.614 1.00 28.17 O
ANISOU 3573 O HOH A 504 3352 3474 3878 0 313 -39 O
HETATM 3574 O HOH A 505 -6.950 11.831 16.919 1.00 35.15 O
ANISOU 3574 O HOH A 505 4676 4275 4403 -30 386 -150 O
HETATM 3575 O HOH A 506 -12.316 3.315 9.833 1.00 55.57 O
ANISOU 3575 O HOH A 506 7740 6387 6988 -228 -113 -671 O
HETATM 3576 O HOH A 507 8.967 27.227 13.148 1.00 52.66 O
ANISOU 3576 O HOH A 507 6568 6281 7160 -281 1656 4 O
HETATM 3577 O HOH A 508 -9.873 49.612 33.807 1.00 50.07 O
ANISOU 3577 O HOH A 508 6671 5334 7018 51 633 -466 O
HETATM 3578 O HOH A 509 -4.160 2.213 34.109 1.00 50.15 O
ANISOU 3578 O HOH A 509 7415 5597 6040 407 809 316 O
HETATM 3579 O HOH A 510 -3.735 12.610 21.998 1.00 29.70 O
ANISOU 3579 O HOH A 510 3829 3667 3789 68 516 -39 O
HETATM 3580 O HOH A 511 -5.259 40.848 28.744 1.00 30.49 O
ANISOU 3580 O HOH A 511 3873 3416 4294 -113 418 -174 O
HETATM 3581 O HOH A 512 -17.066 46.735 15.696 1.00 48.85 O
ANISOU 3581 O HOH A 512 6753 5036 6771 689 -446 386 O
HETATM 3582 O HOH A 513 -4.914 46.038 16.808 1.00 38.93 O
ANISOU 3582 O HOH A 513 5681 3920 5189 -87 643 384 O
HETATM 3583 O HOH A 514 10.247 12.250 22.103 1.00 49.99 O
ANISOU 3583 O HOH A 514 5693 6205 7094 419 650 -197 O
HETATM 3584 O HOH A 515 -1.092 50.816 25.219 1.00 30.63 O
ANISOU 3584 O HOH A 515 4148 2718 4772 -436 729 -122 O
HETATM 3585 O HOH A 516 6.340 39.757 18.872 1.00 32.72 O
ANISOU 3585 O HOH A 516 3965 3479 4989 -572 1199 8 O
HETATM 3586 O HOH A 517 3.636 -7.459 24.995 1.00 48.00 O
ANISOU 3586 O HOH A 517 6900 4970 6367 846 791 59 O
HETATM 3587 O HOH A 518 -12.740 53.655 20.641 1.00 51.93 O
ANISOU 3587 O HOH A 518 7289 5060 7383 405 271 293 O
HETATM 3588 O HOH A 519 3.541 -0.551 33.257 1.00 41.56 O
ANISOU 3588 O HOH A 519 6202 4487 5102 931 243 305 O
HETATM 3589 O HOH A 520 -6.952 10.553 19.330 1.00 44.99 O
ANISOU 3589 O HOH A 520 5851 5503 5741 -24 460 -125 O
HETATM 3590 O HOH A 521 -1.280 44.172 28.079 1.00 29.57 O
ANISOU 3590 O HOH A 521 3737 3114 4385 -313 463 -238 O
HETATM 3591 O HOH A 522 1.855 1.029 27.431 1.00 33.41 O
ANISOU 3591 O HOH A 522 4721 3665 4307 587 545 104 O
HETATM 3592 O HOH A 523 13.748 7.124 22.158 1.00 52.27 O
ANISOU 3592 O HOH A 523 5792 6304 7763 760 667 -277 O
HETATM 3593 O HOH A 524 -2.151 5.093 13.018 1.00 33.78 O
ANISOU 3593 O HOH A 524 4899 3876 4061 102 729 -302 O
HETATM 3594 O HOH A 525 -5.881 2.443 18.813 1.00 50.95 O
ANISOU 3594 O HOH A 525 6869 5940 6550 14 647 -215 O
HETATM 3595 O HOH A 526 10.226 3.821 28.140 1.00 29.95 O
ANISOU 3595 O HOH A 526 3609 3382 4388 966 97 -42 O
HETATM 3596 O HOH A 527 -3.768 1.604 25.385 1.00 47.11 O
ANISOU 3596 O HOH A 527 6463 5393 6045 218 748 29 O
HETATM 3597 O HOH A 528 -9.593 24.858 21.843 1.00 25.03 O
ANISOU 3597 O HOH A 528 3055 3106 3349 -6 281 -5 O
HETATM 3598 O HOH A 529 -0.903 21.920 16.253 1.00 67.30 O
ANISOU 3598 O HOH A 529 8682 8454 8435 -32 649 27 O
HETATM 3599 O HOH A 530 -2.245 42.205 13.977 1.00 60.53 O
ANISOU 3599 O HOH A 530 8514 6794 7690 -179 863 430 O
HETATM 3600 O HOH A 531 -4.767 5.603 12.576 1.00 30.89 O
ANISOU 3600 O HOH A 531 4561 3506 3670 18 541 -335 O
HETATM 3601 O HOH A 532 -5.888 44.914 23.688 1.00 28.54 O
ANISOU 3601 O HOH A 532 3836 2873 4136 -101 497 44 O
HETATM 3602 O HOH A 533 -5.516 5.236 15.200 1.00 37.51 O
ANISOU 3602 O HOH A 533 5225 4357 4671 1 536 -281 O
HETATM 3603 O HOH A 534 -5.678 -0.366 32.949 1.00 53.23 O
ANISOU 3603 O HOH A 534 7841 5818 6566 306 1010 311 O
HETATM 3604 O HOH A 535 23.052 42.511 13.356 1.00 80.81 O
ANISOU 3604 O HOH A 535 8499 8509 13694 -1570 3532 -466 O
HETATM 3605 O HOH A 536 4.267 48.591 13.369 1.00 42.90 O
ANISOU 3605 O HOH A 536 6350 3934 6016 -670 1773 458 O
HETATM 3606 O HOH A 537 -3.313 2.247 11.468 1.00 45.17 O
ANISOU 3606 O HOH A 537 6546 5164 5454 72 698 -427 O
HETATM 3607 O HOH A 538 -0.230 -6.533 3.787 1.00 68.93 O
ANISOU 3607 O HOH A 538 10639 7511 8040 235 1210 -961 O
HETATM 3608 O HOH A 539 -21.517 0.849 9.989 1.00 77.91 O
ANISOU 3608 O HOH A 539 9817 8833 10952 -628 -812 -1158 O
HETATM 3609 O HOH A 540 -7.403 -0.040 10.762 1.00 57.28 O
ANISOU 3609 O HOH A 540 8153 6531 7079 -91 421 -592 O
HETATM 3610 O HOH A 541 10.601 3.728 31.106 1.00 69.71 O
ANISOU 3610 O HOH A 541 8793 8374 9321 1107 -213 14 O
HETATM 3611 O HOH A 542 -5.669 17.922 8.768 1.00 29.61 O
ANISOU 3611 O HOH A 542 4688 3487 3075 35 308 -75 O
HETATM 3612 O HOH A 543 7.854 2.792 20.476 1.00 41.35 O
ANISOU 3612 O HOH A 543 5173 4806 5732 651 820 -164 O
HETATM 3613 O HOH A 544 2.572 -1.871 20.357 1.00 61.64 O
ANISOU 3613 O HOH A 544 8268 7128 8024 513 854 -137 O
HETATM 3614 O HOH A 545 -7.650 51.886 15.470 1.00 52.53 O
ANISOU 3614 O HOH A 545 7870 5126 6963 126 542 574 O
HETATM 3615 O HOH A 546 8.189 42.015 13.488 1.00 51.67 O
ANISOU 3615 O HOH A 546 6836 5465 7333 -734 1948 232 O
HETATM 3616 O HOH A 547 4.074 1.466 12.118 1.00 43.52 O
ANISOU 3616 O HOH A 547 6122 4934 5480 369 1226 -376 O
HETATM 3617 O HOH A 548 -22.872 10.138 12.530 1.00 79.61 O
ANISOU 3617 O HOH A 548 9538 9432 11276 -340 -895 -813 O
HETATM 3618 O HOH A 549 -4.352 -6.554 25.637 1.00 66.41 O
ANISOU 3618 O HOH A 549 9370 7249 8614 263 1028 52 O
HETATM 3619 O HOH A 550 -2.036 49.544 33.307 1.00 61.70 O
ANISOU 3619 O HOH A 550 8036 6863 8545 -343 376 -576 O
HETATM 3620 O HOH A 551 2.456 -4.709 5.327 1.00 71.82 O
ANISOU 3620 O HOH A 551 10677 8029 8582 349 1453 -791 O
HETATM 3621 O HOH A 552 3.147 -6.896 27.611 1.00 37.53 O
ANISOU 3621 O HOH A 552 5690 3640 4931 882 688 179 O
HETATM 3622 O HOH A 553 -16.486 47.460 24.248 1.00 68.35 O
ANISOU 3622 O HOH A 553 8674 7647 9648 468 203 18 O
HETATM 3623 O HOH A 554 5.406 2.140 34.964 1.00 52.82 O
ANISOU 3623 O HOH A 554 7520 6052 6496 1029 -81 266 O
HETATM 3624 O HOH A 555 -4.376 -2.366 23.510 1.00 63.74 O
ANISOU 3624 O HOH A 555 8716 7262 8241 181 860 -48 O
HETATM 3625 O HOH A 556 -23.883 -0.702 12.968 1.00 83.11 O
ANISOU 3625 O HOH A 556 10002 9311 12263 -840 -497 -1201 O
HETATM 3626 O HOH A 557 -6.266 51.447 33.460 1.00 47.99 O
ANISOU 3626 O HOH A 557 6459 4972 6801 -145 537 -525 O
HETATM 3627 O HOH A 558 -6.544 8.013 22.551 1.00 28.23 O
ANISOU 3627 O HOH A 558 3755 3295 3674 14 587 -71 O
HETATM 3628 O HOH A 559 -4.308 2.928 16.757 1.00 51.77 O
ANISOU 3628 O HOH A 559 7032 6084 6555 61 655 -255 O
HETATM 3629 O HOH A 560 6.257 41.480 9.870 1.00 74.32 O
ANISOU 3629 O HOH A 560 10359 8234 9644 -592 2062 457 O
HETATM 3630 O HOH A 561 -5.180 10.349 21.381 1.00 34.10 O
ANISOU 3630 O HOH A 561 4451 4144 4361 38 532 -69 O
HETATM 3631 O HOH A 562 -16.102 58.266 11.847 1.00 70.37 O
ANISOU 3631 O HOH A 562 10817 6591 9331 1043 -382 925 O
HETATM 3632 O HOH A 563 -10.020 -0.637 10.301 1.00 74.14 O
ANISOU 3632 O HOH A 563 10256 8586 9328 -205 210 -701 O
HETATM 3633 O HOH A 564 -18.635 46.894 19.441 1.00 81.24 O
ANISOU 3633 O HOH A 564 10409 9197 11260 685 -273 194 O
HETATM 3634 O HOH A 565 3.241 43.379 12.411 1.00 45.01 O
ANISOU 3634 O HOH A 565 6565 4592 5944 -485 1555 441 O
HETATM 3635 O HOH A 566 3.859 -2.112 4.123 1.00 53.52 O
ANISOU 3635 O HOH A 566 8388 5805 6142 363 1636 -740 O
HETATM 3636 O HOH A 567 -0.798 0.712 20.801 1.00 53.67 O
ANISOU 3636 O HOH A 567 7236 6250 6907 295 765 -113 O
HETATM 3637 O HOH A 568 -9.216 54.010 18.525 1.00 56.98 O
ANISOU 3637 O HOH A 568 8216 5613 7819 190 478 426 O
HETATM 3638 O HOH A 569 2.497 43.679 20.519 1.00 38.28 O
ANISOU 3638 O HOH A 569 4932 4055 5557 -493 950 53 O
HETATM 3639 O HOH A 570 -1.721 45.594 15.045 1.00 63.68 O
ANISOU 3639 O HOH A 570 8921 6993 8280 -252 961 433 O
HETATM 3640 O HOH A 571 15.851 44.523 22.704 1.00 79.61 O
ANISOU 3640 O HOH A 571 8700 8972 12577 -1178 1354 -604 O
HETATM 3641 O HOH A 572 -9.848 -10.021 1.986 1.00 82.34 O
ANISOU 3641 O HOH A 572 12545 8839 9901 -277 54 -1480 O
HETATM 3642 O HOH A 573 0.802 0.346 18.653 1.00 47.41 O
ANISOU 3642 O HOH A 573 6450 5447 6118 343 840 -184 O
HETATM 3643 O HOH A 574 5.786 43.239 13.438 1.00 74.43 O
ANISOU 3643 O HOH A 574 9974 8320 9984 -636 1744 325 O
HETATM 3644 O HOH A 575 -8.916 -5.881 -1.381 1.00 74.00 O
ANISOU 3644 O HOH A 575 11955 7981 8181 -126 -99 -1430 O
HETATM 3645 O HOH A 576 -9.012 41.461 4.988 1.00 68.05 O
ANISOU 3645 O HOH A 576 10846 7410 7599 407 9 784 O
HETATM 3646 O HOH A 577 25.064 42.407 17.467 1.00 88.63 O
ANISOU 3646 O HOH A 577 8615 9631 15431 -1600 2803 -854 O
HETATM 3647 O HOH A 578 -12.197 59.879 8.764 1.00 88.02 O
ANISOU 3647 O HOH A 578 13886 8484 11074 819 91 1229 O
HETATM 3648 O HOH A 579 -20.172 46.868 21.697 1.00130.29 O
ANISOU 3648 O HOH A 579 16349 15420 17735 714 -158 65 O
HETATM 3649 O HOH A 580 -17.106 56.072 16.559 1.00 87.83 O
ANISOU 3649 O HOH A 580 12168 9213 11989 907 -247 549 O
HETATM 3650 O HOH A 581 2.248 43.957 9.934 1.00 78.34 O
ANISOU 3650 O HOH A 581 11234 8663 9868 -406 1618 599 O
HETATM 3651 O HOH A 582 5.081 49.808 9.652 1.00 60.78 O
ANISOU 3651 O HOH A 582 9194 5859 8043 -711 2236 693 O
HETATM 3652 O HOH A 583 -26.193 5.319 28.092 1.00 82.32 O
ANISOU 3652 O HOH A 583 9390 9205 12684 -829 1587 -524 O
HETATM 3653 O HOH A 584 -18.688 42.995 5.964 1.00104.83 O
ANISOU 3653 O HOH A 584 14917 11982 12931 1018 -1471 616 O
HETATM 3654 O HOH A 585 -12.431 4.466 32.762 1.00 63.16 O
ANISOU 3654 O HOH A 585 8625 7189 8186 -111 1356 145 O
HETATM 3655 O HOH A 586 -5.014 1.810 13.553 1.00 57.19 O
ANISOU 3655 O HOH A 586 7919 6681 7130 16 608 -393 O
HETATM 3656 O HOH A 587 9.472 -1.965 4.029 1.00 66.16 O
ANISOU 3656 O HOH A 587 9658 7332 8148 577 2334 -740 O
HETATM 3657 O HOH A 588 14.143 14.429 12.202 1.00 65.91 O
ANISOU 3657 O HOH A 588 7819 7939 9283 183 2000 -314 O
HETATM 3658 O HOH A 589 -11.703 -0.582 25.491 1.00 63.92 O
ANISOU 3658 O HOH A 589 8523 7192 8572 -222 1040 -95 O
HETATM 3659 O HOH A 590 -14.396 25.107 8.563 1.00 64.19 O
ANISOU 3659 O HOH A 590 8902 7738 7749 232 -734 -16 O
HETATM 3660 O HOH A 591 -14.326 50.789 31.168 1.00 81.16 O
ANISOU 3660 O HOH A 591 10460 9120 11256 306 661 -318 O
HETATM 3661 O HOH A 592 11.664 4.507 8.814 1.00 79.11 O
ANISOU 3661 O HOH A 592 10311 9365 10380 492 2105 -465 O
HETATM 3662 O HOH A 593 7.954 43.589 11.266 1.00 79.45 O
ANISOU 3662 O HOH A 593 10746 8760 10682 -760 2211 382 O
HETATM 3663 O HOH A 594 -20.224 26.837 15.501 1.00 69.94 O
ANISOU 3663 O HOH A 594 8466 8484 9624 225 -702 -178 O
HETATM 3664 O HOH A 595 -13.691 -1.466 15.951 1.00 80.27 O
ANISOU 3664 O HOH A 595 10511 9259 10730 -400 385 -593 O
HETATM 3665 O HOH A 596 -20.178 2.728 8.516 1.00 90.97 O
ANISOU 3665 O HOH A 596 11727 10618 12218 -482 -946 -1082 O
HETATM 3666 O HOH A 597 5.390 45.691 12.438 1.00 61.38 O
ANISOU 3666 O HOH A 597 8595 6441 8286 -667 1873 431 O
HETATM 3667 O HOH A 598 -15.124 57.906 19.856 1.00 88.33 O
ANISOU 3667 O HOH A 598 12132 9222 12206 682 158 388 O
HETATM 3668 O HOH A 599 -10.379 -3.251 9.211 1.00 66.70 O
ANISOU 3668 O HOH A 599 9472 7465 8404 -251 196 -843 O
HETATM 3669 O HOH A 600 14.368 8.508 19.212 1.00 88.36 O
ANISOU 3669 O HOH A 600 10302 10868 12404 624 1050 -334 O
HETATM 3670 O HOH A 601 3.282 3.127 36.745 1.00 79.25 O
ANISOU 3670 O HOH A 601 11135 9381 9594 936 12 326 O
HETATM 3671 O HOH A 602 0.981 -6.761 1.255 1.00 73.36 O
ANISOU 3671 O HOH A 602 11557 7970 8348 293 1420 -1071 O
HETATM 3672 O HOH A 603 -17.075 28.260 11.041 1.00 78.07 O
ANISOU 3672 O HOH A 603 10239 9467 9957 312 -864 -4 O
HETATM 3673 O HOH A 604 -17.922 51.114 18.105 1.00 71.86 O
ANISOU 3673 O HOH A 604 9613 7672 10017 791 -288 347 O
HETATM 3674 O HOH A 605 13.069 10.887 9.703 1.00 81.80 O
ANISOU 3674 O HOH A 605 10276 9853 10952 284 2179 -351 O
HETATM 3675 O HOH A 606 -15.589 17.949 25.140 1.00 62.66 O
ANISOU 3675 O HOH A 606 7560 7702 8545 -122 518 -144 O
HETATM 3676 O HOH A 607 0.477 22.104 31.906 1.00 89.41 O
ANISOU 3676 O HOH A 607 11305 11344 11324 155 143 -99 O
HETATM 3677 O HOH A 608 -11.246 -2.117 19.854 1.00 75.88 O
ANISOU 3677 O HOH A 608 10034 8704 10094 -267 740 -346 O
HETATM 3678 O HOH A 609 -18.289 13.298 5.434 1.00 72.08 O
ANISOU 3678 O HOH A 609 9863 8566 8957 -2 -1352 -651 O
HETATM 3679 O HOH A 610 -9.511 -0.704 23.884 1.00 69.19 O
ANISOU 3679 O HOH A 610 9235 7944 9110 -117 904 -113 O
HETATM 3680 O HOH A 611 -23.165 42.142 17.492 1.00 72.13 O
ANISOU 3680 O HOH A 611 8777 8192 10437 827 -802 55 O
HETATM 3681 O HOH A 612 -4.484 48.619 16.092 1.00 39.29 O
ANISOU 3681 O HOH A 612 5924 3737 5269 -111 754 458 O
HETATM 3682 O HOH A 613 11.613 32.338 13.080 1.00 67.78 O
ANISOU 3682 O HOH A 613 8304 7937 9511 -536 2032 0 O
HETATM 3683 O HOH A 614 7.895 29.899 10.443 1.00 62.66 O
ANISOU 3683 O HOH A 614 8299 7367 8140 -346 1874 145 O
HETATM 3684 O HOH A 615 -19.963 19.223 14.742 1.00 53.79 O
ANISOU 3684 O HOH A 615 6409 6461 7568 -16 -641 -369 O
HETATM 3685 O HOH A 616 -21.312 0.122 17.619 1.00 69.80 O
ANISOU 3685 O HOH A 616 8409 7759 10353 -740 242 -808 O
HETATM 3686 O HOH A 617 12.990 27.705 10.292 1.00 68.70 O
ANISOU 3686 O HOH A 617 8541 8058 9503 -404 2403 -36 O
HETATM 3687 O HOH A 618 -15.985 35.818 8.199 1.00 66.04 O
ANISOU 3687 O HOH A 618 9450 7606 8038 566 -956 337 O
HETATM 3688 O HOH A 619 3.649 33.646 36.518 1.00 69.60 O
ANISOU 3688 O HOH A 619 8760 8647 9037 -56 -287 -523 O
HETATM 3689 O HOH A 620 22.215 38.376 23.671 1.00 87.58 O
ANISOU 3689 O HOH A 620 8507 10169 14601 -1044 1143 -985 O
HETATM 3690 O HOH A 621 -26.228 8.052 28.007 1.00 86.91 O
ANISOU 3690 O HOH A 621 9870 9937 13216 -718 1444 -518 O
HETATM 3691 O HOH A 622 -2.660 47.991 14.225 1.00 47.06 O
ANISOU 3691 O HOH A 622 7060 4676 6144 -200 961 532 O
HETATM 3692 O HOH A 623 12.504 11.541 23.376 1.00 65.59 O
ANISOU 3692 O HOH A 623 7449 8144 9327 545 519 -252 O
HETATM 3693 O HOH A 624 -4.392 50.860 11.384 1.00 92.63 O
ANISOU 3693 O HOH A 624 13428 10083 11683 -31 919 777 O
HETATM 3694 O HOH A 625 -2.042 49.593 12.146 1.00 61.10 O
ANISOU 3694 O HOH A 625 9193 6211 7810 -218 1149 676 O
HETATM 3695 O HOH A 626 9.700 38.880 4.544 1.00 81.10 O
ANISOU 3695 O HOH A 626 11747 8837 10230 -663 3019 547 O
HETATM 3696 O HOH A 627 -27.135 9.709 22.721 1.00 86.33 O
ANISOU 3696 O HOH A 627 9469 10025 13308 -635 512 -731 O
HETATM 3697 O HOH A 628 11.031 8.846 3.402 1.00 71.31 O
ANISOU 3697 O HOH A 628 10062 8267 8764 271 2632 -420 O
HETATM 3698 O HOH A 629 -9.089 -2.725 26.689 1.00 73.08 O
ANISOU 3698 O HOH A 629 9955 8251 9562 -53 1098 18 O
HETATM 3699 O HOH A 630 9.286 31.738 11.869 1.00 65.24 O
ANISOU 3699 O HOH A 630 8355 7651 8781 -445 1924 103 O
HETATM 3700 O HOH A 631 7.572 37.692 8.632 1.00 68.15 O
ANISOU 3700 O HOH A 631 9515 7595 8783 -551 2226 391 O
HETATM 3701 O HOH A 632 15.138 36.155 32.015 1.00101.48 O
ANISOU 3701 O HOH A 632 11352 12455 14751 -468 -375 -917 O
HETATM 3702 O HOH A 633 5.978 15.651 3.768 1.00 67.71 O
ANISOU 3702 O HOH A 633 9923 7998 7806 59 1949 -132 O
HETATM 3703 O HOH A 634 -6.020 50.015 14.355 1.00 50.03 O
ANISOU 3703 O HOH A 634 7582 4920 6510 25 662 594 O
HETATM 3704 O HOH A 635 -10.550 21.890 3.672 1.00 79.69 O
ANISOU 3704 O HOH A 635 11743 9595 8942 213 -469 -29 O
HETATM 3705 O HOH A 636 1.584 11.820 33.649 1.00 74.27 O
ANISOU 3705 O HOH A 636 9797 9220 9202 485 119 81 O
HETATM 3706 O HOH A 637 16.737 20.899 15.683 1.00 77.37 O
ANISOU 3706 O HOH A 637 8556 9417 11426 -61 1803 -369 O
HETATM 3707 O HOH A 638 -24.490 3.651 10.964 1.00 66.74 O
ANISOU 3707 O HOH A 638 7902 7460 9995 -633 -1024 -1182 O
HETATM 3708 O HOH A 639 14.000 16.679 22.237 1.00 73.25 O
ANISOU 3708 O HOH A 639 8115 9145 10571 295 698 -334 O
HETATM 3709 O HOH A 640 14.149 11.155 15.540 1.00 72.24 O
ANISOU 3709 O HOH A 640 8397 8809 10240 398 1531 -344 O
HETATM 3710 O HOH A 641 -23.301 15.709 13.425 1.00 83.55 O
ANISOU 3710 O HOH A 641 9905 10064 11775 -134 -964 -637 O
HETATM 3711 O HOH A 642 -6.770 20.734 35.934 1.00 55.50 O
ANISOU 3711 O HOH A 642 7477 6865 6746 145 591 -21 O
HETATM 3712 O HOH A 643 -2.616 27.863 4.338 1.00 73.36 O
ANISOU 3712 O HOH A 643 11079 8674 8121 53 791 321 O
HETATM 3713 O HOH A 644 2.435 -10.067 24.373 1.00 70.83 O
ANISOU 3713 O HOH A 644 9996 7639 9275 801 931 41 O
HETATM 3714 O HOH A 645 -2.426 23.680 34.837 1.00 81.20 O
ANISOU 3714 O HOH A 645 10523 10238 10091 152 225 -111 O
HETATM 3715 O HOH A 646 -23.635 17.574 25.180 1.00 92.37 O
ANISOU 3715 O HOH A 646 10596 11163 13337 -255 588 -410 O
HETATM 3716 O HOH A 647 -25.311 14.522 24.602 1.00 71.27 O
ANISOU 3716 O HOH A 647 7747 8347 10985 -399 620 -525 O
HETATM 3717 O HOH A 648 -22.792 38.721 20.828 1.00 67.96 O
ANISOU 3717 O HOH A 648 7927 7888 10008 587 -365 -96 O
HETATM 3718 O HOH A 649 -3.174 34.255 38.535 1.00 78.77 O
ANISOU 3718 O HOH A 649 10403 9727 9800 38 162 -428 O
HETATM 3719 O HOH A 650 -18.822 18.653 6.602 1.00 82.96 O
ANISOU 3719 O HOH A 650 11088 10018 10414 152 -1389 -427 O
HETATM 3720 O HOH A 651 -23.593 40.567 22.687 1.00 92.77 O
ANISOU 3720 O HOH A 651 10965 10938 13347 642 -185 -144 O
HETATM 3721 O HOH A 652 -20.537 15.600 26.302 1.00 83.38 O
ANISOU 3721 O HOH A 652 9839 10088 11753 -269 756 -285 O
HETATM 3722 O HOH A 653 2.762 21.041 28.764 1.00 61.50 O
ANISOU 3722 O HOH A 653 7547 7836 7985 141 200 -101 O
HETATM 3723 O HOH A 654 6.084 11.590 1.543 1.00 64.11 O
ANISOU 3723 O HOH A 654 9843 7409 7106 153 2088 -293 O
HETATM 3724 O HOH A 655 -12.111 19.618 3.097 1.00 74.87 O
ANISOU 3724 O HOH A 655 11114 8969 8365 207 -730 -172 O
HETATM 3725 O HOH A 656 12.941 36.492 10.981 1.00 65.85 O
ANISOU 3725 O HOH A 656 8284 7333 9402 -763 2577 97 O
HETATM 3726 O HOH A 657 -17.472 40.703 6.808 1.00 88.89 O
ANISOU 3726 O HOH A 657 12709 10163 10902 835 -1237 527 O
HETATM 3727 O HOH A 658 13.879 20.730 6.320 1.00 82.06 O
ANISOU 3727 O HOH A 658 10640 9691 10847 -155 2863 -139 O
HETATM 3728 O HOH A 659 -0.735 26.321 5.573 1.00 66.96 O
ANISOU 3728 O HOH A 659 9976 7950 7516 -12 1017 249 O
HETATM 3729 O HOH B 201 6.342 44.020 24.612 1.00 36.10 O
ANISOU 3729 O HOH B 201 4804 2314 6599 58 833 16 O
HETATM 3730 O HOH B 202 7.444 76.147 31.736 1.00 41.44 O
ANISOU 3730 O HOH B 202 5008 3952 6786 -1116 675 -516 O
HETATM 3731 O HOH B 203 -4.494 66.843 15.316 1.00 46.07 O
ANISOU 3731 O HOH B 203 7998 4504 5001 -133 -870 649 O
HETATM 3732 O HOH B 204 -12.096 68.190 32.570 1.00 38.23 O
ANISOU 3732 O HOH B 204 3724 3883 6919 -354 835 -671 O
HETATM 3733 O HOH B 205 -3.761 52.811 17.397 1.00 41.11 O
ANISOU 3733 O HOH B 205 5989 4175 5455 -773 28 -432 O
HETATM 3734 O HOH B 206 -2.366 70.497 19.229 1.00 42.09 O
ANISOU 3734 O HOH B 206 6957 3866 5171 -254 -165 793 O
HETATM 3735 O HOH B 207 -4.220 50.193 18.247 1.00 29.58 O
ANISOU 3735 O HOH B 207 4313 2541 4383 -883 180 -576 O
HETATM 3736 O HOH B 208 -2.126 63.020 36.243 1.00 44.41 O
ANISOU 3736 O HOH B 208 6105 5068 5699 -614 671 270 O
HETATM 3737 O HOH B 209 -13.019 73.885 31.558 0.50 43.35 O
ANISOU 3737 O HOH B 209 4200 4057 8214 221 321 -858 O
HETATM 3738 O HOH B 210 0.449 45.406 20.415 1.00 38.17 O
ANISOU 3738 O HOH B 210 5380 3020 6102 -703 948 -438 O
HETATM 3739 O HOH B 211 13.391 56.023 20.638 1.00 50.95 O
ANISOU 3739 O HOH B 211 5633 5120 8607 -564 1996 -750 O
HETATM 3740 O HOH B 212 8.231 61.173 36.803 1.00 53.05 O
ANISOU 3740 O HOH B 212 6815 6162 7181 -70 -812 186 O
HETATM 3741 O HOH B 213 -8.001 70.211 22.651 1.00 55.40 O
ANISOU 3741 O HOH B 213 7368 5735 7948 155 -848 307 O
HETATM 3742 O HOH B 214 -8.764 55.467 23.559 1.00 39.32 O
ANISOU 3742 O HOH B 214 4625 4055 6259 -794 3 -313 O
HETATM 3743 O HOH B 215 15.902 63.305 24.073 1.00 50.56 O
ANISOU 3743 O HOH B 215 4808 5188 9213 -958 1785 -915 O
HETATM 3744 O HOH B 216 3.905 75.341 24.162 1.00 44.83 O
ANISOU 3744 O HOH B 216 6639 3930 6464 -891 1028 472 O
HETATM 3745 O HOH B 217 -10.042 74.950 29.342 1.00 45.90 O
ANISOU 3745 O HOH B 217 5248 4292 7898 261 -91 -327 O
HETATM 3746 O HOH B 218 11.036 66.730 34.711 1.00 41.64 O
ANISOU 3746 O HOH B 218 4458 4706 6656 -489 -508 -499 O
HETATM 3747 O HOH B 219 -1.396 60.420 35.911 1.00 60.83 O
ANISOU 3747 O HOH B 219 8313 7071 7727 -584 603 465 O
HETATM 3748 O HOH B 220 0.766 58.877 36.445 1.00 38.73 O
ANISOU 3748 O HOH B 220 5697 4215 4803 -442 313 618 O
HETATM 3749 O HOH B 221 -14.482 67.615 22.933 1.00 63.53 O
ANISOU 3749 O HOH B 221 6951 6827 10362 386 -1564 -548 O
HETATM 3750 O HOH B 222 -8.035 60.891 16.263 1.00 49.85 O
ANISOU 3750 O HOH B 222 7294 5373 6273 -235 -1348 -116 O
HETATM 3751 O HOH B 223 11.387 53.439 27.372 1.00 55.65 O
ANISOU 3751 O HOH B 223 6243 5794 9108 122 318 -102 O
HETATM 3752 O HOH B 224 -3.627 78.422 31.927 1.00 73.54 O
ANISOU 3752 O HOH B 224 9446 7674 10820 -256 489 -291 O
HETATM 3753 O HOH B 225 -13.627 63.399 21.675 1.00 84.79 O
ANISOU 3753 O HOH B 225 9824 9745 12647 -6 -1444 -596 O
HETATM 3754 O HOH B 226 -8.042 58.047 20.017 1.00 44.51 O
ANISOU 3754 O HOH B 226 5772 4792 6348 -522 -633 -258 O
HETATM 3755 O HOH B 227 -2.766 55.405 29.127 1.00 34.21 O
ANISOU 3755 O HOH B 227 4530 3429 5038 -659 615 399 O
HETATM 3756 O HOH B 228 13.899 64.027 33.871 1.00 61.68 O
ANISOU 3756 O HOH B 228 6428 7150 9858 -255 -739 -653 O
HETATM 3757 O HOH B 229 -2.152 64.102 39.993 1.00 59.56 O
ANISOU 3757 O HOH B 229 8542 7025 7063 -685 815 145 O
HETATM 3758 O HOH B 230 3.169 54.264 29.857 1.00 47.96 O
ANISOU 3758 O HOH B 230 6329 5077 6818 -296 335 542 O
HETATM 3759 O HOH B 231 -9.152 55.775 20.702 1.00 47.49 O
ANISOU 3759 O HOH B 231 5838 5109 7097 -693 -504 -472 O
HETATM 3760 O HOH B 232 2.299 76.714 28.071 1.00 53.96 O
ANISOU 3760 O HOH B 232 7340 5219 7942 -732 709 156 O
HETATM 3761 O HOH B 233 -0.614 67.700 12.959 1.00 50.99 O
ANISOU 3761 O HOH B 233 9688 4849 4836 -508 110 894 O
HETATM 3762 O HOH B 234 12.671 48.964 18.607 1.00 57.92 O
ANISOU 3762 O HOH B 234 6761 5500 9746 -217 2168 -1087 O
HETATM 3763 O HOH B 235 -4.716 55.645 31.008 1.00 49.49 O
ANISOU 3763 O HOH B 235 6460 5338 7008 -785 841 382 O
HETATM 3764 O HOH B 236 3.890 73.338 37.079 1.00 43.02 O
ANISOU 3764 O HOH B 236 5531 4747 6067 -746 153 -577 O
HETATM 3765 O HOH B 237 -3.298 74.614 20.093 1.00 68.03 O
ANISOU 3765 O HOH B 237 10379 6692 8776 -39 -329 940 O
HETATM 3766 O HOH B 238 -7.251 62.564 33.932 1.00 56.06 O
ANISOU 3766 O HOH B 238 6979 6401 7920 -735 1046 13 O
HETATM 3767 O HOH B 239 6.576 76.207 21.335 1.00 66.11 O
ANISOU 3767 O HOH B 239 9840 6205 9073 -1287 1784 584 O
HETATM 3768 O HOH B 240 -6.791 78.643 31.015 1.00 46.65 O
ANISOU 3768 O HOH B 240 5830 4098 7799 83 278 -319 O
HETATM 3769 O HOH B 241 0.242 51.086 12.037 1.00 53.04 O
ANISOU 3769 O HOH B 241 8642 5470 6041 -921 747 -885 O
HETATM 3770 O HOH B 242 6.380 66.059 40.300 1.00 70.35 O
ANISOU 3770 O HOH B 242 9468 8556 8707 -354 -764 -180 O
HETATM 3771 O HOH B 243 0.524 53.956 14.015 1.00 49.42 O
ANISOU 3771 O HOH B 243 7898 5159 5721 -815 684 -446 O
HETATM 3772 O HOH B 244 1.280 55.455 45.367 1.00 76.94 O
ANISOU 3772 O HOH B 244 13149 8565 7519 -298 54 1341 O
HETATM 3773 O HOH B 245 13.881 61.470 30.879 1.00 66.59 O
ANISOU 3773 O HOH B 245 6988 7617 10695 -214 -178 -514 O
HETATM 3774 O HOH B 246 3.486 66.047 39.558 1.00 44.85 O
ANISOU 3774 O HOH B 246 6366 5291 5383 -472 -186 -31 O
HETATM 3775 O HOH B 247 5.822 53.683 35.327 1.00 52.80 O
ANISOU 3775 O HOH B 247 7402 5565 7094 116 -407 849 O
HETATM 3776 O HOH B 248 6.817 52.092 11.393 1.00 50.84 O
ANISOU 3776 O HOH B 248 8295 4968 6053 -1034 2393 -1005 O
HETATM 3777 O HOH B 249 2.510 55.230 15.332 1.00 42.90 O
ANISOU 3777 O HOH B 249 6828 4345 5126 -796 1032 -272 O
HETATM 3778 O HOH B 250 -11.082 70.626 23.600 1.00 67.98 O
ANISOU 3778 O HOH B 250 8323 7264 10244 383 -1139 -25 O
HETATM 3779 O HOH B 251 4.131 68.455 9.397 1.00 68.01 O
ANISOU 3779 O HOH B 251 13258 6504 6079 -1181 1838 993 O
HETATM 3780 O HOH B 252 -9.294 65.060 34.885 1.00 44.67 O
ANISOU 3780 O HOH B 252 5249 4906 6817 -707 1264 -309 O
HETATM 3781 O HOH B 253 -5.725 78.953 34.401 1.00 54.35 O
ANISOU 3781 O HOH B 253 6768 5266 8615 -180 707 -696 O
HETATM 3782 O HOH B 254 -0.417 77.678 26.969 1.00 53.96 O
ANISOU 3782 O HOH B 254 7578 4993 7930 -447 475 330 O
HETATM 3783 O HOH B 255 -12.011 63.652 28.809 1.00 59.21 O
ANISOU 3783 O HOH B 255 6399 6631 9467 -465 294 -471 O
HETATM 3784 O HOH B 256 -6.397 60.405 13.126 1.00 65.82 O
ANISOU 3784 O HOH B 256 10296 7314 7399 -301 -1330 -70 O
HETATM 3785 O HOH B 257 -7.378 65.035 16.568 1.00 42.76 O
ANISOU 3785 O HOH B 257 6747 4289 5210 -8 -1379 290 O
HETATM 3786 O HOH B 258 -3.849 77.200 25.926 1.00 66.77 O
ANISOU 3786 O HOH B 258 9184 6579 9608 -50 3 415 O
HETATM 3787 O HOH B 259 13.558 51.508 19.010 1.00 78.77 O
ANISOU 3787 O HOH B 259 9213 8323 12392 -345 2241 -1046 O
HETATM 3788 O HOH B 260 16.765 72.228 16.470 1.00 73.24 O
ANISOU 3788 O HOH B 260 9867 6744 11218 -2609 4878 -573 O
HETATM 3789 O HOH B 261 -0.854 54.004 38.720 1.00 58.92 O
ANISOU 3789 O HOH B 261 9155 6272 6962 -537 705 1084 O
HETATM 3790 O HOH B 262 -1.302 74.498 18.029 1.00 72.70 O
ANISOU 3790 O HOH B 262 11629 7132 8860 -270 41 1142 O
HETATM 3791 O HOH B 263 -12.081 74.327 27.374 1.00 69.82 O
ANISOU 3791 O HOH B 263 8058 7231 11240 516 -618 -356 O
HETATM 3792 O HOH B 264 -9.415 59.338 18.083 1.00 62.58 O
ANISOU 3792 O HOH B 264 8222 7045 8511 -345 -1233 -349 O
HETATM 3793 O HOH B 265 8.796 50.893 30.382 1.00 80.91 O
ANISOU 3793 O HOH B 265 10151 8809 11782 308 -142 441 O
HETATM 3794 O HOH B 266 14.698 53.717 20.086 1.00 66.80 O
ANISOU 3794 O HOH B 266 7354 6924 11102 -403 2181 -1033 O
HETATM 3795 O HOH B 267 1.407 68.463 9.340 1.00 96.76 O
ANISOU 3795 O HOH B 267 16997 10235 9533 -805 813 1105 O
HETATM 3796 O HOH B 268 18.373 70.634 14.675 1.00 88.49 O
ANISOU 3796 O HOH B 268 11755 8575 13290 -2820 5724 -881 O
HETATM 3797 O HOH B 269 2.289 78.174 24.186 1.00 77.94 O
ANISOU 3797 O HOH B 269 11141 7721 10753 -745 886 588 O
HETATM 3798 O HOH B 270 -6.058 60.828 36.397 1.00 63.05 O
ANISOU 3798 O HOH B 270 8377 7260 8319 -843 1275 208 O
HETATM 3799 O HOH B 271 -6.452 63.492 13.041 1.00 75.31 O
ANISOU 3799 O HOH B 271 11826 8359 8429 -103 -1511 264 O
HETATM 3800 O HOH B 272 15.108 50.579 25.210 1.00 92.03 O
ANISOU 3800 O HOH B 272 10109 9942 14917 414 699 -700 O
HETATM 3801 O HOH B 273 -2.265 65.972 42.324 1.00 82.31 O
ANISOU 3801 O HOH B 273 11745 9947 9583 -748 924 -102 O
HETATM 3802 O HOH B 274 17.190 69.393 22.241 1.00 65.62 O
ANISOU 3802 O HOH B 274 7003 6600 11329 -1834 2989 -1060 O
HETATM 3803 O HOH B 275 -11.668 65.768 33.626 1.00 45.75 O
ANISOU 3803 O HOH B 275 4860 4935 7589 -612 1179 -578 O
HETATM 3804 O HOH B 276 2.780 67.296 41.821 1.00 58.15 O
ANISOU 3804 O HOH B 276 8412 7013 6670 -539 -139 -214 O
HETATM 3805 O HOH B 277 0.552 81.449 35.337 1.00 56.92 O
ANISOU 3805 O HOH B 277 7418 5444 8765 -725 730 -873 O
HETATM 3806 O HOH B 278 9.391 58.541 32.356 1.00 66.14 O
ANISOU 3806 O HOH B 278 7958 7604 9567 -37 -344 169 O
HETATM 3807 O HOH B 279 -3.068 61.618 40.639 1.00 76.69 O
ANISOU 3807 O HOH B 279 11022 9072 9044 -766 1068 350 O
HETATM 3808 O HOH B 280 -14.270 60.490 19.760 1.00 98.42 O
ANISOU 3808 O HOH B 280 11553 11504 14339 -168 -1763 -863 O
HETATM 3809 O HOH B 281 -4.736 72.279 18.948 1.00 60.70 O
ANISOU 3809 O HOH B 281 9394 5996 7672 69 -724 857 O
HETATM 3810 O HOH B 282 -6.115 57.814 43.710 1.00 97.40 O
ANISOU 3810 O HOH B 282 14675 11243 11090 -1202 2209 628 O
HETATM 3811 O HOH B 283 -16.511 52.473 24.301 1.00 74.96 O
ANISOU 3811 O HOH B 283 7522 8165 12792 -1383 124 -1507 O
CONECT 6 1975
CONECT 690 1323
CONECT 1323 690
CONECT 1975 6
CONECT 2467 3029
CONECT 2675 3103
CONECT 3029 2467
CONECT 3103 2675
CONECT 3284 3285 3306
CONECT 3285 3284 3286
CONECT 3286 3285 3304 3307
CONECT 3287 3288 3292 3309
CONECT 3288 3287 3289 3293
CONECT 3289 3288 3290
CONECT 3290 3289 3291
CONECT 3291 3290 3292
CONECT 3292 3287 3291
CONECT 3293 3288 3294
CONECT 3294 3293 3311 3316
CONECT 3295 3296 3307
CONECT 3296 3295 3297
CONECT 3297 3296 3298 3300
CONECT 3298 3297 3299
CONECT 3299 3298 3307
CONECT 3300 3297 3312
CONECT 3301 3302 3312
CONECT 3302 3301 3313
CONECT 3303 3313 3314
CONECT 3304 3286 3305
CONECT 3305 3304 3306 3308
CONECT 3306 3284 3305
CONECT 3307 3286 3295 3299
CONECT 3308 3305 3309 3310
CONECT 3309 3287 3308
CONECT 3310 3308
CONECT 3311 3294
CONECT 3312 3300 3301 3314
CONECT 3313 3302 3303 3315
CONECT 3314 3303 3312
CONECT 3315 3313
CONECT 3316 3294
CONECT 3317 3318 3319
CONECT 3318 3317 3320
CONECT 3319 3317 3322
CONECT 3320 3318 3323
CONECT 3321 3331 3333
CONECT 3322 3319
CONECT 3323 3320 3324
CONECT 3324 3323 3325
CONECT 3325 3324 3326
CONECT 3326 3325 3327
CONECT 3327 3326 3328
CONECT 3328 3327 3330
CONECT 3329 3331 3335
CONECT 3330 3328 3332 3335
CONECT 3331 3321 3329 3334
CONECT 3332 3330
CONECT 3333 3321
CONECT 3334 3331
CONECT 3335 3329 3330
CONECT 3336 3337 3338
CONECT 3337 3336 3339
CONECT 3338 3336 3341
CONECT 3339 3337 3342
CONECT 3340 3350 3352
CONECT 3341 3338
CONECT 3342 3339 3343
CONECT 3343 3342 3344
CONECT 3344 3343 3345
CONECT 3345 3344 3346
CONECT 3346 3345 3347
CONECT 3347 3346 3349
CONECT 3348 3350 3354
CONECT 3349 3347 3351 3354
CONECT 3350 3340 3348 3353
CONECT 3351 3349
CONECT 3352 3340
CONECT 3353 3350
CONECT 3354 3348 3349
CONECT 3355 3358
CONECT 3356 3357 3359
CONECT 3357 3356 3360
CONECT 3358 3355 3362
CONECT 3359 3356 3363
CONECT 3360 3357 3364
CONECT 3361 3375 3377
CONECT 3362 3358 3365
CONECT 3363 3359 3366
CONECT 3364 3360 3367
CONECT 3365 3362 3368
CONECT 3366 3363 3368
CONECT 3367 3364 3369
CONECT 3368 3365 3366
CONECT 3369 3367 3370
CONECT 3370 3369 3371
CONECT 3371 3370 3372
CONECT 3372 3371 3374
CONECT 3373 3375 3379
CONECT 3374 3372 3376 3379
CONECT 3375 3361 3373 3378
CONECT 3376 3374
CONECT 3377 3361
CONECT 3378 3375
CONECT 3379 3373 3374
CONECT 3380 3381 3382
CONECT 3381 3380 3383
CONECT 3382 3380 3385
CONECT 3383 3381 3386
CONECT 3384 3394 3396
CONECT 3385 3382
CONECT 3386 3383 3387
CONECT 3387 3386 3388
CONECT 3388 3387 3389
CONECT 3389 3388 3390
CONECT 3390 3389 3391
CONECT 3391 3390 3393
CONECT 3392 3394 3398
CONECT 3393 3391 3395 3398
CONECT 3394 3384 3392 3397
CONECT 3395 3393
CONECT 3396 3384
CONECT 3397 3394
CONECT 3398 3392 3393
CONECT 3399 3400 3401
CONECT 3400 3399 3402
CONECT 3401 3399 3404
CONECT 3402 3400 3405
CONECT 3403 3415 3417
CONECT 3404 3401 3406
CONECT 3405 3402 3407
CONECT 3406 3404 3408
CONECT 3407 3405 3409
CONECT 3408 3406
CONECT 3409 3407 3410
CONECT 3410 3409 3411
CONECT 3411 3410 3412
CONECT 3412 3411 3414
CONECT 3413 3415 3419
CONECT 3414 3412 3416 3419
CONECT 3415 3403 3413 3418
CONECT 3416 3414
CONECT 3417 3403
CONECT 3418 3415
CONECT 3419 3413 3414
CONECT 3420 3429 3431
CONECT 3421 3422
CONECT 3422 3421 3423
CONECT 3423 3422 3424
CONECT 3424 3423 3425
CONECT 3425 3424 3426
CONECT 3426 3425 3428
CONECT 3427 3429 3433
CONECT 3428 3426 3430 3433
CONECT 3429 3420 3427 3432
CONECT 3430 3428
CONECT 3431 3420
CONECT 3432 3429
CONECT 3433 3427 3428
CONECT 3434 3437
CONECT 3435 3436 3438
CONECT 3436 3435 3439
CONECT 3437 3434 3441
CONECT 3438 3435 3442
CONECT 3439 3436 3443
CONECT 3440 3454 3456
CONECT 3441 3437 3444
CONECT 3442 3438 3445
CONECT 3443 3439 3446
CONECT 3444 3441 3447
CONECT 3445 3442 3447
CONECT 3446 3443 3448
CONECT 3447 3444 3445
CONECT 3448 3446 3449
CONECT 3449 3448 3450
CONECT 3450 3449 3451
CONECT 3451 3450 3453
CONECT 3452 3454 3458
CONECT 3453 3451 3455 3458
CONECT 3454 3440 3452 3457
CONECT 3455 3453
CONECT 3456 3440
CONECT 3457 3454
CONECT 3458 3452 3453
CONECT 3459 3464 3466
CONECT 3460 3461
CONECT 3461 3460 3463
CONECT 3462 3464 3468
CONECT 3463 3461 3465 3468
CONECT 3464 3459 3462 3467
CONECT 3465 3463
CONECT 3466 3459
CONECT 3467 3464
CONECT 3468 3462 3463
CONECT 3469 3476 3478
CONECT 3470 3471
CONECT 3471 3470 3472
CONECT 3472 3471 3473
CONECT 3473 3472 3475
CONECT 3474 3476 3480
CONECT 3475 3473 3477 3480
CONECT 3476 3469 3474 3479
CONECT 3477 3475
CONECT 3478 3469
CONECT 3479 3476
CONECT 3480 3474 3475
CONECT 3481 3487 3489
CONECT 3482 3483
CONECT 3483 3482 3484
CONECT 3484 3483 3486
CONECT 3485 3487 3491
CONECT 3486 3484 3488 3491
CONECT 3487 3481 3485 3490
CONECT 3488 3486
CONECT 3489 3481
CONECT 3490 3487
CONECT 3491 3485 3486
CONECT 3492 3495
CONECT 3493 3494 3496
CONECT 3494 3493 3497
CONECT 3495 3492 3499
CONECT 3496 3493 3500
CONECT 3497 3494 3501
CONECT 3498 3512 3514
CONECT 3499 3495 3502
CONECT 3500 3496 3503
CONECT 3501 3497 3504
CONECT 3502 3499 3505
CONECT 3503 3500 3505
CONECT 3504 3501 3506
CONECT 3505 3502 3503
CONECT 3506 3504 3507
CONECT 3507 3506 3508
CONECT 3508 3507 3509
CONECT 3509 3508 3511
CONECT 3510 3512 3516
CONECT 3511 3509 3513 3516
CONECT 3512 3498 3510 3515
CONECT 3513 3511
CONECT 3514 3498
CONECT 3515 3512
CONECT 3516 3510 3511
CONECT 3517 3518
CONECT 3518 3517 3519
CONECT 3519 3518 3521
CONECT 3520 3529 3531
CONECT 3521 3519 3522
CONECT 3522 3521 3523
CONECT 3523 3522 3524
CONECT 3524 3523 3525
CONECT 3525 3524 3526
CONECT 3526 3525 3528
CONECT 3527 3529 3533
CONECT 3528 3526 3530 3533
CONECT 3529 3520 3527 3532
CONECT 3530 3528
CONECT 3531 3520
CONECT 3532 3529
CONECT 3533 3527 3528
CONECT 3534 3537
CONECT 3535 3536 3538
CONECT 3536 3535 3539
CONECT 3537 3534 3541
CONECT 3538 3535 3542
CONECT 3539 3536 3543
CONECT 3540 3554 3556
CONECT 3541 3537 3544
CONECT 3542 3538 3545
CONECT 3543 3539 3546
CONECT 3544 3541 3547
CONECT 3545 3542 3547
CONECT 3546 3543 3548
CONECT 3547 3544 3545
CONECT 3548 3546 3549
CONECT 3549 3548 3550
CONECT 3550 3549 3551
CONECT 3551 3550 3553
CONECT 3552 3554 3558
CONECT 3553 3551 3555 3558
CONECT 3554 3540 3552 3557
CONECT 3555 3553
CONECT 3556 3540
CONECT 3557 3554
CONECT 3558 3552 3553
CONECT 3559 3560 3561
CONECT 3560 3559
CONECT 3561 3559 3562 3563
CONECT 3562 3561
CONECT 3563 3561 3564
CONECT 3564 3563
CONECT 3565 3566 3567 3568 3569
CONECT 3566 3565
CONECT 3567 3565
CONECT 3568 3565
CONECT 3569 3565
MASTER 450 0 16 17 14 0 31 6 3809 2 294 38
END