HEADER MEMBRANE PROTEIN 25-MAR-14 4PXZ
TITLE CRYSTAL STRUCTURE OF P2Y12 RECEPTOR IN COMPLEX WITH 2MESADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P2Y PURINOCEPTOR 12, SOLUBLE CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P2Y12, ADP-GLUCOSE RECEPTOR, ADPG-R, P2T(AC), P2Y(AC),
COMPND 5 P2Y(CYC), P2Y12 PLATELET ADP RECEPTOR, P2Y(ADP), SP1999, CYTOCHROME
COMPND 6 B-562;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: CHIMERA PROTEIN OF N-TERMINAL RESIDUES 2-223 FROM
COMPND 10 P2Y12R (P2Y12_HUMAN), SOLUBLE CYTOCHROME B562 (C562_ECOLX), AND C-
COMPND 11 TERMINAL RESIDUES 224-342 FROM P2Y12R (P2Y12_HUMAN).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: HORK3, P2RY12, P2Y12, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIROUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS PURINERGIC RECEPTOR P2Y12, AGONIST-BOUND, G-PROTEIN COUPLED RECEPTOR
KEYWDS 2 (GPCR), MEMBRANE PROTEIN, SIGNALING PROTEIN-AGONIST COMPLEX, PSI-
KEYWDS 3 BIOLOGY, GPCR NETWORK, STRUCTURAL GENOMICS, SIGNALING MEMBRANE
KEYWDS 4 PROTEIN, GPCR, PLATELET ACTIVATION, MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHANG,K.ZHANG,Z.G.GAO,S.PAOLETTA,D.ZHANG,G.W.HAN,T.LI,L.MA,W.ZHANG,
AUTHOR 2 C.E.MULLER,H.YANG,H.JIANG,V.CHEREZOV,V.KATRITCH,K.A.JACOBSON,
AUTHOR 3 R.C.STEVENS,B.WU,Q.ZHAO,GPCR NETWORK (GPCR)
REVDAT 5 22-NOV-17 4PXZ 1 REMARK
REVDAT 4 16-AUG-17 4PXZ 1 SOURCE REMARK
REVDAT 3 03-SEP-14 4PXZ 1 REMARK
REVDAT 2 28-MAY-14 4PXZ 1 JRNL
REVDAT 1 30-APR-14 4PXZ 0
JRNL AUTH J.ZHANG,K.ZHANG,Z.G.GAO,S.PAOLETTA,D.ZHANG,G.W.HAN,T.LI,
JRNL AUTH 2 L.MA,W.ZHANG,C.E.MULLER,H.YANG,H.JIANG,V.CHEREZOV,
JRNL AUTH 3 V.KATRITCH,K.A.JACOBSON,R.C.STEVENS,B.WU,Q.ZHAO
JRNL TITL AGONIST-BOUND STRUCTURE OF THE HUMAN P2Y12 RECEPTOR
JRNL REF NATURE V. 509 119 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 24784220
JRNL DOI 10.1038/NATURE13288
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 20345
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1041
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2923
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2277
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2772
REMARK 3 BIN R VALUE (WORKING SET) : 0.2242
REMARK 3 BIN FREE R VALUE : 0.2972
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.17
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 151
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3133
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 113
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.57470
REMARK 3 B22 (A**2) : -14.26710
REMARK 3 B33 (A**2) : 8.69240
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.355
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.333
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.226
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.340
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.231
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3327 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4512 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1555 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 63 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 465 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3327 ; 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 : 458 ; 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 : 3973 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.56
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.39
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|15 - A|305 }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.098 -2.326 42.689
REMARK 3 T TENSOR
REMARK 3 T11: 0.1478 T22: 0.1848
REMARK 3 T33: 0.0521 T12: 0.0349
REMARK 3 T13: -0.0277 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.4310 L22: 0.3853
REMARK 3 L33: 3.0322 L12: -0.1829
REMARK 3 L13: -1.1205 L23: 0.2628
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: 0.4098 S13: -0.0245
REMARK 3 S21: -0.1310 S22: -0.1420 S23: -0.0296
REMARK 3 S31: -0.3077 S32: -0.5595 S33: 0.1590
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): 49.247 -17.708 -1.365
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.1069
REMARK 3 T33: 0.1649 T12: 0.0393
REMARK 3 T13: -0.0214 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.9470 L22: 0.8450
REMARK 3 L33: 4.0556 L12: -0.8568
REMARK 3 L13: -1.9554 L23: 0.8316
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: 0.1374 S13: 0.0343
REMARK 3 S21: 0.0158 S22: -0.0526 S23: 0.0957
REMARK 3 S31: -0.2920 S32: -0.5868 S33: 0.0196
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-13; 16-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 17
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; APS
REMARK 200 BEAMLINE : BL41XU; 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 1.033
REMARK 200 MONOCHROMATOR : SI DOUBLE CRYSTAL MONOCHROMATOR;
REMARK 200 SI DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS; MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD; MARMOSAIC
REMARK 200 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20345
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.50
REMARK 200 R MERGE (I) : 0.19400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.99500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3VW7 AND 1M6T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30-40% PEG 400, 0.30-0.45M AMMONIUM
REMARK 280 ACETATE, CITRATE, 3% V/V 1-PROPANOL, 0.1 M SODIUM CITRATE, PH
REMARK 280 5.0, LIPIDIC CUBIC PHASE (LCP), TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.71500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.71500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.55500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.08500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.55500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.08500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.71500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.55500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.08500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.71500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.55500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.08500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A -9
REMARK 465 TYR A -8
REMARK 465 LYS A -7
REMARK 465 ASP A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 GLY A -2
REMARK 465 ALA A -1
REMARK 465 PRO A 0
REMARK 465 GLN A 2
REMARK 465 ALA A 3
REMARK 465 VAL A 4
REMARK 465 ASP A 5
REMARK 465 ASN A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 SER A 9
REMARK 465 ALA A 10
REMARK 465 PRO A 11
REMARK 465 GLY A 12
REMARK 465 ASN A 13
REMARK 465 THR A 14
REMARK 465 PHE A 130
REMARK 465 LYS A 131
REMARK 465 THR A 132
REMARK 465 SER A 133
REMARK 465 ASN A 134
REMARK 465 ARG A 306
REMARK 465 ASN A 307
REMARK 465 SER A 308
REMARK 465 LEU A 309
REMARK 465 ILE A 310
REMARK 465 SER A 311
REMARK 465 MET A 312
REMARK 465 LEU A 313
REMARK 465 LYS A 314
REMARK 465 CYS A 315
REMARK 465 PRO A 316
REMARK 465 ASN A 317
REMARK 465 SER A 318
REMARK 465 ALA A 319
REMARK 465 THR A 320
REMARK 465 SER A 321
REMARK 465 LEU A 322
REMARK 465 SER A 323
REMARK 465 GLN A 324
REMARK 465 ASP A 325
REMARK 465 ASN A 326
REMARK 465 ARG A 327
REMARK 465 LYS A 328
REMARK 465 LYS A 329
REMARK 465 GLU A 330
REMARK 465 GLN A 331
REMARK 465 ASP A 332
REMARK 465 GLY A 333
REMARK 465 GLY A 334
REMARK 465 ASP A 335
REMARK 465 PRO A 336
REMARK 465 ASN A 337
REMARK 465 GLU A 338
REMARK 465 GLU A 339
REMARK 465 THR A 340
REMARK 465 PRO A 341
REMARK 465 MET A 342
REMARK 465 GLY A 343
REMARK 465 ARG A 344
REMARK 465 PRO A 345
REMARK 465 LEU A 346
REMARK 465 GLU A 347
REMARK 465 VAL A 348
REMARK 465 LEU A 349
REMARK 465 PHE A 350
REMARK 465 GLN A 351
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 15 OG
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 50 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 54 CD NE CZ NH1 NH2
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 PRO A 135 CG CD
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 ARG A 168 CZ NH1 NH2
REMARK 470 GLU A 181 CD OE1 OE2
REMARK 470 TYR A 298 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS A 302 SG
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 PHE A 305 CG CD1 CD2 CE1 CE2 CZ
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 VAL A 99 -74.69 -123.44
REMARK 500 PHE A 300 78.79 -102.87
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 1203
REMARK 610 OLC A 1204
REMARK 610 OLC A 1205
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6AD A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NTJ RELATED DB: PDB
REMARK 900 RELATED ID: GPCR-87 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4PY0 RELATED DB: PDB
DBREF 4PXZ A 2 223 UNP Q9H244 P2Y12_HUMAN 2 223
DBREF 4PXZ A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 4PXZ A 224 342 UNP Q9H244 P2Y12_HUMAN 224 342
SEQADV 4PXZ ASP A -9 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ TYR A -8 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ LYS A -7 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ASP A -6 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ASP A -5 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ASP A -4 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ASP A -3 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ GLY A -2 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ALA A -1 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ PRO A 0 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 4PXZ ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 4PXZ LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 4PXZ ASN A 294 UNP Q9H244 ASP 294 ENGINEERED MUTATION
SEQADV 4PXZ GLY A 343 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ ARG A 344 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ PRO A 345 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ LEU A 346 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ GLU A 347 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ VAL A 348 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ LEU A 349 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ PHE A 350 UNP Q9H244 EXPRESSION TAG
SEQADV 4PXZ GLN A 351 UNP Q9H244 EXPRESSION TAG
SEQRES 1 A 466 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO GLN ALA VAL
SEQRES 2 A 466 ASP ASN LEU THR SER ALA PRO GLY ASN THR SER LEU CYS
SEQRES 3 A 466 THR ARG ASP TYR LYS ILE THR GLN VAL LEU PHE PRO LEU
SEQRES 4 A 466 LEU TYR THR VAL LEU PHE PHE VAL GLY LEU ILE THR ASN
SEQRES 5 A 466 GLY LEU ALA MET ARG ILE PHE PHE GLN ILE ARG SER LYS
SEQRES 6 A 466 SER ASN PHE ILE ILE PHE LEU LYS ASN THR VAL ILE SER
SEQRES 7 A 466 ASP LEU LEU MET ILE LEU THR PHE PRO PHE LYS ILE LEU
SEQRES 8 A 466 SER ASP ALA LYS LEU GLY THR GLY PRO LEU ARG THR PHE
SEQRES 9 A 466 VAL CYS GLN VAL THR SER VAL ILE PHE TYR PHE THR MET
SEQRES 10 A 466 TYR ILE SER ILE SER PHE LEU GLY LEU ILE THR ILE ASP
SEQRES 11 A 466 ARG TYR GLN LYS THR THR ARG PRO PHE LYS THR SER ASN
SEQRES 12 A 466 PRO LYS ASN LEU LEU GLY ALA LYS ILE LEU SER VAL VAL
SEQRES 13 A 466 ILE TRP ALA PHE MET PHE LEU LEU SER LEU PRO ASN MET
SEQRES 14 A 466 ILE LEU THR ASN ARG GLN PRO ARG ASP LYS ASN VAL LYS
SEQRES 15 A 466 LYS CYS SER PHE LEU LYS SER GLU PHE GLY LEU VAL TRP
SEQRES 16 A 466 HIS GLU ILE VAL ASN TYR ILE CYS GLN VAL ILE PHE TRP
SEQRES 17 A 466 ILE ASN PHE LEU ILE VAL ILE VAL CYS TYR THR LEU ILE
SEQRES 18 A 466 THR LYS GLU LEU TYR ARG SER TYR VAL ARG THR ALA ASP
SEQRES 19 A 466 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS
SEQRES 20 A 466 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP
SEQRES 21 A 466 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN
SEQRES 22 A 466 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP
SEQRES 23 A 466 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE
SEQRES 24 A 466 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN
SEQRES 25 A 466 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN
SEQRES 26 A 466 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU
SEQRES 27 A 466 ARG GLY VAL GLY LYS VAL PRO ARG LYS LYS VAL ASN VAL
SEQRES 28 A 466 LYS VAL PHE ILE ILE ILE ALA VAL PHE PHE ILE CYS PHE
SEQRES 29 A 466 VAL PRO PHE HIS PHE ALA ARG ILE PRO TYR THR LEU SER
SEQRES 30 A 466 GLN THR ARG ASP VAL PHE ASP CYS THR ALA GLU ASN THR
SEQRES 31 A 466 LEU PHE TYR VAL LYS GLU SER THR LEU TRP LEU THR SER
SEQRES 32 A 466 LEU ASN ALA CYS LEU ASN PRO PHE ILE TYR PHE PHE LEU
SEQRES 33 A 466 CYS LYS SER PHE ARG ASN SER LEU ILE SER MET LEU LYS
SEQRES 34 A 466 CYS PRO ASN SER ALA THR SER LEU SER GLN ASP ASN ARG
SEQRES 35 A 466 LYS LYS GLU GLN ASP GLY GLY ASP PRO ASN GLU GLU THR
SEQRES 36 A 466 PRO MET GLY ARG PRO LEU GLU VAL LEU PHE GLN
HET 6AD A1201 29
HET CLR A1202 28
HET OLC A1203 17
HET OLC A1204 17
HET OLC A1205 15
HET PEG A1206 7
HETNAM 6AD 2-(METHYLSULFANYL)ADENOSINE 5'-(TRIHYDROGEN
HETNAM 2 6AD DIPHOSPHATE)
HETNAM CLR CHOLESTEROL
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 6AD 2-METHYLTHIO-ADENOSINE-5'-DIPHOSPHATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 6AD C11 H17 N5 O10 P2 S
FORMUL 3 CLR C27 H46 O
FORMUL 4 OLC 3(C21 H40 O4)
FORMUL 7 PEG C4 H10 O3
FORMUL 8 HOH *49(H2 O)
HELIX 1 1 ILE A 23 PHE A 51 1 29
HELIX 2 2 SER A 57 LEU A 75 1 19
HELIX 3 3 THR A 76 LYS A 86 1 11
HELIX 4 4 GLY A 90 VAL A 99 1 10
HELIX 5 5 VAL A 99 ARG A 128 1 30
HELIX 6 6 LYS A 136 LEU A 162 1 27
HELIX 7 7 LYS A 174 LYS A 179 5 6
HELIX 8 8 SER A 180 LYS A 1019 1 63
HELIX 9 9 ASN A 1022 LYS A 1042 1 21
HELIX 10 10 SER A 1055 ASN A 1080 1 26
HELIX 11 11 LYS A 1083 GLU A 1092 1 10
HELIX 12 12 GLN A 1093 LYS A 1095 5 3
HELIX 13 13 THR A 1096 GLY A 227 1 15
HELIX 14 14 PRO A 230 VAL A 234 5 5
HELIX 15 15 ASN A 235 PHE A 249 1 15
HELIX 16 16 PHE A 249 ARG A 265 1 17
HELIX 17 17 ASP A 269 ASN A 294 1 26
HELIX 18 18 PRO A 295 PHE A 300 1 6
SSBOND 1 CYS A 17 CYS A 270 1555 1555 2.04
SSBOND 2 CYS A 97 CYS A 175 1555 1555 2.04
SITE 1 AC1 23 ARG A 93 CYS A 97 SER A 101 VAL A 102
SITE 2 AC1 23 TYR A 105 SER A 156 ASN A 159 LYS A 174
SITE 3 AC1 23 CYS A 175 LYS A 179 HIS A 187 VAL A 190
SITE 4 AC1 23 ASN A 191 CYS A 194 ARG A 256 TYR A 259
SITE 5 AC1 23 GLN A 263 LYS A 280 HOH A1319 HOH A1322
SITE 6 AC1 23 HOH A1331 HOH A1336 HOH A1348
SITE 1 AC2 7 SER A 55 ILE A 61 LYS A 64 ASN A 65
SITE 2 AC2 7 ILE A 68 TRP A 149 PHE A 153
SITE 1 AC3 3 GLN A 98 ILE A 161 ASN A 164
SITE 1 AC4 6 ARG A 231 VAL A 236 THR A 275 TYR A 278
SITE 2 AC4 6 SER A 282 OLC A1205
SITE 1 AC5 5 ASP A 20 ILE A 23 LEU A 27 SER A 282
SITE 2 AC5 5 OLC A1204
SITE 1 AC6 5 ASN A1022 GLN A1025 GLN A1041 ARG A1062
SITE 2 AC6 5 HOH A1315
CRYST1 65.110 104.170 169.430 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015359 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009600 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005902 0.00000
ATOM 1 N SER A 15 17.203 0.286 72.985 1.00 88.66 N
ANISOU 1 N SER A 15 11390 12620 9677 894 -499 -753 N
ATOM 2 CA SER A 15 16.713 1.342 73.869 1.00 89.49 C
ANISOU 2 CA SER A 15 11570 12752 9682 975 -502 -869 C
ATOM 3 C SER A 15 17.885 2.188 74.412 1.00 92.47 C
ANISOU 3 C SER A 15 12053 13054 10026 889 -533 -934 C
ATOM 4 O SER A 15 18.028 3.351 74.013 1.00 92.90 O
ANISOU 4 O SER A 15 12259 12955 10083 912 -536 -1019 O
ATOM 5 CB SER A 15 15.889 0.750 75.014 1.00 93.71 C
ANISOU 5 CB SER A 15 11993 13485 10127 1016 -473 -867 C
ATOM 6 N LEU A 16 18.740 1.590 75.287 1.00 86.67 N
ANISOU 6 N LEU A 16 11241 12434 9255 787 -548 -892 N
ATOM 7 CA LEU A 16 19.925 2.231 75.882 1.00 85.77 C
ANISOU 7 CA LEU A 16 11185 12314 9090 680 -579 -956 C
ATOM 8 C LEU A 16 21.024 2.476 74.835 1.00 84.88 C
ANISOU 8 C LEU A 16 11139 12048 9064 580 -602 -940 C
ATOM 9 O LEU A 16 21.948 3.263 75.076 1.00 85.05 O
ANISOU 9 O LEU A 16 11235 12030 9048 478 -620 -1024 O
ATOM 10 CB LEU A 16 20.481 1.371 77.027 1.00 86.09 C
ANISOU 10 CB LEU A 16 11093 12563 9056 622 -590 -892 C
ATOM 11 CG LEU A 16 20.582 2.069 78.379 1.00 92.47 C
ANISOU 11 CG LEU A 16 11911 13500 9722 621 -596 -1002 C
ATOM 12 CD1 LEU A 16 19.346 1.824 79.212 1.00 92.92 C
ANISOU 12 CD1 LEU A 16 11902 13686 9719 735 -561 -990 C
ATOM 13 CD2 LEU A 16 21.794 1.589 79.146 1.00 95.69 C
ANISOU 13 CD2 LEU A 16 12231 14072 10054 515 -629 -971 C
ATOM 14 N CYS A 17 20.911 1.797 73.676 1.00 76.69 N
ANISOU 14 N CYS A 17 10070 10934 8135 597 -594 -841 N
ATOM 15 CA CYS A 17 21.842 1.910 72.562 1.00 74.07 C
ANISOU 15 CA CYS A 17 9790 10461 7891 516 -610 -810 C
ATOM 16 C CYS A 17 21.623 3.215 71.798 1.00 78.30 C
ANISOU 16 C CYS A 17 10506 10798 8447 549 -599 -909 C
ATOM 17 O CYS A 17 20.488 3.557 71.449 1.00 77.82 O
ANISOU 17 O CYS A 17 10496 10687 8386 684 -575 -933 O
ATOM 18 CB CYS A 17 21.734 0.705 71.631 1.00 71.61 C
ANISOU 18 CB CYS A 17 9386 10143 7679 530 -597 -678 C
ATOM 19 SG CYS A 17 22.739 0.849 70.130 1.00 73.72 S
ANISOU 19 SG CYS A 17 9712 10243 8055 446 -612 -637 S
ATOM 20 N THR A 18 22.734 3.907 71.509 1.00 74.99 N
ANISOU 20 N THR A 18 10182 10275 8036 428 -609 -959 N
ATOM 21 CA THR A 18 22.775 5.168 70.764 1.00 75.16 C
ANISOU 21 CA THR A 18 10403 10077 8076 432 -582 -1044 C
ATOM 22 C THR A 18 23.545 4.964 69.458 1.00 75.98 C
ANISOU 22 C THR A 18 10526 10063 8280 360 -588 -971 C
ATOM 23 O THR A 18 24.583 4.299 69.446 1.00 76.02 O
ANISOU 23 O THR A 18 10431 10146 8308 235 -615 -917 O
ATOM 24 CB THR A 18 23.374 6.318 71.625 1.00 88.37 C
ANISOU 24 CB THR A 18 12204 11714 9660 328 -567 -1193 C
ATOM 25 OG1 THR A 18 23.717 7.419 70.778 1.00 91.64 O
ANISOU 25 OG1 THR A 18 12826 11888 10106 291 -525 -1257 O
ATOM 26 CG2 THR A 18 24.609 5.896 72.441 1.00 86.55 C
ANISOU 26 CG2 THR A 18 11853 11653 9380 149 -605 -1201 C
ATOM 27 N ARG A 19 23.034 5.545 68.367 1.00 69.75 N
ANISOU 27 N ARG A 19 9862 9100 7540 453 -559 -967 N
ATOM 28 CA ARG A 19 23.657 5.485 67.046 1.00 67.56 C
ANISOU 28 CA ARG A 19 9622 8697 7350 400 -557 -904 C
ATOM 29 C ARG A 19 24.118 6.888 66.642 1.00 72.79 C
ANISOU 29 C ARG A 19 10516 9141 8001 347 -513 -993 C
ATOM 30 O ARG A 19 23.327 7.835 66.690 1.00 73.32 O
ANISOU 30 O ARG A 19 10741 9090 8026 469 -468 -1059 O
ATOM 31 CB ARG A 19 22.673 4.899 66.019 1.00 62.94 C
ANISOU 31 CB ARG A 19 8987 8106 6823 550 -555 -816 C
ATOM 32 CG ARG A 19 23.273 4.583 64.650 1.00 57.36 C
ANISOU 32 CG ARG A 19 8277 7312 6206 499 -559 -735 C
ATOM 33 CD ARG A 19 22.295 3.777 63.821 1.00 52.30 C
ANISOU 33 CD ARG A 19 7541 6726 5605 624 -561 -658 C
ATOM 34 NE ARG A 19 22.219 2.378 64.245 1.00 51.16 N
ANISOU 34 NE ARG A 19 7203 6753 5483 588 -578 -592 N
ATOM 35 CZ ARG A 19 21.319 1.504 63.801 1.00 64.00 C
ANISOU 35 CZ ARG A 19 8721 8464 7132 663 -571 -543 C
ATOM 36 NH1 ARG A 19 20.401 1.875 62.918 1.00 45.30 N
ANISOU 36 NH1 ARG A 19 6393 6062 4759 787 -560 -552 N
ATOM 37 NH2 ARG A 19 21.328 0.252 64.242 1.00 53.96 N
ANISOU 37 NH2 ARG A 19 7303 7320 5880 613 -566 -485 N
ATOM 38 N ASP A 20 25.399 7.024 66.266 1.00 69.87 N
ANISOU 38 N ASP A 20 10168 8718 7661 167 -514 -996 N
ATOM 39 CA ASP A 20 25.957 8.306 65.843 1.00 71.48 C
ANISOU 39 CA ASP A 20 10597 8704 7856 77 -457 -1081 C
ATOM 40 C ASP A 20 25.516 8.607 64.401 1.00 74.81 C
ANISOU 40 C ASP A 20 11141 8942 8343 195 -421 -1011 C
ATOM 41 O ASP A 20 25.888 7.885 63.468 1.00 73.44 O
ANISOU 41 O ASP A 20 10876 8788 8241 168 -447 -912 O
ATOM 42 CB ASP A 20 27.494 8.316 65.982 1.00 74.13 C
ANISOU 42 CB ASP A 20 10892 9086 8189 -176 -469 -1116 C
ATOM 43 CG ASP A 20 28.155 9.622 65.587 1.00 87.75 C
ANISOU 43 CG ASP A 20 12851 10591 9900 -315 -395 -1216 C
ATOM 44 OD1 ASP A 20 27.751 10.677 66.121 1.00 89.80 O
ANISOU 44 OD1 ASP A 20 13301 10718 10100 -294 -334 -1331 O
ATOM 45 OD2 ASP A 20 29.089 9.586 64.759 1.00 95.46 O
ANISOU 45 OD2 ASP A 20 13825 11523 10922 -453 -389 -1184 O
ATOM 46 N TYR A 21 24.685 9.651 64.242 1.00 71.43 N
ANISOU 46 N TYR A 21 10917 8344 7878 344 -359 -1058 N
ATOM 47 CA TYR A 21 24.134 10.077 62.956 1.00 70.66 C
ANISOU 47 CA TYR A 21 10954 8081 7813 498 -318 -992 C
ATOM 48 C TYR A 21 24.781 11.397 62.472 1.00 76.07 C
ANISOU 48 C TYR A 21 11923 8490 8490 414 -225 -1050 C
ATOM 49 O TYR A 21 24.355 11.936 61.450 1.00 76.42 O
ANISOU 49 O TYR A 21 12121 8372 8546 555 -174 -996 O
ATOM 50 CB TYR A 21 22.591 10.242 63.052 1.00 71.32 C
ANISOU 50 CB TYR A 21 11057 8194 7846 775 -306 -983 C
ATOM 51 CG TYR A 21 21.789 8.960 63.185 1.00 70.07 C
ANISOU 51 CG TYR A 21 10637 8284 7700 872 -377 -912 C
ATOM 52 CD1 TYR A 21 21.639 8.092 62.104 1.00 70.21 C
ANISOU 52 CD1 TYR A 21 10528 8368 7781 910 -411 -805 C
ATOM 53 CD2 TYR A 21 21.097 8.665 64.357 1.00 70.36 C
ANISOU 53 CD2 TYR A 21 10571 8483 7680 930 -399 -958 C
ATOM 54 CE1 TYR A 21 20.866 6.936 62.204 1.00 68.93 C
ANISOU 54 CE1 TYR A 21 10143 8419 7626 978 -458 -753 C
ATOM 55 CE2 TYR A 21 20.323 7.511 64.471 1.00 70.01 C
ANISOU 55 CE2 TYR A 21 10302 8655 7643 1004 -446 -897 C
ATOM 56 CZ TYR A 21 20.206 6.651 63.389 1.00 78.32 C
ANISOU 56 CZ TYR A 21 11237 9761 8760 1021 -472 -798 C
ATOM 57 OH TYR A 21 19.443 5.512 63.490 1.00 80.48 O
ANISOU 57 OH TYR A 21 11303 10237 9040 1069 -503 -751 O
ATOM 58 N LYS A 22 25.816 11.895 63.180 1.00 73.05 N
ANISOU 58 N LYS A 22 11608 8065 8081 180 -198 -1159 N
ATOM 59 CA LYS A 22 26.487 13.161 62.859 1.00 74.52 C
ANISOU 59 CA LYS A 22 12075 7985 8253 53 -93 -1238 C
ATOM 60 C LYS A 22 27.264 13.113 61.539 1.00 78.41 C
ANISOU 60 C LYS A 22 12603 8373 8815 -38 -74 -1152 C
ATOM 61 O LYS A 22 27.290 14.115 60.827 1.00 79.53 O
ANISOU 61 O LYS A 22 13008 8257 8955 -9 26 -1154 O
ATOM 62 CB LYS A 22 27.406 13.610 64.000 1.00 77.56 C
ANISOU 62 CB LYS A 22 12489 8400 8581 -208 -72 -1394 C
ATOM 63 CG LYS A 22 26.640 14.183 65.189 1.00 80.61 C
ANISOU 63 CG LYS A 22 12961 8785 8882 -119 -42 -1510 C
ATOM 64 CD LYS A 22 27.557 14.746 66.279 1.00 91.88 C
ANISOU 64 CD LYS A 22 14441 10232 10237 -390 -9 -1687 C
ATOM 65 CE LYS A 22 28.204 13.715 67.182 1.00 99.78 C
ANISOU 65 CE LYS A 22 15134 11566 11213 -545 -119 -1699 C
ATOM 66 NZ LYS A 22 27.206 12.932 67.964 1.00105.94 N
ANISOU 66 NZ LYS A 22 15729 12557 11966 -351 -196 -1654 N
ATOM 67 N ILE A 23 27.891 11.977 61.216 1.00 74.14 N
ANISOU 67 N ILE A 23 11817 8023 8331 -136 -160 -1073 N
ATOM 68 CA ILE A 23 28.623 11.808 59.953 1.00 73.97 C
ANISOU 68 CA ILE A 23 11800 7932 8374 -214 -150 -987 C
ATOM 69 C ILE A 23 27.594 11.409 58.864 1.00 77.08 C
ANISOU 69 C ILE A 23 12177 8306 8806 48 -166 -855 C
ATOM 70 O ILE A 23 27.674 11.889 57.734 1.00 77.64 O
ANISOU 70 O ILE A 23 12396 8208 8897 88 -110 -797 O
ATOM 71 CB ILE A 23 29.803 10.793 60.110 1.00 76.08 C
ANISOU 71 CB ILE A 23 11814 8418 8675 -424 -226 -965 C
ATOM 72 CG1 ILE A 23 30.899 11.365 61.037 1.00 78.03 C
ANISOU 72 CG1 ILE A 23 12088 8696 8863 -695 -201 -1106 C
ATOM 73 CG2 ILE A 23 30.414 10.383 58.757 1.00 75.75 C
ANISOU 73 CG2 ILE A 23 11736 8341 8702 -466 -227 -860 C
ATOM 74 CD1 ILE A 23 31.282 10.475 62.188 1.00 85.62 C
ANISOU 74 CD1 ILE A 23 12793 9951 9789 -767 -289 -1132 C
ATOM 75 N THR A 24 26.605 10.576 59.239 1.00 71.52 N
ANISOU 75 N THR A 24 11296 7782 8097 220 -236 -815 N
ATOM 76 CA THR A 24 25.517 10.093 58.396 1.00 69.74 C
ANISOU 76 CA THR A 24 11006 7604 7886 458 -260 -714 C
ATOM 77 C THR A 24 24.678 11.282 57.841 1.00 73.82 C
ANISOU 77 C THR A 24 11783 7914 8351 669 -175 -710 C
ATOM 78 O THR A 24 24.391 11.290 56.645 1.00 73.43 O
ANISOU 78 O THR A 24 11767 7818 8315 794 -163 -619 O
ATOM 79 CB THR A 24 24.686 9.058 59.201 1.00 78.10 C
ANISOU 79 CB THR A 24 11832 8907 8935 550 -336 -706 C
ATOM 80 OG1 THR A 24 24.976 7.748 58.710 1.00 77.23 O
ANISOU 80 OG1 THR A 24 11499 8955 8890 494 -399 -622 O
ATOM 81 CG2 THR A 24 23.173 9.309 59.167 1.00 78.14 C
ANISOU 81 CG2 THR A 24 11867 8939 8885 822 -325 -696 C
ATOM 82 N GLN A 25 24.320 12.280 58.685 1.00 70.54 N
ANISOU 82 N GLN A 25 11555 7378 7870 716 -111 -805 N
ATOM 83 CA GLN A 25 23.498 13.432 58.285 1.00 71.51 C
ANISOU 83 CA GLN A 25 11942 7297 7930 945 -16 -800 C
ATOM 84 C GLN A 25 24.234 14.423 57.343 1.00 76.33 C
ANISOU 84 C GLN A 25 12830 7620 8552 875 92 -779 C
ATOM 85 O GLN A 25 23.578 15.263 56.723 1.00 77.53 O
ANISOU 85 O GLN A 25 13202 7599 8655 1094 176 -734 O
ATOM 86 CB GLN A 25 22.949 14.182 59.514 1.00 74.13 C
ANISOU 86 CB GLN A 25 12401 7578 8186 1015 32 -915 C
ATOM 87 CG GLN A 25 24.011 14.910 60.350 1.00 88.80 C
ANISOU 87 CG GLN A 25 14418 9287 10035 747 96 -1050 C
ATOM 88 CD GLN A 25 23.505 16.093 61.141 1.00104.38 C
ANISOU 88 CD GLN A 25 16652 11083 11927 842 200 -1161 C
ATOM 89 OE1 GLN A 25 24.288 16.950 61.557 1.00101.26 O
ANISOU 89 OE1 GLN A 25 16461 10499 11512 642 288 -1275 O
ATOM 90 NE2 GLN A 25 22.200 16.179 61.374 1.00 93.78 N
ANISOU 90 NE2 GLN A 25 15308 9799 10526 1139 199 -1140 N
ATOM 91 N VAL A 26 25.569 14.334 57.239 1.00 71.63 N
ANISOU 91 N VAL A 26 12224 6982 8009 581 95 -806 N
ATOM 92 CA VAL A 26 26.332 15.227 56.372 1.00 72.33 C
ANISOU 92 CA VAL A 26 12567 6808 8109 476 204 -791 C
ATOM 93 C VAL A 26 26.810 14.456 55.131 1.00 74.39 C
ANISOU 93 C VAL A 26 12685 7147 8434 437 154 -670 C
ATOM 94 O VAL A 26 26.684 14.970 54.019 1.00 74.62 O
ANISOU 94 O VAL A 26 12884 7013 8455 546 223 -586 O
ATOM 95 CB VAL A 26 27.512 15.922 57.113 1.00 77.50 C
ANISOU 95 CB VAL A 26 13357 7334 8757 154 275 -932 C
ATOM 96 CG1 VAL A 26 28.183 16.972 56.223 1.00 79.05 C
ANISOU 96 CG1 VAL A 26 13855 7226 8953 48 416 -923 C
ATOM 97 CG2 VAL A 26 27.049 16.555 58.425 1.00 78.51 C
ANISOU 97 CG2 VAL A 26 13598 7416 8817 179 317 -1067 C
ATOM 98 N LEU A 27 27.346 13.234 55.317 1.00 68.45 N
ANISOU 98 N LEU A 27 11631 6641 7738 297 41 -656 N
ATOM 99 CA LEU A 27 27.876 12.438 54.219 1.00 66.91 C
ANISOU 99 CA LEU A 27 11291 6528 7603 245 -5 -555 C
ATOM 100 C LEU A 27 26.775 11.905 53.289 1.00 69.38 C
ANISOU 100 C LEU A 27 11519 6928 7912 519 -46 -440 C
ATOM 101 O LEU A 27 26.853 12.170 52.088 1.00 69.68 O
ANISOU 101 O LEU A 27 11658 6865 7954 583 -3 -357 O
ATOM 102 CB LEU A 27 28.755 11.282 54.736 1.00 65.59 C
ANISOU 102 CB LEU A 27 10841 6592 7487 35 -100 -573 C
ATOM 103 CG LEU A 27 29.421 10.381 53.681 1.00 69.41 C
ANISOU 103 CG LEU A 27 11163 7174 8036 -29 -145 -476 C
ATOM 104 CD1 LEU A 27 30.660 11.041 53.080 1.00 71.07 C
ANISOU 104 CD1 LEU A 27 11511 7233 8259 -235 -72 -482 C
ATOM 105 CD2 LEU A 27 29.785 9.032 54.269 1.00 69.48 C
ANISOU 105 CD2 LEU A 27 10876 7440 8083 -118 -243 -472 C
ATOM 106 N PHE A 28 25.776 11.159 53.815 1.00 63.73 N
ANISOU 106 N PHE A 28 10615 6415 7183 670 -123 -439 N
ATOM 107 CA PHE A 28 24.748 10.538 52.968 1.00 62.17 C
ANISOU 107 CA PHE A 28 10295 6353 6974 897 -168 -349 C
ATOM 108 C PHE A 28 23.812 11.555 52.274 1.00 67.33 C
ANISOU 108 C PHE A 28 11162 6873 7546 1170 -95 -302 C
ATOM 109 O PHE A 28 23.742 11.460 51.045 1.00 66.60 O
ANISOU 109 O PHE A 28 11070 6784 7451 1258 -91 -211 O
ATOM 110 CB PHE A 28 23.980 9.430 53.695 1.00 62.25 C
ANISOU 110 CB PHE A 28 10045 6621 6986 953 -256 -368 C
ATOM 111 CG PHE A 28 24.862 8.218 53.856 1.00 61.72 C
ANISOU 111 CG PHE A 28 9757 6697 6999 741 -322 -360 C
ATOM 112 CD1 PHE A 28 25.199 7.431 52.758 1.00 63.85 C
ANISOU 112 CD1 PHE A 28 9912 7028 7319 706 -348 -284 C
ATOM 113 CD2 PHE A 28 25.424 7.905 55.087 1.00 63.07 C
ANISOU 113 CD2 PHE A 28 9844 6935 7184 581 -349 -428 C
ATOM 114 CE1 PHE A 28 26.060 6.337 52.899 1.00 63.32 C
ANISOU 114 CE1 PHE A 28 9661 7076 7320 528 -394 -272 C
ATOM 115 CE2 PHE A 28 26.283 6.812 55.226 1.00 64.26 C
ANISOU 115 CE2 PHE A 28 9803 7218 7397 413 -399 -406 C
ATOM 116 CZ PHE A 28 26.590 6.032 54.133 1.00 61.44 C
ANISOU 116 CZ PHE A 28 9344 6907 7093 393 -418 -327 C
ATOM 117 N PRO A 29 23.181 12.575 52.925 1.00 65.76 N
ANISOU 117 N PRO A 29 11163 6547 7277 1312 -28 -352 N
ATOM 118 CA PRO A 29 22.388 13.548 52.148 1.00 67.51 C
ANISOU 118 CA PRO A 29 11603 6634 7414 1596 54 -285 C
ATOM 119 C PRO A 29 23.211 14.241 51.051 1.00 73.20 C
ANISOU 119 C PRO A 29 12546 7120 8148 1534 143 -216 C
ATOM 120 O PRO A 29 22.680 14.429 49.964 1.00 73.61 O
ANISOU 120 O PRO A 29 12649 7170 8149 1747 165 -113 O
ATOM 121 CB PRO A 29 21.908 14.541 53.213 1.00 70.62 C
ANISOU 121 CB PRO A 29 12198 6891 7743 1694 128 -369 C
ATOM 122 CG PRO A 29 21.848 13.726 54.454 1.00 73.37 C
ANISOU 122 CG PRO A 29 12320 7436 8123 1560 40 -462 C
ATOM 123 CD PRO A 29 23.094 12.886 54.365 1.00 67.42 C
ANISOU 123 CD PRO A 29 11412 6737 7467 1249 -17 -466 C
ATOM 124 N LEU A 30 24.509 14.549 51.303 1.00 70.59 N
ANISOU 124 N LEU A 30 12321 6623 7876 1236 189 -272 N
ATOM 125 CA LEU A 30 25.419 15.167 50.327 1.00 71.77 C
ANISOU 125 CA LEU A 30 12671 6554 8043 1120 281 -219 C
ATOM 126 C LEU A 30 25.709 14.202 49.163 1.00 73.43 C
ANISOU 126 C LEU A 30 12676 6925 8298 1096 206 -120 C
ATOM 127 O LEU A 30 25.733 14.637 48.008 1.00 73.77 O
ANISOU 127 O LEU A 30 12859 6857 8312 1196 268 -23 O
ATOM 128 CB LEU A 30 26.725 15.616 51.020 1.00 72.99 C
ANISOU 128 CB LEU A 30 12933 6557 8244 773 337 -329 C
ATOM 129 CG LEU A 30 28.028 15.700 50.201 1.00 79.03 C
ANISOU 129 CG LEU A 30 13761 7211 9057 522 386 -302 C
ATOM 130 CD1 LEU A 30 28.140 17.027 49.453 1.00 81.59 C
ANISOU 130 CD1 LEU A 30 14466 7203 9332 589 554 -252 C
ATOM 131 CD2 LEU A 30 29.243 15.513 51.104 1.00 82.98 C
ANISOU 131 CD2 LEU A 30 14185 7741 9601 161 374 -427 C
ATOM 132 N LEU A 31 25.913 12.897 49.468 1.00 67.26 N
ANISOU 132 N LEU A 31 11575 6401 7581 972 83 -143 N
ATOM 133 CA LEU A 31 26.165 11.852 48.467 1.00 64.81 C
ANISOU 133 CA LEU A 31 11052 6257 7315 940 11 -66 C
ATOM 134 C LEU A 31 24.923 11.585 47.614 1.00 66.98 C
ANISOU 134 C LEU A 31 11258 6666 7526 1239 -20 18 C
ATOM 135 O LEU A 31 25.047 11.402 46.403 1.00 67.81 O
ANISOU 135 O LEU A 31 11350 6789 7625 1284 -16 103 O
ATOM 136 CB LEU A 31 26.608 10.537 49.134 1.00 63.03 C
ANISOU 136 CB LEU A 31 10529 6256 7165 758 -95 -114 C
ATOM 137 CG LEU A 31 28.066 10.377 49.584 1.00 67.58 C
ANISOU 137 CG LEU A 31 11071 6799 7805 444 -92 -166 C
ATOM 138 CD1 LEU A 31 28.249 9.050 50.301 1.00 65.49 C
ANISOU 138 CD1 LEU A 31 10516 6775 7594 345 -193 -195 C
ATOM 139 CD2 LEU A 31 29.039 10.441 48.405 1.00 70.71 C
ANISOU 139 CD2 LEU A 31 11518 7117 8233 326 -54 -101 C
ATOM 140 N TYR A 32 23.733 11.552 48.246 1.00 61.07 N
ANISOU 140 N TYR A 32 10451 6033 6720 1441 -50 -11 N
ATOM 141 CA TYR A 32 22.470 11.282 47.564 1.00 59.90 C
ANISOU 141 CA TYR A 32 10203 6067 6491 1725 -85 50 C
ATOM 142 C TYR A 32 21.994 12.477 46.721 1.00 67.36 C
ANISOU 142 C TYR A 32 11413 6849 7332 1984 12 134 C
ATOM 143 O TYR A 32 21.427 12.243 45.649 1.00 67.84 O
ANISOU 143 O TYR A 32 11400 7047 7328 2169 -8 215 O
ATOM 144 CB TYR A 32 21.385 10.839 48.557 1.00 59.14 C
ANISOU 144 CB TYR A 32 9938 6173 6359 1839 -145 -15 C
ATOM 145 CG TYR A 32 21.396 9.347 48.811 1.00 56.57 C
ANISOU 145 CG TYR A 32 9294 6098 6101 1692 -247 -49 C
ATOM 146 CD1 TYR A 32 20.803 8.462 47.911 1.00 57.14 C
ANISOU 146 CD1 TYR A 32 9164 6396 6151 1774 -302 -9 C
ATOM 147 CD2 TYR A 32 22.041 8.813 49.923 1.00 55.17 C
ANISOU 147 CD2 TYR A 32 9026 5932 6003 1467 -280 -121 C
ATOM 148 CE1 TYR A 32 20.839 7.085 48.122 1.00 54.53 C
ANISOU 148 CE1 TYR A 32 8571 6263 5884 1628 -373 -43 C
ATOM 149 CE2 TYR A 32 22.070 7.438 50.152 1.00 53.46 C
ANISOU 149 CE2 TYR A 32 8545 5922 5845 1346 -354 -139 C
ATOM 150 CZ TYR A 32 21.463 6.578 49.251 1.00 57.18 C
ANISOU 150 CZ TYR A 32 8840 6584 6302 1423 -395 -101 C
ATOM 151 OH TYR A 32 21.489 5.220 49.461 1.00 52.64 O
ANISOU 151 OH TYR A 32 8032 6184 5786 1295 -447 -123 O
ATOM 152 N THR A 33 22.243 13.739 47.175 1.00 65.32 N
ANISOU 152 N THR A 33 11466 6302 7049 1997 126 116 N
ATOM 153 CA THR A 33 21.894 14.963 46.432 1.00 67.45 C
ANISOU 153 CA THR A 33 12041 6364 7221 2242 247 207 C
ATOM 154 C THR A 33 22.604 14.943 45.065 1.00 72.01 C
ANISOU 154 C THR A 33 12672 6877 7812 2185 277 309 C
ATOM 155 O THR A 33 21.952 15.177 44.043 1.00 72.44 O
ANISOU 155 O THR A 33 12770 6984 7771 2450 299 418 O
ATOM 156 CB THR A 33 22.236 16.226 47.251 1.00 75.44 C
ANISOU 156 CB THR A 33 13392 7048 8225 2200 379 148 C
ATOM 157 OG1 THR A 33 21.450 16.228 48.440 1.00 75.90 O
ANISOU 157 OG1 THR A 33 13390 7196 8254 2296 348 60 O
ATOM 158 CG2 THR A 33 21.978 17.525 46.487 1.00 75.17 C
ANISOU 158 CG2 THR A 33 13720 6748 8093 2444 532 249 C
ATOM 159 N VAL A 34 23.922 14.622 45.054 1.00 67.93 N
ANISOU 159 N VAL A 34 12129 6278 7403 1848 273 275 N
ATOM 160 CA VAL A 34 24.733 14.514 43.837 1.00 67.75 C
ANISOU 160 CA VAL A 34 12134 6205 7403 1748 299 359 C
ATOM 161 C VAL A 34 24.071 13.476 42.921 1.00 71.60 C
ANISOU 161 C VAL A 34 12345 7000 7860 1895 192 423 C
ATOM 162 O VAL A 34 23.747 13.811 41.784 1.00 72.60 O
ANISOU 162 O VAL A 34 12555 7123 7905 2087 231 532 O
ATOM 163 CB VAL A 34 26.228 14.175 44.133 1.00 70.52 C
ANISOU 163 CB VAL A 34 12442 6481 7871 1353 296 293 C
ATOM 164 CG1 VAL A 34 27.023 13.956 42.844 1.00 69.96 C
ANISOU 164 CG1 VAL A 34 12362 6398 7821 1256 313 380 C
ATOM 165 CG2 VAL A 34 26.887 15.257 44.982 1.00 71.77 C
ANISOU 165 CG2 VAL A 34 12878 6350 8043 1187 412 215 C
ATOM 166 N LEU A 35 23.782 12.261 43.453 1.00 66.44 N
ANISOU 166 N LEU A 35 11375 6611 7257 1818 68 353 N
ATOM 167 CA LEU A 35 23.142 11.172 42.712 1.00 64.92 C
ANISOU 167 CA LEU A 35 10906 6721 7040 1912 -29 382 C
ATOM 168 C LEU A 35 21.740 11.528 42.204 1.00 69.89 C
ANISOU 168 C LEU A 35 11538 7493 7524 2275 -28 441 C
ATOM 169 O LEU A 35 21.355 11.040 41.142 1.00 69.27 O
ANISOU 169 O LEU A 35 11327 7604 7388 2380 -67 497 O
ATOM 170 CB LEU A 35 23.065 9.889 43.551 1.00 63.05 C
ANISOU 170 CB LEU A 35 10373 6701 6883 1755 -135 287 C
ATOM 171 CG LEU A 35 24.332 9.033 43.715 1.00 66.19 C
ANISOU 171 CG LEU A 35 10651 7090 7410 1433 -168 249 C
ATOM 172 CD1 LEU A 35 23.953 7.603 44.058 1.00 64.77 C
ANISOU 172 CD1 LEU A 35 10166 7170 7275 1369 -265 196 C
ATOM 173 CD2 LEU A 35 25.197 9.018 42.451 1.00 68.05 C
ANISOU 173 CD2 LEU A 35 10933 7261 7664 1349 -137 324 C
ATOM 174 N PHE A 36 20.985 12.368 42.941 1.00 67.83 N
ANISOU 174 N PHE A 36 11419 7160 7192 2470 16 425 N
ATOM 175 CA PHE A 36 19.644 12.790 42.531 1.00 69.10 C
ANISOU 175 CA PHE A 36 11587 7471 7198 2845 23 484 C
ATOM 176 C PHE A 36 19.705 13.673 41.272 1.00 75.59 C
ANISOU 176 C PHE A 36 12637 8163 7921 3046 115 623 C
ATOM 177 O PHE A 36 18.980 13.401 40.312 1.00 75.83 O
ANISOU 177 O PHE A 36 12538 8431 7842 3258 77 690 O
ATOM 178 CB PHE A 36 18.905 13.514 43.673 1.00 71.94 C
ANISOU 178 CB PHE A 36 12063 7764 7506 3007 62 434 C
ATOM 179 CG PHE A 36 17.539 14.050 43.301 1.00 75.23 C
ANISOU 179 CG PHE A 36 12502 8334 7747 3422 81 500 C
ATOM 180 CD1 PHE A 36 16.462 13.189 43.112 1.00 77.52 C
ANISOU 180 CD1 PHE A 36 12474 9021 7959 3559 -22 478 C
ATOM 181 CD2 PHE A 36 17.329 15.415 43.141 1.00 79.87 C
ANISOU 181 CD2 PHE A 36 13431 8679 8239 3678 212 584 C
ATOM 182 CE1 PHE A 36 15.204 13.682 42.757 1.00 80.43 C
ANISOU 182 CE1 PHE A 36 12837 9576 8146 3952 -7 537 C
ATOM 183 CE2 PHE A 36 16.066 15.910 42.792 1.00 84.71 C
ANISOU 183 CE2 PHE A 36 14058 9454 8674 4096 233 656 C
ATOM 184 CZ PHE A 36 15.010 15.042 42.614 1.00 82.21 C
ANISOU 184 CZ PHE A 36 13396 9568 8273 4233 117 631 C
ATOM 185 N PHE A 37 20.568 14.708 41.267 1.00 73.88 N
ANISOU 185 N PHE A 37 12755 7581 7735 2972 241 663 N
ATOM 186 CA PHE A 37 20.689 15.603 40.112 1.00 75.94 C
ANISOU 186 CA PHE A 37 13273 7677 7905 3154 351 804 C
ATOM 187 C PHE A 37 21.377 14.891 38.944 1.00 79.99 C
ANISOU 187 C PHE A 37 13654 8288 8452 3005 309 857 C
ATOM 188 O PHE A 37 20.895 15.013 37.817 1.00 81.09 O
ANISOU 188 O PHE A 37 13804 8533 8472 3240 324 970 O
ATOM 189 CB PHE A 37 21.389 16.924 40.474 1.00 79.29 C
ANISOU 189 CB PHE A 37 14112 7664 8351 3094 517 821 C
ATOM 190 CG PHE A 37 20.550 17.785 41.391 1.00 82.34 C
ANISOU 190 CG PHE A 37 14682 7938 8665 3326 586 794 C
ATOM 191 CD1 PHE A 37 19.440 18.471 40.908 1.00 87.55 C
ANISOU 191 CD1 PHE A 37 15458 8650 9157 3761 641 902 C
ATOM 192 CD2 PHE A 37 20.860 17.900 42.739 1.00 83.72 C
ANISOU 192 CD2 PHE A 37 14908 7972 8928 3122 598 660 C
ATOM 193 CE1 PHE A 37 18.651 19.245 41.762 1.00 89.95 C
ANISOU 193 CE1 PHE A 37 15930 8858 9390 3994 709 877 C
ATOM 194 CE2 PHE A 37 20.073 18.680 43.591 1.00 87.98 C
ANISOU 194 CE2 PHE A 37 15618 8411 9397 3339 665 627 C
ATOM 195 CZ PHE A 37 18.973 19.343 43.098 1.00 88.25 C
ANISOU 195 CZ PHE A 37 15771 8489 9272 3776 722 736 C
ATOM 196 N VAL A 38 22.446 14.098 39.209 1.00 74.79 N
ANISOU 196 N VAL A 38 12851 7623 7942 2637 254 776 N
ATOM 197 CA VAL A 38 23.142 13.315 38.176 1.00 73.68 C
ANISOU 197 CA VAL A 38 12563 7588 7844 2478 210 811 C
ATOM 198 C VAL A 38 22.137 12.300 37.573 1.00 77.77 C
ANISOU 198 C VAL A 38 12763 8499 8288 2638 92 811 C
ATOM 199 O VAL A 38 22.078 12.165 36.354 1.00 77.99 O
ANISOU 199 O VAL A 38 12752 8637 8242 2734 91 894 O
ATOM 200 CB VAL A 38 24.446 12.628 38.700 1.00 75.53 C
ANISOU 200 CB VAL A 38 12703 7750 8245 2073 179 721 C
ATOM 201 CG1 VAL A 38 25.027 11.653 37.675 1.00 73.77 C
ANISOU 201 CG1 VAL A 38 12279 7688 8061 1935 120 745 C
ATOM 202 CG2 VAL A 38 25.497 13.664 39.088 1.00 76.48 C
ANISOU 202 CG2 VAL A 38 13132 7511 8415 1896 305 720 C
ATOM 203 N GLY A 39 21.333 11.662 38.429 1.00 73.74 N
ANISOU 203 N GLY A 39 12038 8196 7783 2666 6 717 N
ATOM 204 CA GLY A 39 20.316 10.693 38.029 1.00 73.23 C
ANISOU 204 CA GLY A 39 11665 8513 7646 2784 -98 688 C
ATOM 205 C GLY A 39 19.142 11.261 37.248 1.00 80.30 C
ANISOU 205 C GLY A 39 12582 9582 8345 3169 -83 776 C
ATOM 206 O GLY A 39 18.637 10.596 36.337 1.00 79.24 O
ANISOU 206 O GLY A 39 12234 9746 8128 3248 -145 786 O
ATOM 207 N LEU A 40 18.682 12.488 37.605 1.00 80.00 N
ANISOU 207 N LEU A 40 12802 9374 8221 3420 5 837 N
ATOM 208 CA LEU A 40 17.566 13.160 36.921 1.00 82.57 C
ANISOU 208 CA LEU A 40 13178 9853 8340 3835 34 940 C
ATOM 209 C LEU A 40 17.932 13.569 35.496 1.00 89.26 C
ANISOU 209 C LEU A 40 14156 10656 9104 3945 92 1080 C
ATOM 210 O LEU A 40 17.097 13.453 34.598 1.00 89.77 O
ANISOU 210 O LEU A 40 14086 11017 9004 4201 57 1140 O
ATOM 211 CB LEU A 40 17.091 14.408 37.687 1.00 84.55 C
ANISOU 211 CB LEU A 40 13710 9889 8526 4080 134 976 C
ATOM 212 CG LEU A 40 16.026 14.258 38.788 1.00 89.33 C
ANISOU 212 CG LEU A 40 14166 10688 9088 4212 80 884 C
ATOM 213 CD1 LEU A 40 15.465 15.614 39.148 1.00 91.87 C
ANISOU 213 CD1 LEU A 40 14796 10812 9299 4543 199 956 C
ATOM 214 CD2 LEU A 40 14.859 13.375 38.351 1.00 92.03 C
ANISOU 214 CD2 LEU A 40 14144 11523 9299 4378 -33 857 C
ATOM 215 N ILE A 41 19.171 14.058 35.297 1.00 87.24 N
ANISOU 215 N ILE A 41 14153 10045 8947 3751 184 1128 N
ATOM 216 CA ILE A 41 19.652 14.516 33.996 1.00 88.92 C
ANISOU 216 CA ILE A 41 14526 10168 9092 3825 258 1267 C
ATOM 217 C ILE A 41 20.028 13.316 33.102 1.00 92.33 C
ANISOU 217 C ILE A 41 14669 10856 9557 3638 158 1236 C
ATOM 218 O ILE A 41 19.887 13.420 31.885 1.00 93.66 O
ANISOU 218 O ILE A 41 14835 11149 9601 3803 171 1340 O
ATOM 219 CB ILE A 41 20.806 15.568 34.101 1.00 93.04 C
ANISOU 219 CB ILE A 41 15441 10214 9695 3681 412 1327 C
ATOM 220 CG1 ILE A 41 22.130 14.983 34.641 1.00 91.36 C
ANISOU 220 CG1 ILE A 41 15175 9847 9690 3219 388 1216 C
ATOM 221 CG2 ILE A 41 20.375 16.811 34.890 1.00 95.55 C
ANISOU 221 CG2 ILE A 41 16080 10264 9959 3893 533 1361 C
ATOM 222 CD1 ILE A 41 23.296 15.092 33.669 1.00 98.90 C
ANISOU 222 CD1 ILE A 41 16265 10624 10690 3029 460 1288 C
ATOM 223 N THR A 42 20.479 12.194 33.694 1.00 86.90 N
ANISOU 223 N THR A 42 13746 10248 9025 3312 66 1098 N
ATOM 224 CA THR A 42 20.873 10.985 32.959 1.00 85.43 C
ANISOU 224 CA THR A 42 13297 10278 8886 3114 -18 1051 C
ATOM 225 C THR A 42 19.628 10.243 32.455 1.00 89.72 C
ANISOU 225 C THR A 42 13540 11260 9289 3303 -116 1016 C
ATOM 226 O THR A 42 19.596 9.850 31.289 1.00 89.34 O
ANISOU 226 O THR A 42 13384 11402 9158 3347 -138 1055 O
ATOM 227 CB THR A 42 21.773 10.088 33.840 1.00 92.85 C
ANISOU 227 CB THR A 42 14113 11137 10029 2731 -66 924 C
ATOM 228 OG1 THR A 42 22.936 10.829 34.209 1.00 95.43 O
ANISOU 228 OG1 THR A 42 14704 11096 10458 2557 27 953 O
ATOM 229 CG2 THR A 42 22.210 8.805 33.145 1.00 89.24 C
ANISOU 229 CG2 THR A 42 13405 10874 9628 2527 -137 873 C
ATOM 230 N ASN A 43 18.619 10.049 33.328 1.00 86.86 N
ANISOU 230 N ASN A 43 13037 11071 8894 3402 -170 934 N
ATOM 231 CA ASN A 43 17.387 9.333 32.992 1.00 87.08 C
ANISOU 231 CA ASN A 43 12761 11541 8786 3554 -260 877 C
ATOM 232 C ASN A 43 16.368 10.228 32.280 1.00 94.36 C
ANISOU 232 C ASN A 43 13751 12632 9470 3981 -229 995 C
ATOM 233 O ASN A 43 15.467 9.712 31.615 1.00 93.82 O
ANISOU 233 O ASN A 43 13435 12962 9251 4119 -295 971 O
ATOM 234 CB ASN A 43 16.784 8.676 34.225 1.00 84.55 C
ANISOU 234 CB ASN A 43 12248 11350 8527 3459 -324 737 C
ATOM 235 CG ASN A 43 17.442 7.350 34.516 1.00100.24 C
ANISOU 235 CG ASN A 43 14041 13360 10684 3085 -381 615 C
ATOM 236 OD1 ASN A 43 17.013 6.302 34.028 1.00 93.01 O
ANISOU 236 OD1 ASN A 43 12859 12746 9736 3009 -445 536 O
ATOM 237 ND2 ASN A 43 18.558 7.377 35.232 1.00 88.59 N
ANISOU 237 ND2 ASN A 43 12706 11566 9387 2843 -348 602 N
ATOM 238 N GLY A 44 16.541 11.543 32.396 1.00 93.98 N
ANISOU 238 N GLY A 44 14039 12287 9383 4183 -122 1118 N
ATOM 239 CA GLY A 44 15.708 12.520 31.706 1.00 97.32 C
ANISOU 239 CA GLY A 44 14589 12810 9580 4618 -66 1261 C
ATOM 240 C GLY A 44 16.071 12.541 30.237 1.00103.97 C
ANISOU 240 C GLY A 44 15455 13722 10326 4682 -45 1373 C
ATOM 241 O GLY A 44 15.191 12.553 29.372 1.00105.47 O
ANISOU 241 O GLY A 44 15515 14255 10304 4973 -74 1433 O
ATOM 242 N LEU A 45 17.386 12.472 29.955 1.00100.77 N
ANISOU 242 N LEU A 45 15190 13025 10073 4394 1 1391 N
ATOM 243 CA LEU A 45 17.949 12.436 28.607 1.00101.89 C
ANISOU 243 CA LEU A 45 15365 13192 10155 4389 27 1488 C
ATOM 244 C LEU A 45 18.089 10.977 28.116 1.00105.00 C
ANISOU 244 C LEU A 45 15402 13896 10599 4132 -92 1361 C
ATOM 245 O LEU A 45 18.867 10.690 27.201 1.00104.55 O
ANISOU 245 O LEU A 45 15348 13814 10562 3999 -79 1397 O
ATOM 246 CB LEU A 45 19.299 13.182 28.562 1.00102.15 C
ANISOU 246 CB LEU A 45 15750 12748 10316 4216 153 1576 C
ATOM 247 CG LEU A 45 19.229 14.714 28.691 1.00109.65 C
ANISOU 247 CG LEU A 45 17107 13373 11182 4491 307 1730 C
ATOM 248 CD1 LEU A 45 20.565 15.288 29.115 1.00109.47 C
ANISOU 248 CD1 LEU A 45 17392 12866 11334 4208 423 1742 C
ATOM 249 CD2 LEU A 45 18.757 15.368 27.396 1.00114.70 C
ANISOU 249 CD2 LEU A 45 17856 14132 11594 4855 369 1915 C
ATOM 250 N ALA A 46 17.310 10.067 28.728 1.00100.90 N
ANISOU 250 N ALA A 46 14582 13664 10091 4066 -196 1209 N
ATOM 251 CA ALA A 46 17.215 8.648 28.386 1.00 99.25 C
ANISOU 251 CA ALA A 46 14029 13769 9913 3841 -298 1067 C
ATOM 252 C ALA A 46 15.764 8.310 28.076 1.00104.97 C
ANISOU 252 C ALA A 46 14475 14980 10427 4076 -374 1015 C
ATOM 253 O ALA A 46 15.500 7.507 27.189 1.00104.56 O
ANISOU 253 O ALA A 46 14185 15253 10288 4029 -432 955 O
ATOM 254 CB ALA A 46 17.735 7.782 29.523 1.00 97.35 C
ANISOU 254 CB ALA A 46 13695 13395 9900 3485 -336 919 C
ATOM 255 N MET A 47 14.826 8.949 28.799 1.00103.33 N
ANISOU 255 N MET A 47 14297 14837 10127 4332 -370 1032 N
ATOM 256 CA MET A 47 13.388 8.774 28.621 1.00104.92 C
ANISOU 256 CA MET A 47 14237 15517 10109 4588 -436 987 C
ATOM 257 C MET A 47 12.945 9.485 27.352 1.00111.85 C
ANISOU 257 C MET A 47 15167 16597 10734 4960 -408 1142 C
ATOM 258 O MET A 47 12.266 8.885 26.520 1.00112.26 O
ANISOU 258 O MET A 47 14939 17103 10613 5035 -477 1091 O
ATOM 259 CB MET A 47 12.629 9.311 29.843 1.00107.78 C
ANISOU 259 CB MET A 47 14637 15853 10461 4747 -429 965 C
ATOM 260 CG MET A 47 11.366 8.551 30.142 1.00112.28 C
ANISOU 260 CG MET A 47 14854 16931 10877 4850 -516 843 C
ATOM 261 SD MET A 47 10.720 8.916 31.789 1.00116.42 S
ANISOU 261 SD MET A 47 15384 17394 11455 4905 -516 772 S
ATOM 262 CE MET A 47 9.784 10.415 31.447 1.00116.50 C
ANISOU 262 CE MET A 47 15616 17432 11218 5484 -442 964 C
ATOM 263 N ARG A 48 13.390 10.746 27.177 1.00109.98 N
ANISOU 263 N ARG A 48 15296 16018 10474 5176 -299 1328 N
ATOM 264 CA ARG A 48 13.084 11.599 26.027 1.00112.41 C
ANISOU 264 CA ARG A 48 15728 16437 10545 5560 -243 1514 C
ATOM 265 C ARG A 48 13.685 11.059 24.719 1.00115.39 C
ANISOU 265 C ARG A 48 16022 16931 10888 5432 -261 1537 C
ATOM 266 O ARG A 48 13.302 11.521 23.644 1.00117.76 O
ANISOU 266 O ARG A 48 16342 17439 10962 5740 -239 1670 O
ATOM 267 CB ARG A 48 13.589 13.029 26.282 1.00114.10 C
ANISOU 267 CB ARG A 48 16402 16167 10784 5758 -95 1698 C
ATOM 268 N ILE A 49 14.600 10.077 24.808 1.00108.41 N
ANISOU 268 N ILE A 49 15043 15934 10216 4998 -299 1409 N
ATOM 269 CA ILE A 49 15.266 9.491 23.646 1.00107.49 C
ANISOU 269 CA ILE A 49 14849 15901 10093 4835 -312 1411 C
ATOM 270 C ILE A 49 14.759 8.057 23.386 1.00109.82 C
ANISOU 270 C ILE A 49 14727 16637 10361 4628 -431 1207 C
ATOM 271 O ILE A 49 14.375 7.763 22.250 1.00110.95 O
ANISOU 271 O ILE A 49 14698 17141 10316 4735 -467 1212 O
ATOM 272 CB ILE A 49 16.820 9.543 23.812 1.00108.78 C
ANISOU 272 CB ILE A 49 15257 15569 10505 4511 -240 1438 C
ATOM 273 CG1 ILE A 49 17.343 10.958 24.225 1.00110.38 C
ANISOU 273 CG1 ILE A 49 15886 15301 10751 4657 -107 1609 C
ATOM 274 CG2 ILE A 49 17.571 8.973 22.594 1.00109.01 C
ANISOU 274 CG2 ILE A 49 15222 15670 10528 4350 -244 1447 C
ATOM 275 CD1 ILE A 49 17.048 12.194 23.256 1.00121.39 C
ANISOU 275 CD1 ILE A 49 17528 16678 11915 5078 -8 1839 C
ATOM 276 N PHE A 50 14.771 7.172 24.417 1.00103.33 N
ANISOU 276 N PHE A 50 13753 15785 9720 4330 -481 1030 N
ATOM 277 CA PHE A 50 14.361 5.767 24.287 1.00101.70 C
ANISOU 277 CA PHE A 50 13189 15935 9519 4086 -569 824 C
ATOM 278 C PHE A 50 12.850 5.593 24.112 1.00106.82 C
ANISOU 278 C PHE A 50 13545 17121 9920 4312 -639 750 C
ATOM 279 O PHE A 50 12.445 4.643 23.442 1.00106.47 O
ANISOU 279 O PHE A 50 13216 17455 9783 4193 -697 616 O
ATOM 280 CB PHE A 50 14.843 4.918 25.474 1.00100.82 C
ANISOU 280 CB PHE A 50 13034 15603 9670 3717 -583 676 C
ATOM 281 N PHE A 51 12.014 6.485 24.691 1.00104.58 N
ANISOU 281 N PHE A 51 13324 16890 9522 4633 -629 826 N
ATOM 282 CA PHE A 51 10.557 6.358 24.552 1.00106.13 C
ANISOU 282 CA PHE A 51 13225 17634 9465 4865 -695 757 C
ATOM 283 C PHE A 51 10.040 6.949 23.226 1.00111.83 C
ANISOU 283 C PHE A 51 13906 18700 9886 5232 -698 886 C
ATOM 284 O PHE A 51 8.850 6.816 22.921 1.00113.36 O
ANISOU 284 O PHE A 51 13819 19419 9833 5431 -758 827 O
ATOM 285 CB PHE A 51 9.805 6.931 25.758 1.00108.47 C
ANISOU 285 CB PHE A 51 13560 17902 9751 5053 -690 764 C
ATOM 286 CG PHE A 51 9.598 5.886 26.828 1.00108.17 C
ANISOU 286 CG PHE A 51 13322 17903 9876 4718 -736 556 C
ATOM 287 CD1 PHE A 51 8.529 4.998 26.760 1.00112.14 C
ANISOU 287 CD1 PHE A 51 13445 18922 10240 4659 -810 380 C
ATOM 288 CD2 PHE A 51 10.495 5.758 27.881 1.00107.90 C
ANISOU 288 CD2 PHE A 51 13474 17398 10124 4448 -701 532 C
ATOM 289 CE1 PHE A 51 8.352 4.015 27.738 1.00111.38 C
ANISOU 289 CE1 PHE A 51 13183 18843 10294 4339 -836 193 C
ATOM 290 CE2 PHE A 51 10.310 4.782 28.864 1.00109.08 C
ANISOU 290 CE2 PHE A 51 13449 17583 10415 4154 -735 353 C
ATOM 291 CZ PHE A 51 9.244 3.912 28.782 1.00107.98 C
ANISOU 291 CZ PHE A 51 12955 17930 10144 4098 -798 189 C
ATOM 292 N GLN A 52 10.939 7.547 22.423 1.00107.89 N
ANISOU 292 N GLN A 52 13668 17931 9396 5306 -632 1054 N
ATOM 293 CA GLN A 52 10.626 8.042 21.085 1.00109.88 C
ANISOU 293 CA GLN A 52 13903 18472 9373 5627 -625 1190 C
ATOM 294 C GLN A 52 10.700 6.870 20.107 1.00112.02 C
ANISOU 294 C GLN A 52 13877 19097 9590 5377 -693 1039 C
ATOM 295 O GLN A 52 9.838 6.742 19.234 1.00113.76 O
ANISOU 295 O GLN A 52 13853 19841 9530 5581 -746 1021 O
ATOM 296 CB GLN A 52 11.593 9.161 20.663 1.00111.78 C
ANISOU 296 CB GLN A 52 14562 18254 9654 5783 -510 1431 C
ATOM 297 CG GLN A 52 11.218 10.535 21.192 1.00130.89 C
ANISOU 297 CG GLN A 52 17272 20465 11993 6187 -426 1621 C
ATOM 298 CD GLN A 52 11.959 11.617 20.450 1.00154.01 C
ANISOU 298 CD GLN A 52 20579 23056 14882 6389 -303 1865 C
ATOM 299 OE1 GLN A 52 13.146 11.868 20.685 1.00148.44 O
ANISOU 299 OE1 GLN A 52 20158 21839 14402 6156 -223 1912 O
ATOM 300 NE2 GLN A 52 11.275 12.273 19.524 1.00149.67 N
ANISOU 300 NE2 GLN A 52 20037 22800 14032 6826 -281 2026 N
ATOM 301 N ILE A 53 11.725 5.995 20.288 1.00104.47 N
ANISOU 301 N ILE A 53 12937 17861 8895 4933 -689 922 N
ATOM 302 CA ILE A 53 11.986 4.809 19.465 1.00102.64 C
ANISOU 302 CA ILE A 53 12468 17868 8661 4638 -735 762 C
ATOM 303 C ILE A 53 10.939 3.712 19.782 1.00104.56 C
ANISOU 303 C ILE A 53 12320 18573 8833 4479 -818 514 C
ATOM 304 O ILE A 53 10.494 3.582 20.927 1.00103.27 O
ANISOU 304 O ILE A 53 12113 18365 8761 4425 -832 437 O
ATOM 305 CB ILE A 53 13.466 4.297 19.585 1.00102.75 C
ANISOU 305 CB ILE A 53 12653 17411 8975 4249 -688 735 C
ATOM 306 CG1 ILE A 53 13.682 3.220 20.657 1.00100.16 C
ANISOU 306 CG1 ILE A 53 12223 16935 8898 3859 -709 538 C
ATOM 307 CG2 ILE A 53 14.483 5.438 19.716 1.00103.54 C
ANISOU 307 CG2 ILE A 53 13158 16994 9189 4358 -594 960 C
ATOM 308 CD1 ILE A 53 14.175 1.946 20.100 1.00104.30 C
ANISOU 308 CD1 ILE A 53 12579 17546 9506 3503 -724 368 C
ATOM 309 N ARG A 54 10.537 2.954 18.744 1.00100.40 N
ANISOU 309 N ARG A 54 11515 18501 8133 4403 -866 388 N
ATOM 310 CA ARG A 54 9.527 1.894 18.827 1.00 99.48 C
ANISOU 310 CA ARG A 54 11014 18872 7913 4232 -933 137 C
ATOM 311 C ARG A 54 10.055 0.624 19.516 1.00 97.12 C
ANISOU 311 C ARG A 54 10658 18351 7892 3736 -921 -73 C
ATOM 312 O ARG A 54 11.255 0.343 19.480 1.00 93.98 O
ANISOU 312 O ARG A 54 10449 17544 7716 3508 -874 -48 O
ATOM 313 CB ARG A 54 8.997 1.543 17.424 1.00101.54 C
ANISOU 313 CB ARG A 54 11008 19696 7876 4312 -979 68 C
ATOM 314 CG ARG A 54 7.962 2.527 16.895 1.00114.56 C
ANISOU 314 CG ARG A 54 12576 21771 9180 4813 -1012 212 C
ATOM 315 N SER A 55 9.133 -0.144 20.127 1.00 91.94 N
ANISOU 315 N SER A 55 9739 17985 7211 3580 -956 -276 N
ATOM 316 CA SER A 55 9.422 -1.401 20.810 1.00 89.00 C
ANISOU 316 CA SER A 55 9290 17458 7067 3131 -935 -484 C
ATOM 317 C SER A 55 9.263 -2.572 19.846 1.00 92.75 C
ANISOU 317 C SER A 55 9515 18279 7448 2864 -943 -696 C
ATOM 318 O SER A 55 8.262 -3.299 19.888 1.00 93.32 O
ANISOU 318 O SER A 55 9288 18781 7389 2735 -969 -904 O
ATOM 319 CB SER A 55 8.515 -1.570 22.020 1.00 92.17 C
ANISOU 319 CB SER A 55 9560 17971 7488 3099 -952 -586 C
ATOM 320 OG SER A 55 8.775 -0.591 23.010 1.00 99.14 O
ANISOU 320 OG SER A 55 10695 18480 8493 3295 -934 -412 O
ATOM 321 N LYS A 56 10.258 -2.733 18.957 1.00 88.11 N
ANISOU 321 N LYS A 56 9050 17511 6917 2777 -913 -649 N
ATOM 322 CA LYS A 56 10.280 -3.775 17.928 1.00 88.04 C
ANISOU 322 CA LYS A 56 8848 17778 6823 2533 -908 -835 C
ATOM 323 C LYS A 56 11.037 -5.030 18.402 1.00 86.82 C
ANISOU 323 C LYS A 56 8734 17307 6947 2080 -844 -1004 C
ATOM 324 O LYS A 56 10.943 -6.081 17.754 1.00 87.11 O
ANISOU 324 O LYS A 56 8596 17570 6933 1819 -824 -1211 O
ATOM 325 CB LYS A 56 10.898 -3.230 16.630 1.00 91.65 C
ANISOU 325 CB LYS A 56 9414 18243 7168 2711 -907 -687 C
ATOM 326 N SER A 57 11.766 -4.921 19.537 1.00 77.88 N
ANISOU 326 N SER A 57 7832 15662 6095 1995 -805 -919 N
ATOM 327 CA SER A 57 12.526 -6.026 20.134 1.00 73.67 C
ANISOU 327 CA SER A 57 7368 14791 5833 1613 -737 -1043 C
ATOM 328 C SER A 57 12.295 -6.127 21.653 1.00 73.95 C
ANISOU 328 C SER A 57 7445 14617 6037 1531 -724 -1062 C
ATOM 329 O SER A 57 11.902 -5.146 22.297 1.00 74.07 O
ANISOU 329 O SER A 57 7518 14611 6013 1786 -762 -932 O
ATOM 330 CB SER A 57 14.014 -5.872 19.847 1.00 73.43 C
ANISOU 330 CB SER A 57 7603 14304 5994 1566 -691 -903 C
ATOM 331 OG SER A 57 14.583 -4.810 20.593 1.00 78.06 O
ANISOU 331 OG SER A 57 8436 14523 6701 1760 -695 -683 O
ATOM 332 N ASN A 58 12.557 -7.324 22.211 1.00 66.57 N
ANISOU 332 N ASN A 58 6492 13517 5284 1181 -660 -1222 N
ATOM 333 CA ASN A 58 12.458 -7.639 23.633 1.00 63.48 C
ANISOU 333 CA ASN A 58 6146 12905 5071 1051 -632 -1256 C
ATOM 334 C ASN A 58 13.414 -6.774 24.442 1.00 65.04 C
ANISOU 334 C ASN A 58 6624 12627 5460 1188 -632 -1036 C
ATOM 335 O ASN A 58 13.033 -6.282 25.504 1.00 64.63 O
ANISOU 335 O ASN A 58 6608 12500 5448 1287 -651 -983 O
ATOM 336 CB ASN A 58 12.778 -9.112 23.874 1.00 57.60 C
ANISOU 336 CB ASN A 58 5371 12029 4485 658 -543 -1445 C
ATOM 337 CG ASN A 58 11.821 -10.116 23.294 1.00 69.96 C
ANISOU 337 CG ASN A 58 6670 14022 5889 447 -517 -1701 C
ATOM 338 OD1 ASN A 58 12.055 -11.319 23.382 1.00 61.45 O
ANISOU 338 OD1 ASN A 58 5584 12840 4923 126 -427 -1863 O
ATOM 339 ND2 ASN A 58 10.725 -9.673 22.699 1.00 66.68 N
ANISOU 339 ND2 ASN A 58 6033 14101 5201 614 -586 -1750 N
ATOM 340 N PHE A 59 14.649 -6.580 23.920 1.00 59.46 N
ANISOU 340 N PHE A 59 6109 11621 4862 1185 -607 -919 N
ATOM 341 CA PHE A 59 15.723 -5.786 24.509 1.00 57.30 C
ANISOU 341 CA PHE A 59 6104 10904 4764 1278 -598 -722 C
ATOM 342 C PHE A 59 15.261 -4.365 24.834 1.00 63.18 C
ANISOU 342 C PHE A 59 6933 11667 5407 1611 -649 -559 C
ATOM 343 O PHE A 59 15.481 -3.904 25.953 1.00 62.68 O
ANISOU 343 O PHE A 59 7003 11341 5473 1644 -644 -483 O
ATOM 344 CB PHE A 59 16.948 -5.749 23.569 1.00 58.13 C
ANISOU 344 CB PHE A 59 6348 10812 4926 1247 -567 -636 C
ATOM 345 CG PHE A 59 18.043 -4.776 23.953 1.00 57.81 C
ANISOU 345 CG PHE A 59 6575 10371 5021 1357 -557 -430 C
ATOM 346 CD1 PHE A 59 18.822 -4.990 25.088 1.00 58.77 C
ANISOU 346 CD1 PHE A 59 6828 10131 5373 1212 -522 -404 C
ATOM 347 CD2 PHE A 59 18.291 -3.644 23.184 1.00 59.67 C
ANISOU 347 CD2 PHE A 59 6930 10600 5144 1602 -573 -264 C
ATOM 348 CE1 PHE A 59 19.821 -4.080 25.452 1.00 58.60 C
ANISOU 348 CE1 PHE A 59 7036 9767 5461 1291 -510 -233 C
ATOM 349 CE2 PHE A 59 19.290 -2.738 23.545 1.00 61.66 C
ANISOU 349 CE2 PHE A 59 7433 10479 5516 1675 -549 -88 C
ATOM 350 CZ PHE A 59 20.052 -2.964 24.675 1.00 58.41 C
ANISOU 350 CZ PHE A 59 7134 9730 5329 1509 -519 -82 C
ATOM 351 N ILE A 60 14.626 -3.684 23.867 1.00 62.00 N
ANISOU 351 N ILE A 60 6710 11827 5019 1864 -690 -505 N
ATOM 352 CA ILE A 60 14.137 -2.313 24.026 1.00 63.09 C
ANISOU 352 CA ILE A 60 6939 12004 5029 2223 -725 -340 C
ATOM 353 C ILE A 60 12.968 -2.298 25.018 1.00 68.23 C
ANISOU 353 C ILE A 60 7450 12854 5621 2287 -756 -417 C
ATOM 354 O ILE A 60 12.885 -1.352 25.802 1.00 68.99 O
ANISOU 354 O ILE A 60 7694 12774 5745 2480 -759 -294 O
ATOM 355 CB ILE A 60 13.817 -1.666 22.644 1.00 68.19 C
ANISOU 355 CB ILE A 60 7543 12945 5421 2486 -751 -255 C
ATOM 356 CG1 ILE A 60 15.099 -1.045 22.069 1.00 68.00 C
ANISOU 356 CG1 ILE A 60 7781 12571 5485 2528 -709 -81 C
ATOM 357 CG2 ILE A 60 12.697 -0.614 22.693 1.00 70.47 C
ANISOU 357 CG2 ILE A 60 7789 13505 5482 2869 -793 -160 C
ATOM 358 CD1 ILE A 60 15.624 -1.720 20.843 1.00 79.29 C
ANISOU 358 CD1 ILE A 60 9134 14141 6853 2412 -699 -133 C
ATOM 359 N ILE A 61 12.116 -3.357 25.038 1.00 64.54 N
ANISOU 359 N ILE A 61 6709 12729 5082 2103 -768 -627 N
ATOM 360 CA ILE A 61 11.007 -3.469 26.003 1.00 64.15 C
ANISOU 360 CA ILE A 61 6504 12890 4981 2121 -790 -721 C
ATOM 361 C ILE A 61 11.617 -3.544 27.412 1.00 64.32 C
ANISOU 361 C ILE A 61 6701 12475 5262 1983 -754 -688 C
ATOM 362 O ILE A 61 11.205 -2.781 28.287 1.00 64.72 O
ANISOU 362 O ILE A 61 6815 12471 5304 2168 -772 -611 O
ATOM 363 CB ILE A 61 10.039 -4.660 25.693 1.00 68.10 C
ANISOU 363 CB ILE A 61 6680 13837 5359 1896 -793 -970 C
ATOM 364 CG1 ILE A 61 9.232 -4.395 24.391 1.00 70.88 C
ANISOU 364 CG1 ILE A 61 6822 14708 5399 2092 -844 -999 C
ATOM 365 CG2 ILE A 61 9.105 -4.973 26.884 1.00 68.10 C
ANISOU 365 CG2 ILE A 61 6543 13966 5367 1824 -794 -1080 C
ATOM 366 CD1 ILE A 61 8.328 -5.556 23.878 1.00 76.61 C
ANISOU 366 CD1 ILE A 61 7219 15909 5978 1843 -842 -1264 C
ATOM 367 N PHE A 62 12.635 -4.410 27.597 1.00 58.04 N
ANISOU 367 N PHE A 62 5995 11371 4685 1681 -702 -736 N
ATOM 368 CA PHE A 62 13.352 -4.608 28.865 1.00 55.35 C
ANISOU 368 CA PHE A 62 5815 10624 4590 1530 -664 -707 C
ATOM 369 C PHE A 62 14.124 -3.357 29.261 1.00 61.88 C
ANISOU 369 C PHE A 62 6910 11105 5498 1733 -670 -501 C
ATOM 370 O PHE A 62 14.166 -3.018 30.442 1.00 61.02 O
ANISOU 370 O PHE A 62 6898 10796 5493 1750 -666 -460 O
ATOM 371 CB PHE A 62 14.300 -5.810 28.790 1.00 54.25 C
ANISOU 371 CB PHE A 62 5709 10268 4637 1201 -601 -790 C
ATOM 372 CG PHE A 62 13.665 -7.152 28.488 1.00 55.27 C
ANISOU 372 CG PHE A 62 5617 10663 4720 945 -566 -1009 C
ATOM 373 CD1 PHE A 62 12.364 -7.436 28.898 1.00 58.09 C
ANISOU 373 CD1 PHE A 62 5764 11354 4954 925 -579 -1142 C
ATOM 374 CD2 PHE A 62 14.384 -8.147 27.831 1.00 56.22 C
ANISOU 374 CD2 PHE A 62 5747 10691 4923 711 -507 -1088 C
ATOM 375 CE1 PHE A 62 11.789 -8.680 28.637 1.00 59.58 C
ANISOU 375 CE1 PHE A 62 5760 11776 5100 655 -530 -1357 C
ATOM 376 CE2 PHE A 62 13.808 -9.392 27.572 1.00 59.31 C
ANISOU 376 CE2 PHE A 62 5961 11300 5276 457 -454 -1301 C
ATOM 377 CZ PHE A 62 12.516 -9.651 27.980 1.00 58.62 C
ANISOU 377 CZ PHE A 62 5671 11537 5065 419 -463 -1438 C
ATOM 378 N LEU A 63 14.686 -2.649 28.266 1.00 61.01 N
ANISOU 378 N LEU A 63 6920 10936 5326 1885 -674 -376 N
ATOM 379 CA LEU A 63 15.437 -1.404 28.443 1.00 61.31 C
ANISOU 379 CA LEU A 63 7228 10651 5418 2070 -662 -182 C
ATOM 380 C LEU A 63 14.514 -0.245 28.867 1.00 66.11 C
ANISOU 380 C LEU A 63 7872 11366 5881 2395 -689 -96 C
ATOM 381 O LEU A 63 14.919 0.589 29.676 1.00 65.27 O
ANISOU 381 O LEU A 63 7978 10959 5865 2484 -668 11 O
ATOM 382 CB LEU A 63 16.156 -1.068 27.128 1.00 62.20 C
ANISOU 382 CB LEU A 63 7434 10724 5476 2132 -647 -86 C
ATOM 383 CG LEU A 63 17.432 -0.249 27.202 1.00 66.30 C
ANISOU 383 CG LEU A 63 8241 10822 6127 2152 -605 77 C
ATOM 384 CD1 LEU A 63 18.450 -0.865 28.162 1.00 64.25 C
ANISOU 384 CD1 LEU A 63 8058 10236 6119 1868 -573 37 C
ATOM 385 CD2 LEU A 63 18.028 -0.099 25.820 1.00 68.97 C
ANISOU 385 CD2 LEU A 63 8632 11187 6387 2200 -588 152 C
ATOM 386 N LYS A 64 13.279 -0.205 28.329 1.00 64.44 N
ANISOU 386 N LYS A 64 7452 11594 5439 2569 -730 -151 N
ATOM 387 CA LYS A 64 12.269 0.810 28.662 1.00 65.68 C
ANISOU 387 CA LYS A 64 7606 11923 5426 2907 -754 -79 C
ATOM 388 C LYS A 64 11.755 0.614 30.096 1.00 68.38 C
ANISOU 388 C LYS A 64 7900 12226 5854 2837 -759 -157 C
ATOM 389 O LYS A 64 11.460 1.596 30.772 1.00 68.33 O
ANISOU 389 O LYS A 64 8023 12120 5819 3069 -754 -63 O
ATOM 390 CB LYS A 64 11.097 0.778 27.666 1.00 69.93 C
ANISOU 390 CB LYS A 64 7891 13001 5677 3100 -800 -130 C
ATOM 391 CG LYS A 64 11.355 1.528 26.369 1.00 76.03 C
ANISOU 391 CG LYS A 64 8760 13831 6295 3343 -796 15 C
ATOM 392 CD LYS A 64 10.183 1.347 25.417 1.00 85.97 C
ANISOU 392 CD LYS A 64 9732 15676 7257 3519 -848 -52 C
ATOM 393 CE LYS A 64 10.307 2.162 24.148 1.00 93.26 C
ANISOU 393 CE LYS A 64 10745 16693 7995 3805 -843 108 C
ATOM 394 NZ LYS A 64 9.022 2.210 23.395 1.00 98.69 N
ANISOU 394 NZ LYS A 64 11151 17988 8360 4047 -898 62 N
ATOM 395 N ASN A 65 11.642 -0.646 30.553 1.00 64.29 N
ANISOU 395 N ASN A 65 7208 11781 5436 2524 -759 -327 N
ATOM 396 CA ASN A 65 11.208 -0.966 31.918 1.00 63.98 C
ANISOU 396 CA ASN A 65 7118 11703 5487 2421 -755 -407 C
ATOM 397 C ASN A 65 12.285 -0.550 32.919 1.00 67.57 C
ANISOU 397 C ASN A 65 7843 11664 6166 2354 -721 -309 C
ATOM 398 O ASN A 65 11.964 -0.044 33.994 1.00 67.65 O
ANISOU 398 O ASN A 65 7914 11589 6203 2445 -721 -287 O
ATOM 399 CB ASN A 65 10.898 -2.454 32.057 1.00 62.63 C
ANISOU 399 CB ASN A 65 6719 11712 5364 2090 -743 -605 C
ATOM 400 CG ASN A 65 9.501 -2.828 31.637 1.00 77.22 C
ANISOU 400 CG ASN A 65 8262 14094 6983 2139 -775 -742 C
ATOM 401 OD1 ASN A 65 8.598 -2.991 32.471 1.00 63.15 O
ANISOU 401 OD1 ASN A 65 6340 12499 5154 2135 -782 -826 O
ATOM 402 ND2 ASN A 65 9.303 -3.009 30.334 1.00 68.10 N
ANISOU 402 ND2 ASN A 65 6984 13218 5674 2171 -794 -777 N
ATOM 403 N THR A 66 13.563 -0.725 32.526 1.00 63.46 N
ANISOU 403 N THR A 66 7478 10841 5791 2204 -691 -253 N
ATOM 404 CA THR A 66 14.766 -0.389 33.282 1.00 62.03 C
ANISOU 404 CA THR A 66 7539 10213 5814 2109 -657 -166 C
ATOM 405 C THR A 66 14.862 1.140 33.482 1.00 67.85 C
ANISOU 405 C THR A 66 8509 10768 6502 2392 -647 -12 C
ATOM 406 O THR A 66 15.166 1.562 34.594 1.00 67.22 O
ANISOU 406 O THR A 66 8564 10449 6529 2379 -631 16 O
ATOM 407 CB THR A 66 15.997 -1.006 32.571 1.00 69.96 C
ANISOU 407 CB THR A 66 8607 11031 6943 1896 -628 -155 C
ATOM 408 OG1 THR A 66 16.139 -2.353 33.018 1.00 69.32 O
ANISOU 408 OG1 THR A 66 8394 10964 6980 1607 -611 -287 O
ATOM 409 CG2 THR A 66 17.303 -0.256 32.831 1.00 67.99 C
ANISOU 409 CG2 THR A 66 8626 10371 6834 1882 -595 -24 C
ATOM 410 N VAL A 67 14.588 1.959 32.440 1.00 66.21 N
ANISOU 410 N VAL A 67 8355 10673 6128 2649 -649 86 N
ATOM 411 CA VAL A 67 14.686 3.420 32.559 1.00 67.20 C
ANISOU 411 CA VAL A 67 8735 10598 6201 2926 -616 241 C
ATOM 412 C VAL A 67 13.623 3.985 33.555 1.00 71.63 C
ANISOU 412 C VAL A 67 9276 11261 6678 3134 -627 229 C
ATOM 413 O VAL A 67 13.951 4.908 34.308 1.00 70.75 O
ANISOU 413 O VAL A 67 9397 10857 6629 3223 -587 306 O
ATOM 414 CB VAL A 67 14.658 4.144 31.176 1.00 73.03 C
ANISOU 414 CB VAL A 67 9551 11425 6770 3167 -601 364 C
ATOM 415 CG1 VAL A 67 13.304 4.043 30.501 1.00 75.13 C
ANISOU 415 CG1 VAL A 67 9579 12179 6789 3394 -649 326 C
ATOM 416 CG2 VAL A 67 15.089 5.606 31.283 1.00 73.70 C
ANISOU 416 CG2 VAL A 67 9970 11189 6846 3391 -534 535 C
ATOM 417 N ILE A 68 12.391 3.425 33.587 1.00 68.62 N
ANISOU 417 N ILE A 68 8619 11294 6160 3193 -675 121 N
ATOM 418 CA ILE A 68 11.366 3.962 34.482 1.00 69.32 C
ANISOU 418 CA ILE A 68 8673 11510 6156 3402 -684 109 C
ATOM 419 C ILE A 68 11.586 3.438 35.931 1.00 70.32 C
ANISOU 419 C ILE A 68 8796 11456 6468 3161 -680 19 C
ATOM 420 O ILE A 68 11.284 4.170 36.878 1.00 70.47 O
ANISOU 420 O ILE A 68 8923 11367 6484 3305 -664 49 O
ATOM 421 CB ILE A 68 9.894 3.800 33.975 1.00 74.70 C
ANISOU 421 CB ILE A 68 9066 12731 6585 3609 -732 45 C
ATOM 422 CG1 ILE A 68 9.143 2.595 34.544 1.00 74.96 C
ANISOU 422 CG1 ILE A 68 8797 13056 6628 3384 -769 -144 C
ATOM 423 CG2 ILE A 68 9.718 3.974 32.463 1.00 76.76 C
ANISOU 423 CG2 ILE A 68 9257 13244 6663 3772 -748 100 C
ATOM 424 CD1 ILE A 68 8.113 3.023 35.578 1.00 84.77 C
ANISOU 424 CD1 ILE A 68 9975 14454 7782 3573 -777 -168 C
ATOM 425 N SER A 69 12.125 2.206 36.100 1.00 63.96 N
ANISOU 425 N SER A 69 7879 10608 5815 2810 -687 -86 N
ATOM 426 CA SER A 69 12.426 1.648 37.425 1.00 61.73 C
ANISOU 426 CA SER A 69 7599 10149 5705 2579 -677 -157 C
ATOM 427 C SER A 69 13.581 2.425 38.057 1.00 64.41 C
ANISOU 427 C SER A 69 8235 10041 6197 2556 -639 -56 C
ATOM 428 O SER A 69 13.623 2.567 39.276 1.00 63.62 O
ANISOU 428 O SER A 69 8194 9798 6180 2509 -629 -76 O
ATOM 429 CB SER A 69 12.753 0.162 37.342 1.00 62.98 C
ANISOU 429 CB SER A 69 7593 10361 5975 2240 -676 -275 C
ATOM 430 OG SER A 69 13.922 -0.076 36.580 1.00 69.24 O
ANISOU 430 OG SER A 69 8496 10941 6872 2102 -656 -226 O
ATOM 431 N ASP A 70 14.496 2.949 37.212 1.00 60.67 N
ANISOU 431 N ASP A 70 7942 9365 5746 2586 -614 48 N
ATOM 432 CA ASP A 70 15.603 3.820 37.604 1.00 59.82 C
ANISOU 432 CA ASP A 70 8122 8852 5753 2570 -568 145 C
ATOM 433 C ASP A 70 15.061 5.159 38.054 1.00 65.92 C
ANISOU 433 C ASP A 70 9070 9549 6427 2863 -539 219 C
ATOM 434 O ASP A 70 15.554 5.719 39.023 1.00 66.62 O
ANISOU 434 O ASP A 70 9334 9369 6609 2823 -506 234 O
ATOM 435 CB ASP A 70 16.571 4.061 36.430 1.00 61.22 C
ANISOU 435 CB ASP A 70 8429 8882 5951 2537 -540 235 C
ATOM 436 CG ASP A 70 17.519 2.942 36.040 1.00 66.63 C
ANISOU 436 CG ASP A 70 9023 9524 6768 2237 -546 185 C
ATOM 437 OD1 ASP A 70 17.648 1.963 36.818 1.00 64.95 O
ANISOU 437 OD1 ASP A 70 8693 9314 6670 2020 -561 91 O
ATOM 438 OD2 ASP A 70 18.121 3.038 34.948 1.00 70.50 O
ANISOU 438 OD2 ASP A 70 9566 9979 7241 2230 -530 244 O
ATOM 439 N LEU A 71 14.053 5.685 37.343 1.00 63.76 N
ANISOU 439 N LEU A 71 8750 9523 5953 3166 -546 264 N
ATOM 440 CA LEU A 71 13.477 6.978 37.666 1.00 65.32 C
ANISOU 440 CA LEU A 71 9124 9661 6034 3493 -506 346 C
ATOM 441 C LEU A 71 12.651 6.917 38.935 1.00 68.12 C
ANISOU 441 C LEU A 71 9384 10119 6380 3532 -525 261 C
ATOM 442 O LEU A 71 12.701 7.858 39.721 1.00 68.04 O
ANISOU 442 O LEU A 71 9586 9887 6379 3661 -477 303 O
ATOM 443 CB LEU A 71 12.655 7.523 36.513 1.00 67.91 C
ANISOU 443 CB LEU A 71 9416 10252 6134 3831 -506 429 C
ATOM 444 CG LEU A 71 12.992 8.959 36.163 1.00 75.08 C
ANISOU 444 CG LEU A 71 10665 10882 6980 4095 -420 592 C
ATOM 445 CD1 LEU A 71 13.118 9.143 34.646 1.00 77.02 C
ANISOU 445 CD1 LEU A 71 10908 11281 7076 4271 -413 695 C
ATOM 446 CD2 LEU A 71 12.003 9.932 36.800 1.00 79.15 C
ANISOU 446 CD2 LEU A 71 11298 11389 7385 4412 -380 628 C
ATOM 447 N LEU A 72 11.939 5.802 39.163 1.00 64.02 N
ANISOU 447 N LEU A 72 8561 9918 5846 3402 -585 136 N
ATOM 448 CA LEU A 72 11.159 5.597 40.381 1.00 64.17 C
ANISOU 448 CA LEU A 72 8465 10058 5860 3405 -602 46 C
ATOM 449 C LEU A 72 12.057 5.589 41.616 1.00 67.20 C
ANISOU 449 C LEU A 72 9004 10088 6439 3188 -576 25 C
ATOM 450 O LEU A 72 11.696 6.199 42.623 1.00 67.76 O
ANISOU 450 O LEU A 72 9163 10087 6496 3304 -556 19 O
ATOM 451 CB LEU A 72 10.361 4.291 40.316 1.00 64.05 C
ANISOU 451 CB LEU A 72 8099 10433 5803 3250 -655 -90 C
ATOM 452 CG LEU A 72 8.858 4.423 40.105 1.00 71.50 C
ANISOU 452 CG LEU A 72 8826 11824 6517 3513 -685 -128 C
ATOM 453 CD1 LEU A 72 8.271 3.116 39.644 1.00 71.80 C
ANISOU 453 CD1 LEU A 72 8535 12244 6502 3323 -726 -258 C
ATOM 454 CD2 LEU A 72 8.152 4.887 41.374 1.00 75.19 C
ANISOU 454 CD2 LEU A 72 9293 12320 6955 3634 -676 -160 C
ATOM 455 N MET A 73 13.238 4.939 41.535 1.00 62.18 N
ANISOU 455 N MET A 73 8405 9244 5974 2888 -574 15 N
ATOM 456 CA MET A 73 14.132 4.884 42.682 1.00 60.84 C
ANISOU 456 CA MET A 73 8360 8780 5975 2679 -554 -5 C
ATOM 457 C MET A 73 14.937 6.189 42.863 1.00 63.45 C
ANISOU 457 C MET A 73 9019 8748 6341 2765 -494 87 C
ATOM 458 O MET A 73 15.346 6.464 43.987 1.00 63.10 O
ANISOU 458 O MET A 73 9086 8505 6384 2674 -474 62 O
ATOM 459 CB MET A 73 15.007 3.617 42.688 1.00 61.76 C
ANISOU 459 CB MET A 73 8368 8849 6248 2339 -571 -57 C
ATOM 460 CG MET A 73 16.304 3.686 41.951 1.00 65.61 C
ANISOU 460 CG MET A 73 8993 9109 6827 2214 -549 10 C
ATOM 461 SD MET A 73 17.185 2.098 42.165 1.00 68.33 S
ANISOU 461 SD MET A 73 9192 9424 7344 1847 -561 -58 S
ATOM 462 CE MET A 73 16.448 1.138 40.808 1.00 65.44 C
ANISOU 462 CE MET A 73 8591 9388 6885 1844 -586 -107 C
ATOM 463 N ILE A 74 15.083 7.020 41.815 1.00 59.80 N
ANISOU 463 N ILE A 74 8712 8210 5798 2944 -458 189 N
ATOM 464 CA ILE A 74 15.756 8.326 41.909 1.00 59.93 C
ANISOU 464 CA ILE A 74 9064 7878 5828 3037 -379 277 C
ATOM 465 C ILE A 74 14.812 9.312 42.625 1.00 66.01 C
ANISOU 465 C ILE A 74 9945 8649 6485 3323 -343 285 C
ATOM 466 O ILE A 74 15.274 10.118 43.434 1.00 66.86 O
ANISOU 466 O ILE A 74 10285 8471 6648 3306 -284 288 O
ATOM 467 CB ILE A 74 16.224 8.844 40.504 1.00 63.50 C
ANISOU 467 CB ILE A 74 9655 8249 6225 3134 -339 393 C
ATOM 468 CG1 ILE A 74 17.518 8.125 40.062 1.00 61.83 C
ANISOU 468 CG1 ILE A 74 9422 7910 6160 2817 -349 388 C
ATOM 469 CG2 ILE A 74 16.436 10.373 40.478 1.00 65.43 C
ANISOU 469 CG2 ILE A 74 10253 8195 6413 3345 -236 497 C
ATOM 470 CD1 ILE A 74 17.734 8.059 38.560 1.00 70.85 C
ANISOU 470 CD1 ILE A 74 10555 9128 7238 2872 -344 466 C
ATOM 471 N LEU A 75 13.492 9.215 42.361 1.00 63.79 N
ANISOU 471 N LEU A 75 9485 8708 6042 3574 -378 277 N
ATOM 472 CA LEU A 75 12.458 10.077 42.961 1.00 65.57 C
ANISOU 472 CA LEU A 75 9776 9003 6135 3887 -347 286 C
ATOM 473 C LEU A 75 12.255 9.795 44.466 1.00 68.54 C
ANISOU 473 C LEU A 75 10086 9369 6586 3760 -366 176 C
ATOM 474 O LEU A 75 11.637 10.590 45.167 1.00 69.30 O
ANISOU 474 O LEU A 75 10283 9445 6604 3978 -328 175 O
ATOM 475 CB LEU A 75 11.122 9.916 42.206 1.00 67.14 C
ANISOU 475 CB LEU A 75 9748 9637 6128 4172 -390 299 C
ATOM 476 CG LEU A 75 11.042 10.515 40.795 1.00 72.94 C
ANISOU 476 CG LEU A 75 10577 10415 6720 4428 -359 429 C
ATOM 477 CD1 LEU A 75 9.868 9.947 40.041 1.00 73.96 C
ANISOU 477 CD1 LEU A 75 10386 11048 6666 4595 -428 404 C
ATOM 478 CD2 LEU A 75 10.959 12.036 40.831 1.00 76.82 C
ANISOU 478 CD2 LEU A 75 11408 10664 7118 4768 -254 547 C
ATOM 479 N THR A 76 12.790 8.664 44.938 1.00 63.86 N
ANISOU 479 N THR A 76 9333 8791 6141 3419 -417 91 N
ATOM 480 CA THR A 76 12.788 8.162 46.314 1.00 62.45 C
ANISOU 480 CA THR A 76 9071 8606 6051 3241 -438 -8 C
ATOM 481 C THR A 76 13.852 8.916 47.159 1.00 64.62 C
ANISOU 481 C THR A 76 9627 8484 6442 3121 -380 -1 C
ATOM 482 O THR A 76 13.666 9.080 48.367 1.00 65.10 O
ANISOU 482 O THR A 76 9711 8503 6521 3103 -372 -63 O
ATOM 483 CB THR A 76 13.034 6.626 46.251 1.00 68.50 C
ANISOU 483 CB THR A 76 9566 9546 6914 2940 -501 -80 C
ATOM 484 OG1 THR A 76 11.869 5.923 46.669 1.00 71.56 O
ANISOU 484 OG1 THR A 76 9692 10277 7219 2984 -541 -161 O
ATOM 485 CG2 THR A 76 14.250 6.161 47.029 1.00 65.09 C
ANISOU 485 CG2 THR A 76 9189 8876 6664 2625 -499 -113 C
ATOM 486 N PHE A 77 14.958 9.352 46.514 1.00 59.01 N
ANISOU 486 N PHE A 77 9119 7503 5800 3029 -338 65 N
ATOM 487 CA PHE A 77 16.103 10.019 47.139 1.00 57.62 C
ANISOU 487 CA PHE A 77 9199 6967 5729 2869 -279 63 C
ATOM 488 C PHE A 77 15.744 11.329 47.885 1.00 64.51 C
ANISOU 488 C PHE A 77 10328 7652 6531 3075 -198 61 C
ATOM 489 O PHE A 77 16.205 11.439 49.016 1.00 64.37 O
ANISOU 489 O PHE A 77 10380 7490 6587 2916 -183 -10 O
ATOM 490 CB PHE A 77 17.233 10.286 46.120 1.00 58.20 C
ANISOU 490 CB PHE A 77 9431 6822 5861 2755 -239 139 C
ATOM 491 CG PHE A 77 17.830 9.098 45.389 1.00 56.24 C
ANISOU 491 CG PHE A 77 8980 6694 5694 2535 -300 141 C
ATOM 492 CD1 PHE A 77 17.700 7.805 45.892 1.00 56.31 C
ANISOU 492 CD1 PHE A 77 8722 6904 5771 2354 -374 64 C
ATOM 493 CD2 PHE A 77 18.580 9.279 44.233 1.00 57.02 C
ANISOU 493 CD2 PHE A 77 9176 6685 5805 2502 -271 221 C
ATOM 494 CE1 PHE A 77 18.267 6.715 45.220 1.00 54.95 C
ANISOU 494 CE1 PHE A 77 8387 6817 5673 2160 -414 64 C
ATOM 495 CE2 PHE A 77 19.150 8.187 43.567 1.00 57.21 C
ANISOU 495 CE2 PHE A 77 9021 6813 5902 2304 -321 218 C
ATOM 496 CZ PHE A 77 18.977 6.914 44.057 1.00 53.17 C
ANISOU 496 CZ PHE A 77 8252 6495 5456 2140 -390 138 C
ATOM 497 N PRO A 78 14.950 12.313 47.363 1.00 64.07 N
ANISOU 497 N PRO A 78 10419 7595 6329 3424 -138 134 N
ATOM 498 CA PRO A 78 14.681 13.538 48.160 1.00 65.78 C
ANISOU 498 CA PRO A 78 10908 7599 6488 3608 -44 125 C
ATOM 499 C PRO A 78 14.100 13.267 49.555 1.00 69.39 C
ANISOU 499 C PRO A 78 11243 8174 6948 3586 -79 14 C
ATOM 500 O PRO A 78 14.514 13.913 50.520 1.00 69.76 O
ANISOU 500 O PRO A 78 11490 7981 7035 3515 -18 -41 O
ATOM 501 CB PRO A 78 13.691 14.333 47.296 1.00 69.68 C
ANISOU 501 CB PRO A 78 11492 8181 6803 4029 6 230 C
ATOM 502 CG PRO A 78 13.202 13.383 46.267 1.00 73.44 C
ANISOU 502 CG PRO A 78 11662 9015 7226 4063 -88 262 C
ATOM 503 CD PRO A 78 14.309 12.407 46.035 1.00 66.83 C
ANISOU 503 CD PRO A 78 10713 8127 6550 3677 -143 231 C
ATOM 504 N PHE A 79 13.177 12.288 49.668 1.00 64.34 N
ANISOU 504 N PHE A 79 10273 7908 6264 3620 -171 -26 N
ATOM 505 CA PHE A 79 12.559 11.884 50.930 1.00 62.91 C
ANISOU 505 CA PHE A 79 9937 7887 6079 3591 -209 -127 C
ATOM 506 C PHE A 79 13.631 11.354 51.872 1.00 64.70 C
ANISOU 506 C PHE A 79 10155 7963 6466 3224 -231 -203 C
ATOM 507 O PHE A 79 13.625 11.687 53.058 1.00 64.60 O
ANISOU 507 O PHE A 79 10213 7870 6463 3192 -208 -275 O
ATOM 508 CB PHE A 79 11.472 10.823 50.690 1.00 63.94 C
ANISOU 508 CB PHE A 79 9705 8453 6134 3653 -295 -153 C
ATOM 509 CG PHE A 79 10.344 11.276 49.798 1.00 67.34 C
ANISOU 509 CG PHE A 79 10093 9110 6382 4022 -285 -87 C
ATOM 510 CD1 PHE A 79 9.210 11.873 50.333 1.00 72.00 C
ANISOU 510 CD1 PHE A 79 10676 9852 6829 4325 -259 -104 C
ATOM 511 CD2 PHE A 79 10.414 11.106 48.417 1.00 70.05 C
ANISOU 511 CD2 PHE A 79 10391 9539 6684 4079 -301 -8 C
ATOM 512 CE1 PHE A 79 8.161 12.289 49.505 1.00 75.00 C
ANISOU 512 CE1 PHE A 79 10999 10479 7020 4691 -251 -37 C
ATOM 513 CE2 PHE A 79 9.363 11.521 47.590 1.00 74.30 C
ANISOU 513 CE2 PHE A 79 10873 10325 7032 4436 -295 57 C
ATOM 514 CZ PHE A 79 8.243 12.107 48.140 1.00 74.03 C
ANISOU 514 CZ PHE A 79 10824 10453 6851 4745 -271 44 C
ATOM 515 N LYS A 80 14.587 10.573 51.320 1.00 59.04 N
ANISOU 515 N LYS A 80 9360 7210 5863 2960 -270 -184 N
ATOM 516 CA LYS A 80 15.704 10.001 52.069 1.00 56.43 C
ANISOU 516 CA LYS A 80 9005 6761 5674 2622 -293 -239 C
ATOM 517 C LYS A 80 16.670 11.113 52.504 1.00 60.55 C
ANISOU 517 C LYS A 80 9841 6930 6237 2543 -211 -252 C
ATOM 518 O LYS A 80 17.001 11.172 53.690 1.00 60.05 O
ANISOU 518 O LYS A 80 9803 6800 6213 2405 -208 -331 O
ATOM 519 CB LYS A 80 16.434 8.915 51.249 1.00 55.82 C
ANISOU 519 CB LYS A 80 8768 6749 5692 2402 -345 -207 C
ATOM 520 CG LYS A 80 17.517 8.215 52.052 1.00 54.66 C
ANISOU 520 CG LYS A 80 8567 6524 5676 2084 -371 -254 C
ATOM 521 CD LYS A 80 18.274 7.176 51.275 1.00 55.89 C
ANISOU 521 CD LYS A 80 8572 6743 5920 1889 -413 -221 C
ATOM 522 CE LYS A 80 19.271 6.457 52.148 1.00 58.64 C
ANISOU 522 CE LYS A 80 8855 7047 6380 1615 -435 -259 C
ATOM 523 NZ LYS A 80 18.636 5.809 53.330 1.00 67.27 N
ANISOU 523 NZ LYS A 80 9793 8303 7465 1590 -466 -322 N
ATOM 524 N ILE A 81 17.101 11.989 51.554 1.00 57.02 N
ANISOU 524 N ILE A 81 9630 6266 5771 2624 -140 -178 N
ATOM 525 CA ILE A 81 18.029 13.111 51.783 1.00 57.66 C
ANISOU 525 CA ILE A 81 10037 5991 5881 2536 -39 -189 C
ATOM 526 C ILE A 81 17.588 13.949 52.997 1.00 64.10 C
ANISOU 526 C ILE A 81 11011 6701 6642 2636 20 -270 C
ATOM 527 O ILE A 81 18.375 14.139 53.924 1.00 63.29 O
ANISOU 527 O ILE A 81 10992 6454 6601 2411 42 -356 O
ATOM 528 CB ILE A 81 18.201 14.013 50.510 1.00 61.43 C
ANISOU 528 CB ILE A 81 10758 6273 6311 2689 49 -81 C
ATOM 529 CG1 ILE A 81 18.858 13.239 49.358 1.00 59.83 C
ANISOU 529 CG1 ILE A 81 10424 6135 6173 2537 -1 -14 C
ATOM 530 CG2 ILE A 81 19.018 15.277 50.822 1.00 63.05 C
ANISOU 530 CG2 ILE A 81 11337 6093 6528 2617 181 -104 C
ATOM 531 CD1 ILE A 81 18.559 13.759 47.945 1.00 65.31 C
ANISOU 531 CD1 ILE A 81 11229 6802 6783 2766 46 110 C
ATOM 532 N LEU A 82 16.334 14.424 52.987 1.00 63.46 N
ANISOU 532 N LEU A 82 10957 6718 6438 2973 46 -248 N
ATOM 533 CA LEU A 82 15.785 15.299 54.020 1.00 65.53 C
ANISOU 533 CA LEU A 82 11387 6883 6629 3125 115 -316 C
ATOM 534 C LEU A 82 15.482 14.576 55.347 1.00 70.50 C
ANISOU 534 C LEU A 82 11794 7712 7281 3005 40 -425 C
ATOM 535 O LEU A 82 15.562 15.221 56.398 1.00 71.83 O
ANISOU 535 O LEU A 82 12118 7741 7435 2985 96 -512 O
ATOM 536 CB LEU A 82 14.532 16.020 53.500 1.00 67.42 C
ANISOU 536 CB LEU A 82 11714 7189 6715 3558 169 -243 C
ATOM 537 CG LEU A 82 14.750 16.951 52.306 1.00 73.21 C
ANISOU 537 CG LEU A 82 12726 7691 7398 3735 272 -125 C
ATOM 538 CD1 LEU A 82 13.487 17.090 51.482 1.00 74.75 C
ANISOU 538 CD1 LEU A 82 12841 8120 7439 4144 266 -25 C
ATOM 539 CD2 LEU A 82 15.268 18.308 52.742 1.00 76.96 C
ANISOU 539 CD2 LEU A 82 13624 7752 7866 3750 431 -154 C
ATOM 540 N SER A 83 15.150 13.265 55.322 1.00 65.95 N
ANISOU 540 N SER A 83 10874 7449 6736 2920 -75 -424 N
ATOM 541 CA SER A 83 14.894 12.520 56.563 1.00 64.88 C
ANISOU 541 CA SER A 83 10532 7500 6621 2799 -138 -514 C
ATOM 542 C SER A 83 16.219 12.163 57.242 1.00 68.35 C
ANISOU 542 C SER A 83 10977 7812 7179 2442 -156 -571 C
ATOM 543 O SER A 83 16.327 12.257 58.470 1.00 68.18 O
ANISOU 543 O SER A 83 10964 7784 7159 2351 -153 -660 O
ATOM 544 CB SER A 83 14.057 11.271 56.308 1.00 67.57 C
ANISOU 544 CB SER A 83 10528 8204 6944 2831 -231 -495 C
ATOM 545 OG SER A 83 14.742 10.308 55.522 1.00 77.72 O
ANISOU 545 OG SER A 83 11668 9540 8323 2623 -286 -451 O
ATOM 546 N ASP A 84 17.237 11.802 56.433 1.00 64.91 N
ANISOU 546 N ASP A 84 10539 7291 6834 2250 -172 -520 N
ATOM 547 CA ASP A 84 18.578 11.455 56.909 1.00 64.39 C
ANISOU 547 CA ASP A 84 10466 7130 6871 1922 -190 -562 C
ATOM 548 C ASP A 84 19.330 12.711 57.346 1.00 70.71 C
ANISOU 548 C ASP A 84 11573 7629 7664 1843 -95 -624 C
ATOM 549 O ASP A 84 20.248 12.601 58.157 1.00 70.73 O
ANISOU 549 O ASP A 84 11571 7591 7714 1596 -104 -698 O
ATOM 550 CB ASP A 84 19.376 10.669 55.844 1.00 65.31 C
ANISOU 550 CB ASP A 84 10477 7267 7073 1765 -231 -487 C
ATOM 551 CG ASP A 84 18.937 9.220 55.615 1.00 76.81 C
ANISOU 551 CG ASP A 84 11618 9006 8560 1738 -320 -454 C
ATOM 552 OD1 ASP A 84 17.768 8.885 55.942 1.00 78.40 O
ANISOU 552 OD1 ASP A 84 11681 9409 8699 1893 -347 -470 O
ATOM 553 OD2 ASP A 84 19.747 8.432 55.071 1.00 80.76 O
ANISOU 553 OD2 ASP A 84 12018 9526 9142 1561 -354 -414 O
ATOM 554 N ALA A 85 18.915 13.904 56.854 1.00 69.52 N
ANISOU 554 N ALA A 85 11693 7279 7443 2058 4 -599 N
ATOM 555 CA ALA A 85 19.489 15.203 57.233 1.00 70.97 C
ANISOU 555 CA ALA A 85 12214 7145 7608 2005 125 -664 C
ATOM 556 C ALA A 85 19.164 15.528 58.699 1.00 76.59 C
ANISOU 556 C ALA A 85 12954 7872 8274 1998 140 -790 C
ATOM 557 O ALA A 85 19.959 16.190 59.370 1.00 77.22 O
ANISOU 557 O ALA A 85 13207 7766 8367 1800 202 -889 O
ATOM 558 CB ALA A 85 18.964 16.298 56.323 1.00 73.51 C
ANISOU 558 CB ALA A 85 12813 7264 7854 2287 236 -589 C
ATOM 559 N LYS A 86 17.999 15.048 59.189 1.00 73.28 N
ANISOU 559 N LYS A 86 12354 7694 7796 2201 85 -792 N
ATOM 560 CA LYS A 86 17.552 15.219 60.570 1.00 73.79 C
ANISOU 560 CA LYS A 86 12404 7826 7809 2220 88 -902 C
ATOM 561 C LYS A 86 18.173 14.115 61.432 1.00 77.79 C
ANISOU 561 C LYS A 86 12648 8529 8381 1940 -13 -954 C
ATOM 562 O LYS A 86 18.210 12.953 61.018 1.00 75.86 O
ANISOU 562 O LYS A 86 12144 8490 8190 1877 -105 -886 O
ATOM 563 CB LYS A 86 16.013 15.205 60.657 1.00 76.43 C
ANISOU 563 CB LYS A 86 12648 8352 8041 2566 79 -876 C
ATOM 564 CG LYS A 86 15.462 15.781 61.960 1.00 90.43 C
ANISOU 564 CG LYS A 86 14499 10125 9735 2654 122 -988 C
ATOM 565 CD LYS A 86 13.939 15.691 62.058 1.00 96.90 C
ANISOU 565 CD LYS A 86 15192 11179 10447 2992 107 -961 C
ATOM 566 CE LYS A 86 13.450 16.125 63.423 1.00104.09 C
ANISOU 566 CE LYS A 86 16153 12112 11282 3060 144 -1077 C
ATOM 567 NZ LYS A 86 11.976 15.982 63.567 1.00110.04 N
ANISOU 567 NZ LYS A 86 16752 13133 11925 3378 126 -1055 N
ATOM 568 N LEU A 87 18.682 14.489 62.614 1.00 76.46 N
ANISOU 568 N LEU A 87 12558 8294 8200 1775 13 -1074 N
ATOM 569 CA LEU A 87 19.326 13.582 63.566 1.00 75.56 C
ANISOU 569 CA LEU A 87 12224 8360 8126 1524 -70 -1127 C
ATOM 570 C LEU A 87 18.299 12.635 64.226 1.00 80.11 C
ANISOU 570 C LEU A 87 12533 9239 8667 1644 -147 -1114 C
ATOM 571 O LEU A 87 18.572 11.439 64.358 1.00 78.37 O
ANISOU 571 O LEU A 87 12062 9218 8498 1509 -231 -1074 O
ATOM 572 CB LEU A 87 20.078 14.402 64.629 1.00 76.90 C
ANISOU 572 CB LEU A 87 12569 8385 8263 1339 -10 -1271 C
ATOM 573 CG LEU A 87 21.456 13.899 65.079 1.00 80.53 C
ANISOU 573 CG LEU A 87 12916 8907 8776 998 -60 -1315 C
ATOM 574 CD1 LEU A 87 22.487 13.963 63.951 1.00 79.92 C
ANISOU 574 CD1 LEU A 87 12913 8679 8773 841 -41 -1258 C
ATOM 575 CD2 LEU A 87 21.960 14.721 66.258 1.00 84.53 C
ANISOU 575 CD2 LEU A 87 13561 9339 9219 842 -6 -1478 C
ATOM 576 N GLY A 88 17.134 13.174 64.600 1.00 78.21 N
ANISOU 576 N GLY A 88 12354 9026 8335 1897 -107 -1145 N
ATOM 577 CA GLY A 88 16.046 12.414 65.214 1.00 77.51 C
ANISOU 577 CA GLY A 88 12031 9224 8197 2025 -163 -1142 C
ATOM 578 C GLY A 88 14.994 11.943 64.225 1.00 81.25 C
ANISOU 578 C GLY A 88 12365 9855 8651 2248 -190 -1042 C
ATOM 579 O GLY A 88 15.113 12.194 63.020 1.00 81.09 O
ANISOU 579 O GLY A 88 12431 9725 8654 2319 -171 -968 O
ATOM 580 N THR A 89 13.943 11.260 64.731 1.00 77.12 N
ANISOU 580 N THR A 89 11620 9608 8074 2355 -232 -1045 N
ATOM 581 CA THR A 89 12.837 10.745 63.910 1.00 76.23 C
ANISOU 581 CA THR A 89 11333 9708 7922 2550 -260 -974 C
ATOM 582 C THR A 89 11.781 11.856 63.681 1.00 80.55 C
ANISOU 582 C THR A 89 12033 10225 8348 2896 -192 -981 C
ATOM 583 O THR A 89 11.901 12.952 64.234 1.00 82.26 O
ANISOU 583 O THR A 89 12493 10242 8519 2973 -118 -1045 O
ATOM 584 CB THR A 89 12.238 9.455 64.536 1.00 83.27 C
ANISOU 584 CB THR A 89 11914 10915 8808 2477 -323 -979 C
ATOM 585 OG1 THR A 89 11.520 8.730 63.532 1.00 83.23 O
ANISOU 585 OG1 THR A 89 11720 11105 8798 2555 -357 -911 O
ATOM 586 CG2 THR A 89 11.332 9.726 65.741 1.00 81.65 C
ANISOU 586 CG2 THR A 89 11674 10850 8499 2610 -301 -1057 C
ATOM 587 N GLY A 90 10.769 11.546 62.872 1.00 75.61 N
ANISOU 587 N GLY A 90 11261 9804 7661 3100 -213 -919 N
ATOM 588 CA GLY A 90 9.671 12.450 62.545 1.00 76.73 C
ANISOU 588 CA GLY A 90 11499 9985 7669 3465 -156 -906 C
ATOM 589 C GLY A 90 8.683 11.855 61.557 1.00 78.97 C
ANISOU 589 C GLY A 90 11549 10569 7888 3634 -201 -838 C
ATOM 590 O GLY A 90 8.832 10.690 61.170 1.00 77.23 O
ANISOU 590 O GLY A 90 11097 10514 7734 3444 -271 -813 O
ATOM 591 N PRO A 91 7.660 12.629 61.111 1.00 75.86 N
ANISOU 591 N PRO A 91 11210 10260 7353 3997 -156 -809 N
ATOM 592 CA PRO A 91 6.684 12.075 60.153 1.00 75.04 C
ANISOU 592 CA PRO A 91 10857 10492 7162 4162 -202 -754 C
ATOM 593 C PRO A 91 7.304 11.670 58.812 1.00 74.65 C
ANISOU 593 C PRO A 91 10788 10391 7184 4056 -236 -670 C
ATOM 594 O PRO A 91 6.866 10.666 58.251 1.00 73.24 O
ANISOU 594 O PRO A 91 10332 10501 6996 3992 -300 -658 O
ATOM 595 CB PRO A 91 5.664 13.206 59.978 1.00 79.70 C
ANISOU 595 CB PRO A 91 11573 11129 7580 4596 -133 -731 C
ATOM 596 CG PRO A 91 6.380 14.440 60.389 1.00 85.62 C
ANISOU 596 CG PRO A 91 12716 11457 8358 4644 -35 -742 C
ATOM 597 CD PRO A 91 7.321 14.020 61.477 1.00 79.63 C
ANISOU 597 CD PRO A 91 11971 10552 7731 4282 -56 -829 C
ATOM 598 N LEU A 92 8.327 12.413 58.316 1.00 69.25 N
ANISOU 598 N LEU A 92 10396 9346 6571 4017 -187 -622 N
ATOM 599 CA LEU A 92 8.995 12.110 57.043 1.00 67.31 C
ANISOU 599 CA LEU A 92 10158 9025 6393 3917 -210 -540 C
ATOM 600 C LEU A 92 9.813 10.825 57.143 1.00 67.86 C
ANISOU 600 C LEU A 92 10039 9135 6608 3534 -284 -562 C
ATOM 601 O LEU A 92 9.765 10.015 56.210 1.00 66.49 O
ANISOU 601 O LEU A 92 9686 9126 6453 3469 -335 -521 O
ATOM 602 CB LEU A 92 9.879 13.271 56.538 1.00 68.09 C
ANISOU 602 CB LEU A 92 10628 8720 6522 3965 -123 -484 C
ATOM 603 CG LEU A 92 10.631 13.038 55.205 1.00 72.09 C
ANISOU 603 CG LEU A 92 11166 9134 7092 3871 -137 -393 C
ATOM 604 CD1 LEU A 92 9.685 13.033 54.000 1.00 73.10 C
ANISOU 604 CD1 LEU A 92 11189 9499 7086 4171 -149 -307 C
ATOM 605 CD2 LEU A 92 11.727 14.051 55.011 1.00 75.51 C
ANISOU 605 CD2 LEU A 92 11960 9141 7588 3802 -47 -366 C
ATOM 606 N ARG A 93 10.555 10.636 58.260 1.00 62.79 N
ANISOU 606 N ARG A 93 9439 8356 6061 3291 -286 -628 N
ATOM 607 CA ARG A 93 11.357 9.429 58.493 1.00 59.89 C
ANISOU 607 CA ARG A 93 8906 8024 5825 2950 -346 -642 C
ATOM 608 C ARG A 93 10.429 8.207 58.562 1.00 62.83 C
ANISOU 608 C ARG A 93 8947 8760 6165 2921 -403 -662 C
ATOM 609 O ARG A 93 10.760 7.168 57.994 1.00 61.39 O
ANISOU 609 O ARG A 93 8607 8661 6056 2736 -444 -638 O
ATOM 610 CB ARG A 93 12.236 9.564 59.757 1.00 58.23 C
ANISOU 610 CB ARG A 93 8804 7633 5689 2740 -333 -707 C
ATOM 611 CG ARG A 93 13.088 8.333 60.120 1.00 60.51 C
ANISOU 611 CG ARG A 93 8928 7967 6097 2417 -388 -712 C
ATOM 612 CD ARG A 93 13.985 7.822 58.995 1.00 61.21 C
ANISOU 612 CD ARG A 93 9005 7971 6283 2262 -411 -643 C
ATOM 613 NE ARG A 93 14.503 6.485 59.295 1.00 60.36 N
ANISOU 613 NE ARG A 93 8700 7969 6266 2012 -458 -639 N
ATOM 614 CZ ARG A 93 15.012 5.642 58.400 1.00 66.21 C
ANISOU 614 CZ ARG A 93 9345 8728 7082 1880 -484 -586 C
ATOM 615 NH1 ARG A 93 15.074 5.979 57.116 1.00 52.54 N
ANISOU 615 NH1 ARG A 93 7681 6934 5347 1963 -476 -533 N
ATOM 616 NH2 ARG A 93 15.455 4.453 58.780 1.00 48.93 N
ANISOU 616 NH2 ARG A 93 7001 6621 4969 1676 -510 -581 N
ATOM 617 N THR A 94 9.247 8.357 59.192 1.00 60.68 N
ANISOU 617 N THR A 94 8576 8704 5774 3110 -394 -709 N
ATOM 618 CA THR A 94 8.227 7.305 59.271 1.00 59.92 C
ANISOU 618 CA THR A 94 8168 8976 5623 3095 -432 -740 C
ATOM 619 C THR A 94 7.740 6.974 57.848 1.00 62.82 C
ANISOU 619 C THR A 94 8404 9527 5940 3186 -456 -693 C
ATOM 620 O THR A 94 7.645 5.796 57.504 1.00 61.40 O
ANISOU 620 O THR A 94 8004 9528 5798 3004 -490 -704 O
ATOM 621 CB THR A 94 7.085 7.725 60.205 1.00 66.50 C
ANISOU 621 CB THR A 94 8945 9997 6326 3301 -409 -801 C
ATOM 622 OG1 THR A 94 7.640 8.105 61.467 1.00 65.41 O
ANISOU 622 OG1 THR A 94 8953 9666 6232 3211 -384 -847 O
ATOM 623 CG2 THR A 94 6.061 6.615 60.412 1.00 63.98 C
ANISOU 623 CG2 THR A 94 8299 10063 5948 3246 -438 -846 C
ATOM 624 N PHE A 95 7.502 8.014 57.018 1.00 60.08 N
ANISOU 624 N PHE A 95 8208 9115 5505 3460 -430 -639 N
ATOM 625 CA PHE A 95 7.051 7.893 55.626 1.00 59.91 C
ANISOU 625 CA PHE A 95 8087 9268 5409 3592 -450 -586 C
ATOM 626 C PHE A 95 8.107 7.184 54.747 1.00 62.23 C
ANISOU 626 C PHE A 95 8378 9430 5836 3336 -477 -544 C
ATOM 627 O PHE A 95 7.734 6.398 53.880 1.00 62.52 O
ANISOU 627 O PHE A 95 8212 9699 5845 3293 -512 -542 O
ATOM 628 CB PHE A 95 6.683 9.271 55.050 1.00 63.32 C
ANISOU 628 CB PHE A 95 8731 9610 5716 3963 -400 -519 C
ATOM 629 CG PHE A 95 6.141 9.239 53.640 1.00 65.36 C
ANISOU 629 CG PHE A 95 8884 10083 5865 4147 -419 -457 C
ATOM 630 CD1 PHE A 95 4.866 8.750 53.379 1.00 69.10 C
ANISOU 630 CD1 PHE A 95 9064 11003 6188 4289 -454 -493 C
ATOM 631 CD2 PHE A 95 6.897 9.714 52.576 1.00 66.64 C
ANISOU 631 CD2 PHE A 95 9237 10021 6063 4177 -400 -366 C
ATOM 632 CE1 PHE A 95 4.364 8.726 52.075 1.00 70.77 C
ANISOU 632 CE1 PHE A 95 9162 11448 6279 4460 -476 -442 C
ATOM 633 CE2 PHE A 95 6.392 9.693 51.275 1.00 70.02 C
ANISOU 633 CE2 PHE A 95 9563 10665 6375 4357 -419 -305 C
ATOM 634 CZ PHE A 95 5.133 9.194 51.032 1.00 69.25 C
ANISOU 634 CZ PHE A 95 9163 11025 6122 4499 -460 -345 C
ATOM 635 N VAL A 96 9.405 7.449 54.979 1.00 56.89 N
ANISOU 635 N VAL A 96 7917 8402 5295 3162 -459 -519 N
ATOM 636 CA VAL A 96 10.514 6.808 54.269 1.00 54.66 C
ANISOU 636 CA VAL A 96 7644 7979 5145 2914 -480 -481 C
ATOM 637 C VAL A 96 10.521 5.302 54.624 1.00 58.15 C
ANISOU 637 C VAL A 96 7831 8601 5663 2644 -519 -531 C
ATOM 638 O VAL A 96 10.553 4.456 53.731 1.00 56.88 O
ANISOU 638 O VAL A 96 7528 8560 5525 2541 -542 -520 O
ATOM 639 CB VAL A 96 11.877 7.504 54.574 1.00 57.66 C
ANISOU 639 CB VAL A 96 8304 7969 5634 2793 -445 -455 C
ATOM 640 CG1 VAL A 96 13.059 6.676 54.077 1.00 55.29 C
ANISOU 640 CG1 VAL A 96 7973 7559 5474 2507 -470 -427 C
ATOM 641 CG2 VAL A 96 11.927 8.900 53.967 1.00 59.05 C
ANISOU 641 CG2 VAL A 96 8750 7944 5742 3035 -386 -396 C
ATOM 642 N CYS A 97 10.436 4.990 55.923 1.00 55.98 N
ANISOU 642 N CYS A 97 7507 8349 5413 2543 -516 -588 N
ATOM 643 CA CYS A 97 10.408 3.635 56.475 1.00 55.45 C
ANISOU 643 CA CYS A 97 7233 8427 5410 2304 -531 -629 C
ATOM 644 C CYS A 97 9.263 2.800 55.903 1.00 58.25 C
ANISOU 644 C CYS A 97 7326 9127 5678 2329 -543 -667 C
ATOM 645 O CYS A 97 9.447 1.633 55.563 1.00 55.36 O
ANISOU 645 O CYS A 97 6818 8839 5376 2118 -546 -679 O
ATOM 646 CB CYS A 97 10.309 3.703 57.996 1.00 56.61 C
ANISOU 646 CB CYS A 97 7391 8561 5557 2265 -518 -677 C
ATOM 647 SG CYS A 97 11.898 3.905 58.838 1.00 59.92 S
ANISOU 647 SG CYS A 97 8009 8646 6110 2064 -512 -658 S
ATOM 648 N GLN A 98 8.078 3.414 55.830 1.00 56.88 N
ANISOU 648 N GLN A 98 7092 9168 5351 2587 -542 -691 N
ATOM 649 CA GLN A 98 6.821 2.814 55.435 1.00 57.21 C
ANISOU 649 CA GLN A 98 6870 9595 5272 2643 -551 -745 C
ATOM 650 C GLN A 98 6.593 2.802 53.923 1.00 60.94 C
ANISOU 650 C GLN A 98 7277 10196 5682 2729 -572 -717 C
ATOM 651 O GLN A 98 6.024 1.832 53.432 1.00 60.61 O
ANISOU 651 O GLN A 98 7005 10419 5606 2609 -580 -771 O
ATOM 652 CB GLN A 98 5.702 3.596 56.134 1.00 60.72 C
ANISOU 652 CB GLN A 98 7283 10224 5565 2910 -540 -780 C
ATOM 653 CG GLN A 98 4.293 3.042 56.021 1.00 78.15 C
ANISOU 653 CG GLN A 98 9192 12877 7625 2969 -545 -854 C
ATOM 654 CD GLN A 98 3.375 3.627 57.066 1.00 97.60 C
ANISOU 654 CD GLN A 98 11620 15494 9971 3165 -527 -897 C
ATOM 655 OE1 GLN A 98 3.500 4.789 57.482 1.00 90.91 O
ANISOU 655 OE1 GLN A 98 10980 14470 9091 3391 -511 -862 O
ATOM 656 NE2 GLN A 98 2.427 2.824 57.518 1.00 94.53 N
ANISOU 656 NE2 GLN A 98 10972 15434 9511 3074 -519 -979 N
ATOM 657 N VAL A 99 6.985 3.859 53.181 1.00 57.26 N
ANISOU 657 N VAL A 99 7006 9561 5188 2933 -573 -640 N
ATOM 658 CA VAL A 99 6.652 3.892 51.757 1.00 57.38 C
ANISOU 658 CA VAL A 99 6945 9744 5115 3049 -592 -609 C
ATOM 659 C VAL A 99 7.880 4.044 50.827 1.00 60.49 C
ANISOU 659 C VAL A 99 7521 9846 5617 2963 -593 -529 C
ATOM 660 O VAL A 99 8.216 3.075 50.147 1.00 58.48 O
ANISOU 660 O VAL A 99 7150 9646 5424 2755 -609 -545 O
ATOM 661 CB VAL A 99 5.565 4.974 51.427 1.00 63.27 C
ANISOU 661 CB VAL A 99 7689 10697 5655 3450 -589 -584 C
ATOM 662 CG1 VAL A 99 5.074 4.854 49.985 1.00 63.95 C
ANISOU 662 CG1 VAL A 99 7635 11046 5619 3568 -615 -562 C
ATOM 663 CG2 VAL A 99 4.378 4.900 52.388 1.00 63.96 C
ANISOU 663 CG2 VAL A 99 7597 11077 5626 3550 -585 -663 C
ATOM 664 N THR A 100 8.487 5.254 50.733 1.00 57.89 N
ANISOU 664 N THR A 100 7473 9225 5298 3128 -567 -447 N
ATOM 665 CA THR A 100 9.550 5.561 49.761 1.00 56.52 C
ANISOU 665 CA THR A 100 7479 8798 5199 3085 -558 -365 C
ATOM 666 C THR A 100 10.773 4.649 49.823 1.00 56.71 C
ANISOU 666 C THR A 100 7507 8632 5407 2734 -567 -372 C
ATOM 667 O THR A 100 11.282 4.317 48.751 1.00 56.21 O
ANISOU 667 O THR A 100 7435 8546 5377 2658 -577 -336 O
ATOM 668 CB THR A 100 9.981 7.025 49.784 1.00 63.49 C
ANISOU 668 CB THR A 100 8682 9378 6063 3292 -507 -286 C
ATOM 669 OG1 THR A 100 10.410 7.389 51.084 1.00 63.28 O
ANISOU 669 OG1 THR A 100 8792 9140 6113 3212 -481 -322 O
ATOM 670 CG2 THR A 100 8.890 7.952 49.319 1.00 63.69 C
ANISOU 670 CG2 THR A 100 8734 9572 5895 3682 -487 -243 C
ATOM 671 N SER A 101 11.240 4.209 51.012 1.00 50.60 N
ANISOU 671 N SER A 101 6740 7742 4743 2534 -563 -416 N
ATOM 672 CA SER A 101 12.406 3.303 51.001 1.00 47.65 C
ANISOU 672 CA SER A 101 6362 7214 4530 2231 -568 -411 C
ATOM 673 C SER A 101 11.979 1.877 50.605 1.00 48.64 C
ANISOU 673 C SER A 101 6229 7586 4665 2064 -584 -464 C
ATOM 674 O SER A 101 12.811 1.118 50.118 1.00 46.60 O
ANISOU 674 O SER A 101 5957 7238 4509 1866 -583 -449 O
ATOM 675 CB SER A 101 13.190 3.322 52.316 1.00 49.57 C
ANISOU 675 CB SER A 101 6706 7251 4875 2080 -555 -427 C
ATOM 676 OG SER A 101 12.563 2.645 53.393 1.00 54.41 O
ANISOU 676 OG SER A 101 7166 8028 5481 2011 -558 -492 O
ATOM 677 N VAL A 102 10.680 1.538 50.762 1.00 45.97 N
ANISOU 677 N VAL A 102 5692 7563 4212 2145 -591 -531 N
ATOM 678 CA VAL A 102 10.122 0.251 50.319 1.00 45.51 C
ANISOU 678 CA VAL A 102 5389 7763 4139 1986 -591 -600 C
ATOM 679 C VAL A 102 10.076 0.267 48.779 1.00 50.63 C
ANISOU 679 C VAL A 102 5997 8512 4727 2050 -608 -579 C
ATOM 680 O VAL A 102 10.445 -0.736 48.163 1.00 49.88 O
ANISOU 680 O VAL A 102 5816 8440 4696 1847 -600 -604 O
ATOM 681 CB VAL A 102 8.740 -0.096 50.947 1.00 49.19 C
ANISOU 681 CB VAL A 102 5642 8559 4489 2031 -586 -690 C
ATOM 682 CG1 VAL A 102 8.255 -1.467 50.483 1.00 48.60 C
ANISOU 682 CG1 VAL A 102 5334 8724 4409 1814 -568 -775 C
ATOM 683 CG2 VAL A 102 8.798 -0.048 52.473 1.00 48.10 C
ANISOU 683 CG2 VAL A 102 5556 8321 4400 1986 -568 -704 C
ATOM 684 N ILE A 103 9.678 1.427 48.166 1.00 48.71 N
ANISOU 684 N ILE A 103 5837 8312 4361 2341 -624 -525 N
ATOM 685 CA ILE A 103 9.628 1.624 46.709 1.00 49.10 C
ANISOU 685 CA ILE A 103 5868 8459 4328 2450 -639 -486 C
ATOM 686 C ILE A 103 11.046 1.481 46.143 1.00 53.73 C
ANISOU 686 C ILE A 103 6615 8738 5063 2284 -630 -422 C
ATOM 687 O ILE A 103 11.223 0.802 45.123 1.00 54.14 O
ANISOU 687 O ILE A 103 6571 8880 5119 2176 -637 -436 O
ATOM 688 CB ILE A 103 8.952 2.953 46.263 1.00 53.77 C
ANISOU 688 CB ILE A 103 6546 9134 4750 2826 -644 -421 C
ATOM 689 CG1 ILE A 103 7.482 3.011 46.723 1.00 54.58 C
ANISOU 689 CG1 ILE A 103 6450 9602 4685 3005 -656 -489 C
ATOM 690 CG2 ILE A 103 9.054 3.150 44.715 1.00 55.83 C
ANISOU 690 CG2 ILE A 103 6807 9477 4929 2936 -657 -362 C
ATOM 691 CD1 ILE A 103 6.818 4.369 46.556 1.00 57.38 C
ANISOU 691 CD1 ILE A 103 6908 10023 4869 3410 -649 -417 C
ATOM 692 N PHE A 104 12.054 2.079 46.824 1.00 49.60 N
ANISOU 692 N PHE A 104 6320 7871 4654 2248 -611 -363 N
ATOM 693 CA PHE A 104 13.457 1.962 46.416 1.00 48.25 C
ANISOU 693 CA PHE A 104 6294 7419 4622 2080 -599 -306 C
ATOM 694 C PHE A 104 13.851 0.497 46.228 1.00 51.08 C
ANISOU 694 C PHE A 104 6498 7832 5080 1801 -599 -358 C
ATOM 695 O PHE A 104 14.369 0.137 45.175 1.00 51.58 O
ANISOU 695 O PHE A 104 6552 7877 5167 1730 -598 -336 O
ATOM 696 CB PHE A 104 14.420 2.611 47.437 1.00 49.39 C
ANISOU 696 CB PHE A 104 6653 7241 4871 2024 -578 -270 C
ATOM 697 CG PHE A 104 15.866 2.447 47.012 1.00 50.16 C
ANISOU 697 CG PHE A 104 6871 7091 5099 1843 -565 -219 C
ATOM 698 CD1 PHE A 104 16.430 3.297 46.066 1.00 54.20 C
ANISOU 698 CD1 PHE A 104 7551 7451 5590 1936 -548 -140 C
ATOM 699 CD2 PHE A 104 16.633 1.384 47.486 1.00 50.74 C
ANISOU 699 CD2 PHE A 104 6875 7101 5301 1586 -565 -244 C
ATOM 700 CE1 PHE A 104 17.742 3.108 45.626 1.00 54.34 C
ANISOU 700 CE1 PHE A 104 7658 7271 5718 1761 -535 -98 C
ATOM 701 CE2 PHE A 104 17.939 1.191 47.036 1.00 52.75 C
ANISOU 701 CE2 PHE A 104 7217 7166 5660 1435 -554 -196 C
ATOM 702 CZ PHE A 104 18.487 2.061 46.118 1.00 51.95 C
ANISOU 702 CZ PHE A 104 7271 6928 5540 1515 -541 -128 C
ATOM 703 N TYR A 105 13.636 -0.329 47.264 1.00 45.47 N
ANISOU 703 N TYR A 105 5681 7174 4423 1650 -589 -423 N
ATOM 704 CA TYR A 105 14.000 -1.737 47.254 1.00 43.40 C
ANISOU 704 CA TYR A 105 5301 6931 4258 1391 -566 -468 C
ATOM 705 C TYR A 105 13.255 -2.543 46.205 1.00 48.75 C
ANISOU 705 C TYR A 105 5789 7876 4860 1348 -563 -536 C
ATOM 706 O TYR A 105 13.900 -3.318 45.514 1.00 46.39 O
ANISOU 706 O TYR A 105 5476 7517 4632 1191 -543 -538 O
ATOM 707 CB TYR A 105 13.781 -2.368 48.630 1.00 43.23 C
ANISOU 707 CB TYR A 105 5218 6922 4286 1271 -543 -514 C
ATOM 708 CG TYR A 105 14.801 -1.978 49.679 1.00 42.60 C
ANISOU 708 CG TYR A 105 5301 6576 4309 1223 -540 -459 C
ATOM 709 CD1 TYR A 105 16.161 -2.212 49.482 1.00 42.63 C
ANISOU 709 CD1 TYR A 105 5409 6355 4433 1090 -530 -402 C
ATOM 710 CD2 TYR A 105 14.400 -1.465 50.909 1.00 43.44 C
ANISOU 710 CD2 TYR A 105 5436 6683 4386 1297 -543 -474 C
ATOM 711 CE1 TYR A 105 17.099 -1.900 50.468 1.00 40.45 C
ANISOU 711 CE1 TYR A 105 5255 5879 4235 1034 -529 -362 C
ATOM 712 CE2 TYR A 105 15.326 -1.162 51.903 1.00 43.57 C
ANISOU 712 CE2 TYR A 105 5585 6487 4484 1237 -540 -438 C
ATOM 713 CZ TYR A 105 16.674 -1.390 51.683 1.00 47.42 C
ANISOU 713 CZ TYR A 105 6163 6772 5082 1101 -535 -384 C
ATOM 714 OH TYR A 105 17.575 -1.100 52.680 1.00 47.92 O
ANISOU 714 OH TYR A 105 6332 6667 5207 1036 -534 -358 O
ATOM 715 N PHE A 106 11.914 -2.383 46.075 1.00 49.82 N
ANISOU 715 N PHE A 106 5770 8319 4842 1481 -578 -600 N
ATOM 716 CA PHE A 106 11.158 -3.179 45.107 1.00 51.18 C
ANISOU 716 CA PHE A 106 5736 8787 4923 1417 -573 -687 C
ATOM 717 C PHE A 106 11.514 -2.779 43.645 1.00 55.31 C
ANISOU 717 C PHE A 106 6302 9319 5396 1512 -597 -639 C
ATOM 718 O PHE A 106 11.547 -3.666 42.791 1.00 54.25 O
ANISOU 718 O PHE A 106 6058 9293 5260 1362 -581 -698 O
ATOM 719 CB PHE A 106 9.636 -3.197 45.400 1.00 55.17 C
ANISOU 719 CB PHE A 106 6034 9662 5265 1514 -582 -780 C
ATOM 720 CG PHE A 106 8.702 -2.196 44.758 1.00 59.28 C
ANISOU 720 CG PHE A 106 6491 10445 5589 1815 -627 -766 C
ATOM 721 CD1 PHE A 106 8.409 -2.265 43.397 1.00 63.24 C
ANISOU 721 CD1 PHE A 106 6882 11169 5978 1864 -646 -789 C
ATOM 722 CD2 PHE A 106 7.985 -1.295 45.537 1.00 63.30 C
ANISOU 722 CD2 PHE A 106 7020 11027 6005 2052 -644 -744 C
ATOM 723 CE1 PHE A 106 7.521 -1.364 42.807 1.00 66.24 C
ANISOU 723 CE1 PHE A 106 7191 11820 6155 2167 -686 -767 C
ATOM 724 CE2 PHE A 106 7.073 -0.405 44.950 1.00 68.40 C
ANISOU 724 CE2 PHE A 106 7603 11935 6453 2359 -677 -725 C
ATOM 725 CZ PHE A 106 6.851 -0.445 43.589 1.00 67.24 C
ANISOU 725 CZ PHE A 106 7353 12002 6193 2421 -699 -731 C
ATOM 726 N THR A 107 11.866 -1.497 43.379 1.00 52.67 N
ANISOU 726 N THR A 107 6143 8842 5028 1740 -623 -531 N
ATOM 727 CA THR A 107 12.293 -1.077 42.033 1.00 53.15 C
ANISOU 727 CA THR A 107 6270 8882 5043 1833 -636 -466 C
ATOM 728 C THR A 107 13.758 -1.510 41.778 1.00 55.14 C
ANISOU 728 C THR A 107 6655 8827 5467 1629 -612 -419 C
ATOM 729 O THR A 107 14.141 -1.687 40.614 1.00 55.04 O
ANISOU 729 O THR A 107 6637 8836 5439 1605 -613 -402 O
ATOM 730 CB THR A 107 12.095 0.435 41.786 1.00 62.23 C
ANISOU 730 CB THR A 107 7574 9988 6082 2157 -653 -363 C
ATOM 731 OG1 THR A 107 12.821 1.182 42.756 1.00 63.84 O
ANISOU 731 OG1 THR A 107 8000 9866 6391 2175 -635 -296 O
ATOM 732 CG2 THR A 107 10.642 0.842 41.787 1.00 62.76 C
ANISOU 732 CG2 THR A 107 7490 10406 5950 2398 -676 -401 C
ATOM 733 N MET A 108 14.569 -1.681 42.856 1.00 49.14 N
ANISOU 733 N MET A 108 6005 7808 4859 1491 -592 -398 N
ATOM 734 CA MET A 108 15.957 -2.135 42.754 1.00 47.54 C
ANISOU 734 CA MET A 108 5907 7344 4811 1303 -568 -355 C
ATOM 735 C MET A 108 15.982 -3.574 42.244 1.00 50.39 C
ANISOU 735 C MET A 108 6118 7812 5216 1089 -538 -434 C
ATOM 736 O MET A 108 16.779 -3.899 41.363 1.00 50.52 O
ANISOU 736 O MET A 108 6171 7744 5282 1007 -525 -409 O
ATOM 737 CB MET A 108 16.691 -2.018 44.101 1.00 49.26 C
ANISOU 737 CB MET A 108 6240 7325 5150 1219 -555 -325 C
ATOM 738 CG MET A 108 18.168 -2.399 44.035 1.00 52.46 C
ANISOU 738 CG MET A 108 6745 7489 5700 1048 -533 -274 C
ATOM 739 SD MET A 108 18.805 -2.895 45.657 1.00 57.14 S
ANISOU 739 SD MET A 108 7366 7931 6415 897 -513 -276 S
ATOM 740 CE MET A 108 20.161 -3.823 45.191 1.00 53.14 C
ANISOU 740 CE MET A 108 6877 7279 6035 704 -480 -242 C
ATOM 741 N TYR A 109 15.078 -4.423 42.764 1.00 45.58 N
ANISOU 741 N TYR A 109 5345 7393 4579 998 -519 -534 N
ATOM 742 CA TYR A 109 15.002 -5.824 42.359 1.00 44.32 C
ANISOU 742 CA TYR A 109 5058 7327 4456 779 -469 -625 C
ATOM 743 C TYR A 109 14.283 -5.964 41.018 1.00 49.54 C
ANISOU 743 C TYR A 109 5582 8261 4981 817 -482 -693 C
ATOM 744 O TYR A 109 14.473 -6.978 40.342 1.00 49.51 O
ANISOU 744 O TYR A 109 5512 8293 5006 642 -439 -760 O
ATOM 745 CB TYR A 109 14.401 -6.700 43.474 1.00 43.91 C
ANISOU 745 CB TYR A 109 4908 7343 4433 639 -424 -705 C
ATOM 746 CG TYR A 109 15.390 -6.813 44.613 1.00 41.58 C
ANISOU 746 CG TYR A 109 4750 6766 4284 564 -401 -632 C
ATOM 747 CD1 TYR A 109 16.507 -7.639 44.511 1.00 42.10 C
ANISOU 747 CD1 TYR A 109 4884 6633 4481 401 -350 -602 C
ATOM 748 CD2 TYR A 109 15.302 -5.976 45.724 1.00 41.38 C
ANISOU 748 CD2 TYR A 109 4795 6671 4255 682 -433 -584 C
ATOM 749 CE1 TYR A 109 17.476 -7.677 45.515 1.00 39.95 C
ANISOU 749 CE1 TYR A 109 4725 6130 4323 357 -336 -525 C
ATOM 750 CE2 TYR A 109 16.263 -6.009 46.737 1.00 40.45 C
ANISOU 750 CE2 TYR A 109 4796 6320 4255 619 -419 -519 C
ATOM 751 CZ TYR A 109 17.353 -6.855 46.622 1.00 44.86 C
ANISOU 751 CZ TYR A 109 5402 6710 4933 461 -374 -486 C
ATOM 752 OH TYR A 109 18.298 -6.904 47.616 1.00 45.89 O
ANISOU 752 OH TYR A 109 5628 6650 5160 412 -362 -420 O
ATOM 753 N ILE A 110 13.548 -4.910 40.589 1.00 46.46 N
ANISOU 753 N ILE A 110 5165 8050 4438 1059 -538 -668 N
ATOM 754 CA ILE A 110 12.931 -4.845 39.268 1.00 47.15 C
ANISOU 754 CA ILE A 110 5130 8415 4372 1144 -561 -710 C
ATOM 755 C ILE A 110 14.087 -4.663 38.262 1.00 50.13 C
ANISOU 755 C ILE A 110 5643 8595 4809 1137 -560 -627 C
ATOM 756 O ILE A 110 14.165 -5.421 37.301 1.00 50.60 O
ANISOU 756 O ILE A 110 5615 8762 4849 1016 -541 -691 O
ATOM 757 CB ILE A 110 11.820 -3.751 39.182 1.00 51.43 C
ANISOU 757 CB ILE A 110 5609 9211 4721 1441 -615 -690 C
ATOM 758 CG1 ILE A 110 10.511 -4.290 39.785 1.00 52.32 C
ANISOU 758 CG1 ILE A 110 5499 9646 4735 1397 -609 -820 C
ATOM 759 CG2 ILE A 110 11.582 -3.291 37.733 1.00 52.55 C
ANISOU 759 CG2 ILE A 110 5710 9549 4709 1610 -648 -662 C
ATOM 760 CD1 ILE A 110 9.534 -3.274 40.196 1.00 58.87 C
ANISOU 760 CD1 ILE A 110 6289 10664 5416 1676 -650 -793 C
ATOM 761 N SER A 111 15.022 -3.727 38.549 1.00 45.89 N
ANISOU 761 N SER A 111 5320 7764 4351 1238 -572 -495 N
ATOM 762 CA SER A 111 16.232 -3.449 37.765 1.00 45.29 C
ANISOU 762 CA SER A 111 5394 7470 4343 1224 -564 -403 C
ATOM 763 C SER A 111 17.109 -4.686 37.606 1.00 48.62 C
ANISOU 763 C SER A 111 5799 7769 4904 961 -516 -446 C
ATOM 764 O SER A 111 17.487 -4.999 36.478 1.00 49.71 O
ANISOU 764 O SER A 111 5921 7942 5026 917 -506 -452 O
ATOM 765 CB SER A 111 17.052 -2.330 38.402 1.00 49.45 C
ANISOU 765 CB SER A 111 6147 7699 4942 1325 -569 -279 C
ATOM 766 OG SER A 111 16.479 -1.060 38.133 1.00 64.08 O
ANISOU 766 OG SER A 111 8075 9613 6660 1596 -594 -210 O
ATOM 767 N ILE A 112 17.413 -5.399 38.719 1.00 43.57 N
ANISOU 767 N ILE A 112 5165 6996 4392 801 -482 -475 N
ATOM 768 CA ILE A 112 18.239 -6.620 38.741 1.00 42.03 C
ANISOU 768 CA ILE A 112 4971 6668 4331 572 -422 -506 C
ATOM 769 C ILE A 112 17.598 -7.714 37.853 1.00 47.50 C
ANISOU 769 C ILE A 112 5503 7583 4963 445 -383 -635 C
ATOM 770 O ILE A 112 18.321 -8.431 37.165 1.00 46.92 O
ANISOU 770 O ILE A 112 5449 7430 4950 322 -340 -647 O
ATOM 771 CB ILE A 112 18.468 -7.111 40.205 1.00 43.80 C
ANISOU 771 CB ILE A 112 5222 6749 4669 466 -389 -507 C
ATOM 772 CG1 ILE A 112 19.360 -6.126 40.993 1.00 42.97 C
ANISOU 772 CG1 ILE A 112 5282 6410 4634 549 -419 -390 C
ATOM 773 CG2 ILE A 112 19.054 -8.530 40.259 1.00 43.67 C
ANISOU 773 CG2 ILE A 112 5188 6641 4765 248 -308 -550 C
ATOM 774 CD1 ILE A 112 19.334 -6.318 42.536 1.00 43.97 C
ANISOU 774 CD1 ILE A 112 5423 6458 4825 505 -407 -389 C
ATOM 775 N SER A 113 16.255 -7.832 37.880 1.00 45.59 N
ANISOU 775 N SER A 113 5102 7628 4594 471 -394 -737 N
ATOM 776 CA SER A 113 15.499 -8.802 37.088 1.00 46.26 C
ANISOU 776 CA SER A 113 5014 7969 4593 337 -357 -884 C
ATOM 777 C SER A 113 15.623 -8.512 35.593 1.00 51.19 C
ANISOU 777 C SER A 113 5613 8718 5117 412 -386 -880 C
ATOM 778 O SER A 113 15.850 -9.442 34.814 1.00 51.01 O
ANISOU 778 O SER A 113 5547 8724 5111 248 -334 -961 O
ATOM 779 CB SER A 113 14.030 -8.799 37.497 1.00 49.66 C
ANISOU 779 CB SER A 113 5267 8713 4887 368 -372 -988 C
ATOM 780 OG SER A 113 13.880 -9.163 38.858 1.00 56.43 O
ANISOU 780 OG SER A 113 6142 9468 5830 286 -336 -997 O
ATOM 781 N PHE A 114 15.503 -7.225 35.197 1.00 47.78 N
ANISOU 781 N PHE A 114 5224 8347 4582 664 -459 -782 N
ATOM 782 CA PHE A 114 15.594 -6.836 33.793 1.00 48.16 C
ANISOU 782 CA PHE A 114 5258 8523 4517 769 -488 -757 C
ATOM 783 C PHE A 114 17.032 -6.888 33.291 1.00 49.55 C
ANISOU 783 C PHE A 114 5596 8409 4821 705 -462 -667 C
ATOM 784 O PHE A 114 17.232 -7.158 32.104 1.00 49.25 O
ANISOU 784 O PHE A 114 5520 8465 4727 675 -453 -695 O
ATOM 785 CB PHE A 114 14.947 -5.464 33.526 1.00 51.18 C
ANISOU 785 CB PHE A 114 5650 9060 4736 1078 -558 -668 C
ATOM 786 CG PHE A 114 13.438 -5.538 33.559 1.00 54.13 C
ANISOU 786 CG PHE A 114 5804 9835 4929 1152 -586 -778 C
ATOM 787 CD1 PHE A 114 12.738 -6.258 32.595 1.00 57.97 C
ANISOU 787 CD1 PHE A 114 6083 10667 5277 1067 -582 -916 C
ATOM 788 CD2 PHE A 114 12.718 -4.921 34.575 1.00 56.43 C
ANISOU 788 CD2 PHE A 114 6084 10177 5180 1293 -612 -757 C
ATOM 789 CE1 PHE A 114 11.347 -6.370 32.657 1.00 60.57 C
ANISOU 789 CE1 PHE A 114 6184 11401 5428 1113 -606 -1032 C
ATOM 790 CE2 PHE A 114 11.322 -5.032 34.635 1.00 60.51 C
ANISOU 790 CE2 PHE A 114 6378 11092 5523 1355 -635 -865 C
ATOM 791 CZ PHE A 114 10.649 -5.756 33.680 1.00 60.03 C
ANISOU 791 CZ PHE A 114 6099 11386 5323 1261 -632 -1002 C
ATOM 792 N LEU A 115 18.029 -6.698 34.189 1.00 43.72 N
ANISOU 792 N LEU A 115 5022 7344 4246 670 -446 -573 N
ATOM 793 CA LEU A 115 19.440 -6.789 33.810 1.00 41.58 C
ANISOU 793 CA LEU A 115 4888 6814 4096 597 -417 -493 C
ATOM 794 C LEU A 115 19.773 -8.230 33.498 1.00 46.10 C
ANISOU 794 C LEU A 115 5396 7376 4745 367 -346 -595 C
ATOM 795 O LEU A 115 20.464 -8.489 32.510 1.00 46.06 O
ANISOU 795 O LEU A 115 5417 7332 4750 322 -323 -585 O
ATOM 796 CB LEU A 115 20.392 -6.194 34.858 1.00 40.12 C
ANISOU 796 CB LEU A 115 4872 6328 4044 614 -420 -377 C
ATOM 797 CG LEU A 115 20.417 -4.646 34.912 1.00 45.16 C
ANISOU 797 CG LEU A 115 5640 6899 4620 831 -468 -258 C
ATOM 798 CD1 LEU A 115 21.208 -4.134 36.104 1.00 43.98 C
ANISOU 798 CD1 LEU A 115 5635 6486 4591 814 -465 -182 C
ATOM 799 CD2 LEU A 115 20.913 -4.028 33.602 1.00 47.25 C
ANISOU 799 CD2 LEU A 115 5979 7151 4823 918 -473 -182 C
ATOM 800 N GLY A 116 19.195 -9.150 34.273 1.00 43.39 N
ANISOU 800 N GLY A 116 4967 7080 4438 229 -302 -698 N
ATOM 801 CA GLY A 116 19.310 -10.588 34.069 1.00 43.57 C
ANISOU 801 CA GLY A 116 4939 7094 4523 5 -211 -813 C
ATOM 802 C GLY A 116 18.632 -11.000 32.774 1.00 50.62 C
ANISOU 802 C GLY A 116 5695 8259 5278 -42 -202 -938 C
ATOM 803 O GLY A 116 19.157 -11.849 32.054 1.00 52.32 O
ANISOU 803 O GLY A 116 5919 8425 5533 -179 -136 -995 O
ATOM 804 N LEU A 117 17.496 -10.343 32.427 1.00 47.05 N
ANISOU 804 N LEU A 117 5117 8108 4652 89 -269 -978 N
ATOM 805 CA LEU A 117 16.751 -10.604 31.195 1.00 47.75 C
ANISOU 805 CA LEU A 117 5048 8522 4574 69 -275 -1100 C
ATOM 806 C LEU A 117 17.465 -10.038 29.968 1.00 51.73 C
ANISOU 806 C LEU A 117 5615 9011 5030 182 -308 -1015 C
ATOM 807 O LEU A 117 17.512 -10.726 28.951 1.00 51.88 O
ANISOU 807 O LEU A 117 5566 9146 4999 68 -270 -1114 O
ATOM 808 CB LEU A 117 15.317 -10.052 31.264 1.00 49.29 C
ANISOU 808 CB LEU A 117 5073 9075 4579 200 -339 -1157 C
ATOM 809 CG LEU A 117 14.275 -10.858 32.056 1.00 54.61 C
ANISOU 809 CG LEU A 117 5603 9913 5233 38 -294 -1310 C
ATOM 810 CD1 LEU A 117 12.918 -10.189 31.962 1.00 56.02 C
ANISOU 810 CD1 LEU A 117 5600 10485 5201 204 -367 -1355 C
ATOM 811 CD2 LEU A 117 14.148 -12.296 31.528 1.00 57.79 C
ANISOU 811 CD2 LEU A 117 5916 10399 5641 -255 -193 -1499 C
ATOM 812 N ILE A 118 18.010 -8.796 30.055 1.00 48.43 N
ANISOU 812 N ILE A 118 5331 8450 4621 395 -369 -839 N
ATOM 813 CA ILE A 118 18.779 -8.122 28.990 1.00 48.67 C
ANISOU 813 CA ILE A 118 5454 8425 4615 512 -392 -730 C
ATOM 814 C ILE A 118 19.999 -8.991 28.610 1.00 52.78 C
ANISOU 814 C ILE A 118 6053 8725 5277 328 -321 -740 C
ATOM 815 O ILE A 118 20.291 -9.161 27.417 1.00 53.54 O
ANISOU 815 O ILE A 118 6127 8907 5310 314 -309 -761 O
ATOM 816 CB ILE A 118 19.203 -6.676 29.417 1.00 51.20 C
ANISOU 816 CB ILE A 118 5940 8565 4949 736 -443 -543 C
ATOM 817 CG1 ILE A 118 17.993 -5.712 29.400 1.00 52.95 C
ANISOU 817 CG1 ILE A 118 6091 9043 4986 975 -507 -522 C
ATOM 818 CG2 ILE A 118 20.342 -6.124 28.536 1.00 50.93 C
ANISOU 818 CG2 ILE A 118 6048 8367 4935 793 -437 -419 C
ATOM 819 CD1 ILE A 118 18.155 -4.406 30.218 1.00 59.26 C
ANISOU 819 CD1 ILE A 118 7058 9649 5812 1171 -536 -373 C
ATOM 820 N THR A 119 20.660 -9.573 29.630 1.00 47.51 N
ANISOU 820 N THR A 119 5468 7795 4789 197 -270 -728 N
ATOM 821 CA THR A 119 21.829 -10.446 29.494 1.00 46.33 C
ANISOU 821 CA THR A 119 5397 7424 4782 41 -193 -728 C
ATOM 822 C THR A 119 21.456 -11.735 28.728 1.00 50.20 C
ANISOU 822 C THR A 119 5779 8062 5235 -141 -118 -903 C
ATOM 823 O THR A 119 22.216 -12.133 27.849 1.00 49.33 O
ANISOU 823 O THR A 119 5704 7894 5146 -198 -76 -908 O
ATOM 824 CB THR A 119 22.441 -10.735 30.886 1.00 48.64 C
ANISOU 824 CB THR A 119 5785 7451 5245 -25 -160 -672 C
ATOM 825 OG1 THR A 119 22.672 -9.493 31.537 1.00 48.68 O
ANISOU 825 OG1 THR A 119 5879 7356 5260 131 -229 -537 O
ATOM 826 CG2 THR A 119 23.764 -11.458 30.812 1.00 44.52 C
ANISOU 826 CG2 THR A 119 5357 6697 4861 -130 -87 -634 C
ATOM 827 N ILE A 120 20.307 -12.377 29.061 1.00 47.96 N
ANISOU 827 N ILE A 120 5366 7967 4891 -242 -94 -1051 N
ATOM 828 CA ILE A 120 19.838 -13.599 28.374 1.00 49.29 C
ANISOU 828 CA ILE A 120 5431 8288 5009 -443 -10 -1243 C
ATOM 829 C ILE A 120 19.549 -13.243 26.902 1.00 54.53 C
ANISOU 829 C ILE A 120 5998 9222 5497 -373 -56 -1287 C
ATOM 830 O ILE A 120 19.976 -13.969 25.999 1.00 54.34 O
ANISOU 830 O ILE A 120 5976 9199 5473 -490 8 -1366 O
ATOM 831 CB ILE A 120 18.598 -14.265 29.073 1.00 52.93 C
ANISOU 831 CB ILE A 120 5766 8918 5426 -579 30 -1399 C
ATOM 832 CG1 ILE A 120 18.925 -14.713 30.514 1.00 51.90 C
ANISOU 832 CG1 ILE A 120 5741 8511 5468 -659 93 -1354 C
ATOM 833 CG2 ILE A 120 18.065 -15.462 28.260 1.00 54.29 C
ANISOU 833 CG2 ILE A 120 5825 9283 5519 -804 121 -1620 C
ATOM 834 CD1 ILE A 120 17.686 -14.972 31.449 1.00 54.00 C
ANISOU 834 CD1 ILE A 120 5898 8931 5687 -721 99 -1445 C
ATOM 835 N ASP A 121 18.870 -12.095 26.685 1.00 51.73 N
ANISOU 835 N ASP A 121 5573 9090 4993 -165 -162 -1225 N
ATOM 836 CA ASP A 121 18.506 -11.560 25.376 1.00 53.56 C
ANISOU 836 CA ASP A 121 5710 9610 5031 -42 -219 -1236 C
ATOM 837 C ASP A 121 19.748 -11.299 24.520 1.00 57.59 C
ANISOU 837 C ASP A 121 6349 9944 5587 8 -210 -1124 C
ATOM 838 O ASP A 121 19.817 -11.777 23.391 1.00 57.69 O
ANISOU 838 O ASP A 121 6300 10105 5516 -61 -183 -1212 O
ATOM 839 CB ASP A 121 17.685 -10.269 25.530 1.00 56.26 C
ANISOU 839 CB ASP A 121 5999 10152 5225 220 -323 -1141 C
ATOM 840 CG ASP A 121 17.331 -9.616 24.214 1.00 68.76 C
ANISOU 840 CG ASP A 121 7497 12035 6593 392 -382 -1121 C
ATOM 841 OD1 ASP A 121 16.372 -10.079 23.563 1.00 72.60 O
ANISOU 841 OD1 ASP A 121 7783 12896 6906 338 -388 -1280 O
ATOM 842 OD2 ASP A 121 18.041 -8.673 23.814 1.00 73.00 O
ANISOU 842 OD2 ASP A 121 8170 12439 7130 572 -415 -949 O
ATOM 843 N ARG A 122 20.721 -10.562 25.074 1.00 53.60 N
ANISOU 843 N ARG A 122 6019 9137 5212 113 -229 -940 N
ATOM 844 CA ARG A 122 21.970 -10.220 24.403 1.00 52.92 C
ANISOU 844 CA ARG A 122 6062 8866 5178 158 -219 -819 C
ATOM 845 C ARG A 122 22.825 -11.470 24.158 1.00 56.90 C
ANISOU 845 C ARG A 122 6598 9214 5806 -52 -119 -901 C
ATOM 846 O ARG A 122 23.451 -11.549 23.101 1.00 57.54 O
ANISOU 846 O ARG A 122 6702 9305 5855 -55 -100 -888 O
ATOM 847 CB ARG A 122 22.740 -9.136 25.181 1.00 50.86 C
ANISOU 847 CB ARG A 122 5970 8336 5019 293 -254 -622 C
ATOM 848 CG ARG A 122 22.111 -7.742 25.025 1.00 62.15 C
ANISOU 848 CG ARG A 122 7416 9895 6304 541 -335 -512 C
ATOM 849 CD ARG A 122 22.509 -7.093 23.712 1.00 77.50 C
ANISOU 849 CD ARG A 122 9399 11914 8132 661 -348 -429 C
ATOM 850 NE ARG A 122 21.405 -6.425 23.014 1.00 90.51 N
ANISOU 850 NE ARG A 122 10952 13882 9555 859 -406 -424 N
ATOM 851 CZ ARG A 122 20.582 -7.017 22.151 1.00105.81 C
ANISOU 851 CZ ARG A 122 12706 16166 11334 832 -415 -563 C
ATOM 852 NH1 ARG A 122 19.639 -6.316 21.539 1.00 92.73 N
ANISOU 852 NH1 ARG A 122 10960 14815 9457 1044 -472 -539 N
ATOM 853 NH2 ARG A 122 20.683 -8.315 21.910 1.00 95.63 N
ANISOU 853 NH2 ARG A 122 11318 14924 10093 596 -362 -732 N
ATOM 854 N TYR A 123 22.802 -12.467 25.074 1.00 52.56 N
ANISOU 854 N TYR A 123 6054 8535 5383 -220 -49 -988 N
ATOM 855 CA TYR A 123 23.542 -13.713 24.851 1.00 52.02 C
ANISOU 855 CA TYR A 123 6029 8312 5423 -403 64 -1068 C
ATOM 856 C TYR A 123 22.921 -14.497 23.679 1.00 57.15 C
ANISOU 856 C TYR A 123 6558 9215 5942 -525 110 -1258 C
ATOM 857 O TYR A 123 23.656 -15.002 22.829 1.00 56.06 O
ANISOU 857 O TYR A 123 6459 9022 5820 -587 170 -1287 O
ATOM 858 CB TYR A 123 23.622 -14.598 26.113 1.00 52.07 C
ANISOU 858 CB TYR A 123 6088 8113 5584 -534 143 -1103 C
ATOM 859 CG TYR A 123 24.088 -16.007 25.808 1.00 55.01 C
ANISOU 859 CG TYR A 123 6499 8366 6035 -721 281 -1218 C
ATOM 860 CD1 TYR A 123 25.417 -16.269 25.481 1.00 56.78 C
ANISOU 860 CD1 TYR A 123 6834 8382 6357 -712 332 -1136 C
ATOM 861 CD2 TYR A 123 23.183 -17.064 25.753 1.00 57.07 C
ANISOU 861 CD2 TYR A 123 6686 8738 6259 -907 369 -1416 C
ATOM 862 CE1 TYR A 123 25.839 -17.554 25.137 1.00 57.78 C
ANISOU 862 CE1 TYR A 123 7008 8399 6545 -860 469 -1240 C
ATOM 863 CE2 TYR A 123 23.594 -18.353 25.413 1.00 58.67 C
ANISOU 863 CE2 TYR A 123 6950 8814 6527 -1078 515 -1528 C
ATOM 864 CZ TYR A 123 24.926 -18.594 25.115 1.00 66.53 C
ANISOU 864 CZ TYR A 123 8067 9587 7622 -1041 565 -1435 C
ATOM 865 OH TYR A 123 25.336 -19.864 24.791 1.00 69.88 O
ANISOU 865 OH TYR A 123 8568 9875 8109 -1188 720 -1541 O
ATOM 866 N GLN A 124 21.573 -14.597 23.646 1.00 55.48 N
ANISOU 866 N GLN A 124 6193 9294 5594 -564 86 -1396 N
ATOM 867 CA GLN A 124 20.829 -15.312 22.603 1.00 56.74 C
ANISOU 867 CA GLN A 124 6208 9748 5602 -699 126 -1603 C
ATOM 868 C GLN A 124 21.013 -14.671 21.222 1.00 62.19 C
ANISOU 868 C GLN A 124 6854 10637 6139 -570 64 -1564 C
ATOM 869 O GLN A 124 20.986 -15.387 20.225 1.00 63.15 O
ANISOU 869 O GLN A 124 6916 10894 6184 -695 121 -1708 O
ATOM 870 CB GLN A 124 19.354 -15.411 22.965 1.00 58.98 C
ANISOU 870 CB GLN A 124 6320 10331 5759 -753 100 -1743 C
ATOM 871 CG GLN A 124 19.096 -16.542 23.954 1.00 65.94 C
ANISOU 871 CG GLN A 124 7226 11062 6765 -978 212 -1863 C
ATOM 872 CD GLN A 124 17.695 -16.575 24.515 1.00 78.65 C
ANISOU 872 CD GLN A 124 8670 12950 8262 -1033 189 -1986 C
ATOM 873 OE1 GLN A 124 16.788 -15.838 24.097 1.00 67.53 O
ANISOU 873 OE1 GLN A 124 7101 11894 6664 -904 87 -2002 O
ATOM 874 NE2 GLN A 124 17.494 -17.454 25.484 1.00 75.38 N
ANISOU 874 NE2 GLN A 124 8291 12392 7958 -1221 290 -2071 N
ATOM 875 N LYS A 125 21.265 -13.352 21.173 1.00 59.53 N
ANISOU 875 N LYS A 125 6564 10295 5761 -325 -39 -1368 N
ATOM 876 CA LYS A 125 21.552 -12.611 19.946 1.00 61.18 C
ANISOU 876 CA LYS A 125 6764 10651 5831 -172 -92 -1288 C
ATOM 877 C LYS A 125 22.912 -13.028 19.350 1.00 67.44 C
ANISOU 877 C LYS A 125 7681 11212 6732 -239 -22 -1245 C
ATOM 878 O LYS A 125 23.072 -12.988 18.130 1.00 68.45 O
ANISOU 878 O LYS A 125 7768 11503 6738 -216 -23 -1270 O
ATOM 879 CB LYS A 125 21.546 -11.097 20.214 1.00 63.37 C
ANISOU 879 CB LYS A 125 7106 10910 6061 100 -192 -1075 C
ATOM 880 CG LYS A 125 21.219 -10.267 18.978 1.00 83.04 C
ANISOU 880 CG LYS A 125 9537 13683 8332 290 -255 -1018 C
ATOM 881 CD LYS A 125 22.012 -8.970 18.893 1.00 92.68 C
ANISOU 881 CD LYS A 125 10928 14713 9573 509 -295 -774 C
ATOM 882 CE LYS A 125 21.510 -8.112 17.755 1.00105.89 C
ANISOU 882 CE LYS A 125 12543 16685 11005 727 -352 -708 C
ATOM 883 NZ LYS A 125 22.203 -6.799 17.702 1.00115.99 N
ANISOU 883 NZ LYS A 125 14013 17762 12297 936 -370 -469 N
ATOM 884 N THR A 126 23.887 -13.408 20.205 1.00 64.51 N
ANISOU 884 N THR A 126 7452 10484 6576 -312 37 -1177 N
ATOM 885 CA THR A 126 25.234 -13.817 19.769 1.00 64.62 C
ANISOU 885 CA THR A 126 7579 10274 6699 -364 108 -1128 C
ATOM 886 C THR A 126 25.214 -15.216 19.133 1.00 74.46 C
ANISOU 886 C THR A 126 8781 11566 7943 -571 221 -1332 C
ATOM 887 O THR A 126 26.035 -15.492 18.256 1.00 74.44 O
ANISOU 887 O THR A 126 8824 11514 7947 -593 270 -1330 O
ATOM 888 CB THR A 126 26.255 -13.764 20.920 1.00 63.67 C
ANISOU 888 CB THR A 126 7605 9797 6788 -359 133 -990 C
ATOM 889 OG1 THR A 126 26.002 -14.810 21.857 1.00 61.42 O
ANISOU 889 OG1 THR A 126 7325 9396 6616 -507 209 -1093 O
ATOM 890 CG2 THR A 126 26.311 -12.406 21.622 1.00 58.44 C
ANISOU 890 CG2 THR A 126 7005 9062 6136 -181 37 -803 C
ATOM 891 N THR A 127 24.283 -16.091 19.579 1.00 75.54 N
ANISOU 891 N THR A 127 8839 11792 8070 -729 272 -1511 N
ATOM 892 CA THR A 127 24.127 -17.463 19.077 1.00 78.40 C
ANISOU 892 CA THR A 127 9175 12186 8429 -955 400 -1732 C
ATOM 893 C THR A 127 23.239 -17.492 17.822 1.00 89.77 C
ANISOU 893 C THR A 127 10449 14021 9640 -996 374 -1895 C
ATOM 894 O THR A 127 23.363 -18.412 17.009 1.00 91.15 O
ANISOU 894 O THR A 127 10614 14239 9782 -1150 470 -2055 O
ATOM 895 CB THR A 127 23.550 -18.388 20.164 1.00 85.78 C
ANISOU 895 CB THR A 127 10114 13022 9454 -1125 483 -1850 C
ATOM 896 OG1 THR A 127 22.236 -17.948 20.507 1.00 86.96 O
ANISOU 896 OG1 THR A 127 10119 13442 9481 -1101 398 -1902 O
ATOM 897 CG2 THR A 127 24.430 -18.472 21.413 1.00 81.78 C
ANISOU 897 CG2 THR A 127 9769 12140 9164 -1092 523 -1700 C
ATOM 898 N ARG A 128 22.336 -16.493 17.686 1.00 90.34 N
ANISOU 898 N ARG A 128 10389 14391 9547 -853 248 -1859 N
ATOM 899 CA ARG A 128 21.384 -16.309 16.583 1.00 93.68 C
ANISOU 899 CA ARG A 128 10624 15254 9718 -841 196 -1987 C
ATOM 900 C ARG A 128 22.122 -16.238 15.218 1.00101.66 C
ANISOU 900 C ARG A 128 11657 16317 10651 -798 207 -1968 C
ATOM 901 O ARG A 128 23.129 -15.525 15.112 1.00100.54 O
ANISOU 901 O ARG A 128 11639 15985 10578 -633 171 -1758 O
ATOM 902 CB ARG A 128 20.537 -15.037 16.838 1.00 94.74 C
ANISOU 902 CB ARG A 128 10657 15630 9708 -607 54 -1869 C
ATOM 903 CG ARG A 128 19.616 -14.587 15.703 1.00109.47 C
ANISOU 903 CG ARG A 128 12333 17970 11289 -505 -23 -1935 C
ATOM 904 CD ARG A 128 20.187 -13.379 14.971 1.00120.82 C
ANISOU 904 CD ARG A 128 13841 19414 12651 -213 -112 -1696 C
ATOM 905 NE ARG A 128 19.284 -12.867 13.938 1.00129.62 N
ANISOU 905 NE ARG A 128 14775 20998 13476 -72 -189 -1733 N
ATOM 906 CZ ARG A 128 18.356 -11.935 14.144 1.00142.14 C
ANISOU 906 CZ ARG A 128 16262 22842 14903 146 -287 -1656 C
ATOM 907 NH1 ARG A 128 18.187 -11.409 15.353 1.00127.03 N
ANISOU 907 NH1 ARG A 128 14417 20751 13097 239 -320 -1544 N
ATOM 908 NH2 ARG A 128 17.584 -11.529 13.146 1.00128.47 N
ANISOU 908 NH2 ARG A 128 14360 21559 12893 286 -350 -1688 N
ATOM 909 N PRO A 129 21.627 -16.957 14.173 1.00101.58 N
ANISOU 909 N PRO A 129 11529 16572 10496 -957 261 -2191 N
ATOM 910 CA PRO A 129 22.313 -16.930 12.866 1.00107.29 C
ANISOU 910 CA PRO A 129 12266 17366 11134 -921 275 -2184 C
ATOM 911 C PRO A 129 22.094 -15.617 12.104 1.00148.90 C
ANISOU 911 C PRO A 129 17500 22829 16248 -633 142 -1982 C
ATOM 912 O PRO A 129 22.494 -15.485 10.945 1.00115.46 O
ANISOU 912 O PRO A 129 13173 18875 11820 -580 116 -2021 O
ATOM 913 CB PRO A 129 21.686 -18.116 12.123 1.00110.68 C
ANISOU 913 CB PRO A 129 12538 18118 11398 -1148 343 -2487 C
ATOM 914 CG PRO A 129 20.316 -18.224 12.692 1.00114.34 C
ANISOU 914 CG PRO A 129 12850 18811 11782 -1227 312 -2613 C
ATOM 915 CD PRO A 129 20.453 -17.857 14.145 1.00106.59 C
ANISOU 915 CD PRO A 129 12009 17458 11030 -1193 320 -2470 C
ATOM 916 N PRO A 135 4.476 -9.602 16.668 1.00111.17 N
ANISOU 916 N PRO A 135 9818 23605 8816 1073 -915 -2537 N
ATOM 917 CA PRO A 135 5.085 -10.827 17.207 1.00109.29 C
ANISOU 917 CA PRO A 135 9699 22964 8861 602 -798 -2711 C
ATOM 918 C PRO A 135 4.514 -11.248 18.567 1.00111.52 C
ANISOU 918 C PRO A 135 9946 23149 9276 413 -754 -2810 C
ATOM 919 O PRO A 135 4.069 -10.404 19.356 1.00110.44 O
ANISOU 919 O PRO A 135 9824 23010 9130 681 -809 -2659 O
ATOM 920 CB PRO A 135 6.566 -10.464 17.328 1.00108.18 C
ANISOU 920 CB PRO A 135 9944 22154 9006 678 -767 -2476 C
ATOM 921 N LYS A 136 4.539 -12.574 18.830 1.00106.79 N
ANISOU 921 N LYS A 136 9314 22461 8801 -54 -641 -3065 N
ATOM 922 CA LYS A 136 4.058 -13.194 20.070 1.00105.16 C
ANISOU 922 CA LYS A 136 9084 22142 8731 -306 -570 -3188 C
ATOM 923 C LYS A 136 5.170 -13.221 21.131 1.00102.13 C
ANISOU 923 C LYS A 136 9062 21024 8717 -337 -510 -3009 C
ATOM 924 O LYS A 136 4.875 -13.411 22.313 1.00101.22 O
ANISOU 924 O LYS A 136 8976 20757 8726 -424 -474 -3020 O
ATOM 925 CB LYS A 136 3.527 -14.612 19.797 1.00109.66 C
ANISOU 925 CB LYS A 136 9469 22950 9247 -798 -457 -3545 C
ATOM 926 N ASN A 137 6.445 -13.034 20.703 1.00 93.56 N
ANISOU 926 N ASN A 137 8241 19511 7795 -265 -499 -2849 N
ATOM 927 CA ASN A 137 7.617 -12.967 21.587 1.00 88.18 C
ANISOU 927 CA ASN A 137 7895 18165 7443 -263 -453 -2665 C
ATOM 928 C ASN A 137 7.643 -11.606 22.282 1.00 85.77 C
ANISOU 928 C ASN A 137 7698 17736 7157 134 -550 -2395 C
ATOM 929 O ASN A 137 8.111 -11.524 23.416 1.00 84.34 O
ANISOU 929 O ASN A 137 7704 17143 7200 123 -521 -2289 O
ATOM 930 CB ASN A 137 8.933 -13.247 20.837 1.00 88.14 C
ANISOU 930 CB ASN A 137 8107 17802 7581 -325 -407 -2600 C
ATOM 931 CG ASN A 137 9.211 -12.351 19.652 1.00119.24 C
ANISOU 931 CG ASN A 137 12036 21919 11349 -31 -495 -2462 C
ATOM 932 OD1 ASN A 137 8.889 -12.679 18.502 1.00118.72 O
ANISOU 932 OD1 ASN A 137 11797 22231 11081 -97 -501 -2606 O
ATOM 933 ND2 ASN A 137 9.869 -11.226 19.897 1.00110.50 N
ANISOU 933 ND2 ASN A 137 11132 20531 10323 286 -556 -2183 N
ATOM 934 N LEU A 138 7.127 -10.547 21.605 1.00 79.29 N
ANISOU 934 N LEU A 138 6761 17276 6088 488 -656 -2286 N
ATOM 935 CA LEU A 138 6.981 -9.191 22.150 1.00 76.80 C
ANISOU 935 CA LEU A 138 6535 16904 5741 895 -739 -2042 C
ATOM 936 C LEU A 138 5.897 -9.214 23.214 1.00 79.31 C
ANISOU 936 C LEU A 138 6695 17427 6011 887 -749 -2122 C
ATOM 937 O LEU A 138 6.030 -8.546 24.240 1.00 78.07 O
ANISOU 937 O LEU A 138 6694 16988 5981 1050 -764 -1965 O
ATOM 938 CB LEU A 138 6.636 -8.145 21.070 1.00 78.21 C
ANISOU 938 CB LEU A 138 6625 17451 5640 1277 -831 -1917 C
ATOM 939 CG LEU A 138 7.633 -7.880 19.943 1.00 81.60 C
ANISOU 939 CG LEU A 138 7213 17714 6079 1362 -832 -1797 C
ATOM 940 CD1 LEU A 138 6.996 -7.022 18.865 1.00 83.96 C
ANISOU 940 CD1 LEU A 138 7357 18498 6045 1714 -915 -1719 C
ATOM 941 CD2 LEU A 138 8.911 -7.215 20.449 1.00 79.29 C
ANISOU 941 CD2 LEU A 138 7285 16793 6048 1479 -812 -1548 C
ATOM 942 N LEU A 139 4.828 -10.003 22.967 1.00 75.85 N
ANISOU 942 N LEU A 139 5945 17486 5388 676 -734 -2379 N
ATOM 943 CA LEU A 139 3.739 -10.226 23.909 1.00 75.61 C
ANISOU 943 CA LEU A 139 5725 17707 5298 596 -728 -2502 C
ATOM 944 C LEU A 139 4.314 -10.946 25.127 1.00 77.56 C
ANISOU 944 C LEU A 139 6169 17439 5861 304 -629 -2527 C
ATOM 945 O LEU A 139 4.123 -10.481 26.250 1.00 76.92 O
ANISOU 945 O LEU A 139 6153 17210 5864 416 -641 -2432 O
ATOM 946 CB LEU A 139 2.578 -11.023 23.261 1.00 78.14 C
ANISOU 946 CB LEU A 139 5666 18675 5349 375 -718 -2796 C
ATOM 947 CG LEU A 139 1.428 -11.480 24.187 1.00 83.20 C
ANISOU 947 CG LEU A 139 6080 19606 5925 193 -686 -2978 C
ATOM 948 CD1 LEU A 139 0.690 -10.299 24.805 1.00 83.44 C
ANISOU 948 CD1 LEU A 139 6026 19862 5817 601 -781 -2822 C
ATOM 949 CD2 LEU A 139 0.456 -12.367 23.450 1.00 87.66 C
ANISOU 949 CD2 LEU A 139 6296 20763 6248 -104 -654 -3294 C
ATOM 950 N GLY A 140 5.069 -12.019 24.879 1.00 72.90 N
ANISOU 950 N GLY A 140 5690 16571 5439 -40 -530 -2638 N
ATOM 951 CA GLY A 140 5.746 -12.804 25.904 1.00 70.87 C
ANISOU 951 CA GLY A 140 5640 15809 5478 -316 -421 -2655 C
ATOM 952 C GLY A 140 6.679 -11.969 26.761 1.00 72.94 C
ANISOU 952 C GLY A 140 6195 15558 5960 -86 -451 -2384 C
ATOM 953 O GLY A 140 6.713 -12.143 27.982 1.00 71.75 O
ANISOU 953 O GLY A 140 6137 15155 5971 -170 -408 -2360 O
ATOM 954 N ALA A 141 7.413 -11.025 26.126 1.00 68.58 N
ANISOU 954 N ALA A 141 5787 14871 5401 204 -522 -2180 N
ATOM 955 CA ALA A 141 8.314 -10.093 26.811 1.00 65.96 C
ANISOU 955 CA ALA A 141 5729 14083 5248 435 -554 -1924 C
ATOM 956 C ALA A 141 7.513 -9.074 27.623 1.00 70.65 C
ANISOU 956 C ALA A 141 6272 14825 5746 724 -626 -1822 C
ATOM 957 O ALA A 141 7.941 -8.702 28.717 1.00 69.02 O
ANISOU 957 O ALA A 141 6249 14262 5713 788 -620 -1695 O
ATOM 958 CB ALA A 141 9.209 -9.378 25.805 1.00 66.03 C
ANISOU 958 CB ALA A 141 5890 13950 5248 637 -595 -1759 C
ATOM 959 N LYS A 142 6.345 -8.636 27.090 1.00 70.01 N
ANISOU 959 N LYS A 142 5936 15285 5379 904 -692 -1882 N
ATOM 960 CA LYS A 142 5.447 -7.678 27.742 1.00 70.89 C
ANISOU 960 CA LYS A 142 5967 15612 5357 1207 -758 -1800 C
ATOM 961 C LYS A 142 4.786 -8.293 28.970 1.00 75.29 C
ANISOU 961 C LYS A 142 6426 16199 5983 1003 -712 -1928 C
ATOM 962 O LYS A 142 4.755 -7.631 30.002 1.00 73.26 O
ANISOU 962 O LYS A 142 6281 15754 5802 1172 -730 -1805 O
ATOM 963 CB LYS A 142 4.370 -7.156 26.774 1.00 75.82 C
ANISOU 963 CB LYS A 142 6320 16851 5635 1457 -834 -1837 C
ATOM 964 CG LYS A 142 4.833 -5.995 25.913 1.00 84.00 C
ANISOU 964 CG LYS A 142 7497 17845 6575 1838 -895 -1616 C
ATOM 965 CD LYS A 142 3.696 -5.447 25.068 1.00 90.69 C
ANISOU 965 CD LYS A 142 8072 19324 7061 2131 -969 -1634 C
ATOM 966 CE LYS A 142 4.205 -4.673 23.882 1.00 93.79 C
ANISOU 966 CE LYS A 142 8571 19726 7337 2412 -1007 -1466 C
ATOM 967 NZ LYS A 142 3.168 -3.756 23.345 1.00103.26 N
ANISOU 967 NZ LYS A 142 9580 21455 8197 2828 -1080 -1396 N
ATOM 968 N ILE A 143 4.265 -9.546 28.869 1.00 74.82 N
ANISOU 968 N ILE A 143 6169 16365 5893 633 -644 -2177 N
ATOM 969 CA ILE A 143 3.606 -10.223 29.996 1.00 75.98 C
ANISOU 969 CA ILE A 143 6219 16554 6097 405 -583 -2311 C
ATOM 970 C ILE A 143 4.637 -10.461 31.089 1.00 77.56 C
ANISOU 970 C ILE A 143 6717 16140 6613 287 -519 -2203 C
ATOM 971 O ILE A 143 4.335 -10.215 32.256 1.00 77.64 O
ANISOU 971 O ILE A 143 6758 16058 6684 342 -518 -2154 O
ATOM 972 CB ILE A 143 2.809 -11.523 29.634 1.00 81.81 C
ANISOU 972 CB ILE A 143 6693 17667 6725 10 -505 -2613 C
ATOM 973 CG1 ILE A 143 3.684 -12.788 29.504 1.00 81.89 C
ANISOU 973 CG1 ILE A 143 6854 17313 6946 -392 -379 -2721 C
ATOM 974 CG2 ILE A 143 1.859 -11.338 28.441 1.00 85.13 C
ANISOU 974 CG2 ILE A 143 6796 18737 6812 110 -572 -2736 C
ATOM 975 CD1 ILE A 143 3.568 -13.745 30.714 1.00 90.11 C
ANISOU 975 CD1 ILE A 143 7947 18130 8161 -716 -257 -2824 C
ATOM 976 N LEU A 144 5.864 -10.882 30.696 1.00 71.50 N
ANISOU 976 N LEU A 144 6163 14972 6032 149 -470 -2155 N
ATOM 977 CA LEU A 144 7.000 -11.134 31.585 1.00 68.28 C
ANISOU 977 CA LEU A 144 6037 13991 5915 47 -410 -2044 C
ATOM 978 C LEU A 144 7.390 -9.855 32.330 1.00 69.30 C
ANISOU 978 C LEU A 144 6345 13876 6112 375 -485 -1811 C
ATOM 979 O LEU A 144 7.666 -9.911 33.529 1.00 67.06 O
ANISOU 979 O LEU A 144 6184 13306 5988 328 -452 -1756 O
ATOM 980 CB LEU A 144 8.194 -11.684 30.781 1.00 67.31 C
ANISOU 980 CB LEU A 144 6076 13576 5922 -93 -361 -2028 C
ATOM 981 CG LEU A 144 9.401 -12.222 31.556 1.00 70.41 C
ANISOU 981 CG LEU A 144 6731 13420 6600 -246 -281 -1945 C
ATOM 982 CD1 LEU A 144 8.999 -13.283 32.592 1.00 70.87 C
ANISOU 982 CD1 LEU A 144 6761 13408 6756 -547 -168 -2083 C
ATOM 983 CD2 LEU A 144 10.431 -12.783 30.609 1.00 72.77 C
ANISOU 983 CD2 LEU A 144 7148 13518 6982 -351 -238 -1941 C
ATOM 984 N SER A 145 7.383 -8.708 31.626 1.00 65.41 N
ANISOU 984 N SER A 145 5866 13503 5484 707 -575 -1679 N
ATOM 985 CA SER A 145 7.690 -7.412 32.217 1.00 64.04 C
ANISOU 985 CA SER A 145 5871 13117 5346 1032 -635 -1467 C
ATOM 986 C SER A 145 6.638 -7.033 33.273 1.00 69.15 C
ANISOU 986 C SER A 145 6405 13958 5913 1146 -656 -1488 C
ATOM 987 O SER A 145 7.014 -6.552 34.335 1.00 67.97 O
ANISOU 987 O SER A 145 6427 13501 5899 1225 -655 -1377 O
ATOM 988 CB SER A 145 7.783 -6.340 31.136 1.00 67.42 C
ANISOU 988 CB SER A 145 6329 13671 5616 1353 -705 -1337 C
ATOM 989 OG SER A 145 8.893 -6.590 30.289 1.00 72.36 O
ANISOU 989 OG SER A 145 7104 14047 6345 1266 -683 -1286 O
ATOM 990 N VAL A 146 5.337 -7.297 33.000 1.00 67.51 N
ANISOU 990 N VAL A 146 5899 14269 5482 1137 -673 -1642 N
ATOM 991 CA VAL A 146 4.220 -7.015 33.916 1.00 68.18 C
ANISOU 991 CA VAL A 146 5831 14614 5460 1237 -690 -1686 C
ATOM 992 C VAL A 146 4.343 -7.904 35.164 1.00 70.28 C
ANISOU 992 C VAL A 146 6144 14636 5922 933 -608 -1763 C
ATOM 993 O VAL A 146 4.180 -7.401 36.280 1.00 68.96 O
ANISOU 993 O VAL A 146 6050 14342 5809 1052 -617 -1687 O
ATOM 994 CB VAL A 146 2.829 -7.187 33.235 1.00 74.94 C
ANISOU 994 CB VAL A 146 6326 16130 6016 1268 -722 -1851 C
ATOM 995 CG1 VAL A 146 1.691 -6.815 34.181 1.00 76.16 C
ANISOU 995 CG1 VAL A 146 6318 16567 6051 1397 -740 -1885 C
ATOM 996 CG2 VAL A 146 2.733 -6.363 31.964 1.00 76.17 C
ANISOU 996 CG2 VAL A 146 6433 16545 5964 1581 -798 -1765 C
ATOM 997 N VAL A 147 4.647 -9.211 34.965 1.00 66.20 N
ANISOU 997 N VAL A 147 5603 14045 5507 552 -522 -1909 N
ATOM 998 CA VAL A 147 4.793 -10.217 36.026 1.00 64.90 C
ANISOU 998 CA VAL A 147 5492 13647 5521 237 -421 -1989 C
ATOM 999 C VAL A 147 5.925 -9.809 37.004 1.00 64.58 C
ANISOU 999 C VAL A 147 5753 13067 5719 316 -416 -1799 C
ATOM 1000 O VAL A 147 5.733 -9.920 38.216 1.00 64.15 O
ANISOU 1000 O VAL A 147 5727 12906 5740 271 -385 -1791 O
ATOM 1001 CB VAL A 147 4.994 -11.650 35.443 1.00 69.26 C
ANISOU 1001 CB VAL A 147 6001 14185 6129 -158 -313 -2166 C
ATOM 1002 CG1 VAL A 147 5.412 -12.655 36.519 1.00 68.11 C
ANISOU 1002 CG1 VAL A 147 5990 13688 6200 -450 -192 -2199 C
ATOM 1003 CG2 VAL A 147 3.728 -12.133 34.742 1.00 71.48 C
ANISOU 1003 CG2 VAL A 147 5958 15033 6168 -292 -303 -2392 C
ATOM 1004 N ILE A 148 7.064 -9.300 36.489 1.00 57.89 N
ANISOU 1004 N ILE A 148 5115 11909 4971 437 -448 -1651 N
ATOM 1005 CA ILE A 148 8.191 -8.861 37.323 1.00 55.00 C
ANISOU 1005 CA ILE A 148 5021 11063 4813 507 -447 -1479 C
ATOM 1006 C ILE A 148 7.747 -7.711 38.243 1.00 59.51 C
ANISOU 1006 C ILE A 148 5626 11650 5334 786 -510 -1373 C
ATOM 1007 O ILE A 148 7.978 -7.792 39.448 1.00 59.07 O
ANISOU 1007 O ILE A 148 5672 11365 5407 735 -482 -1334 O
ATOM 1008 CB ILE A 148 9.445 -8.498 36.477 1.00 56.20 C
ANISOU 1008 CB ILE A 148 5364 10938 5052 578 -468 -1354 C
ATOM 1009 CG1 ILE A 148 10.144 -9.782 36.010 1.00 55.34 C
ANISOU 1009 CG1 ILE A 148 5286 10676 5066 267 -380 -1442 C
ATOM 1010 CG2 ILE A 148 10.440 -7.592 37.251 1.00 54.72 C
ANISOU 1010 CG2 ILE A 148 5432 10348 5012 741 -496 -1162 C
ATOM 1011 CD1 ILE A 148 10.851 -9.659 34.732 1.00 57.74 C
ANISOU 1011 CD1 ILE A 148 5653 10928 5359 305 -397 -1400 C
ATOM 1012 N TRP A 149 7.091 -6.677 37.679 1.00 57.18 N
ANISOU 1012 N TRP A 149 5248 11633 4844 1085 -586 -1331 N
ATOM 1013 CA TRP A 149 6.596 -5.501 38.399 1.00 57.24 C
ANISOU 1013 CA TRP A 149 5292 11680 4775 1392 -639 -1233 C
ATOM 1014 C TRP A 149 5.547 -5.884 39.466 1.00 62.87 C
ANISOU 1014 C TRP A 149 5834 12616 5437 1314 -615 -1343 C
ATOM 1015 O TRP A 149 5.695 -5.494 40.626 1.00 60.99 O
ANISOU 1015 O TRP A 149 5714 12172 5287 1378 -611 -1275 O
ATOM 1016 CB TRP A 149 6.008 -4.490 37.405 1.00 57.44 C
ANISOU 1016 CB TRP A 149 5245 12004 4575 1728 -708 -1175 C
ATOM 1017 CG TRP A 149 7.039 -3.643 36.723 1.00 57.35 C
ANISOU 1017 CG TRP A 149 5476 11697 4618 1906 -732 -1005 C
ATOM 1018 CD1 TRP A 149 7.703 -3.931 35.573 1.00 59.87 C
ANISOU 1018 CD1 TRP A 149 5832 11962 4953 1829 -728 -993 C
ATOM 1019 CD2 TRP A 149 7.519 -2.362 37.154 1.00 56.70 C
ANISOU 1019 CD2 TRP A 149 5638 11331 4576 2179 -750 -830 C
ATOM 1020 NE1 TRP A 149 8.565 -2.909 35.251 1.00 58.88 N
ANISOU 1020 NE1 TRP A 149 5954 11545 4875 2035 -745 -815 N
ATOM 1021 CE2 TRP A 149 8.468 -1.928 36.201 1.00 60.17 C
ANISOU 1021 CE2 TRP A 149 6253 11557 5053 2246 -754 -716 C
ATOM 1022 CE3 TRP A 149 7.212 -1.516 38.234 1.00 57.78 C
ANISOU 1022 CE3 TRP A 149 5864 11381 4708 2373 -757 -765 C
ATOM 1023 CZ2 TRP A 149 9.136 -0.701 36.312 1.00 58.98 C
ANISOU 1023 CZ2 TRP A 149 6372 11095 4943 2478 -756 -542 C
ATOM 1024 CZ3 TRP A 149 7.869 -0.302 38.342 1.00 58.80 C
ANISOU 1024 CZ3 TRP A 149 6265 11196 4879 2607 -759 -599 C
ATOM 1025 CH2 TRP A 149 8.824 0.093 37.395 1.00 59.04 C
ANISOU 1025 CH2 TRP A 149 6475 11006 4952 2649 -755 -491 C
ATOM 1026 N ALA A 150 4.516 -6.672 39.071 1.00 62.47 N
ANISOU 1026 N ALA A 150 5506 12987 5243 1155 -593 -1522 N
ATOM 1027 CA ALA A 150 3.425 -7.144 39.929 1.00 63.56 C
ANISOU 1027 CA ALA A 150 5443 13399 5307 1043 -560 -1651 C
ATOM 1028 C ALA A 150 3.944 -8.002 41.075 1.00 67.62 C
ANISOU 1028 C ALA A 150 6076 13577 6038 758 -475 -1672 C
ATOM 1029 O ALA A 150 3.476 -7.836 42.201 1.00 66.94 O
ANISOU 1029 O ALA A 150 5966 13515 5954 788 -463 -1673 O
ATOM 1030 CB ALA A 150 2.411 -7.930 39.114 1.00 66.21 C
ANISOU 1030 CB ALA A 150 5469 14233 5453 873 -541 -1852 C
ATOM 1031 N PHE A 151 4.930 -8.888 40.803 1.00 64.53 N
ANISOU 1031 N PHE A 151 5820 12875 5822 505 -412 -1678 N
ATOM 1032 CA PHE A 151 5.518 -9.754 41.825 1.00 63.49 C
ANISOU 1032 CA PHE A 151 5818 12411 5892 252 -320 -1680 C
ATOM 1033 C PHE A 151 6.256 -8.940 42.902 1.00 65.87 C
ANISOU 1033 C PHE A 151 6344 12358 6328 429 -354 -1507 C
ATOM 1034 O PHE A 151 6.066 -9.218 44.083 1.00 64.97 O
ANISOU 1034 O PHE A 151 6242 12169 6273 347 -310 -1515 O
ATOM 1035 CB PHE A 151 6.457 -10.811 41.215 1.00 64.41 C
ANISOU 1035 CB PHE A 151 6038 12281 6152 -16 -242 -1714 C
ATOM 1036 CG PHE A 151 7.171 -11.646 42.254 1.00 64.74 C
ANISOU 1036 CG PHE A 151 6242 11956 6399 -229 -144 -1684 C
ATOM 1037 CD1 PHE A 151 6.485 -12.610 42.988 1.00 68.97 C
ANISOU 1037 CD1 PHE A 151 6684 12585 6937 -472 -41 -1805 C
ATOM 1038 CD2 PHE A 151 8.518 -11.439 42.530 1.00 64.72 C
ANISOU 1038 CD2 PHE A 151 6485 11530 6577 -179 -149 -1530 C
ATOM 1039 CE1 PHE A 151 7.141 -13.366 43.966 1.00 68.97 C
ANISOU 1039 CE1 PHE A 151 6845 12245 7115 -642 57 -1760 C
ATOM 1040 CE2 PHE A 151 9.173 -12.198 43.503 1.00 66.62 C
ANISOU 1040 CE2 PHE A 151 6864 11460 6987 -347 -60 -1492 C
ATOM 1041 CZ PHE A 151 8.482 -13.156 44.214 1.00 65.83 C
ANISOU 1041 CZ PHE A 151 6682 11443 6886 -567 44 -1600 C
ATOM 1042 N MET A 152 7.098 -7.961 42.500 1.00 61.79 N
ANISOU 1042 N MET A 152 6002 11624 5850 654 -422 -1359 N
ATOM 1043 CA MET A 152 7.849 -7.115 43.442 1.00 60.44 C
ANISOU 1043 CA MET A 152 6050 11122 5794 810 -452 -1208 C
ATOM 1044 C MET A 152 6.927 -6.255 44.280 1.00 65.83 C
ANISOU 1044 C MET A 152 6671 11979 6363 1028 -491 -1196 C
ATOM 1045 O MET A 152 7.236 -5.976 45.439 1.00 65.21 O
ANISOU 1045 O MET A 152 6712 11690 6377 1050 -483 -1136 O
ATOM 1046 CB MET A 152 8.864 -6.222 42.718 1.00 62.10 C
ANISOU 1046 CB MET A 152 6450 11097 6048 986 -504 -1070 C
ATOM 1047 CG MET A 152 9.999 -6.987 42.094 1.00 64.63 C
ANISOU 1047 CG MET A 152 6872 11174 6511 785 -463 -1055 C
ATOM 1048 SD MET A 152 10.772 -8.234 43.150 1.00 66.98 S
ANISOU 1048 SD MET A 152 7255 11178 7017 481 -367 -1072 S
ATOM 1049 CE MET A 152 11.527 -9.214 41.878 1.00 63.83 C
ANISOU 1049 CE MET A 152 6868 10705 6680 280 -315 -1116 C
ATOM 1050 N PHE A 153 5.794 -5.846 43.689 1.00 64.56 N
ANISOU 1050 N PHE A 153 6318 12220 5992 1196 -533 -1256 N
ATOM 1051 CA PHE A 153 4.730 -5.066 44.310 1.00 65.81 C
ANISOU 1051 CA PHE A 153 6375 12631 6000 1430 -568 -1261 C
ATOM 1052 C PHE A 153 4.004 -5.915 45.375 1.00 69.24 C
ANISOU 1052 C PHE A 153 6659 13211 6438 1220 -508 -1378 C
ATOM 1053 O PHE A 153 3.673 -5.405 46.443 1.00 68.28 O
ANISOU 1053 O PHE A 153 6561 13078 6304 1341 -515 -1348 O
ATOM 1054 CB PHE A 153 3.761 -4.597 43.212 1.00 69.96 C
ANISOU 1054 CB PHE A 153 6707 13590 6286 1648 -621 -1300 C
ATOM 1055 CG PHE A 153 2.564 -3.822 43.698 1.00 73.64 C
ANISOU 1055 CG PHE A 153 7033 14387 6561 1918 -655 -1312 C
ATOM 1056 CD1 PHE A 153 2.692 -2.503 44.110 1.00 77.31 C
ANISOU 1056 CD1 PHE A 153 7673 14698 7002 2258 -692 -1174 C
ATOM 1057 CD2 PHE A 153 1.307 -4.411 43.740 1.00 77.44 C
ANISOU 1057 CD2 PHE A 153 7206 15340 6879 1829 -641 -1468 C
ATOM 1058 CE1 PHE A 153 1.587 -1.789 44.567 1.00 80.20 C
ANISOU 1058 CE1 PHE A 153 7917 15368 7188 2529 -714 -1183 C
ATOM 1059 CE2 PHE A 153 0.202 -3.695 44.191 1.00 82.28 C
ANISOU 1059 CE2 PHE A 153 7675 16283 7306 2093 -671 -1479 C
ATOM 1060 CZ PHE A 153 0.350 -2.389 44.604 1.00 80.80 C
ANISOU 1060 CZ PHE A 153 7673 15929 7100 2453 -708 -1332 C
ATOM 1061 N LEU A 154 3.772 -7.213 45.061 1.00 66.86 N
ANISOU 1061 N LEU A 154 6214 13038 6150 899 -441 -1515 N
ATOM 1062 CA LEU A 154 3.136 -8.235 45.901 1.00 67.12 C
ANISOU 1062 CA LEU A 154 6113 13198 6194 634 -356 -1640 C
ATOM 1063 C LEU A 154 3.938 -8.413 47.186 1.00 67.54 C
ANISOU 1063 C LEU A 154 6372 12847 6442 545 -310 -1552 C
ATOM 1064 O LEU A 154 3.343 -8.458 48.261 1.00 67.35 O
ANISOU 1064 O LEU A 154 6287 12908 6396 519 -280 -1583 O
ATOM 1065 CB LEU A 154 3.048 -9.568 45.113 1.00 68.25 C
ANISOU 1065 CB LEU A 154 6132 13461 6338 294 -275 -1791 C
ATOM 1066 CG LEU A 154 2.129 -10.690 45.622 1.00 74.82 C
ANISOU 1066 CG LEU A 154 6789 14502 7137 -18 -167 -1958 C
ATOM 1067 CD1 LEU A 154 1.585 -11.497 44.463 1.00 76.40 C
ANISOU 1067 CD1 LEU A 154 6782 15030 7217 -238 -123 -2139 C
ATOM 1068 CD2 LEU A 154 2.865 -11.635 46.572 1.00 76.92 C
ANISOU 1068 CD2 LEU A 154 7246 14359 7620 -271 -58 -1923 C
ATOM 1069 N LEU A 155 5.287 -8.501 47.073 1.00 61.43 N
ANISOU 1069 N LEU A 155 5832 11660 5847 504 -306 -1443 N
ATOM 1070 CA LEU A 155 6.206 -8.638 48.212 1.00 59.11 C
ANISOU 1070 CA LEU A 155 5739 10988 5732 439 -271 -1347 C
ATOM 1071 C LEU A 155 6.317 -7.355 49.024 1.00 61.38 C
ANISOU 1071 C LEU A 155 6142 11171 6010 717 -342 -1236 C
ATOM 1072 O LEU A 155 6.457 -7.424 50.245 1.00 60.98 O
ANISOU 1072 O LEU A 155 6158 10985 6027 681 -315 -1205 O
ATOM 1073 CB LEU A 155 7.625 -9.014 47.738 1.00 57.66 C
ANISOU 1073 CB LEU A 155 5748 10441 5720 329 -249 -1267 C
ATOM 1074 CG LEU A 155 7.906 -10.423 47.230 1.00 61.82 C
ANISOU 1074 CG LEU A 155 6248 10920 6321 23 -147 -1351 C
ATOM 1075 CD1 LEU A 155 9.329 -10.512 46.755 1.00 60.03 C
ANISOU 1075 CD1 LEU A 155 6211 10358 6238 -1 -147 -1253 C
ATOM 1076 CD2 LEU A 155 7.670 -11.469 48.311 1.00 63.41 C
ANISOU 1076 CD2 LEU A 155 6445 11057 6590 -200 -36 -1393 C
ATOM 1077 N SER A 156 6.332 -6.193 48.339 1.00 57.50 N
ANISOU 1077 N SER A 156 5693 10719 5435 990 -425 -1174 N
ATOM 1078 CA SER A 156 6.509 -4.864 48.930 1.00 56.90 C
ANISOU 1078 CA SER A 156 5763 10512 5345 1267 -482 -1070 C
ATOM 1079 C SER A 156 5.331 -4.399 49.784 1.00 62.26 C
ANISOU 1079 C SER A 156 6318 11451 5888 1416 -490 -1117 C
ATOM 1080 O SER A 156 5.558 -3.787 50.824 1.00 60.89 O
ANISOU 1080 O SER A 156 6271 11108 5756 1517 -497 -1059 O
ATOM 1081 CB SER A 156 6.789 -3.832 47.837 1.00 60.21 C
ANISOU 1081 CB SER A 156 6272 10906 5700 1510 -544 -993 C
ATOM 1082 OG SER A 156 5.823 -2.794 47.752 1.00 67.39 O
ANISOU 1082 OG SER A 156 7109 12071 6427 1813 -587 -989 O
ATOM 1083 N LEU A 157 4.089 -4.642 49.324 1.00 61.65 N
ANISOU 1083 N LEU A 157 5988 11796 5639 1436 -490 -1226 N
ATOM 1084 CA LEU A 157 2.852 -4.187 49.960 1.00 63.60 C
ANISOU 1084 CA LEU A 157 6076 12367 5724 1599 -500 -1280 C
ATOM 1085 C LEU A 157 2.733 -4.550 51.467 1.00 65.70 C
ANISOU 1085 C LEU A 157 6356 12547 6060 1475 -450 -1299 C
ATOM 1086 O LEU A 157 2.499 -3.614 52.243 1.00 65.27 O
ANISOU 1086 O LEU A 157 6371 12469 5961 1702 -476 -1251 O
ATOM 1087 CB LEU A 157 1.627 -4.675 49.178 1.00 66.22 C
ANISOU 1087 CB LEU A 157 6100 13194 5866 1556 -496 -1416 C
ATOM 1088 CG LEU A 157 0.578 -3.624 48.797 1.00 73.72 C
ANISOU 1088 CG LEU A 157 6911 14517 6583 1913 -557 -1417 C
ATOM 1089 CD1 LEU A 157 1.207 -2.347 48.232 1.00 73.89 C
ANISOU 1089 CD1 LEU A 157 7152 14322 6600 2240 -617 -1269 C
ATOM 1090 CD2 LEU A 157 -0.399 -4.192 47.790 1.00 78.00 C
ANISOU 1090 CD2 LEU A 157 7149 15543 6944 1838 -560 -1551 C
ATOM 1091 N PRO A 158 2.941 -5.812 51.948 1.00 60.54 N
ANISOU 1091 N PRO A 158 5668 11819 5514 1143 -372 -1356 N
ATOM 1092 CA PRO A 158 2.834 -6.055 53.401 1.00 59.47 C
ANISOU 1092 CA PRO A 158 5560 11606 5431 1061 -324 -1355 C
ATOM 1093 C PRO A 158 3.904 -5.317 54.220 1.00 61.12 C
ANISOU 1093 C PRO A 158 6032 11425 5767 1177 -353 -1226 C
ATOM 1094 O PRO A 158 3.639 -5.017 55.381 1.00 62.21 O
ANISOU 1094 O PRO A 158 6187 11562 5888 1241 -344 -1217 O
ATOM 1095 CB PRO A 158 2.966 -7.575 53.524 1.00 60.73 C
ANISOU 1095 CB PRO A 158 5666 11724 5684 689 -222 -1424 C
ATOM 1096 CG PRO A 158 2.657 -8.102 52.153 1.00 65.85 C
ANISOU 1096 CG PRO A 158 6174 12579 6268 583 -215 -1514 C
ATOM 1097 CD PRO A 158 3.222 -7.075 51.236 1.00 61.17 C
ANISOU 1097 CD PRO A 158 5690 11890 5662 835 -310 -1426 C
ATOM 1098 N ASN A 159 5.065 -4.961 53.618 1.00 54.83 N
ANISOU 1098 N ASN A 159 5428 10325 5081 1211 -387 -1133 N
ATOM 1099 CA ASN A 159 6.123 -4.191 54.295 1.00 52.94 C
ANISOU 1099 CA ASN A 159 5432 9735 4948 1309 -415 -1023 C
ATOM 1100 C ASN A 159 5.651 -2.773 54.597 1.00 57.56 C
ANISOU 1100 C ASN A 159 6072 10376 5420 1630 -467 -996 C
ATOM 1101 O ASN A 159 6.040 -2.212 55.614 1.00 56.96 O
ANISOU 1101 O ASN A 159 6133 10123 5387 1695 -470 -954 O
ATOM 1102 CB ASN A 159 7.426 -4.124 53.463 1.00 50.55 C
ANISOU 1102 CB ASN A 159 5301 9135 4770 1265 -435 -942 C
ATOM 1103 CG ASN A 159 8.276 -5.373 53.442 1.00 57.65 C
ANISOU 1103 CG ASN A 159 6225 9865 5814 978 -377 -935 C
ATOM 1104 OD1 ASN A 159 8.899 -5.687 52.438 1.00 61.23 O
ANISOU 1104 OD1 ASN A 159 6708 10235 6321 902 -377 -920 O
ATOM 1105 ND2 ASN A 159 8.388 -6.086 54.551 1.00 42.85 N
ANISOU 1105 ND2 ASN A 159 4356 7920 4005 826 -321 -937 N
ATOM 1106 N MET A 160 4.821 -2.199 53.709 1.00 55.63 N
ANISOU 1106 N MET A 160 5725 10387 5026 1835 -501 -1021 N
ATOM 1107 CA MET A 160 4.241 -0.857 53.835 1.00 56.39 C
ANISOU 1107 CA MET A 160 5871 10566 4990 2179 -537 -992 C
ATOM 1108 C MET A 160 3.144 -0.834 54.903 1.00 62.30 C
ANISOU 1108 C MET A 160 6474 11569 5630 2244 -517 -1061 C
ATOM 1109 O MET A 160 3.077 0.091 55.711 1.00 63.64 O
ANISOU 1109 O MET A 160 6762 11647 5769 2438 -523 -1030 O
ATOM 1110 CB MET A 160 3.658 -0.380 52.485 1.00 59.66 C
ANISOU 1110 CB MET A 160 6196 11214 5257 2389 -574 -990 C
ATOM 1111 CG MET A 160 4.677 -0.302 51.350 1.00 62.11 C
ANISOU 1111 CG MET A 160 6649 11297 5653 2355 -593 -917 C
ATOM 1112 SD MET A 160 4.026 0.521 49.870 1.00 68.16 S
ANISOU 1112 SD MET A 160 7354 12320 6224 2673 -635 -886 S
ATOM 1113 CE MET A 160 5.472 0.582 48.870 1.00 63.43 C
ANISOU 1113 CE MET A 160 6968 11363 5770 2578 -643 -792 C
ATOM 1114 N ILE A 161 2.299 -1.869 54.910 1.00 58.15 N
ANISOU 1114 N ILE A 161 5694 11358 5042 2067 -486 -1163 N
ATOM 1115 CA ILE A 161 1.147 -2.015 55.796 1.00 58.36 C
ANISOU 1115 CA ILE A 161 5534 11692 4949 2093 -459 -1245 C
ATOM 1116 C ILE A 161 1.579 -2.419 57.225 1.00 61.70 C
ANISOU 1116 C ILE A 161 6046 11909 5488 1924 -413 -1235 C
ATOM 1117 O ILE A 161 1.000 -1.925 58.193 1.00 61.80 O
ANISOU 1117 O ILE A 161 6035 12023 5424 2058 -407 -1252 O
ATOM 1118 CB ILE A 161 0.161 -3.033 55.139 1.00 61.93 C
ANISOU 1118 CB ILE A 161 5682 12559 5291 1923 -431 -1367 C
ATOM 1119 CG1 ILE A 161 -0.352 -2.467 53.798 1.00 63.18 C
ANISOU 1119 CG1 ILE A 161 5739 12971 5297 2147 -486 -1372 C
ATOM 1120 CG2 ILE A 161 -1.015 -3.401 56.044 1.00 63.59 C
ANISOU 1120 CG2 ILE A 161 5670 13110 5381 1879 -389 -1466 C
ATOM 1121 CD1 ILE A 161 -0.736 -3.452 52.786 1.00 67.39 C
ANISOU 1121 CD1 ILE A 161 6060 13766 5778 1936 -471 -1469 C
ATOM 1122 N LEU A 162 2.594 -3.275 57.367 1.00 57.43 N
ANISOU 1122 N LEU A 162 5611 11089 5121 1655 -381 -1202 N
ATOM 1123 CA LEU A 162 2.976 -3.735 58.704 1.00 56.78 C
ANISOU 1123 CA LEU A 162 5597 10844 5131 1501 -334 -1185 C
ATOM 1124 C LEU A 162 4.017 -2.824 59.424 1.00 60.29 C
ANISOU 1124 C LEU A 162 6301 10940 5666 1623 -368 -1091 C
ATOM 1125 O LEU A 162 4.469 -3.169 60.511 1.00 58.98 O
ANISOU 1125 O LEU A 162 6204 10629 5576 1503 -336 -1068 O
ATOM 1126 CB LEU A 162 3.440 -5.194 58.655 1.00 55.86 C
ANISOU 1126 CB LEU A 162 5451 10639 5135 1158 -263 -1198 C
ATOM 1127 CG LEU A 162 2.423 -6.213 58.104 1.00 60.82 C
ANISOU 1127 CG LEU A 162 5832 11597 5679 975 -204 -1314 C
ATOM 1128 CD1 LEU A 162 3.103 -7.479 57.681 1.00 59.86 C
ANISOU 1128 CD1 LEU A 162 5748 11308 5689 674 -134 -1314 C
ATOM 1129 CD2 LEU A 162 1.298 -6.492 59.085 1.00 63.17 C
ANISOU 1129 CD2 LEU A 162 5959 12172 5870 930 -149 -1392 C
ATOM 1130 N THR A 163 4.313 -1.631 58.865 1.00 58.14 N
ANISOU 1130 N THR A 163 6168 10555 5368 1865 -424 -1043 N
ATOM 1131 CA THR A 163 5.150 -0.592 59.487 1.00 57.53 C
ANISOU 1131 CA THR A 163 6336 10177 5346 1994 -447 -978 C
ATOM 1132 C THR A 163 4.148 0.387 60.130 1.00 64.30 C
ANISOU 1132 C THR A 163 7170 11209 6054 2265 -452 -1015 C
ATOM 1133 O THR A 163 4.048 1.548 59.722 1.00 65.01 O
ANISOU 1133 O THR A 163 7380 11245 6077 2527 -476 -987 O
ATOM 1134 CB THR A 163 6.083 0.047 58.432 1.00 61.43 C
ANISOU 1134 CB THR A 163 7010 10426 5904 2065 -483 -907 C
ATOM 1135 OG1 THR A 163 6.674 -0.979 57.647 1.00 59.66 O
ANISOU 1135 OG1 THR A 163 6739 10149 5779 1837 -475 -893 O
ATOM 1136 CG2 THR A 163 7.182 0.899 59.049 1.00 57.38 C
ANISOU 1136 CG2 THR A 163 6756 9570 5477 2101 -493 -849 C
ATOM 1137 N ASN A 164 3.343 -0.123 61.082 1.00 62.42 N
ANISOU 1137 N ASN A 164 6772 11192 5752 2204 -418 -1077 N
ATOM 1138 CA ASN A 164 2.228 0.604 61.697 1.00 64.73 C
ANISOU 1138 CA ASN A 164 6987 11720 5886 2442 -413 -1126 C
ATOM 1139 C ASN A 164 2.509 1.175 63.099 1.00 70.05 C
ANISOU 1139 C ASN A 164 7805 12235 6576 2494 -399 -1122 C
ATOM 1140 O ASN A 164 1.680 1.941 63.610 1.00 71.55 O
ANISOU 1140 O ASN A 164 7973 12577 6637 2727 -393 -1158 O
ATOM 1141 CB ASN A 164 0.985 -0.306 61.762 1.00 66.85 C
ANISOU 1141 CB ASN A 164 6952 12401 6046 2346 -380 -1214 C
ATOM 1142 CG ASN A 164 1.217 -1.704 62.308 1.00 86.47 C
ANISOU 1142 CG ASN A 164 9351 14875 8629 1995 -325 -1235 C
ATOM 1143 OD1 ASN A 164 2.163 -1.975 63.056 1.00 82.77 O
ANISOU 1143 OD1 ASN A 164 9032 14127 8290 1851 -310 -1184 O
ATOM 1144 ND2 ASN A 164 0.347 -2.631 61.946 1.00 77.00 N
ANISOU 1144 ND2 ASN A 164 7909 13989 7359 1849 -286 -1313 N
ATOM 1145 N ARG A 165 3.642 0.813 63.723 1.00 65.30 N
ANISOU 1145 N ARG A 165 7340 11354 6118 2291 -392 -1082 N
ATOM 1146 CA ARG A 165 3.965 1.306 65.066 1.00 65.23 C
ANISOU 1146 CA ARG A 165 7456 11212 6118 2315 -380 -1085 C
ATOM 1147 C ARG A 165 4.558 2.718 65.014 1.00 71.06 C
ANISOU 1147 C ARG A 165 8451 11690 6857 2520 -402 -1061 C
ATOM 1148 O ARG A 165 5.240 3.075 64.058 1.00 69.85 O
ANISOU 1148 O ARG A 165 8427 11345 6767 2539 -425 -1013 O
ATOM 1149 CB ARG A 165 4.924 0.349 65.812 1.00 63.37 C
ANISOU 1149 CB ARG A 165 7250 10815 6011 2029 -360 -1050 C
ATOM 1150 CG ARG A 165 4.520 -1.134 65.791 1.00 75.87 C
ANISOU 1150 CG ARG A 165 8628 12583 7615 1794 -315 -1061 C
ATOM 1151 CD ARG A 165 3.334 -1.452 66.686 1.00 91.41 C
ANISOU 1151 CD ARG A 165 10420 14846 9467 1804 -269 -1126 C
ATOM 1152 NE ARG A 165 2.802 -2.802 66.477 1.00102.25 N
ANISOU 1152 NE ARG A 165 11597 16410 10842 1580 -210 -1152 N
ATOM 1153 CZ ARG A 165 3.222 -3.889 67.123 1.00118.68 C
ANISOU 1153 CZ ARG A 165 13670 18424 12999 1341 -149 -1120 C
ATOM 1154 NH1 ARG A 165 4.222 -3.809 67.996 1.00103.33 N
ANISOU 1154 NH1 ARG A 165 11882 16249 11130 1302 -153 -1055 N
ATOM 1155 NH2 ARG A 165 2.665 -5.069 66.879 1.00106.69 N
ANISOU 1155 NH2 ARG A 165 11992 17069 11476 1137 -77 -1152 N
ATOM 1156 N GLN A 166 4.264 3.522 66.038 1.00 71.35 N
ANISOU 1156 N GLN A 166 8566 11723 6819 2669 -386 -1100 N
ATOM 1157 CA GLN A 166 4.774 4.884 66.213 1.00 72.62 C
ANISOU 1157 CA GLN A 166 8993 11627 6972 2848 -383 -1098 C
ATOM 1158 C GLN A 166 6.143 4.834 66.922 1.00 76.34 C
ANISOU 1158 C GLN A 166 9631 11807 7569 2637 -388 -1081 C
ATOM 1159 O GLN A 166 6.354 3.922 67.732 1.00 74.02 O
ANISOU 1159 O GLN A 166 9234 11573 7317 2434 -385 -1083 O
ATOM 1160 CB GLN A 166 3.788 5.718 67.048 1.00 76.09 C
ANISOU 1160 CB GLN A 166 9437 12209 7266 3096 -352 -1161 C
ATOM 1161 CG GLN A 166 2.411 5.946 66.421 1.00 99.27 C
ANISOU 1161 CG GLN A 166 12217 15453 10049 3361 -346 -1179 C
ATOM 1162 CD GLN A 166 1.389 6.494 67.408 1.00125.07 C
ANISOU 1162 CD GLN A 166 15431 18921 13169 3569 -311 -1246 C
ATOM 1163 OE1 GLN A 166 1.714 7.036 68.479 1.00117.99 O
ANISOU 1163 OE1 GLN A 166 14692 17867 12271 3597 -286 -1281 O
ATOM 1164 NE2 GLN A 166 0.114 6.381 67.055 1.00122.79 N
ANISOU 1164 NE2 GLN A 166 14910 19004 12739 3726 -307 -1274 N
ATOM 1165 N PRO A 167 7.088 5.777 66.661 1.00 74.98 N
ANISOU 1165 N PRO A 167 9711 11331 7447 2676 -389 -1064 N
ATOM 1166 CA PRO A 167 8.380 5.731 67.384 1.00 74.36 C
ANISOU 1166 CA PRO A 167 9763 11022 7466 2466 -395 -1062 C
ATOM 1167 C PRO A 167 8.234 6.175 68.861 1.00 80.46 C
ANISOU 1167 C PRO A 167 10584 11815 8172 2492 -371 -1135 C
ATOM 1168 O PRO A 167 7.745 7.276 69.137 1.00 82.42 O
ANISOU 1168 O PRO A 167 10961 12027 8329 2706 -339 -1189 O
ATOM 1169 CB PRO A 167 9.293 6.671 66.581 1.00 75.97 C
ANISOU 1169 CB PRO A 167 10214 10928 7724 2504 -391 -1037 C
ATOM 1170 CG PRO A 167 8.452 7.236 65.458 1.00 81.22 C
ANISOU 1170 CG PRO A 167 10893 11652 8316 2758 -379 -1014 C
ATOM 1171 CD PRO A 167 7.019 6.932 65.739 1.00 77.70 C
ANISOU 1171 CD PRO A 167 10236 11537 7750 2911 -374 -1047 C
ATOM 1172 N ARG A 168 8.618 5.288 69.804 1.00 75.52 N
ANISOU 1172 N ARG A 168 9855 11257 7582 2286 -381 -1132 N
ATOM 1173 CA ARG A 168 8.533 5.513 71.252 1.00 75.85 C
ANISOU 1173 CA ARG A 168 9911 11352 7558 2278 -363 -1196 C
ATOM 1174 C ARG A 168 9.636 6.489 71.721 1.00 78.67 C
ANISOU 1174 C ARG A 168 10510 11446 7936 2235 -359 -1241 C
ATOM 1175 O ARG A 168 9.369 7.333 72.576 1.00 78.94 O
ANISOU 1175 O ARG A 168 10645 11466 7884 2341 -330 -1324 O
ATOM 1176 CB ARG A 168 8.617 4.171 72.008 1.00 76.18 C
ANISOU 1176 CB ARG A 168 9764 11555 7626 2075 -368 -1159 C
ATOM 1177 CG ARG A 168 8.147 4.225 73.460 1.00 88.10 C
ANISOU 1177 CG ARG A 168 11221 13217 9037 2101 -344 -1217 C
ATOM 1178 CD ARG A 168 8.207 2.857 74.118 1.00 97.02 C
ANISOU 1178 CD ARG A 168 12177 14497 10190 1910 -335 -1162 C
ATOM 1179 NE ARG A 168 7.781 2.904 75.514 1.00105.46 N
ANISOU 1179 NE ARG A 168 13197 15718 11156 1934 -309 -1211 N
ATOM 1180 N ASP A 169 10.869 6.358 71.169 1.00 73.23 N
ANISOU 1180 N ASP A 169 9906 10563 7354 2069 -384 -1196 N
ATOM 1181 CA ASP A 169 12.018 7.232 71.439 1.00 72.49 C
ANISOU 1181 CA ASP A 169 10030 10227 7286 1984 -378 -1243 C
ATOM 1182 C ASP A 169 12.257 8.058 70.179 1.00 75.76 C
ANISOU 1182 C ASP A 169 10623 10423 7740 2074 -360 -1225 C
ATOM 1183 O ASP A 169 12.394 7.484 69.099 1.00 74.29 O
ANISOU 1183 O ASP A 169 10367 10234 7626 2038 -385 -1143 O
ATOM 1184 CB ASP A 169 13.267 6.406 71.840 1.00 72.69 C
ANISOU 1184 CB ASP A 169 9992 10239 7387 1720 -415 -1204 C
ATOM 1185 CG ASP A 169 14.503 7.181 72.304 1.00 78.69 C
ANISOU 1185 CG ASP A 169 10929 10815 8155 1590 -412 -1269 C
ATOM 1186 OD1 ASP A 169 14.798 8.248 71.719 1.00 78.49 O
ANISOU 1186 OD1 ASP A 169 11112 10574 8138 1639 -382 -1311 O
ATOM 1187 OD2 ASP A 169 15.224 6.675 73.193 1.00 83.89 O
ANISOU 1187 OD2 ASP A 169 11515 11552 8809 1427 -436 -1272 O
ATOM 1188 N LYS A 170 12.296 9.397 70.309 1.00 73.83 N
ANISOU 1188 N LYS A 170 10619 9990 7444 2191 -309 -1300 N
ATOM 1189 CA LYS A 170 12.475 10.302 69.171 1.00 74.78 C
ANISOU 1189 CA LYS A 170 10947 9881 7586 2299 -271 -1279 C
ATOM 1190 C LYS A 170 13.890 10.217 68.553 1.00 77.45 C
ANISOU 1190 C LYS A 170 11372 10021 8036 2071 -289 -1243 C
ATOM 1191 O LYS A 170 14.069 10.581 67.391 1.00 77.60 O
ANISOU 1191 O LYS A 170 11500 9892 8093 2128 -271 -1190 O
ATOM 1192 CB LYS A 170 12.118 11.762 69.540 1.00 80.49 C
ANISOU 1192 CB LYS A 170 11932 10434 8217 2492 -188 -1370 C
ATOM 1193 CG LYS A 170 13.188 12.561 70.299 1.00106.68 C
ANISOU 1193 CG LYS A 170 15475 13518 11542 2322 -145 -1472 C
ATOM 1194 CD LYS A 170 13.774 13.664 69.417 1.00122.40 C
ANISOU 1194 CD LYS A 170 17761 15182 13562 2352 -73 -1470 C
ATOM 1195 CE LYS A 170 14.930 14.388 70.061 1.00137.02 C
ANISOU 1195 CE LYS A 170 19824 16810 15429 2128 -26 -1579 C
ATOM 1196 NZ LYS A 170 15.648 15.243 69.078 1.00148.82 N
ANISOU 1196 NZ LYS A 170 21575 17998 16974 2093 41 -1559 N
ATOM 1197 N ASN A 171 14.877 9.747 69.315 1.00 72.59 N
ANISOU 1197 N ASN A 171 10701 9421 7460 1826 -321 -1268 N
ATOM 1198 CA ASN A 171 16.247 9.656 68.826 1.00 71.41 C
ANISOU 1198 CA ASN A 171 10610 9121 7401 1606 -337 -1241 C
ATOM 1199 C ASN A 171 16.465 8.407 67.965 1.00 72.05 C
ANISOU 1199 C ASN A 171 10495 9307 7573 1523 -394 -1122 C
ATOM 1200 O ASN A 171 17.405 8.388 67.169 1.00 71.26 O
ANISOU 1200 O ASN A 171 10450 9076 7549 1403 -401 -1080 O
ATOM 1201 CB ASN A 171 17.232 9.682 69.996 1.00 73.94 C
ANISOU 1201 CB ASN A 171 10937 9450 7706 1390 -348 -1320 C
ATOM 1202 CG ASN A 171 17.004 10.836 70.944 1.00104.66 C
ANISOU 1202 CG ASN A 171 15015 13251 11501 1446 -288 -1457 C
ATOM 1203 OD1 ASN A 171 17.305 11.998 70.641 1.00102.59 O
ANISOU 1203 OD1 ASN A 171 15008 12746 11227 1475 -218 -1519 O
ATOM 1204 ND2 ASN A 171 16.432 10.543 72.102 1.00 98.05 N
ANISOU 1204 ND2 ASN A 171 14066 12600 10588 1466 -302 -1507 N
ATOM 1205 N VAL A 172 15.598 7.379 68.112 1.00 66.32 N
ANISOU 1205 N VAL A 172 9549 8813 6835 1581 -424 -1075 N
ATOM 1206 CA VAL A 172 15.688 6.099 67.391 1.00 63.45 C
ANISOU 1206 CA VAL A 172 8997 8561 6549 1499 -462 -974 C
ATOM 1207 C VAL A 172 14.990 6.208 66.021 1.00 64.73 C
ANISOU 1207 C VAL A 172 9164 8708 6722 1653 -455 -926 C
ATOM 1208 O VAL A 172 13.761 6.300 65.948 1.00 65.05 O
ANISOU 1208 O VAL A 172 9148 8879 6689 1841 -441 -939 O
ATOM 1209 CB VAL A 172 15.131 4.919 68.239 1.00 66.45 C
ANISOU 1209 CB VAL A 172 9154 9186 6906 1460 -479 -955 C
ATOM 1210 CG1 VAL A 172 15.219 3.601 67.477 1.00 64.62 C
ANISOU 1210 CG1 VAL A 172 8756 9043 6755 1370 -497 -861 C
ATOM 1211 CG2 VAL A 172 15.857 4.810 69.579 1.00 66.17 C
ANISOU 1211 CG2 VAL A 172 9111 9182 6847 1323 -487 -992 C
ATOM 1212 N LYS A 173 15.795 6.170 64.940 1.00 58.75 N
ANISOU 1212 N LYS A 173 8462 7816 6046 1573 -464 -869 N
ATOM 1213 CA LYS A 173 15.330 6.284 63.552 1.00 57.57 C
ANISOU 1213 CA LYS A 173 8326 7645 5905 1700 -459 -816 C
ATOM 1214 C LYS A 173 15.183 4.926 62.818 1.00 58.69 C
ANISOU 1214 C LYS A 173 8254 7939 6104 1621 -491 -746 C
ATOM 1215 O LYS A 173 14.710 4.922 61.675 1.00 58.63 O
ANISOU 1215 O LYS A 173 8226 7960 6090 1724 -491 -710 O
ATOM 1216 CB LYS A 173 16.293 7.171 62.738 1.00 59.52 C
ANISOU 1216 CB LYS A 173 8791 7631 6195 1668 -435 -799 C
ATOM 1217 CG LYS A 173 16.294 8.649 63.104 1.00 65.83 C
ANISOU 1217 CG LYS A 173 9846 8237 6929 1782 -376 -866 C
ATOM 1218 CD LYS A 173 16.775 9.507 61.931 1.00 71.51 C
ANISOU 1218 CD LYS A 173 10776 8724 7671 1826 -333 -826 C
ATOM 1219 CE LYS A 173 18.265 9.447 61.674 1.00 69.08 C
ANISOU 1219 CE LYS A 173 10539 8255 7453 1573 -336 -817 C
ATOM 1220 NZ LYS A 173 18.662 10.231 60.475 1.00 69.29 N
ANISOU 1220 NZ LYS A 173 10763 8065 7497 1616 -287 -771 N
ATOM 1221 N LYS A 174 15.577 3.792 63.442 1.00 52.75 N
ANISOU 1221 N LYS A 174 7357 7285 5402 1447 -509 -728 N
ATOM 1222 CA LYS A 174 15.508 2.484 62.776 1.00 51.48 C
ANISOU 1222 CA LYS A 174 7023 7235 5300 1353 -520 -668 C
ATOM 1223 C LYS A 174 14.074 2.025 62.482 1.00 56.28 C
ANISOU 1223 C LYS A 174 7477 8063 5845 1469 -510 -684 C
ATOM 1224 O LYS A 174 13.223 2.050 63.372 1.00 57.79 O
ANISOU 1224 O LYS A 174 7602 8395 5960 1540 -498 -729 O
ATOM 1225 CB LYS A 174 16.296 1.384 63.512 1.00 52.43 C
ANISOU 1225 CB LYS A 174 7050 7389 5482 1159 -523 -633 C
ATOM 1226 CG LYS A 174 16.095 1.249 64.998 1.00 57.02 C
ANISOU 1226 CG LYS A 174 7588 8067 6009 1140 -516 -668 C
ATOM 1227 CD LYS A 174 17.435 1.074 65.711 1.00 61.29 C
ANISOU 1227 CD LYS A 174 8166 8532 6588 988 -528 -645 C
ATOM 1228 CE LYS A 174 17.799 -0.367 65.971 1.00 63.07 C
ANISOU 1228 CE LYS A 174 8254 8846 6864 862 -516 -569 C
ATOM 1229 NZ LYS A 174 19.005 -0.481 66.829 1.00 64.24 N
ANISOU 1229 NZ LYS A 174 8420 8970 7017 751 -530 -545 N
ATOM 1230 N CYS A 175 13.826 1.611 61.211 1.00 51.44 N
ANISOU 1230 N CYS A 175 6798 7493 5253 1481 -514 -651 N
ATOM 1231 CA CYS A 175 12.531 1.156 60.693 1.00 52.05 C
ANISOU 1231 CA CYS A 175 6712 7802 5262 1570 -507 -674 C
ATOM 1232 C CYS A 175 12.010 -0.072 61.430 1.00 52.85 C
ANISOU 1232 C CYS A 175 6630 8088 5363 1444 -482 -693 C
ATOM 1233 O CYS A 175 10.797 -0.264 61.469 1.00 53.50 O
ANISOU 1233 O CYS A 175 6575 8393 5357 1523 -468 -739 O
ATOM 1234 CB CYS A 175 12.594 0.885 59.188 1.00 52.97 C
ANISOU 1234 CB CYS A 175 6799 7921 5407 1567 -516 -640 C
ATOM 1235 SG CYS A 175 13.013 2.329 58.174 1.00 58.19 S
ANISOU 1235 SG CYS A 175 7675 8385 6047 1742 -529 -607 S
ATOM 1236 N SER A 176 12.906 -0.933 61.939 1.00 47.13 N
ANISOU 1236 N SER A 176 5897 7282 4727 1253 -469 -653 N
ATOM 1237 CA SER A 176 12.543 -2.161 62.656 1.00 47.09 C
ANISOU 1237 CA SER A 176 5751 7411 4730 1122 -426 -652 C
ATOM 1238 C SER A 176 11.687 -1.882 63.907 1.00 53.00 C
ANISOU 1238 C SER A 176 6451 8303 5383 1198 -412 -702 C
ATOM 1239 O SER A 176 10.888 -2.735 64.295 1.00 53.60 O
ANISOU 1239 O SER A 176 6385 8555 5425 1136 -368 -722 O
ATOM 1240 CB SER A 176 13.797 -2.935 63.058 1.00 49.42 C
ANISOU 1240 CB SER A 176 6088 7566 5124 951 -411 -582 C
ATOM 1241 OG SER A 176 14.679 -2.154 63.848 1.00 57.35 O
ANISOU 1241 OG SER A 176 7217 8443 6130 970 -442 -572 O
ATOM 1242 N PHE A 177 11.846 -0.694 64.523 1.00 50.26 N
ANISOU 1242 N PHE A 177 6227 7879 4989 1323 -440 -729 N
ATOM 1243 CA PHE A 177 11.115 -0.297 65.725 1.00 51.85 C
ANISOU 1243 CA PHE A 177 6405 8202 5095 1410 -428 -782 C
ATOM 1244 C PHE A 177 9.706 0.197 65.384 1.00 55.30 C
ANISOU 1244 C PHE A 177 6760 8833 5420 1600 -424 -843 C
ATOM 1245 O PHE A 177 8.859 0.279 66.273 1.00 56.01 O
ANISOU 1245 O PHE A 177 6775 9085 5420 1667 -404 -890 O
ATOM 1246 CB PHE A 177 11.910 0.766 66.517 1.00 54.84 C
ANISOU 1246 CB PHE A 177 6958 8412 5465 1453 -451 -798 C
ATOM 1247 CG PHE A 177 12.960 0.206 67.459 1.00 56.88 C
ANISOU 1247 CG PHE A 177 7233 8604 5776 1286 -449 -760 C
ATOM 1248 CD1 PHE A 177 13.786 -0.849 67.069 1.00 59.54 C
ANISOU 1248 CD1 PHE A 177 7530 8885 6209 1123 -443 -683 C
ATOM 1249 CD2 PHE A 177 13.151 0.758 68.721 1.00 61.08 C
ANISOU 1249 CD2 PHE A 177 7824 9136 6249 1304 -452 -800 C
ATOM 1250 CE1 PHE A 177 14.755 -1.362 67.936 1.00 60.45 C
ANISOU 1250 CE1 PHE A 177 7653 8962 6354 1000 -440 -636 C
ATOM 1251 CE2 PHE A 177 14.128 0.246 69.588 1.00 63.68 C
ANISOU 1251 CE2 PHE A 177 8152 9438 6606 1164 -455 -762 C
ATOM 1252 CZ PHE A 177 14.922 -0.810 69.189 1.00 60.61 C
ANISOU 1252 CZ PHE A 177 7714 9008 6305 1022 -449 -674 C
ATOM 1253 N LEU A 178 9.446 0.474 64.096 1.00 50.93 N
ANISOU 1253 N LEU A 178 6205 8287 4859 1689 -440 -838 N
ATOM 1254 CA LEU A 178 8.150 0.910 63.587 1.00 51.37 C
ANISOU 1254 CA LEU A 178 6166 8557 4795 1887 -440 -885 C
ATOM 1255 C LEU A 178 7.314 -0.274 63.096 1.00 53.65 C
ANISOU 1255 C LEU A 178 6223 9100 5061 1782 -416 -907 C
ATOM 1256 O LEU A 178 6.202 -0.073 62.617 1.00 54.79 O
ANISOU 1256 O LEU A 178 6244 9480 5094 1923 -417 -952 O
ATOM 1257 CB LEU A 178 8.332 1.918 62.435 1.00 52.01 C
ANISOU 1257 CB LEU A 178 6382 8520 4861 2063 -466 -863 C
ATOM 1258 CG LEU A 178 9.092 3.226 62.689 1.00 57.51 C
ANISOU 1258 CG LEU A 178 7336 8945 5570 2172 -471 -851 C
ATOM 1259 CD1 LEU A 178 8.925 4.171 61.514 1.00 58.83 C
ANISOU 1259 CD1 LEU A 178 7619 9040 5695 2377 -476 -824 C
ATOM 1260 CD2 LEU A 178 8.602 3.926 63.930 1.00 60.71 C
ANISOU 1260 CD2 LEU A 178 7789 9388 5891 2294 -452 -908 C
ATOM 1261 N LYS A 179 7.820 -1.500 63.249 1.00 48.55 N
ANISOU 1261 N LYS A 179 5518 8420 4509 1537 -386 -880 N
ATOM 1262 CA LYS A 179 7.152 -2.688 62.727 1.00 48.92 C
ANISOU 1262 CA LYS A 179 5374 8666 4548 1394 -345 -909 C
ATOM 1263 C LYS A 179 6.454 -3.558 63.758 1.00 53.58 C
ANISOU 1263 C LYS A 179 5826 9433 5099 1271 -282 -945 C
ATOM 1264 O LYS A 179 6.932 -3.745 64.881 1.00 52.52 O
ANISOU 1264 O LYS A 179 5755 9200 5000 1206 -261 -912 O
ATOM 1265 CB LYS A 179 8.163 -3.565 61.966 1.00 50.09 C
ANISOU 1265 CB LYS A 179 5565 8637 4828 1199 -332 -854 C
ATOM 1266 CG LYS A 179 8.665 -2.892 60.699 1.00 55.91 C
ANISOU 1266 CG LYS A 179 6395 9256 5592 1296 -383 -827 C
ATOM 1267 CD LYS A 179 9.235 -3.870 59.720 1.00 55.19 C
ANISOU 1267 CD LYS A 179 6285 9088 5597 1115 -362 -799 C
ATOM 1268 CE LYS A 179 9.654 -3.140 58.477 1.00 53.09 C
ANISOU 1268 CE LYS A 179 6103 8728 5340 1224 -412 -773 C
ATOM 1269 NZ LYS A 179 8.543 -3.006 57.500 1.00 49.98 N
ANISOU 1269 NZ LYS A 179 5568 8590 4832 1332 -423 -832 N
ATOM 1270 N SER A 180 5.354 -4.167 63.317 1.00 51.36 N
ANISOU 1270 N SER A 180 5349 9424 4743 1221 -245 -1012 N
ATOM 1271 CA SER A 180 4.599 -5.140 64.096 1.00 52.39 C
ANISOU 1271 CA SER A 180 5331 9743 4831 1065 -165 -1055 C
ATOM 1272 C SER A 180 5.358 -6.500 64.114 1.00 56.18 C
ANISOU 1272 C SER A 180 5845 10062 5440 789 -90 -1005 C
ATOM 1273 O SER A 180 6.351 -6.649 63.395 1.00 55.04 O
ANISOU 1273 O SER A 180 5810 9701 5401 738 -110 -949 O
ATOM 1274 CB SER A 180 3.193 -5.292 63.515 1.00 56.53 C
ANISOU 1274 CB SER A 180 5628 10629 5221 1093 -147 -1157 C
ATOM 1275 OG SER A 180 3.219 -5.790 62.189 1.00 65.06 O
ANISOU 1275 OG SER A 180 6648 11746 6326 1000 -146 -1181 O
ATOM 1276 N GLU A 181 4.891 -7.483 64.919 1.00 53.22 N
ANISOU 1276 N GLU A 181 5384 9789 5049 620 4 -1021 N
ATOM 1277 CA GLU A 181 5.507 -8.816 64.996 1.00 52.12 C
ANISOU 1277 CA GLU A 181 5290 9496 5016 373 101 -969 C
ATOM 1278 C GLU A 181 5.563 -9.471 63.605 1.00 54.75 C
ANISOU 1278 C GLU A 181 5586 9817 5400 244 126 -1002 C
ATOM 1279 O GLU A 181 6.656 -9.828 63.172 1.00 53.60 O
ANISOU 1279 O GLU A 181 5569 9424 5372 178 130 -928 O
ATOM 1280 CB GLU A 181 4.779 -9.731 66.001 1.00 54.50 C
ANISOU 1280 CB GLU A 181 5501 9939 5269 219 217 -991 C
ATOM 1281 CG GLU A 181 5.028 -9.375 67.454 1.00 65.14 C
ANISOU 1281 CG GLU A 181 6918 11237 6594 300 212 -931 C
ATOM 1282 N PHE A 182 4.421 -9.558 62.878 1.00 51.58 N
ANISOU 1282 N PHE A 182 5004 9695 4899 221 137 -1116 N
ATOM 1283 CA PHE A 182 4.406 -10.146 61.537 1.00 51.33 C
ANISOU 1283 CA PHE A 182 4922 9686 4896 95 160 -1166 C
ATOM 1284 C PHE A 182 5.175 -9.270 60.524 1.00 55.57 C
ANISOU 1284 C PHE A 182 5557 10082 5476 264 48 -1121 C
ATOM 1285 O PHE A 182 5.709 -9.805 59.548 1.00 55.03 O
ANISOU 1285 O PHE A 182 5525 9904 5481 156 65 -1116 O
ATOM 1286 CB PHE A 182 2.987 -10.454 61.028 1.00 54.89 C
ANISOU 1286 CB PHE A 182 5134 10512 5210 14 200 -1311 C
ATOM 1287 CG PHE A 182 3.018 -11.345 59.800 1.00 56.91 C
ANISOU 1287 CG PHE A 182 5342 10781 5500 -188 256 -1375 C
ATOM 1288 CD1 PHE A 182 3.450 -12.667 59.887 1.00 59.71 C
ANISOU 1288 CD1 PHE A 182 5770 10961 5956 -464 390 -1365 C
ATOM 1289 CD2 PHE A 182 2.693 -10.841 58.545 1.00 58.95 C
ANISOU 1289 CD2 PHE A 182 5503 11207 5687 -89 179 -1438 C
ATOM 1290 CE1 PHE A 182 3.533 -13.472 58.745 1.00 60.63 C
ANISOU 1290 CE1 PHE A 182 5863 11067 6106 -651 449 -1433 C
ATOM 1291 CE2 PHE A 182 2.765 -11.649 57.407 1.00 61.90 C
ANISOU 1291 CE2 PHE A 182 5835 11596 6087 -279 229 -1505 C
ATOM 1292 CZ PHE A 182 3.187 -12.959 57.514 1.00 59.92 C
ANISOU 1292 CZ PHE A 182 5660 11163 5942 -566 365 -1508 C
ATOM 1293 N GLY A 183 5.259 -7.964 60.790 1.00 52.06 N
ANISOU 1293 N GLY A 183 5170 9623 4986 518 -52 -1088 N
ATOM 1294 CA GLY A 183 6.028 -7.021 59.987 1.00 51.01 C
ANISOU 1294 CA GLY A 183 5162 9327 4891 686 -147 -1034 C
ATOM 1295 C GLY A 183 7.500 -7.383 59.964 1.00 54.04 C
ANISOU 1295 C GLY A 183 5729 9373 5432 588 -140 -934 C
ATOM 1296 O GLY A 183 8.130 -7.369 58.904 1.00 53.69 O
ANISOU 1296 O GLY A 183 5742 9213 5446 580 -168 -910 O
ATOM 1297 N LEU A 184 8.029 -7.776 61.129 1.00 49.64 N
ANISOU 1297 N LEU A 184 5249 8679 4933 511 -99 -876 N
ATOM 1298 CA LEU A 184 9.409 -8.213 61.322 1.00 48.08 C
ANISOU 1298 CA LEU A 184 5203 8197 4866 422 -83 -775 C
ATOM 1299 C LEU A 184 9.635 -9.567 60.647 1.00 53.57 C
ANISOU 1299 C LEU A 184 5878 8837 5638 208 10 -774 C
ATOM 1300 O LEU A 184 10.716 -9.803 60.102 1.00 53.08 O
ANISOU 1300 O LEU A 184 5921 8571 5675 167 6 -709 O
ATOM 1301 CB LEU A 184 9.697 -8.296 62.832 1.00 47.61 C
ANISOU 1301 CB LEU A 184 5199 8079 4812 416 -57 -721 C
ATOM 1302 CG LEU A 184 10.749 -7.354 63.446 1.00 51.31 C
ANISOU 1302 CG LEU A 184 5815 8371 5311 538 -133 -652 C
ATOM 1303 CD1 LEU A 184 10.895 -6.031 62.701 1.00 51.27 C
ANISOU 1303 CD1 LEU A 184 5872 8327 5283 711 -230 -674 C
ATOM 1304 CD2 LEU A 184 10.457 -7.097 64.898 1.00 52.74 C
ANISOU 1304 CD2 LEU A 184 5990 8620 5427 585 -125 -650 C
ATOM 1305 N VAL A 185 8.599 -10.445 60.659 1.00 50.92 N
ANISOU 1305 N VAL A 185 5407 8691 5249 66 101 -855 N
ATOM 1306 CA VAL A 185 8.627 -11.783 60.049 1.00 50.53 C
ANISOU 1306 CA VAL A 185 5340 8603 5256 -162 215 -881 C
ATOM 1307 C VAL A 185 8.676 -11.645 58.520 1.00 53.87 C
ANISOU 1307 C VAL A 185 5729 9056 5684 -159 172 -934 C
ATOM 1308 O VAL A 185 9.549 -12.241 57.886 1.00 53.08 O
ANISOU 1308 O VAL A 185 5721 8766 5683 -250 207 -892 O
ATOM 1309 CB VAL A 185 7.431 -12.668 60.523 1.00 54.80 C
ANISOU 1309 CB VAL A 185 5745 9352 5723 -332 334 -971 C
ATOM 1310 CG1 VAL A 185 7.312 -13.957 59.697 1.00 54.71 C
ANISOU 1310 CG1 VAL A 185 5712 9322 5753 -581 461 -1033 C
ATOM 1311 CG2 VAL A 185 7.559 -12.994 62.004 1.00 54.21 C
ANISOU 1311 CG2 VAL A 185 5731 9207 5658 -356 398 -897 C
ATOM 1312 N TRP A 186 7.748 -10.854 57.948 1.00 50.61 N
ANISOU 1312 N TRP A 186 5184 8889 5154 -38 98 -1019 N
ATOM 1313 CA TRP A 186 7.652 -10.600 56.517 1.00 50.93 C
ANISOU 1313 CA TRP A 186 5173 9012 5167 -4 48 -1071 C
ATOM 1314 C TRP A 186 8.937 -9.930 55.979 1.00 52.11 C
ANISOU 1314 C TRP A 186 5488 8903 5407 120 -33 -967 C
ATOM 1315 O TRP A 186 9.408 -10.303 54.903 1.00 50.94 O
ANISOU 1315 O TRP A 186 5363 8687 5306 54 -27 -972 O
ATOM 1316 CB TRP A 186 6.415 -9.750 56.198 1.00 51.53 C
ANISOU 1316 CB TRP A 186 5078 9424 5079 154 -18 -1161 C
ATOM 1317 CG TRP A 186 6.142 -9.650 54.730 1.00 53.59 C
ANISOU 1317 CG TRP A 186 5250 9831 5281 172 -54 -1225 C
ATOM 1318 CD1 TRP A 186 6.401 -8.586 53.919 1.00 56.24 C
ANISOU 1318 CD1 TRP A 186 5628 10158 5582 392 -157 -1185 C
ATOM 1319 CD2 TRP A 186 5.658 -10.697 53.879 1.00 55.07 C
ANISOU 1319 CD2 TRP A 186 5309 10174 5442 -49 22 -1337 C
ATOM 1320 NE1 TRP A 186 6.048 -8.882 52.623 1.00 56.73 N
ANISOU 1320 NE1 TRP A 186 5579 10392 5585 340 -159 -1261 N
ATOM 1321 CE2 TRP A 186 5.604 -10.177 52.566 1.00 59.52 C
ANISOU 1321 CE2 TRP A 186 5822 10850 5942 63 -52 -1362 C
ATOM 1322 CE3 TRP A 186 5.228 -12.019 54.105 1.00 57.65 C
ANISOU 1322 CE3 TRP A 186 5564 10559 5783 -338 157 -1424 C
ATOM 1323 CZ2 TRP A 186 5.124 -10.928 51.482 1.00 60.37 C
ANISOU 1323 CZ2 TRP A 186 5791 11153 5993 -105 -7 -1482 C
ATOM 1324 CZ3 TRP A 186 4.749 -12.759 53.034 1.00 60.60 C
ANISOU 1324 CZ3 TRP A 186 5813 11105 6106 -519 211 -1550 C
ATOM 1325 CH2 TRP A 186 4.703 -12.217 51.740 1.00 61.55 C
ANISOU 1325 CH2 TRP A 186 5868 11360 6158 -405 125 -1582 C
ATOM 1326 N HIS A 187 9.510 -8.983 56.755 1.00 47.32 N
ANISOU 1326 N HIS A 187 5000 8158 4823 281 -100 -882 N
ATOM 1327 CA HIS A 187 10.766 -8.273 56.477 1.00 45.14 C
ANISOU 1327 CA HIS A 187 4888 7636 4628 381 -169 -787 C
ATOM 1328 C HIS A 187 11.906 -9.273 56.270 1.00 48.98 C
ANISOU 1328 C HIS A 187 5467 7897 5246 215 -108 -724 C
ATOM 1329 O HIS A 187 12.705 -9.106 55.356 1.00 47.04 O
ANISOU 1329 O HIS A 187 5291 7526 5055 229 -139 -688 O
ATOM 1330 CB HIS A 187 11.101 -7.312 57.639 1.00 44.58 C
ANISOU 1330 CB HIS A 187 4915 7474 4548 524 -221 -731 C
ATOM 1331 CG HIS A 187 12.403 -6.587 57.476 1.00 46.33 C
ANISOU 1331 CG HIS A 187 5305 7452 4848 593 -279 -646 C
ATOM 1332 ND1 HIS A 187 12.509 -5.469 56.670 1.00 47.66 N
ANISOU 1332 ND1 HIS A 187 5534 7590 4983 749 -351 -641 N
ATOM 1333 CD2 HIS A 187 13.614 -6.851 58.015 1.00 46.10 C
ANISOU 1333 CD2 HIS A 187 5385 7216 4914 521 -268 -565 C
ATOM 1334 CE1 HIS A 187 13.772 -5.088 56.751 1.00 45.53 C
ANISOU 1334 CE1 HIS A 187 5411 7093 4796 744 -376 -567 C
ATOM 1335 NE2 HIS A 187 14.474 -5.892 57.545 1.00 45.13 N
ANISOU 1335 NE2 HIS A 187 5381 6945 4820 611 -334 -522 N
ATOM 1336 N GLU A 188 11.965 -10.311 57.121 1.00 47.78 N
ANISOU 1336 N GLU A 188 5318 7700 5137 69 -12 -705 N
ATOM 1337 CA GLU A 188 12.961 -11.377 57.064 1.00 47.61 C
ANISOU 1337 CA GLU A 188 5387 7474 5229 -73 69 -638 C
ATOM 1338 C GLU A 188 12.743 -12.248 55.812 1.00 53.37 C
ANISOU 1338 C GLU A 188 6068 8233 5977 -215 135 -707 C
ATOM 1339 O GLU A 188 13.711 -12.568 55.124 1.00 53.28 O
ANISOU 1339 O GLU A 188 6142 8052 6050 -250 147 -657 O
ATOM 1340 CB GLU A 188 12.885 -12.225 58.336 1.00 49.15 C
ANISOU 1340 CB GLU A 188 5598 7636 5439 -167 168 -599 C
ATOM 1341 CG GLU A 188 14.193 -12.864 58.754 1.00 61.95 C
ANISOU 1341 CG GLU A 188 7354 9022 7162 -206 218 -476 C
ATOM 1342 CD GLU A 188 14.059 -13.860 59.891 1.00 96.53 C
ANISOU 1342 CD GLU A 188 11758 13370 11548 -299 340 -429 C
ATOM 1343 OE1 GLU A 188 13.674 -13.444 61.008 1.00103.26 O
ANISOU 1343 OE1 GLU A 188 12583 14311 12340 -239 319 -419 O
ATOM 1344 OE2 GLU A 188 14.336 -15.060 59.664 1.00 92.70 O
ANISOU 1344 OE2 GLU A 188 11331 12767 11125 -428 465 -397 O
ATOM 1345 N ILE A 189 11.475 -12.610 55.519 1.00 51.50 N
ANISOU 1345 N ILE A 189 5687 8228 5654 -300 179 -828 N
ATOM 1346 CA ILE A 189 11.059 -13.431 54.369 1.00 51.99 C
ANISOU 1346 CA ILE A 189 5676 8372 5705 -459 248 -928 C
ATOM 1347 C ILE A 189 11.421 -12.722 53.050 1.00 55.47 C
ANISOU 1347 C ILE A 189 6116 8822 6137 -352 149 -935 C
ATOM 1348 O ILE A 189 11.993 -13.350 52.153 1.00 55.14 O
ANISOU 1348 O ILE A 189 6121 8672 6157 -451 193 -939 O
ATOM 1349 CB ILE A 189 9.525 -13.760 54.440 1.00 56.24 C
ANISOU 1349 CB ILE A 189 6029 9217 6122 -564 301 -1072 C
ATOM 1350 CG1 ILE A 189 9.208 -14.712 55.621 1.00 57.37 C
ANISOU 1350 CG1 ILE A 189 6189 9326 6285 -721 434 -1068 C
ATOM 1351 CG2 ILE A 189 9.005 -14.345 53.113 1.00 57.10 C
ANISOU 1351 CG2 ILE A 189 6033 9474 6187 -712 346 -1203 C
ATOM 1352 CD1 ILE A 189 7.709 -14.877 55.965 1.00 67.18 C
ANISOU 1352 CD1 ILE A 189 7245 10884 7395 -805 478 -1198 C
ATOM 1353 N VAL A 190 11.054 -11.424 52.937 1.00 50.93 N
ANISOU 1353 N VAL A 190 5497 8377 5476 -144 28 -934 N
ATOM 1354 CA VAL A 190 11.268 -10.574 51.763 1.00 49.37 C
ANISOU 1354 CA VAL A 190 5303 8209 5245 -6 -66 -929 C
ATOM 1355 C VAL A 190 12.771 -10.448 51.478 1.00 49.53 C
ANISOU 1355 C VAL A 190 5496 7932 5390 14 -88 -815 C
ATOM 1356 O VAL A 190 13.192 -10.676 50.341 1.00 49.19 O
ANISOU 1356 O VAL A 190 5467 7850 5372 -27 -85 -825 O
ATOM 1357 CB VAL A 190 10.556 -9.205 51.945 1.00 53.61 C
ANISOU 1357 CB VAL A 190 5791 8914 5663 233 -169 -933 C
ATOM 1358 CG1 VAL A 190 11.157 -8.128 51.066 1.00 53.25 C
ANISOU 1358 CG1 VAL A 190 5840 8778 5614 415 -260 -867 C
ATOM 1359 CG2 VAL A 190 9.073 -9.334 51.659 1.00 54.78 C
ANISOU 1359 CG2 VAL A 190 5730 9422 5661 228 -159 -1061 C
ATOM 1360 N ASN A 191 13.577 -10.175 52.519 1.00 44.01 N
ANISOU 1360 N ASN A 191 4916 7044 4761 61 -101 -717 N
ATOM 1361 CA ASN A 191 15.033 -10.052 52.403 1.00 41.57 C
ANISOU 1361 CA ASN A 191 4753 6482 4560 74 -119 -611 C
ATOM 1362 C ASN A 191 15.690 -11.373 51.990 1.00 45.23 C
ANISOU 1362 C ASN A 191 5250 6818 5116 -99 -19 -598 C
ATOM 1363 O ASN A 191 16.725 -11.329 51.332 1.00 44.30 O
ANISOU 1363 O ASN A 191 5213 6555 5064 -92 -34 -541 O
ATOM 1364 CB ASN A 191 15.643 -9.498 53.680 1.00 36.18 C
ANISOU 1364 CB ASN A 191 4161 5679 3907 148 -151 -528 C
ATOM 1365 CG ASN A 191 15.597 -7.988 53.696 1.00 51.01 C
ANISOU 1365 CG ASN A 191 6082 7573 5726 334 -254 -516 C
ATOM 1366 OD1 ASN A 191 16.269 -7.304 52.920 1.00 48.94 O
ANISOU 1366 OD1 ASN A 191 5898 7215 5483 403 -306 -479 O
ATOM 1367 ND2 ASN A 191 14.754 -7.428 54.523 1.00 41.78 N
ANISOU 1367 ND2 ASN A 191 4872 6525 4479 421 -276 -550 N
ATOM 1368 N TYR A 192 15.065 -12.526 52.303 1.00 43.51 N
ANISOU 1368 N TYR A 192 4976 6658 4898 -255 93 -656 N
ATOM 1369 CA TYR A 192 15.537 -13.853 51.901 1.00 44.71 C
ANISOU 1369 CA TYR A 192 5175 6684 5129 -423 215 -657 C
ATOM 1370 C TYR A 192 15.248 -14.072 50.418 1.00 48.90 C
ANISOU 1370 C TYR A 192 5645 7302 5632 -488 221 -752 C
ATOM 1371 O TYR A 192 16.148 -14.471 49.678 1.00 47.89 O
ANISOU 1371 O TYR A 192 5594 7027 5575 -524 249 -717 O
ATOM 1372 CB TYR A 192 14.863 -14.952 52.742 1.00 49.12 C
ANISOU 1372 CB TYR A 192 5711 7270 5684 -575 350 -696 C
ATOM 1373 CG TYR A 192 15.569 -16.294 52.723 1.00 54.91 C
ANISOU 1373 CG TYR A 192 6554 7798 6512 -715 497 -654 C
ATOM 1374 CD1 TYR A 192 15.637 -17.056 51.558 1.00 58.09 C
ANISOU 1374 CD1 TYR A 192 6963 8169 6940 -846 577 -728 C
ATOM 1375 CD2 TYR A 192 16.073 -16.853 53.895 1.00 56.77 C
ANISOU 1375 CD2 TYR A 192 6887 7882 6800 -714 572 -545 C
ATOM 1376 CE1 TYR A 192 16.277 -18.295 51.538 1.00 61.06 C
ANISOU 1376 CE1 TYR A 192 7461 8337 7401 -960 728 -689 C
ATOM 1377 CE2 TYR A 192 16.681 -18.111 53.896 1.00 58.58 C
ANISOU 1377 CE2 TYR A 192 7233 7918 7107 -816 724 -495 C
ATOM 1378 CZ TYR A 192 16.799 -18.818 52.711 1.00 70.31 C
ANISOU 1378 CZ TYR A 192 8742 9348 8625 -935 805 -567 C
ATOM 1379 OH TYR A 192 17.425 -20.040 52.707 1.00 77.77 O
ANISOU 1379 OH TYR A 192 9822 10080 9645 -1019 968 -515 O
ATOM 1380 N ILE A 193 13.983 -13.824 49.984 1.00 45.98 N
ANISOU 1380 N ILE A 193 5128 7194 5148 -499 197 -874 N
ATOM 1381 CA ILE A 193 13.547 -13.966 48.590 1.00 45.59 C
ANISOU 1381 CA ILE A 193 4990 7293 5039 -554 194 -979 C
ATOM 1382 C ILE A 193 14.435 -13.093 47.690 1.00 48.59 C
ANISOU 1382 C ILE A 193 5437 7586 5439 -404 91 -905 C
ATOM 1383 O ILE A 193 14.921 -13.578 46.677 1.00 49.39 O
ANISOU 1383 O ILE A 193 5563 7628 5573 -478 124 -925 O
ATOM 1384 CB ILE A 193 12.030 -13.647 48.428 1.00 49.28 C
ANISOU 1384 CB ILE A 193 5264 8106 5352 -549 165 -1111 C
ATOM 1385 CG1 ILE A 193 11.182 -14.723 49.140 1.00 50.26 C
ANISOU 1385 CG1 ILE A 193 5321 8316 5460 -760 297 -1205 C
ATOM 1386 CG2 ILE A 193 11.636 -13.521 46.936 1.00 49.88 C
ANISOU 1386 CG2 ILE A 193 5234 8378 5339 -552 129 -1207 C
ATOM 1387 CD1 ILE A 193 9.678 -14.486 49.201 1.00 55.60 C
ANISOU 1387 CD1 ILE A 193 5792 9353 5981 -769 280 -1334 C
ATOM 1388 N CYS A 194 14.685 -11.835 48.094 1.00 43.76 N
ANISOU 1388 N CYS A 194 4868 6949 4809 -206 -19 -820 N
ATOM 1389 CA CYS A 194 15.509 -10.879 47.360 1.00 42.51 C
ANISOU 1389 CA CYS A 194 4791 6697 4664 -62 -109 -743 C
ATOM 1390 C CYS A 194 16.971 -11.349 47.215 1.00 45.30 C
ANISOU 1390 C CYS A 194 5278 6786 5148 -123 -73 -652 C
ATOM 1391 O CYS A 194 17.548 -11.181 46.137 1.00 44.52 O
ANISOU 1391 O CYS A 194 5211 6643 5061 -102 -97 -636 O
ATOM 1392 CB CYS A 194 15.406 -9.501 47.992 1.00 42.24 C
ANISOU 1392 CB CYS A 194 4795 6673 4582 138 -206 -683 C
ATOM 1393 SG CYS A 194 13.828 -8.686 47.646 1.00 47.54 S
ANISOU 1393 SG CYS A 194 5316 7673 5073 287 -268 -772 S
ATOM 1394 N GLN A 195 17.523 -12.013 48.251 1.00 41.13 N
ANISOU 1394 N GLN A 195 4817 6106 4706 -195 -8 -596 N
ATOM 1395 CA GLN A 195 18.842 -12.656 48.207 1.00 39.80 C
ANISOU 1395 CA GLN A 195 4756 5718 4649 -250 45 -512 C
ATOM 1396 C GLN A 195 18.861 -13.733 47.107 1.00 44.59 C
ANISOU 1396 C GLN A 195 5349 6315 5279 -387 137 -580 C
ATOM 1397 O GLN A 195 19.816 -13.796 46.352 1.00 44.76 O
ANISOU 1397 O GLN A 195 5432 6223 5352 -380 136 -534 O
ATOM 1398 CB GLN A 195 19.188 -13.290 49.565 1.00 40.74 C
ANISOU 1398 CB GLN A 195 4929 5725 4825 -291 112 -446 C
ATOM 1399 CG GLN A 195 19.783 -12.310 50.586 1.00 50.70 C
ANISOU 1399 CG GLN A 195 6244 6927 6092 -165 27 -351 C
ATOM 1400 CD GLN A 195 21.179 -11.835 50.257 1.00 50.80 C
ANISOU 1400 CD GLN A 195 6341 6799 6162 -107 -21 -259 C
ATOM 1401 OE1 GLN A 195 22.013 -12.579 49.742 1.00 43.89 O
ANISOU 1401 OE1 GLN A 195 5508 5818 5351 -162 38 -222 O
ATOM 1402 NE2 GLN A 195 21.477 -10.591 50.596 1.00 37.95 N
ANISOU 1402 NE2 GLN A 195 4745 5166 4507 0 -120 -224 N
ATOM 1403 N VAL A 196 17.783 -14.544 46.992 1.00 41.54 N
ANISOU 1403 N VAL A 196 4877 6060 4847 -520 219 -699 N
ATOM 1404 CA VAL A 196 17.627 -15.594 45.977 1.00 41.84 C
ANISOU 1404 CA VAL A 196 4897 6111 4891 -679 321 -796 C
ATOM 1405 C VAL A 196 17.505 -14.936 44.575 1.00 45.89 C
ANISOU 1405 C VAL A 196 5343 6758 5333 -621 236 -849 C
ATOM 1406 O VAL A 196 18.149 -15.409 43.644 1.00 45.11 O
ANISOU 1406 O VAL A 196 5289 6576 5275 -675 276 -857 O
ATOM 1407 CB VAL A 196 16.425 -16.531 46.299 1.00 46.63 C
ANISOU 1407 CB VAL A 196 5423 6843 5451 -858 434 -926 C
ATOM 1408 CG1 VAL A 196 16.194 -17.567 45.201 1.00 47.14 C
ANISOU 1408 CG1 VAL A 196 5468 6937 5508 -1044 545 -1055 C
ATOM 1409 CG2 VAL A 196 16.607 -17.217 47.649 1.00 46.26 C
ANISOU 1409 CG2 VAL A 196 5461 6643 5471 -909 533 -858 C
ATOM 1410 N ILE A 197 16.717 -13.834 44.446 1.00 43.18 N
ANISOU 1410 N ILE A 197 4903 6622 4882 -494 123 -876 N
ATOM 1411 CA ILE A 197 16.522 -13.066 43.199 1.00 43.17 C
ANISOU 1411 CA ILE A 197 4841 6771 4790 -397 37 -906 C
ATOM 1412 C ILE A 197 17.873 -12.518 42.732 1.00 45.95 C
ANISOU 1412 C ILE A 197 5321 6922 5217 -299 -12 -783 C
ATOM 1413 O ILE A 197 18.188 -12.601 41.536 1.00 45.54 O
ANISOU 1413 O ILE A 197 5265 6889 5149 -313 -14 -805 O
ATOM 1414 CB ILE A 197 15.458 -11.928 43.371 1.00 46.61 C
ANISOU 1414 CB ILE A 197 5172 7445 5092 -234 -66 -928 C
ATOM 1415 CG1 ILE A 197 14.038 -12.509 43.539 1.00 47.96 C
ANISOU 1415 CG1 ILE A 197 5176 7886 5161 -345 -17 -1074 C
ATOM 1416 CG2 ILE A 197 15.499 -10.889 42.214 1.00 46.87 C
ANISOU 1416 CG2 ILE A 197 5189 7584 5036 -70 -161 -905 C
ATOM 1417 CD1 ILE A 197 13.079 -11.556 44.174 1.00 56.78 C
ANISOU 1417 CD1 ILE A 197 6209 9195 6171 -185 -95 -1075 C
ATOM 1418 N PHE A 198 18.675 -11.983 43.684 1.00 41.42 N
ANISOU 1418 N PHE A 198 4852 6169 4716 -213 -48 -661 N
ATOM 1419 CA PHE A 198 19.992 -11.441 43.388 1.00 40.41 C
ANISOU 1419 CA PHE A 198 4839 5862 4655 -140 -89 -549 C
ATOM 1420 C PHE A 198 20.938 -12.515 42.835 1.00 45.19 C
ANISOU 1420 C PHE A 198 5496 6323 5350 -258 -1 -537 C
ATOM 1421 O PHE A 198 21.477 -12.326 41.745 1.00 43.96 O
ANISOU 1421 O PHE A 198 5362 6150 5193 -239 -19 -525 O
ATOM 1422 CB PHE A 198 20.646 -10.760 44.614 1.00 40.96 C
ANISOU 1422 CB PHE A 198 4994 5794 4774 -55 -133 -442 C
ATOM 1423 CG PHE A 198 22.098 -10.436 44.334 1.00 41.16 C
ANISOU 1423 CG PHE A 198 5125 5642 4874 -30 -151 -341 C
ATOM 1424 CD1 PHE A 198 22.446 -9.475 43.384 1.00 43.23 C
ANISOU 1424 CD1 PHE A 198 5424 5902 5101 54 -214 -310 C
ATOM 1425 CD2 PHE A 198 23.117 -11.167 44.933 1.00 42.58 C
ANISOU 1425 CD2 PHE A 198 5360 5672 5148 -93 -95 -276 C
ATOM 1426 CE1 PHE A 198 23.785 -9.240 43.061 1.00 43.05 C
ANISOU 1426 CE1 PHE A 198 5486 5732 5141 53 -220 -226 C
ATOM 1427 CE2 PHE A 198 24.455 -10.915 44.623 1.00 44.20 C
ANISOU 1427 CE2 PHE A 198 5636 5750 5407 -76 -109 -190 C
ATOM 1428 CZ PHE A 198 24.779 -9.945 43.697 1.00 41.71 C
ANISOU 1428 CZ PHE A 198 5350 5437 5060 -14 -172 -171 C
ATOM 1429 N TRP A 199 21.158 -13.603 43.605 1.00 43.50 N
ANISOU 1429 N TRP A 199 5315 6002 5211 -363 100 -532 N
ATOM 1430 CA TRP A 199 22.090 -14.678 43.273 1.00 44.83 C
ANISOU 1430 CA TRP A 199 5555 6011 5467 -451 202 -506 C
ATOM 1431 C TRP A 199 21.698 -15.478 42.026 1.00 48.29 C
ANISOU 1431 C TRP A 199 5953 6516 5878 -568 275 -624 C
ATOM 1432 O TRP A 199 22.607 -15.892 41.302 1.00 48.14 O
ANISOU 1432 O TRP A 199 5994 6388 5911 -587 317 -597 O
ATOM 1433 CB TRP A 199 22.323 -15.598 44.472 1.00 45.03 C
ANISOU 1433 CB TRP A 199 5638 5909 5562 -506 301 -461 C
ATOM 1434 CG TRP A 199 23.116 -14.911 45.544 1.00 46.61 C
ANISOU 1434 CG TRP A 199 5889 6025 5797 -393 235 -331 C
ATOM 1435 CD1 TRP A 199 22.632 -14.351 46.687 1.00 49.75 C
ANISOU 1435 CD1 TRP A 199 6266 6472 6165 -341 187 -310 C
ATOM 1436 CD2 TRP A 199 24.509 -14.583 45.498 1.00 46.80 C
ANISOU 1436 CD2 TRP A 199 5979 5931 5874 -319 201 -219 C
ATOM 1437 NE1 TRP A 199 23.647 -13.743 47.389 1.00 49.21 N
ANISOU 1437 NE1 TRP A 199 6250 6318 6128 -251 129 -197 N
ATOM 1438 CE2 TRP A 199 24.814 -13.882 46.688 1.00 51.00 C
ANISOU 1438 CE2 TRP A 199 6525 6449 6404 -240 137 -140 C
ATOM 1439 CE3 TRP A 199 25.545 -14.848 44.584 1.00 48.66 C
ANISOU 1439 CE3 TRP A 199 6254 6084 6150 -320 224 -183 C
ATOM 1440 CZ2 TRP A 199 26.104 -13.422 46.976 1.00 50.42 C
ANISOU 1440 CZ2 TRP A 199 6496 6298 6364 -175 94 -36 C
ATOM 1441 CZ3 TRP A 199 26.829 -14.420 44.885 1.00 50.12 C
ANISOU 1441 CZ3 TRP A 199 6482 6191 6372 -246 183 -71 C
ATOM 1442 CH2 TRP A 199 27.096 -13.699 46.056 1.00 50.65 C
ANISOU 1442 CH2 TRP A 199 6553 6261 6430 -181 117 -2 C
ATOM 1443 N ILE A 200 20.395 -15.660 41.742 1.00 44.81 N
ANISOU 1443 N ILE A 200 5405 6271 5349 -646 289 -759 N
ATOM 1444 CA ILE A 200 19.972 -16.353 40.522 1.00 46.17 C
ANISOU 1444 CA ILE A 200 5523 6544 5475 -772 353 -893 C
ATOM 1445 C ILE A 200 20.322 -15.463 39.306 1.00 48.80 C
ANISOU 1445 C ILE A 200 5830 6958 5752 -663 250 -873 C
ATOM 1446 O ILE A 200 20.882 -15.971 38.331 1.00 49.49 O
ANISOU 1446 O ILE A 200 5948 6996 5860 -720 300 -901 O
ATOM 1447 CB ILE A 200 18.475 -16.781 40.541 1.00 51.02 C
ANISOU 1447 CB ILE A 200 6007 7386 5992 -902 396 -1056 C
ATOM 1448 CG1 ILE A 200 18.265 -17.991 41.488 1.00 52.08 C
ANISOU 1448 CG1 ILE A 200 6199 7395 6193 -1067 552 -1091 C
ATOM 1449 CG2 ILE A 200 17.957 -17.095 39.108 1.00 52.72 C
ANISOU 1449 CG2 ILE A 200 6124 7796 6112 -995 411 -1204 C
ATOM 1450 CD1 ILE A 200 16.768 -18.430 41.698 1.00 58.52 C
ANISOU 1450 CD1 ILE A 200 6887 8434 6914 -1224 611 -1254 C
ATOM 1451 N ASN A 201 20.045 -14.142 39.396 1.00 43.51 N
ANISOU 1451 N ASN A 201 5122 6396 5013 -500 119 -819 N
ATOM 1452 CA ASN A 201 20.359 -13.181 38.332 1.00 43.04 C
ANISOU 1452 CA ASN A 201 5060 6401 4894 -376 28 -779 C
ATOM 1453 C ASN A 201 21.869 -12.965 38.183 1.00 46.86 C
ANISOU 1453 C ASN A 201 5670 6657 5476 -329 23 -652 C
ATOM 1454 O ASN A 201 22.341 -12.848 37.058 1.00 47.00 O
ANISOU 1454 O ASN A 201 5699 6686 5474 -317 14 -649 O
ATOM 1455 CB ASN A 201 19.646 -11.861 38.540 1.00 40.06 C
ANISOU 1455 CB ASN A 201 4636 6171 4414 -205 -86 -748 C
ATOM 1456 CG ASN A 201 18.222 -11.923 38.068 1.00 51.27 C
ANISOU 1456 CG ASN A 201 5896 7895 5690 -218 -99 -881 C
ATOM 1457 OD1 ASN A 201 17.945 -11.859 36.869 1.00 44.14 O
ANISOU 1457 OD1 ASN A 201 4923 7157 4692 -207 -116 -940 O
ATOM 1458 ND2 ASN A 201 17.290 -12.124 38.992 1.00 38.52 N
ANISOU 1458 ND2 ASN A 201 4208 6383 4046 -252 -84 -938 N
ATOM 1459 N PHE A 202 22.624 -12.957 39.296 1.00 43.17 N
ANISOU 1459 N PHE A 202 5289 6008 5107 -310 32 -552 N
ATOM 1460 CA PHE A 202 24.076 -12.830 39.268 1.00 42.46 C
ANISOU 1460 CA PHE A 202 5299 5731 5104 -278 33 -437 C
ATOM 1461 C PHE A 202 24.674 -14.067 38.582 1.00 46.71 C
ANISOU 1461 C PHE A 202 5861 6187 5699 -387 142 -471 C
ATOM 1462 O PHE A 202 25.570 -13.918 37.761 1.00 46.21 O
ANISOU 1462 O PHE A 202 5836 6068 5654 -363 136 -425 O
ATOM 1463 CB PHE A 202 24.632 -12.642 40.686 1.00 43.85 C
ANISOU 1463 CB PHE A 202 5532 5780 5348 -243 23 -342 C
ATOM 1464 CG PHE A 202 26.117 -12.366 40.810 1.00 45.80 C
ANISOU 1464 CG PHE A 202 5859 5878 5665 -203 10 -225 C
ATOM 1465 CD1 PHE A 202 26.752 -11.466 39.961 1.00 49.77 C
ANISOU 1465 CD1 PHE A 202 6392 6374 6145 -144 -52 -178 C
ATOM 1466 CD2 PHE A 202 26.864 -12.949 41.821 1.00 49.11 C
ANISOU 1466 CD2 PHE A 202 6318 6182 6160 -221 61 -157 C
ATOM 1467 CE1 PHE A 202 28.116 -11.189 40.099 1.00 50.00 C
ANISOU 1467 CE1 PHE A 202 6478 6290 6228 -127 -60 -80 C
ATOM 1468 CE2 PHE A 202 28.226 -12.655 41.970 1.00 51.86 C
ANISOU 1468 CE2 PHE A 202 6714 6438 6554 -183 43 -55 C
ATOM 1469 CZ PHE A 202 28.842 -11.785 41.100 1.00 49.04 C
ANISOU 1469 CZ PHE A 202 6375 6084 6176 -148 -16 -24 C
ATOM 1470 N LEU A 203 24.123 -15.264 38.864 1.00 44.67 N
ANISOU 1470 N LEU A 203 5587 5924 5460 -510 251 -558 N
ATOM 1471 CA LEU A 203 24.547 -16.527 38.260 1.00 46.20 C
ANISOU 1471 CA LEU A 203 5824 6025 5704 -623 382 -609 C
ATOM 1472 C LEU A 203 24.284 -16.544 36.763 1.00 48.64 C
ANISOU 1472 C LEU A 203 6081 6458 5943 -664 378 -706 C
ATOM 1473 O LEU A 203 25.133 -17.010 36.007 1.00 46.97 O
ANISOU 1473 O LEU A 203 5921 6156 5769 -684 433 -695 O
ATOM 1474 CB LEU A 203 23.832 -17.724 38.913 1.00 48.29 C
ANISOU 1474 CB LEU A 203 6094 6265 5988 -759 510 -696 C
ATOM 1475 CG LEU A 203 24.722 -18.822 39.519 1.00 55.41 C
ANISOU 1475 CG LEU A 203 7118 6942 6996 -798 652 -636 C
ATOM 1476 CD1 LEU A 203 25.548 -19.556 38.440 1.00 56.85 C
ANISOU 1476 CD1 LEU A 203 7358 7036 7206 -862 758 -682 C
ATOM 1477 CD2 LEU A 203 25.606 -18.281 40.662 1.00 57.43 C
ANISOU 1477 CD2 LEU A 203 7430 7079 7313 -658 598 -461 C
ATOM 1478 N ILE A 204 23.106 -16.038 36.343 1.00 45.35 N
ANISOU 1478 N ILE A 204 5554 6266 5411 -666 312 -801 N
ATOM 1479 CA ILE A 204 22.697 -15.928 34.945 1.00 44.91 C
ANISOU 1479 CA ILE A 204 5422 6389 5254 -688 291 -898 C
ATOM 1480 C ILE A 204 23.718 -15.060 34.206 1.00 48.13 C
ANISOU 1480 C ILE A 204 5877 6747 5663 -559 213 -785 C
ATOM 1481 O ILE A 204 24.224 -15.478 33.158 1.00 48.84 O
ANISOU 1481 O ILE A 204 5980 6828 5749 -601 256 -817 O
ATOM 1482 CB ILE A 204 21.251 -15.364 34.843 1.00 48.45 C
ANISOU 1482 CB ILE A 204 5729 7117 5562 -670 219 -994 C
ATOM 1483 CG1 ILE A 204 20.205 -16.453 35.190 1.00 48.99 C
ANISOU 1483 CG1 ILE A 204 5728 7279 5608 -859 325 -1155 C
ATOM 1484 CG2 ILE A 204 20.985 -14.756 33.451 1.00 50.44 C
ANISOU 1484 CG2 ILE A 204 5901 7579 5684 -600 145 -1032 C
ATOM 1485 CD1 ILE A 204 18.753 -15.966 35.326 1.00 45.25 C
ANISOU 1485 CD1 ILE A 204 5100 7094 5000 -845 261 -1246 C
ATOM 1486 N VAL A 205 24.039 -13.874 34.777 1.00 42.94 N
ANISOU 1486 N VAL A 205 5254 6048 5012 -415 111 -657 N
ATOM 1487 CA VAL A 205 24.990 -12.894 34.234 1.00 42.20 C
ANISOU 1487 CA VAL A 205 5221 5896 4919 -300 42 -541 C
ATOM 1488 C VAL A 205 26.400 -13.520 34.122 1.00 46.91 C
ANISOU 1488 C VAL A 205 5899 6299 5623 -343 111 -476 C
ATOM 1489 O VAL A 205 27.021 -13.393 33.070 1.00 47.60 O
ANISOU 1489 O VAL A 205 6001 6391 5692 -329 111 -458 O
ATOM 1490 CB VAL A 205 24.980 -11.585 35.070 1.00 44.94 C
ANISOU 1490 CB VAL A 205 5605 6213 5255 -167 -56 -435 C
ATOM 1491 CG1 VAL A 205 26.131 -10.671 34.688 1.00 44.36 C
ANISOU 1491 CG1 VAL A 205 5619 6036 5201 -86 -100 -315 C
ATOM 1492 CG2 VAL A 205 23.653 -10.851 34.907 1.00 45.26 C
ANISOU 1492 CG2 VAL A 205 5566 6463 5167 -83 -124 -489 C
ATOM 1493 N ILE A 206 26.867 -14.226 35.175 1.00 43.56 N
ANISOU 1493 N ILE A 206 5524 5727 5300 -387 176 -440 N
ATOM 1494 CA ILE A 206 28.163 -14.921 35.227 1.00 43.46 C
ANISOU 1494 CA ILE A 206 5582 5550 5383 -405 252 -373 C
ATOM 1495 C ILE A 206 28.247 -15.992 34.116 1.00 47.70 C
ANISOU 1495 C ILE A 206 6119 6089 5915 -495 356 -468 C
ATOM 1496 O ILE A 206 29.267 -16.067 33.432 1.00 48.36 O
ANISOU 1496 O ILE A 206 6235 6118 6021 -472 375 -422 O
ATOM 1497 CB ILE A 206 28.387 -15.532 36.653 1.00 46.59 C
ANISOU 1497 CB ILE A 206 6021 5820 5862 -416 309 -322 C
ATOM 1498 CG1 ILE A 206 28.867 -14.465 37.642 1.00 45.99 C
ANISOU 1498 CG1 ILE A 206 5961 5714 5801 -322 212 -205 C
ATOM 1499 CG2 ILE A 206 29.332 -16.769 36.666 1.00 47.51 C
ANISOU 1499 CG2 ILE A 206 6204 5789 6059 -448 439 -294 C
ATOM 1500 CD1 ILE A 206 28.573 -14.821 39.143 1.00 54.38 C
ANISOU 1500 CD1 ILE A 206 7035 6725 6903 -325 238 -179 C
ATOM 1501 N VAL A 207 27.191 -16.810 33.951 1.00 43.85 N
ANISOU 1501 N VAL A 207 5594 5672 5396 -606 428 -608 N
ATOM 1502 CA VAL A 207 27.126 -17.892 32.960 1.00 44.75 C
ANISOU 1502 CA VAL A 207 5715 5790 5499 -720 542 -730 C
ATOM 1503 C VAL A 207 27.174 -17.301 31.535 1.00 48.36 C
ANISOU 1503 C VAL A 207 6117 6393 5864 -692 478 -764 C
ATOM 1504 O VAL A 207 28.010 -17.725 30.733 1.00 49.21 O
ANISOU 1504 O VAL A 207 6266 6438 5994 -702 534 -760 O
ATOM 1505 CB VAL A 207 25.879 -18.811 33.179 1.00 49.51 C
ANISOU 1505 CB VAL A 207 6284 6456 6073 -874 635 -889 C
ATOM 1506 CG1 VAL A 207 25.610 -19.706 31.967 1.00 50.39 C
ANISOU 1506 CG1 VAL A 207 6380 6629 6135 -1011 735 -1051 C
ATOM 1507 CG2 VAL A 207 26.041 -19.657 34.439 1.00 49.19 C
ANISOU 1507 CG2 VAL A 207 6334 6224 6132 -911 744 -848 C
ATOM 1508 N CYS A 208 26.297 -16.322 31.244 1.00 43.78 N
ANISOU 1508 N CYS A 208 5448 6010 5176 -639 364 -787 N
ATOM 1509 CA CYS A 208 26.197 -15.645 29.950 1.00 43.66 C
ANISOU 1509 CA CYS A 208 5378 6161 5051 -587 296 -806 C
ATOM 1510 C CYS A 208 27.527 -14.992 29.567 1.00 46.07 C
ANISOU 1510 C CYS A 208 5755 6353 5397 -486 259 -661 C
ATOM 1511 O CYS A 208 27.953 -15.151 28.419 1.00 46.50 O
ANISOU 1511 O CYS A 208 5806 6449 5413 -498 282 -686 O
ATOM 1512 CB CYS A 208 25.064 -14.625 29.952 1.00 44.08 C
ANISOU 1512 CB CYS A 208 5339 6428 4981 -504 183 -821 C
ATOM 1513 SG CYS A 208 23.409 -15.344 29.813 1.00 49.13 S
ANISOU 1513 SG CYS A 208 5838 7320 5509 -635 220 -1031 S
ATOM 1514 N TYR A 209 28.185 -14.291 30.527 1.00 40.54 N
ANISOU 1514 N TYR A 209 5115 5521 4767 -402 208 -521 N
ATOM 1515 CA TYR A 209 29.481 -13.637 30.324 1.00 39.70 C
ANISOU 1515 CA TYR A 209 5072 5313 4700 -330 178 -387 C
ATOM 1516 C TYR A 209 30.563 -14.665 29.975 1.00 44.99 C
ANISOU 1516 C TYR A 209 5781 5866 5445 -384 282 -385 C
ATOM 1517 O TYR A 209 31.297 -14.460 29.010 1.00 45.13 O
ANISOU 1517 O TYR A 209 5810 5898 5441 -363 283 -353 O
ATOM 1518 CB TYR A 209 29.896 -12.813 31.555 1.00 39.79 C
ANISOU 1518 CB TYR A 209 5130 5222 4766 -262 117 -267 C
ATOM 1519 CG TYR A 209 31.300 -12.255 31.450 1.00 41.17 C
ANISOU 1519 CG TYR A 209 5361 5298 4983 -223 102 -145 C
ATOM 1520 CD1 TYR A 209 31.574 -11.138 30.661 1.00 42.29 C
ANISOU 1520 CD1 TYR A 209 5526 5483 5059 -165 42 -87 C
ATOM 1521 CD2 TYR A 209 32.364 -12.860 32.119 1.00 42.05 C
ANISOU 1521 CD2 TYR A 209 5500 5286 5190 -244 156 -86 C
ATOM 1522 CE1 TYR A 209 32.871 -10.638 30.540 1.00 40.76 C
ANISOU 1522 CE1 TYR A 209 5380 5210 4898 -156 40 14 C
ATOM 1523 CE2 TYR A 209 33.666 -12.381 31.987 1.00 42.75 C
ANISOU 1523 CE2 TYR A 209 5617 5323 5304 -221 145 14 C
ATOM 1524 CZ TYR A 209 33.912 -11.264 31.205 1.00 49.85 C
ANISOU 1524 CZ TYR A 209 6536 6264 6141 -190 88 58 C
ATOM 1525 OH TYR A 209 35.192 -10.784 31.101 1.00 56.26 O
ANISOU 1525 OH TYR A 209 7371 7032 6973 -192 86 149 O
ATOM 1526 N THR A 210 30.656 -15.761 30.759 1.00 42.39 N
ANISOU 1526 N THR A 210 5482 5425 5200 -443 376 -412 N
ATOM 1527 CA THR A 210 31.610 -16.861 30.574 1.00 42.49 C
ANISOU 1527 CA THR A 210 5547 5311 5284 -472 496 -407 C
ATOM 1528 C THR A 210 31.440 -17.511 29.181 1.00 47.45 C
ANISOU 1528 C THR A 210 6162 6009 5859 -542 566 -528 C
ATOM 1529 O THR A 210 32.443 -17.831 28.537 1.00 48.15 O
ANISOU 1529 O THR A 210 6282 6044 5969 -522 617 -496 O
ATOM 1530 CB THR A 210 31.438 -17.880 31.716 1.00 48.81 C
ANISOU 1530 CB THR A 210 6396 5986 6165 -511 594 -419 C
ATOM 1531 OG1 THR A 210 31.651 -17.197 32.951 1.00 47.40 O
ANISOU 1531 OG1 THR A 210 6218 5770 6020 -441 519 -308 O
ATOM 1532 CG2 THR A 210 32.400 -19.073 31.619 1.00 45.97 C
ANISOU 1532 CG2 THR A 210 6113 5478 5877 -510 735 -398 C
ATOM 1533 N LEU A 211 30.187 -17.681 28.715 1.00 44.17 N
ANISOU 1533 N LEU A 211 5689 5731 5363 -623 565 -670 N
ATOM 1534 CA LEU A 211 29.897 -18.281 27.414 1.00 44.61 C
ANISOU 1534 CA LEU A 211 5716 5886 5346 -708 628 -809 C
ATOM 1535 C LEU A 211 30.295 -17.354 26.253 1.00 48.45 C
ANISOU 1535 C LEU A 211 6164 6498 5748 -632 542 -763 C
ATOM 1536 O LEU A 211 30.840 -17.838 25.250 1.00 48.43 O
ANISOU 1536 O LEU A 211 6175 6500 5727 -660 605 -807 O
ATOM 1537 CB LEU A 211 28.423 -18.691 27.314 1.00 45.45 C
ANISOU 1537 CB LEU A 211 5751 6144 5374 -827 647 -982 C
ATOM 1538 CG LEU A 211 28.026 -19.954 28.093 1.00 50.15 C
ANISOU 1538 CG LEU A 211 6403 6611 6042 -957 788 -1075 C
ATOM 1539 CD1 LEU A 211 26.509 -20.098 28.173 1.00 50.93 C
ANISOU 1539 CD1 LEU A 211 6405 6894 6051 -1077 783 -1234 C
ATOM 1540 CD2 LEU A 211 28.631 -21.202 27.480 1.00 51.73 C
ANISOU 1540 CD2 LEU A 211 6691 6677 6287 -1043 953 -1154 C
ATOM 1541 N ILE A 212 30.067 -16.029 26.407 1.00 44.75 N
ANISOU 1541 N ILE A 212 5661 6115 5225 -531 409 -670 N
ATOM 1542 CA ILE A 212 30.452 -15.013 25.418 1.00 44.78 C
ANISOU 1542 CA ILE A 212 5651 6216 5146 -444 332 -598 C
ATOM 1543 C ILE A 212 31.995 -14.875 25.395 1.00 48.04 C
ANISOU 1543 C ILE A 212 6134 6478 5640 -401 355 -469 C
ATOM 1544 O ILE A 212 32.572 -14.740 24.314 1.00 47.98 O
ANISOU 1544 O ILE A 212 6126 6518 5586 -386 366 -457 O
ATOM 1545 CB ILE A 212 29.726 -13.659 25.678 1.00 47.75 C
ANISOU 1545 CB ILE A 212 6000 6699 5442 -340 206 -532 C
ATOM 1546 CG1 ILE A 212 28.236 -13.773 25.287 1.00 49.23 C
ANISOU 1546 CG1 ILE A 212 6086 7115 5505 -365 181 -669 C
ATOM 1547 CG2 ILE A 212 30.408 -12.475 24.936 1.00 47.62 C
ANISOU 1547 CG2 ILE A 212 6021 6705 5369 -234 142 -406 C
ATOM 1548 CD1 ILE A 212 27.314 -12.818 26.005 1.00 58.98 C
ANISOU 1548 CD1 ILE A 212 7293 8428 6689 -272 86 -628 C
ATOM 1549 N THR A 213 32.649 -14.952 26.577 1.00 44.12 N
ANISOU 1549 N THR A 213 5687 5823 5255 -382 365 -377 N
ATOM 1550 CA THR A 213 34.110 -14.859 26.727 1.00 43.58 C
ANISOU 1550 CA THR A 213 5661 5640 5256 -344 387 -258 C
ATOM 1551 C THR A 213 34.756 -16.080 26.090 1.00 47.86 C
ANISOU 1551 C THR A 213 6220 6133 5832 -384 509 -314 C
ATOM 1552 O THR A 213 35.716 -15.903 25.349 1.00 48.25 O
ANISOU 1552 O THR A 213 6273 6191 5870 -356 522 -261 O
ATOM 1553 CB THR A 213 34.502 -14.667 28.207 1.00 50.98 C
ANISOU 1553 CB THR A 213 6626 6463 6282 -314 365 -163 C
ATOM 1554 OG1 THR A 213 33.770 -13.557 28.714 1.00 49.75 O
ANISOU 1554 OG1 THR A 213 6463 6353 6085 -280 261 -134 O
ATOM 1555 CG2 THR A 213 35.989 -14.398 28.404 1.00 46.84 C
ANISOU 1555 CG2 THR A 213 6120 5872 5806 -275 370 -41 C
ATOM 1556 N LYS A 214 34.205 -17.299 26.321 1.00 45.25 N
ANISOU 1556 N LYS A 214 5905 5753 5534 -453 609 -427 N
ATOM 1557 CA LYS A 214 34.694 -18.537 25.690 1.00 46.46 C
ANISOU 1557 CA LYS A 214 6099 5841 5713 -494 748 -501 C
ATOM 1558 C LYS A 214 34.645 -18.415 24.144 1.00 50.96 C
ANISOU 1558 C LYS A 214 6633 6547 6184 -523 748 -580 C
ATOM 1559 O LYS A 214 35.602 -18.790 23.468 1.00 51.59 O
ANISOU 1559 O LYS A 214 6735 6592 6273 -503 816 -567 O
ATOM 1560 CB LYS A 214 33.882 -19.764 26.157 1.00 49.91 C
ANISOU 1560 CB LYS A 214 6578 6197 6187 -587 864 -626 C
ATOM 1561 CG LYS A 214 34.413 -20.390 27.436 1.00 71.11 C
ANISOU 1561 CG LYS A 214 9335 8700 8982 -541 937 -539 C
ATOM 1562 CD LYS A 214 33.602 -21.608 27.875 1.00 86.02 C
ANISOU 1562 CD LYS A 214 11290 10489 10905 -641 1071 -658 C
ATOM 1563 CE LYS A 214 34.146 -22.210 29.155 1.00101.53 C
ANISOU 1563 CE LYS A 214 13337 12274 12967 -571 1151 -552 C
ATOM 1564 NZ LYS A 214 33.257 -23.273 29.707 1.00112.80 N
ANISOU 1564 NZ LYS A 214 14844 13591 14425 -675 1286 -655 N
ATOM 1565 N GLU A 215 33.542 -17.847 23.613 1.00 46.55 N
ANISOU 1565 N GLU A 215 6010 6159 5521 -554 667 -654 N
ATOM 1566 CA GLU A 215 33.312 -17.607 22.196 1.00 46.97 C
ANISOU 1566 CA GLU A 215 6013 6382 5453 -569 649 -725 C
ATOM 1567 C GLU A 215 34.336 -16.615 21.630 1.00 50.49 C
ANISOU 1567 C GLU A 215 6462 6848 5873 -473 586 -582 C
ATOM 1568 O GLU A 215 34.778 -16.791 20.492 1.00 51.30 O
ANISOU 1568 O GLU A 215 6556 7015 5919 -478 624 -612 O
ATOM 1569 CB GLU A 215 31.866 -17.112 21.953 1.00 48.73 C
ANISOU 1569 CB GLU A 215 6153 6809 5556 -594 568 -818 C
ATOM 1570 CG GLU A 215 31.484 -16.904 20.487 1.00 58.41 C
ANISOU 1570 CG GLU A 215 7310 8253 6630 -603 547 -901 C
ATOM 1571 CD GLU A 215 31.855 -17.986 19.483 1.00 82.28 C
ANISOU 1571 CD GLU A 215 10344 11284 9636 -695 668 -1033 C
ATOM 1572 OE1 GLU A 215 31.830 -19.185 19.847 1.00 79.13 O
ANISOU 1572 OE1 GLU A 215 9990 10765 9310 -801 789 -1142 O
ATOM 1573 OE2 GLU A 215 32.128 -17.631 18.313 1.00 78.22 O
ANISOU 1573 OE2 GLU A 215 9800 10894 9025 -662 650 -1030 O
ATOM 1574 N LEU A 216 34.709 -15.585 22.420 1.00 45.69 N
ANISOU 1574 N LEU A 216 5872 6185 5302 -398 500 -433 N
ATOM 1575 CA LEU A 216 35.721 -14.601 22.029 1.00 44.55 C
ANISOU 1575 CA LEU A 216 5744 6040 5141 -331 452 -294 C
ATOM 1576 C LEU A 216 37.083 -15.292 21.899 1.00 49.36 C
ANISOU 1576 C LEU A 216 6377 6555 5822 -333 543 -255 C
ATOM 1577 O LEU A 216 37.761 -15.110 20.881 1.00 49.92 O
ANISOU 1577 O LEU A 216 6440 6685 5842 -320 560 -231 O
ATOM 1578 CB LEU A 216 35.789 -13.413 23.022 1.00 43.02 C
ANISOU 1578 CB LEU A 216 5577 5791 4976 -278 359 -166 C
ATOM 1579 CG LEU A 216 36.800 -12.284 22.716 1.00 46.73 C
ANISOU 1579 CG LEU A 216 6080 6249 5426 -236 318 -26 C
ATOM 1580 CD1 LEU A 216 36.640 -11.741 21.296 1.00 47.71 C
ANISOU 1580 CD1 LEU A 216 6199 6504 5424 -209 301 -28 C
ATOM 1581 CD2 LEU A 216 36.648 -11.149 23.683 1.00 47.34 C
ANISOU 1581 CD2 LEU A 216 6197 6268 5521 -203 239 66 C
ATOM 1582 N TYR A 217 37.455 -16.109 22.907 1.00 46.01 N
ANISOU 1582 N TYR A 217 5979 5998 5506 -338 606 -246 N
ATOM 1583 CA TYR A 217 38.723 -16.846 22.938 1.00 46.58 C
ANISOU 1583 CA TYR A 217 6070 5987 5643 -309 700 -202 C
ATOM 1584 C TYR A 217 38.785 -17.847 21.785 1.00 50.85 C
ANISOU 1584 C TYR A 217 6619 6552 6148 -341 809 -317 C
ATOM 1585 O TYR A 217 39.836 -17.971 21.157 1.00 51.07 O
ANISOU 1585 O TYR A 217 6644 6591 6171 -306 856 -275 O
ATOM 1586 CB TYR A 217 38.941 -17.542 24.299 1.00 48.25 C
ANISOU 1586 CB TYR A 217 6312 6062 5959 -284 750 -166 C
ATOM 1587 CG TYR A 217 39.158 -16.604 25.477 1.00 50.32 C
ANISOU 1587 CG TYR A 217 6560 6303 6256 -251 654 -48 C
ATOM 1588 CD1 TYR A 217 39.495 -15.263 25.280 1.00 52.49 C
ANISOU 1588 CD1 TYR A 217 6811 6648 6487 -243 553 39 C
ATOM 1589 CD2 TYR A 217 39.057 -17.063 26.787 1.00 50.89 C
ANISOU 1589 CD2 TYR A 217 6653 6282 6401 -231 675 -23 C
ATOM 1590 CE1 TYR A 217 39.687 -14.397 26.354 1.00 52.81 C
ANISOU 1590 CE1 TYR A 217 6848 6662 6554 -230 475 130 C
ATOM 1591 CE2 TYR A 217 39.276 -16.212 27.871 1.00 51.31 C
ANISOU 1591 CE2 TYR A 217 6688 6328 6477 -206 588 75 C
ATOM 1592 CZ TYR A 217 39.585 -14.878 27.649 1.00 60.74 C
ANISOU 1592 CZ TYR A 217 7860 7592 7628 -212 489 143 C
ATOM 1593 OH TYR A 217 39.780 -14.022 28.704 1.00 64.21 O
ANISOU 1593 OH TYR A 217 8292 8021 8085 -205 412 222 O
ATOM 1594 N ARG A 218 37.645 -18.491 21.462 1.00 47.41 N
ANISOU 1594 N ARG A 218 6191 6145 5678 -416 847 -471 N
ATOM 1595 CA ARG A 218 37.521 -19.432 20.349 1.00 48.56 C
ANISOU 1595 CA ARG A 218 6348 6326 5776 -474 953 -614 C
ATOM 1596 C ARG A 218 37.724 -18.711 19.006 1.00 53.40 C
ANISOU 1596 C ARG A 218 6910 7106 6274 -462 899 -611 C
ATOM 1597 O ARG A 218 38.420 -19.238 18.138 1.00 54.75 O
ANISOU 1597 O ARG A 218 7091 7287 6423 -460 981 -646 O
ATOM 1598 CB ARG A 218 36.158 -20.141 20.375 1.00 49.21 C
ANISOU 1598 CB ARG A 218 6435 6430 5832 -587 996 -791 C
ATOM 1599 CG ARG A 218 36.157 -21.418 21.209 1.00 65.30 C
ANISOU 1599 CG ARG A 218 8564 8276 7973 -624 1139 -846 C
ATOM 1600 CD ARG A 218 34.907 -22.255 20.981 1.00 85.63 C
ANISOU 1600 CD ARG A 218 11149 10879 10507 -774 1216 -1053 C
ATOM 1601 NE ARG A 218 33.737 -21.721 21.685 1.00100.02 N
ANISOU 1601 NE ARG A 218 12916 12779 12308 -820 1121 -1073 N
ATOM 1602 CZ ARG A 218 33.333 -22.125 22.885 1.00117.83 C
ANISOU 1602 CZ ARG A 218 15220 14907 14645 -847 1161 -1066 C
ATOM 1603 NH1 ARG A 218 33.996 -23.078 23.532 1.00106.58 N
ANISOU 1603 NH1 ARG A 218 13907 13262 13324 -824 1297 -1031 N
ATOM 1604 NH2 ARG A 218 32.262 -21.582 23.448 1.00107.56 N
ANISOU 1604 NH2 ARG A 218 13856 13702 13311 -884 1069 -1088 N
ATOM 1605 N SER A 219 37.139 -17.498 18.855 1.00 48.43 N
ANISOU 1605 N SER A 219 6232 6602 5566 -443 768 -560 N
ATOM 1606 CA SER A 219 37.250 -16.660 17.656 1.00 47.85 C
ANISOU 1606 CA SER A 219 6121 6689 5371 -413 711 -530 C
ATOM 1607 C SER A 219 38.674 -16.187 17.462 1.00 50.05 C
ANISOU 1607 C SER A 219 6416 6923 5677 -354 716 -386 C
ATOM 1608 O SER A 219 39.134 -16.118 16.318 1.00 50.47 O
ANISOU 1608 O SER A 219 6454 7071 5653 -346 739 -389 O
ATOM 1609 CB SER A 219 36.308 -15.466 17.738 1.00 50.66 C
ANISOU 1609 CB SER A 219 6446 7161 5642 -378 584 -489 C
ATOM 1610 OG SER A 219 34.970 -15.880 17.523 1.00 60.81 O
ANISOU 1610 OG SER A 219 7683 8563 6857 -435 580 -642 O
ATOM 1611 N TYR A 220 39.381 -15.905 18.583 1.00 44.56 N
ANISOU 1611 N TYR A 220 5745 6101 5086 -321 701 -267 N
ATOM 1612 CA TYR A 220 40.780 -15.482 18.609 1.00 43.84 C
ANISOU 1612 CA TYR A 220 5652 5979 5026 -282 709 -134 C
ATOM 1613 C TYR A 220 41.697 -16.581 18.064 1.00 47.36 C
ANISOU 1613 C TYR A 220 6095 6405 5495 -270 831 -176 C
ATOM 1614 O TYR A 220 42.565 -16.259 17.256 1.00 47.82 O
ANISOU 1614 O TYR A 220 6131 6533 5506 -253 846 -122 O
ATOM 1615 CB TYR A 220 41.220 -15.087 20.040 1.00 44.74 C
ANISOU 1615 CB TYR A 220 5776 5989 5236 -260 668 -25 C
ATOM 1616 CG TYR A 220 42.717 -14.864 20.175 1.00 47.46 C
ANISOU 1616 CG TYR A 220 6096 6325 5612 -234 693 89 C
ATOM 1617 CD1 TYR A 220 43.278 -13.611 19.950 1.00 49.51 C
ANISOU 1617 CD1 TYR A 220 6348 6638 5825 -249 632 194 C
ATOM 1618 CD2 TYR A 220 43.574 -15.915 20.497 1.00 48.55 C
ANISOU 1618 CD2 TYR A 220 6220 6412 5815 -193 788 90 C
ATOM 1619 CE1 TYR A 220 44.656 -13.413 20.015 1.00 50.72 C
ANISOU 1619 CE1 TYR A 220 6461 6816 5993 -248 660 284 C
ATOM 1620 CE2 TYR A 220 44.954 -15.732 20.551 1.00 49.90 C
ANISOU 1620 CE2 TYR A 220 6344 6621 5995 -162 811 188 C
ATOM 1621 CZ TYR A 220 45.490 -14.474 20.328 1.00 58.62 C
ANISOU 1621 CZ TYR A 220 7422 7800 7050 -201 743 280 C
ATOM 1622 OH TYR A 220 46.846 -14.269 20.426 1.00 61.62 O
ANISOU 1622 OH TYR A 220 7739 8242 7430 -193 767 367 O
ATOM 1623 N VAL A 221 41.527 -17.860 18.512 1.00 43.84 N
ANISOU 1623 N VAL A 221 5681 5856 5119 -274 930 -265 N
ATOM 1624 CA VAL A 221 42.402 -18.967 18.086 1.00 44.35 C
ANISOU 1624 CA VAL A 221 5766 5875 5210 -240 1065 -301 C
ATOM 1625 C VAL A 221 42.187 -19.271 16.588 1.00 48.88 C
ANISOU 1625 C VAL A 221 6333 6556 5683 -280 1113 -417 C
ATOM 1626 O VAL A 221 43.165 -19.523 15.889 1.00 48.36 O
ANISOU 1626 O VAL A 221 6257 6522 5597 -239 1179 -396 O
ATOM 1627 CB VAL A 221 42.365 -20.255 18.972 1.00 48.13 C
ANISOU 1627 CB VAL A 221 6312 6188 5786 -217 1182 -350 C
ATOM 1628 CG1 VAL A 221 42.446 -19.914 20.458 1.00 46.67 C
ANISOU 1628 CG1 VAL A 221 6126 5923 5684 -174 1126 -235 C
ATOM 1629 CG2 VAL A 221 41.165 -21.144 18.679 1.00 48.57 C
ANISOU 1629 CG2 VAL A 221 6422 6205 5828 -309 1249 -531 C
ATOM 1630 N ARG A 222 40.934 -19.171 16.096 1.00 45.61 N
ANISOU 1630 N ARG A 222 5910 6225 5193 -355 1073 -535 N
ATOM 1631 CA ARG A 222 40.612 -19.378 14.690 1.00 46.55 C
ANISOU 1631 CA ARG A 222 6008 6484 5195 -399 1104 -654 C
ATOM 1632 C ARG A 222 41.270 -18.300 13.813 1.00 50.47 C
ANISOU 1632 C ARG A 222 6458 7118 5602 -355 1034 -542 C
ATOM 1633 O ARG A 222 41.681 -18.603 12.692 1.00 49.73 O
ANISOU 1633 O ARG A 222 6350 7111 5435 -356 1093 -594 O
ATOM 1634 CB ARG A 222 39.100 -19.400 14.481 1.00 48.75 C
ANISOU 1634 CB ARG A 222 6264 6861 5397 -485 1062 -797 C
ATOM 1635 CG ARG A 222 38.470 -20.742 14.820 1.00 64.77 C
ANISOU 1635 CG ARG A 222 8346 8786 7478 -573 1181 -969 C
ATOM 1636 CD ARG A 222 37.035 -20.836 14.327 1.00 78.56 C
ANISOU 1636 CD ARG A 222 10043 10691 9116 -682 1153 -1143 C
ATOM 1637 NE ARG A 222 36.120 -20.123 15.216 1.00 85.85 N
ANISOU 1637 NE ARG A 222 10931 11640 10047 -683 1040 -1098 N
ATOM 1638 CZ ARG A 222 35.209 -19.241 14.818 1.00 96.03 C
ANISOU 1638 CZ ARG A 222 12138 13135 11215 -680 922 -1109 C
ATOM 1639 NH1 ARG A 222 35.066 -18.960 13.525 1.00 75.48 N
ANISOU 1639 NH1 ARG A 222 9475 10740 8464 -678 897 -1161 N
ATOM 1640 NH2 ARG A 222 34.426 -18.641 15.707 1.00 79.69 N
ANISOU 1640 NH2 ARG A 222 10044 11073 9160 -665 831 -1066 N
ATOM 1641 N THR A 223 41.416 -17.058 14.349 1.00 47.43 N
ANISOU 1641 N THR A 223 6058 6740 5223 -319 923 -390 N
ATOM 1642 CA THR A 223 42.075 -15.944 13.656 1.00 47.15 C
ANISOU 1642 CA THR A 223 6001 6803 5111 -287 870 -266 C
ATOM 1643 C THR A 223 43.598 -16.151 13.695 1.00 51.36 C
ANISOU 1643 C THR A 223 6525 7290 5700 -255 938 -178 C
ATOM 1644 O THR A 223 44.258 -15.999 12.662 1.00 51.00 O
ANISOU 1644 O THR A 223 6457 7342 5580 -246 971 -157 O
ATOM 1645 CB THR A 223 41.635 -14.597 14.253 1.00 50.39 C
ANISOU 1645 CB THR A 223 6425 7212 5508 -272 749 -149 C
ATOM 1646 OG1 THR A 223 40.261 -14.426 13.927 1.00 51.16 O
ANISOU 1646 OG1 THR A 223 6514 7405 5520 -279 694 -235 O
ATOM 1647 CG2 THR A 223 42.417 -13.410 13.676 1.00 48.79 C
ANISOU 1647 CG2 THR A 223 6229 7070 5238 -251 716 -6 C
ATOM 1648 N ALA A1001 44.144 -16.502 14.881 1.00 39.47 N
ANISOU 1648 N ALA A1001 5321 4237 5440 -116 -93 -211 N
ATOM 1649 CA ALA A1001 45.573 -16.752 15.067 1.00 40.05 C
ANISOU 1649 CA ALA A1001 5375 4349 5492 -56 -68 -178 C
ATOM 1650 C ALA A1001 46.039 -17.962 14.226 1.00 45.68 C
ANISOU 1650 C ALA A1001 6149 5041 6167 -3 -14 -183 C
ATOM 1651 O ALA A1001 47.140 -17.904 13.680 1.00 46.46 O
ANISOU 1651 O ALA A1001 6216 5200 6235 40 -1 -161 O
ATOM 1652 CB ALA A1001 45.891 -16.964 16.540 1.00 40.57 C
ANISOU 1652 CB ALA A1001 5424 4434 5557 -8 -65 -162 C
ATOM 1653 N ASP A1002 45.203 -19.024 14.089 1.00 42.72 N
ANISOU 1653 N ASP A1002 5861 4580 5792 -20 33 -224 N
ATOM 1654 CA ASP A1002 45.518 -20.198 13.256 1.00 44.51 C
ANISOU 1654 CA ASP A1002 6174 4757 5983 13 108 -248 C
ATOM 1655 C ASP A1002 45.657 -19.775 11.782 1.00 49.67 C
ANISOU 1655 C ASP A1002 6791 5472 6609 -14 76 -272 C
ATOM 1656 O ASP A1002 46.605 -20.167 11.096 1.00 50.80 O
ANISOU 1656 O ASP A1002 6954 5635 6714 49 110 -255 O
ATOM 1657 CB ASP A1002 44.438 -21.297 13.379 1.00 47.62 C
ANISOU 1657 CB ASP A1002 6675 5031 6388 -51 189 -321 C
ATOM 1658 CG ASP A1002 44.452 -22.155 14.639 1.00 66.77 C
ANISOU 1658 CG ASP A1002 9201 7351 8819 9 282 -284 C
ATOM 1659 OD1 ASP A1002 45.490 -22.170 15.345 1.00 70.16 O
ANISOU 1659 OD1 ASP A1002 9625 7818 9215 149 289 -198 O
ATOM 1660 OD2 ASP A1002 43.430 -22.838 14.906 1.00 72.06 O
ANISOU 1660 OD2 ASP A1002 9952 7915 9513 -79 360 -347 O
ATOM 1661 N LEU A1003 44.717 -18.940 11.330 1.00 44.67 N
ANISOU 1661 N LEU A1003 6106 4884 5982 -84 14 -302 N
ATOM 1662 CA LEU A1003 44.634 -18.383 9.990 1.00 44.68 C
ANISOU 1662 CA LEU A1003 6076 4961 5938 -86 -17 -313 C
ATOM 1663 C LEU A1003 45.815 -17.451 9.711 1.00 48.41 C
ANISOU 1663 C LEU A1003 6510 5479 6406 -38 -23 -231 C
ATOM 1664 O LEU A1003 46.404 -17.516 8.631 1.00 49.37 O
ANISOU 1664 O LEU A1003 6638 5638 6483 -5 -2 -221 O
ATOM 1665 CB LEU A1003 43.293 -17.636 9.874 1.00 44.75 C
ANISOU 1665 CB LEU A1003 6039 5029 5936 -127 -75 -347 C
ATOM 1666 CG LEU A1003 42.791 -17.206 8.513 1.00 50.42 C
ANISOU 1666 CG LEU A1003 6728 5857 6572 -102 -106 -374 C
ATOM 1667 CD1 LEU A1003 42.745 -18.366 7.539 1.00 51.70 C
ANISOU 1667 CD1 LEU A1003 6917 6044 6681 -128 -72 -472 C
ATOM 1668 CD2 LEU A1003 41.409 -16.621 8.639 1.00 53.36 C
ANISOU 1668 CD2 LEU A1003 7043 6318 6915 -110 -159 -410 C
ATOM 1669 N GLU A1004 46.178 -16.617 10.690 1.00 43.50 N
ANISOU 1669 N GLU A1004 5846 4856 5828 -48 -38 -185 N
ATOM 1670 CA GLU A1004 47.289 -15.679 10.592 1.00 42.90 C
ANISOU 1670 CA GLU A1004 5723 4822 5756 -48 -21 -137 C
ATOM 1671 C GLU A1004 48.630 -16.422 10.602 1.00 46.51 C
ANISOU 1671 C GLU A1004 6153 5330 6188 5 18 -129 C
ATOM 1672 O GLU A1004 49.576 -15.942 9.991 1.00 45.95 O
ANISOU 1672 O GLU A1004 6042 5319 6098 2 48 -108 O
ATOM 1673 CB GLU A1004 47.207 -14.643 11.723 1.00 44.18 C
ANISOU 1673 CB GLU A1004 5847 4974 5967 -98 -37 -127 C
ATOM 1674 CG GLU A1004 47.864 -13.306 11.401 1.00 59.26 C
ANISOU 1674 CG GLU A1004 7735 6893 7886 -149 6 -101 C
ATOM 1675 CD GLU A1004 47.155 -12.319 10.485 1.00 75.57 C
ANISOU 1675 CD GLU A1004 9870 8908 9936 -145 31 -62 C
ATOM 1676 OE1 GLU A1004 47.363 -11.102 10.686 1.00 79.22 O
ANISOU 1676 OE1 GLU A1004 10354 9322 10425 -197 83 -44 O
ATOM 1677 OE2 GLU A1004 46.451 -12.744 9.539 1.00 64.42 O
ANISOU 1677 OE2 GLU A1004 8494 7512 8471 -83 12 -53 O
ATOM 1678 N ASP A1005 48.699 -17.618 11.237 1.00 43.51 N
ANISOU 1678 N ASP A1005 5805 4930 5796 66 32 -141 N
ATOM 1679 CA ASP A1005 49.899 -18.473 11.245 1.00 43.30 C
ANISOU 1679 CA ASP A1005 5770 4961 5719 170 79 -123 C
ATOM 1680 C ASP A1005 50.193 -18.974 9.825 1.00 45.51 C
ANISOU 1680 C ASP A1005 6097 5239 5957 201 116 -130 C
ATOM 1681 O ASP A1005 51.356 -19.134 9.456 1.00 45.70 O
ANISOU 1681 O ASP A1005 6078 5350 5936 269 149 -108 O
ATOM 1682 CB ASP A1005 49.725 -19.668 12.208 1.00 45.39 C
ANISOU 1682 CB ASP A1005 6111 5166 5969 260 116 -118 C
ATOM 1683 CG ASP A1005 49.886 -19.371 13.695 1.00 57.37 C
ANISOU 1683 CG ASP A1005 7566 6742 7489 293 91 -99 C
ATOM 1684 OD1 ASP A1005 50.252 -18.221 14.042 1.00 58.46 O
ANISOU 1684 OD1 ASP A1005 7587 6981 7646 228 42 -108 O
ATOM 1685 OD2 ASP A1005 49.623 -20.281 14.514 1.00 63.29 O
ANISOU 1685 OD2 ASP A1005 8397 7432 8219 379 134 -79 O
ATOM 1686 N ASN A1006 49.122 -19.211 9.038 1.00 41.01 N
ANISOU 1686 N ASN A1006 5600 4594 5389 151 110 -171 N
ATOM 1687 CA ASN A1006 49.164 -19.629 7.638 1.00 40.93 C
ANISOU 1687 CA ASN A1006 5633 4591 5327 168 137 -198 C
ATOM 1688 C ASN A1006 49.779 -18.522 6.777 1.00 43.16 C
ANISOU 1688 C ASN A1006 5848 4961 5588 159 127 -154 C
ATOM 1689 O ASN A1006 50.610 -18.806 5.916 1.00 42.91 O
ANISOU 1689 O ASN A1006 5817 4978 5508 213 167 -141 O
ATOM 1690 CB ASN A1006 47.761 -19.967 7.137 1.00 42.38 C
ANISOU 1690 CB ASN A1006 5871 4728 5503 99 121 -280 C
ATOM 1691 CG ASN A1006 47.218 -21.288 7.593 1.00 59.32 C
ANISOU 1691 CG ASN A1006 8116 6765 7659 82 182 -350 C
ATOM 1692 OD1 ASN A1006 47.767 -22.339 7.302 1.00 47.84 O
ANISOU 1692 OD1 ASN A1006 6749 5255 6173 137 263 -369 O
ATOM 1693 ND2 ASN A1006 46.055 -21.271 8.205 1.00 60.08 N
ANISOU 1693 ND2 ASN A1006 8213 6820 7794 0 162 -396 N
ATOM 1694 N TRP A1007 49.402 -17.262 7.045 1.00 38.51 N
ANISOU 1694 N TRP A1007 5217 4380 5035 97 93 -126 N
ATOM 1695 CA TRP A1007 49.925 -16.100 6.343 1.00 38.50 C
ANISOU 1695 CA TRP A1007 5185 4421 5021 77 121 -76 C
ATOM 1696 C TRP A1007 51.402 -15.878 6.661 1.00 43.84 C
ANISOU 1696 C TRP A1007 5782 5169 5706 69 170 -56 C
ATOM 1697 O TRP A1007 52.168 -15.563 5.750 1.00 43.57 O
ANISOU 1697 O TRP A1007 5733 5185 5638 73 225 -30 O
ATOM 1698 CB TRP A1007 49.095 -14.864 6.670 1.00 37.09 C
ANISOU 1698 CB TRP A1007 5017 4200 4876 25 102 -53 C
ATOM 1699 CG TRP A1007 47.792 -14.863 5.936 1.00 38.20 C
ANISOU 1699 CG TRP A1007 5207 4342 4965 62 65 -66 C
ATOM 1700 CD1 TRP A1007 46.553 -15.071 6.463 1.00 40.70 C
ANISOU 1700 CD1 TRP A1007 5527 4647 5292 50 6 -111 C
ATOM 1701 CD2 TRP A1007 47.611 -14.727 4.516 1.00 38.83 C
ANISOU 1701 CD2 TRP A1007 5321 4478 4955 127 81 -49 C
ATOM 1702 NE1 TRP A1007 45.602 -15.035 5.467 1.00 40.75 N
ANISOU 1702 NE1 TRP A1007 5547 4722 5214 100 -20 -134 N
ATOM 1703 CE2 TRP A1007 46.226 -14.838 4.259 1.00 43.04 C
ANISOU 1703 CE2 TRP A1007 5860 5058 5436 158 22 -94 C
ATOM 1704 CE3 TRP A1007 48.486 -14.518 3.434 1.00 40.48 C
ANISOU 1704 CE3 TRP A1007 5548 4723 5111 169 144 -3 C
ATOM 1705 CZ2 TRP A1007 45.693 -14.717 2.971 1.00 43.14 C
ANISOU 1705 CZ2 TRP A1007 5886 5174 5331 245 14 -97 C
ATOM 1706 CZ3 TRP A1007 47.958 -14.432 2.156 1.00 42.76 C
ANISOU 1706 CZ3 TRP A1007 5872 5083 5291 255 143 6 C
ATOM 1707 CH2 TRP A1007 46.578 -14.532 1.933 1.00 43.65 C
ANISOU 1707 CH2 TRP A1007 5982 5263 5340 299 74 -43 C
ATOM 1708 N GLU A1008 51.811 -16.098 7.933 1.00 41.73 N
ANISOU 1708 N GLU A1008 5453 4934 5469 65 153 -74 N
ATOM 1709 CA GLU A1008 53.206 -16.001 8.369 1.00 42.99 C
ANISOU 1709 CA GLU A1008 5496 5227 5612 69 186 -81 C
ATOM 1710 C GLU A1008 54.043 -17.074 7.650 1.00 47.59 C
ANISOU 1710 C GLU A1008 6076 5883 6122 187 221 -72 C
ATOM 1711 O GLU A1008 55.122 -16.754 7.146 1.00 47.99 O
ANISOU 1711 O GLU A1008 6044 6050 6142 178 271 -70 O
ATOM 1712 CB GLU A1008 53.366 -16.131 9.900 1.00 44.64 C
ANISOU 1712 CB GLU A1008 5632 5494 5836 79 149 -109 C
ATOM 1713 CG GLU A1008 52.420 -15.311 10.767 1.00 58.98 C
ANISOU 1713 CG GLU A1008 7467 7226 7718 -14 110 -123 C
ATOM 1714 CD GLU A1008 52.558 -13.800 10.836 1.00 90.27 C
ANISOU 1714 CD GLU A1008 11390 11183 11727 -160 145 -143 C
ATOM 1715 OE1 GLU A1008 52.588 -13.139 9.771 1.00 77.92 O
ANISOU 1715 OE1 GLU A1008 9872 9569 10165 -208 204 -117 O
ATOM 1716 OE2 GLU A1008 52.512 -13.269 11.970 1.00 93.75 O
ANISOU 1716 OE2 GLU A1008 11776 11648 12197 -222 126 -185 O
ATOM 1717 N THR A1009 53.515 -18.322 7.555 1.00 43.51 N
ANISOU 1717 N THR A1009 5662 5289 5580 287 213 -74 N
ATOM 1718 CA THR A1009 54.162 -19.444 6.856 1.00 44.50 C
ANISOU 1718 CA THR A1009 5830 5443 5633 415 263 -68 C
ATOM 1719 C THR A1009 54.423 -19.075 5.396 1.00 50.31 C
ANISOU 1719 C THR A1009 6572 6203 6339 389 294 -60 C
ATOM 1720 O THR A1009 55.538 -19.252 4.907 1.00 51.57 O
ANISOU 1720 O THR A1009 6674 6477 6445 452 341 -45 O
ATOM 1721 CB THR A1009 53.283 -20.703 6.946 1.00 50.82 C
ANISOU 1721 CB THR A1009 6783 6098 6428 476 279 -92 C
ATOM 1722 OG1 THR A1009 53.123 -21.068 8.310 1.00 51.65 O
ANISOU 1722 OG1 THR A1009 6896 6177 6550 518 273 -82 O
ATOM 1723 CG2 THR A1009 53.839 -21.875 6.148 1.00 48.45 C
ANISOU 1723 CG2 THR A1009 6569 5787 6054 604 355 -95 C
ATOM 1724 N LEU A1010 53.392 -18.548 4.716 1.00 46.60 N
ANISOU 1724 N LEU A1010 6167 5650 5890 312 270 -68 N
ATOM 1725 CA LEU A1010 53.451 -18.144 3.320 1.00 47.28 C
ANISOU 1725 CA LEU A1010 6276 5758 5929 308 299 -51 C
ATOM 1726 C LEU A1010 54.457 -17.010 3.109 1.00 50.64 C
ANISOU 1726 C LEU A1010 6612 6269 6361 253 355 -5 C
ATOM 1727 O LEU A1010 55.229 -17.068 2.154 1.00 51.55 O
ANISOU 1727 O LEU A1010 6713 6452 6420 292 413 14 O
ATOM 1728 CB LEU A1010 52.052 -17.731 2.827 1.00 47.44 C
ANISOU 1728 CB LEU A1010 6365 5711 5947 267 255 -65 C
ATOM 1729 CG LEU A1010 51.932 -17.420 1.335 1.00 54.37 C
ANISOU 1729 CG LEU A1010 7282 6632 6745 304 280 -47 C
ATOM 1730 CD1 LEU A1010 50.813 -18.207 0.703 1.00 55.36 C
ANISOU 1730 CD1 LEU A1010 7470 6754 6810 332 237 -127 C
ATOM 1731 CD2 LEU A1010 51.755 -15.924 1.093 1.00 58.09 C
ANISOU 1731 CD2 LEU A1010 7753 7097 7220 268 305 25 C
ATOM 1732 N ASN A1011 54.448 -15.990 3.981 1.00 46.45 N
ANISOU 1732 N ASN A1011 6025 5728 5894 151 354 0 N
ATOM 1733 CA ASN A1011 55.331 -14.832 3.833 1.00 46.47 C
ANISOU 1733 CA ASN A1011 5957 5788 5913 52 438 17 C
ATOM 1734 C ASN A1011 56.785 -15.169 4.192 1.00 51.13 C
ANISOU 1734 C ASN A1011 6397 6552 6477 58 474 -17 C
ATOM 1735 O ASN A1011 57.690 -14.674 3.515 1.00 52.71 O
ANISOU 1735 O ASN A1011 6541 6833 6655 6 565 -12 O
ATOM 1736 CB ASN A1011 54.802 -13.635 4.618 1.00 44.17 C
ANISOU 1736 CB ASN A1011 5675 5414 5695 -72 445 14 C
ATOM 1737 CG ASN A1011 53.538 -13.062 3.997 1.00 61.00 C
ANISOU 1737 CG ASN A1011 7944 7412 7821 -52 440 66 C
ATOM 1738 OD1 ASN A1011 53.495 -12.694 2.814 1.00 60.47 O
ANISOU 1738 OD1 ASN A1011 7950 7324 7701 -14 503 121 O
ATOM 1739 ND2 ASN A1011 52.462 -13.022 4.758 1.00 49.07 N
ANISOU 1739 ND2 ASN A1011 6466 5830 6347 -54 366 53 N
ATOM 1740 N ASP A1012 57.003 -16.072 5.176 1.00 46.34 N
ANISOU 1740 N ASP A1012 5730 6019 5857 142 414 -49 N
ATOM 1741 CA ASP A1012 58.329 -16.540 5.589 1.00 46.50 C
ANISOU 1741 CA ASP A1012 5595 6254 5817 208 435 -81 C
ATOM 1742 C ASP A1012 59.003 -17.338 4.470 1.00 50.15 C
ANISOU 1742 C ASP A1012 6073 6783 6198 334 483 -53 C
ATOM 1743 O ASP A1012 60.193 -17.147 4.207 1.00 51.26 O
ANISOU 1743 O ASP A1012 6074 7111 6290 328 543 -72 O
ATOM 1744 CB ASP A1012 58.239 -17.397 6.867 1.00 48.41 C
ANISOU 1744 CB ASP A1012 5810 6544 6037 326 369 -96 C
ATOM 1745 CG ASP A1012 58.077 -16.626 8.175 1.00 66.93 C
ANISOU 1745 CG ASP A1012 8065 8933 8432 218 329 -144 C
ATOM 1746 OD1 ASP A1012 58.205 -15.373 8.156 1.00 69.32 O
ANISOU 1746 OD1 ASP A1012 8309 9240 8789 31 366 -183 O
ATOM 1747 OD2 ASP A1012 57.828 -17.275 9.220 1.00 74.83 O
ANISOU 1747 OD2 ASP A1012 9066 9954 9411 323 277 -144 O
ATOM 1748 N ASN A1013 58.238 -18.220 3.807 1.00 45.25 N
ANISOU 1748 N ASN A1013 5614 6021 5558 435 465 -24 N
ATOM 1749 CA ASN A1013 58.721 -19.058 2.715 1.00 45.44 C
ANISOU 1749 CA ASN A1013 5686 6077 5502 560 512 -7 C
ATOM 1750 C ASN A1013 59.006 -18.235 1.457 1.00 48.39 C
ANISOU 1750 C ASN A1013 6054 6470 5863 480 575 17 C
ATOM 1751 O ASN A1013 59.890 -18.606 0.676 1.00 48.41 O
ANISOU 1751 O ASN A1013 6021 6580 5794 559 635 27 O
ATOM 1752 CB ASN A1013 57.740 -20.179 2.424 1.00 45.95 C
ANISOU 1752 CB ASN A1013 5929 5977 5552 653 487 -14 C
ATOM 1753 CG ASN A1013 57.891 -21.331 3.370 1.00 55.55 C
ANISOU 1753 CG ASN A1013 7181 7186 6740 797 488 -19 C
ATOM 1754 OD1 ASN A1013 58.844 -22.101 3.295 1.00 53.02 O
ANISOU 1754 OD1 ASN A1013 6841 6967 6337 958 540 -3 O
ATOM 1755 ND2 ASN A1013 56.967 -21.462 4.292 1.00 46.53 N
ANISOU 1755 ND2 ASN A1013 6098 5927 5654 760 444 -32 N
ATOM 1756 N LEU A1014 58.309 -17.095 1.292 1.00 44.48 N
ANISOU 1756 N LEU A1014 5599 5875 5427 341 579 33 N
ATOM 1757 CA LEU A1014 58.561 -16.183 0.184 1.00 45.67 C
ANISOU 1757 CA LEU A1014 5769 6023 5559 274 669 75 C
ATOM 1758 C LEU A1014 59.967 -15.580 0.341 1.00 52.04 C
ANISOU 1758 C LEU A1014 6412 6996 6364 184 766 54 C
ATOM 1759 O LEU A1014 60.687 -15.475 -0.649 1.00 53.45 O
ANISOU 1759 O LEU A1014 6572 7245 6489 196 856 78 O
ATOM 1760 CB LEU A1014 57.497 -15.075 0.114 1.00 45.35 C
ANISOU 1760 CB LEU A1014 5828 5833 5569 179 673 110 C
ATOM 1761 CG LEU A1014 56.969 -14.600 -1.267 1.00 50.23 C
ANISOU 1761 CG LEU A1014 6575 6384 6126 223 725 177 C
ATOM 1762 CD1 LEU A1014 56.562 -13.155 -1.208 1.00 50.15 C
ANISOU 1762 CD1 LEU A1014 6633 6265 6157 125 799 230 C
ATOM 1763 CD2 LEU A1014 57.981 -14.811 -2.428 1.00 53.39 C
ANISOU 1763 CD2 LEU A1014 6956 6884 6447 273 821 205 C
ATOM 1764 N LYS A1015 60.370 -15.242 1.589 1.00 48.94 N
ANISOU 1764 N LYS A1015 5886 6689 6020 93 749 -4 N
ATOM 1765 CA LYS A1015 61.694 -14.684 1.905 1.00 50.11 C
ANISOU 1765 CA LYS A1015 5835 7046 6160 -22 834 -67 C
ATOM 1766 C LYS A1015 62.799 -15.689 1.551 1.00 55.20 C
ANISOU 1766 C LYS A1015 6357 7915 6700 133 844 -79 C
ATOM 1767 O LYS A1015 63.821 -15.294 0.982 1.00 56.23 O
ANISOU 1767 O LYS A1015 6372 8196 6796 63 951 -102 O
ATOM 1768 CB LYS A1015 61.781 -14.265 3.382 1.00 52.27 C
ANISOU 1768 CB LYS A1015 5981 7396 6482 -127 789 -150 C
ATOM 1769 CG LYS A1015 61.063 -12.949 3.684 1.00 62.71 C
ANISOU 1769 CG LYS A1015 7391 8531 7904 -326 834 -158 C
ATOM 1770 CD LYS A1015 61.079 -12.596 5.176 1.00 72.75 C
ANISOU 1770 CD LYS A1015 8542 9881 9217 -427 783 -253 C
ATOM 1771 CE LYS A1015 59.834 -13.050 5.905 1.00 87.22 C
ANISOU 1771 CE LYS A1015 10491 11565 11084 -326 652 -216 C
ATOM 1772 NZ LYS A1015 59.861 -12.678 7.344 1.00 99.64 N
ANISOU 1772 NZ LYS A1015 11952 13218 12688 -418 608 -306 N
ATOM 1773 N VAL A1016 62.549 -16.995 1.828 1.00 50.46 N
ANISOU 1773 N VAL A1016 5806 7319 6048 348 753 -59 N
ATOM 1774 CA VAL A1016 63.443 -18.119 1.535 1.00 50.41 C
ANISOU 1774 CA VAL A1016 5736 7489 5929 556 765 -53 C
ATOM 1775 C VAL A1016 63.720 -18.168 0.018 1.00 55.43 C
ANISOU 1775 C VAL A1016 6440 8101 6519 582 848 -11 C
ATOM 1776 O VAL A1016 64.881 -18.267 -0.374 1.00 56.86 O
ANISOU 1776 O VAL A1016 6480 8500 6626 625 917 -26 O
ATOM 1777 CB VAL A1016 62.867 -19.464 2.071 1.00 52.39 C
ANISOU 1777 CB VAL A1016 6111 7648 6145 773 688 -27 C
ATOM 1778 CG1 VAL A1016 63.748 -20.648 1.683 1.00 52.95 C
ANISOU 1778 CG1 VAL A1016 6168 7860 6090 1020 728 -6 C
ATOM 1779 CG2 VAL A1016 62.675 -19.421 3.583 1.00 51.46 C
ANISOU 1779 CG2 VAL A1016 5921 7578 6053 770 619 -58 C
ATOM 1780 N ILE A1017 62.658 -18.064 -0.818 1.00 51.27 N
ANISOU 1780 N ILE A1017 6114 7341 6025 561 840 36 N
ATOM 1781 CA ILE A1017 62.719 -18.071 -2.290 1.00 51.06 C
ANISOU 1781 CA ILE A1017 6178 7279 5944 596 909 80 C
ATOM 1782 C ILE A1017 63.629 -16.931 -2.790 1.00 56.12 C
ANISOU 1782 C ILE A1017 6705 8031 6589 443 1039 86 C
ATOM 1783 O ILE A1017 64.468 -17.163 -3.657 1.00 56.42 O
ANISOU 1783 O ILE A1017 6697 8191 6550 504 1119 100 O
ATOM 1784 CB ILE A1017 61.280 -17.985 -2.901 1.00 52.53 C
ANISOU 1784 CB ILE A1017 6571 7237 6153 591 862 112 C
ATOM 1785 CG1 ILE A1017 60.552 -19.341 -2.779 1.00 51.52 C
ANISOU 1785 CG1 ILE A1017 6561 7018 5996 737 778 81 C
ATOM 1786 CG2 ILE A1017 61.292 -17.499 -4.373 1.00 53.99 C
ANISOU 1786 CG2 ILE A1017 6833 7403 6278 592 946 165 C
ATOM 1787 CD1 ILE A1017 59.077 -19.265 -2.815 1.00 51.24 C
ANISOU 1787 CD1 ILE A1017 6661 6808 5999 693 705 69 C
ATOM 1788 N GLU A1018 63.466 -15.719 -2.230 1.00 53.17 N
ANISOU 1788 N GLU A1018 6295 7606 6302 239 1077 69 N
ATOM 1789 CA GLU A1018 64.239 -14.536 -2.605 1.00 55.01 C
ANISOU 1789 CA GLU A1018 6450 7897 6556 47 1237 60 C
ATOM 1790 C GLU A1018 65.727 -14.723 -2.330 1.00 61.60 C
ANISOU 1790 C GLU A1018 7030 9038 7339 19 1297 -21 C
ATOM 1791 O GLU A1018 66.541 -14.351 -3.171 1.00 63.34 O
ANISOU 1791 O GLU A1018 7195 9350 7521 -45 1436 -16 O
ATOM 1792 CB GLU A1018 63.730 -13.293 -1.870 1.00 56.31 C
ANISOU 1792 CB GLU A1018 6643 7924 6826 -167 1275 36 C
ATOM 1793 CG GLU A1018 62.285 -12.947 -2.180 1.00 66.35 C
ANISOU 1793 CG GLU A1018 8153 8925 8131 -132 1238 122 C
ATOM 1794 CD GLU A1018 61.589 -12.045 -1.178 1.00 85.49 C
ANISOU 1794 CD GLU A1018 10620 11207 10653 -277 1230 99 C
ATOM 1795 OE1 GLU A1018 62.023 -11.991 -0.005 1.00 74.72 O
ANISOU 1795 OE1 GLU A1018 9105 9949 9336 -372 1189 3 O
ATOM 1796 OE2 GLU A1018 60.584 -11.410 -1.567 1.00 83.31 O
ANISOU 1796 OE2 GLU A1018 10532 10729 10394 -273 1263 177 O
ATOM 1797 N LYS A1019 66.078 -15.323 -1.178 1.00 58.43 N
ANISOU 1797 N LYS A1019 6467 8815 6918 85 1197 -94 N
ATOM 1798 CA LYS A1019 67.461 -15.556 -0.780 1.00 60.13 C
ANISOU 1798 CA LYS A1019 6404 9387 7055 96 1232 -183 C
ATOM 1799 C LYS A1019 68.026 -16.921 -1.293 1.00 64.65 C
ANISOU 1799 C LYS A1019 6954 10115 7497 395 1196 -142 C
ATOM 1800 O LYS A1019 69.188 -17.233 -1.012 1.00 66.11 O
ANISOU 1800 O LYS A1019 6902 10632 7587 466 1217 -206 O
ATOM 1801 CB LYS A1019 67.611 -15.421 0.750 1.00 62.96 C
ANISOU 1801 CB LYS A1019 6583 9908 7432 32 1155 -288 C
ATOM 1802 CG LYS A1019 66.905 -16.481 1.599 1.00 83.28 C
ANISOU 1802 CG LYS A1019 9244 12411 9989 253 994 -250 C
ATOM 1803 CD LYS A1019 67.151 -16.291 3.105 1.00 95.88 C
ANISOU 1803 CD LYS A1019 10646 14203 11581 199 928 -353 C
ATOM 1804 CE LYS A1019 66.309 -15.196 3.720 1.00111.65 C
ANISOU 1804 CE LYS A1019 12718 15994 13712 -51 926 -390 C
ATOM 1805 NZ LYS A1019 66.554 -15.062 5.180 1.00124.79 N
ANISOU 1805 NZ LYS A1019 14189 17868 15358 -96 858 -502 N
ATOM 1806 N ALA A1020 67.236 -17.691 -2.082 1.00 59.68 N
ANISOU 1806 N ALA A1020 6563 9261 6850 565 1156 -49 N
ATOM 1807 CA ALA A1020 67.637 -19.003 -2.613 1.00 59.87 C
ANISOU 1807 CA ALA A1020 6624 9367 6757 844 1142 -13 C
ATOM 1808 C ALA A1020 68.464 -18.903 -3.906 1.00 65.82 C
ANISOU 1808 C ALA A1020 7336 10235 7438 856 1263 9 C
ATOM 1809 O ALA A1020 68.409 -17.889 -4.612 1.00 65.74 O
ANISOU 1809 O ALA A1020 7355 10147 7476 664 1358 25 O
ATOM 1810 CB ALA A1020 66.413 -19.876 -2.852 1.00 58.93 C
ANISOU 1810 CB ALA A1020 6776 8961 6653 982 1062 42 C
ATOM 1811 N ASP A1021 69.225 -19.983 -4.206 1.00 63.58 N
ANISOU 1811 N ASP A1021 7001 10129 7028 1103 1274 17 N
ATOM 1812 CA ASP A1021 70.097 -20.108 -5.378 1.00 64.87 C
ANISOU 1812 CA ASP A1021 7114 10434 7099 1166 1384 36 C
ATOM 1813 C ASP A1021 69.964 -21.504 -6.050 1.00 68.39 C
ANISOU 1813 C ASP A1021 7738 10805 7444 1467 1367 86 C
ATOM 1814 O ASP A1021 70.801 -21.861 -6.887 1.00 69.83 O
ANISOU 1814 O ASP A1021 7867 11142 7521 1586 1449 99 O
ATOM 1815 CB ASP A1021 71.567 -19.840 -4.968 1.00 68.89 C
ANISOU 1815 CB ASP A1021 7287 11356 7532 1140 1453 -39 C
ATOM 1816 CG ASP A1021 72.231 -20.933 -4.140 1.00 78.89 C
ANISOU 1816 CG ASP A1021 8415 12885 8674 1424 1390 -62 C
ATOM 1817 OD1 ASP A1021 71.556 -21.506 -3.255 1.00 78.43 O
ANISOU 1817 OD1 ASP A1021 8464 12701 8635 1541 1286 -45 O
ATOM 1818 OD2 ASP A1021 73.432 -21.199 -4.364 1.00 86.59 O
ANISOU 1818 OD2 ASP A1021 9173 14204 9522 1541 1454 -93 O
ATOM 1819 N ASN A1022 68.924 -22.285 -5.680 1.00 62.30 N
ANISOU 1819 N ASN A1022 7178 9793 6700 1577 1276 102 N
ATOM 1820 CA ASN A1022 68.683 -23.621 -6.235 1.00 61.48 C
ANISOU 1820 CA ASN A1022 7279 9568 6512 1827 1282 125 C
ATOM 1821 C ASN A1022 67.181 -23.939 -6.276 1.00 62.68 C
ANISOU 1821 C ASN A1022 7696 9378 6743 1779 1212 119 C
ATOM 1822 O ASN A1022 66.421 -23.427 -5.448 1.00 61.44 O
ANISOU 1822 O ASN A1022 7547 9109 6690 1632 1139 107 O
ATOM 1823 CB ASN A1022 69.458 -24.698 -5.458 1.00 61.68 C
ANISOU 1823 CB ASN A1022 7241 9764 6429 2110 1290 128 C
ATOM 1824 CG ASN A1022 69.027 -24.883 -4.024 1.00 73.79 C
ANISOU 1824 CG ASN A1022 8771 11258 8008 2135 1211 120 C
ATOM 1825 OD1 ASN A1022 68.238 -25.773 -3.706 1.00 67.00 O
ANISOU 1825 OD1 ASN A1022 8137 10161 7160 2249 1191 134 O
ATOM 1826 ND2 ASN A1022 69.565 -24.077 -3.122 1.00 61.76 N
ANISOU 1826 ND2 ASN A1022 6990 9974 6503 2025 1179 88 N
ATOM 1827 N ALA A1023 66.766 -24.776 -7.253 1.00 58.24 N
ANISOU 1827 N ALA A1023 7337 8671 6122 1894 1242 111 N
ATOM 1828 CA ALA A1023 65.384 -25.197 -7.502 1.00 56.19 C
ANISOU 1828 CA ALA A1023 7313 8131 5907 1845 1193 70 C
ATOM 1829 C ALA A1023 64.804 -26.048 -6.359 1.00 58.66 C
ANISOU 1829 C ALA A1023 7741 8289 6259 1916 1157 44 C
ATOM 1830 O ALA A1023 63.599 -25.967 -6.110 1.00 56.93 O
ANISOU 1830 O ALA A1023 7637 7875 6120 1787 1095 5 O
ATOM 1831 CB ALA A1023 65.302 -25.964 -8.812 1.00 57.59 C
ANISOU 1831 CB ALA A1023 7648 8247 5985 1955 1253 39 C
ATOM 1832 N ALA A1024 65.648 -26.837 -5.657 1.00 55.93 N
ANISOU 1832 N ALA A1024 7363 8044 5845 2131 1205 71 N
ATOM 1833 CA ALA A1024 65.215 -27.678 -4.533 1.00 55.53 C
ANISOU 1833 CA ALA A1024 7439 7849 5810 2240 1204 70 C
ATOM 1834 C ALA A1024 64.664 -26.832 -3.375 1.00 58.88 C
ANISOU 1834 C ALA A1024 7759 8263 6349 2066 1104 74 C
ATOM 1835 O ALA A1024 63.617 -27.182 -2.821 1.00 58.12 O
ANISOU 1835 O ALA A1024 7818 7942 6320 2012 1077 48 O
ATOM 1836 CB ALA A1024 66.364 -28.549 -4.050 1.00 57.84 C
ANISOU 1836 CB ALA A1024 7698 8305 5974 2552 1286 122 C
ATOM 1837 N GLN A1025 65.353 -25.713 -3.027 1.00 55.18 N
ANISOU 1837 N GLN A1025 7029 8035 5901 1963 1062 95 N
ATOM 1838 CA GLN A1025 64.927 -24.808 -1.953 1.00 53.75 C
ANISOU 1838 CA GLN A1025 6736 7864 5823 1787 976 87 C
ATOM 1839 C GLN A1025 63.673 -24.029 -2.341 1.00 54.75 C
ANISOU 1839 C GLN A1025 6958 7777 6067 1540 918 62 C
ATOM 1840 O GLN A1025 62.794 -23.823 -1.502 1.00 52.98 O
ANISOU 1840 O GLN A1025 6778 7423 5927 1445 854 49 O
ATOM 1841 CB GLN A1025 66.044 -23.828 -1.568 1.00 55.87 C
ANISOU 1841 CB GLN A1025 6704 8450 6073 1715 974 83 C
ATOM 1842 CG GLN A1025 67.036 -24.400 -0.562 1.00 78.88 C
ANISOU 1842 CG GLN A1025 9466 11625 8879 1939 982 92 C
ATOM 1843 CD GLN A1025 66.565 -24.461 0.884 1.00 91.95 C
ANISOU 1843 CD GLN A1025 11118 13246 10571 1952 912 90 C
ATOM 1844 OE1 GLN A1025 65.401 -24.197 1.227 1.00 80.16 O
ANISOU 1844 OE1 GLN A1025 9756 11504 9197 1794 857 82 O
ATOM 1845 NE2 GLN A1025 67.474 -24.856 1.767 1.00 86.78 N
ANISOU 1845 NE2 GLN A1025 10306 12870 9797 2165 915 100 N
ATOM 1846 N VAL A1026 63.594 -23.607 -3.613 1.00 51.12 N
ANISOU 1846 N VAL A1026 6527 7299 5596 1462 946 61 N
ATOM 1847 CA VAL A1026 62.471 -22.851 -4.161 1.00 49.87 C
ANISOU 1847 CA VAL A1026 6454 6987 5507 1281 903 49 C
ATOM 1848 C VAL A1026 61.205 -23.752 -4.185 1.00 53.89 C
ANISOU 1848 C VAL A1026 7175 7270 6031 1303 865 -6 C
ATOM 1849 O VAL A1026 60.165 -23.310 -3.710 1.00 52.78 O
ANISOU 1849 O VAL A1026 7069 7015 5971 1173 797 -26 O
ATOM 1850 CB VAL A1026 62.847 -22.240 -5.538 1.00 53.56 C
ANISOU 1850 CB VAL A1026 6901 7530 5921 1245 963 74 C
ATOM 1851 CG1 VAL A1026 61.620 -21.832 -6.343 1.00 52.37 C
ANISOU 1851 CG1 VAL A1026 6880 7232 5784 1152 926 64 C
ATOM 1852 CG2 VAL A1026 63.782 -21.047 -5.351 1.00 53.65 C
ANISOU 1852 CG2 VAL A1026 6711 7718 5956 1131 1014 110 C
ATOM 1853 N LYS A1027 61.327 -25.022 -4.640 1.00 51.65 N
ANISOU 1853 N LYS A1027 7028 6928 5670 1460 924 -41 N
ATOM 1854 CA LYS A1027 60.242 -26.019 -4.685 1.00 50.90 C
ANISOU 1854 CA LYS A1027 7141 6617 5580 1462 930 -125 C
ATOM 1855 C LYS A1027 59.706 -26.313 -3.271 1.00 53.31 C
ANISOU 1855 C LYS A1027 7488 6804 5963 1444 904 -127 C
ATOM 1856 O LYS A1027 58.490 -26.399 -3.090 1.00 52.19 O
ANISOU 1856 O LYS A1027 7443 6507 5879 1320 867 -194 O
ATOM 1857 CB LYS A1027 60.726 -27.320 -5.360 1.00 54.09 C
ANISOU 1857 CB LYS A1027 7693 6977 5881 1643 1039 -162 C
ATOM 1858 CG LYS A1027 59.636 -28.364 -5.575 1.00 63.09 C
ANISOU 1858 CG LYS A1027 9061 7889 7021 1602 1079 -284 C
ATOM 1859 CD LYS A1027 60.190 -29.667 -6.137 1.00 70.18 C
ANISOU 1859 CD LYS A1027 10135 8711 7821 1789 1219 -322 C
ATOM 1860 CE LYS A1027 59.104 -30.697 -6.328 1.00 77.34 C
ANISOU 1860 CE LYS A1027 11279 9372 8735 1708 1290 -472 C
ATOM 1861 NZ LYS A1027 59.627 -31.932 -6.959 1.00 88.26 N
ANISOU 1861 NZ LYS A1027 12859 10659 10018 1873 1448 -524 N
ATOM 1862 N ASP A1028 60.611 -26.455 -2.283 1.00 50.04 N
ANISOU 1862 N ASP A1028 6987 6491 5535 1573 925 -59 N
ATOM 1863 CA ASP A1028 60.279 -26.716 -0.874 1.00 49.50 C
ANISOU 1863 CA ASP A1028 6945 6345 5516 1597 910 -42 C
ATOM 1864 C ASP A1028 59.392 -25.596 -0.288 1.00 51.30 C
ANISOU 1864 C ASP A1028 7086 6547 5860 1375 799 -53 C
ATOM 1865 O ASP A1028 58.307 -25.882 0.229 1.00 50.15 O
ANISOU 1865 O ASP A1028 7055 6225 5775 1297 781 -94 O
ATOM 1866 CB ASP A1028 61.559 -26.881 -0.036 1.00 52.22 C
ANISOU 1866 CB ASP A1028 7160 6895 5788 1802 940 34 C
ATOM 1867 CG ASP A1028 61.280 -27.179 1.424 1.00 62.98 C
ANISOU 1867 CG ASP A1028 8550 8205 7173 1867 930 63 C
ATOM 1868 OD1 ASP A1028 60.955 -28.344 1.738 1.00 64.01 O
ANISOU 1868 OD1 ASP A1028 8899 8150 7270 2011 1024 69 O
ATOM 1869 OD2 ASP A1028 61.353 -26.236 2.248 1.00 69.40 O
ANISOU 1869 OD2 ASP A1028 9183 9151 8036 1768 843 76 O
ATOM 1870 N ALA A1029 59.857 -24.333 -0.392 1.00 47.22 N
ANISOU 1870 N ALA A1029 6377 6198 5368 1270 745 -21 N
ATOM 1871 CA ALA A1029 59.155 -23.141 0.081 1.00 45.66 C
ANISOU 1871 CA ALA A1029 6101 5981 5269 1075 662 -22 C
ATOM 1872 C ALA A1029 57.804 -22.975 -0.617 1.00 47.40 C
ANISOU 1872 C ALA A1029 6441 6042 5526 951 624 -70 C
ATOM 1873 O ALA A1029 56.800 -22.775 0.065 1.00 46.58 O
ANISOU 1873 O ALA A1029 6371 5836 5493 856 568 -94 O
ATOM 1874 CB ALA A1029 60.018 -21.904 -0.143 1.00 46.75 C
ANISOU 1874 CB ALA A1029 6050 6301 5411 988 665 11 C
ATOM 1875 N LEU A1030 57.775 -23.113 -1.962 1.00 42.86 N
ANISOU 1875 N LEU A1030 5921 5475 4888 965 653 -92 N
ATOM 1876 CA LEU A1030 56.561 -22.997 -2.775 1.00 42.13 C
ANISOU 1876 CA LEU A1030 5916 5303 4788 878 615 -153 C
ATOM 1877 C LEU A1030 55.503 -24.016 -2.365 1.00 45.42 C
ANISOU 1877 C LEU A1030 6468 5563 5226 853 609 -250 C
ATOM 1878 O LEU A1030 54.331 -23.654 -2.314 1.00 44.86 O
ANISOU 1878 O LEU A1030 6409 5449 5187 740 546 -302 O
ATOM 1879 CB LEU A1030 56.874 -23.125 -4.282 1.00 42.72 C
ANISOU 1879 CB LEU A1030 6022 5449 4761 935 657 -166 C
ATOM 1880 CG LEU A1030 57.426 -21.869 -4.955 1.00 46.29 C
ANISOU 1880 CG LEU A1030 6373 6025 5192 908 670 -79 C
ATOM 1881 CD1 LEU A1030 58.015 -22.188 -6.298 1.00 46.48 C
ANISOU 1881 CD1 LEU A1030 6425 6131 5104 1002 734 -79 C
ATOM 1882 CD2 LEU A1030 56.365 -20.777 -5.065 1.00 48.39 C
ANISOU 1882 CD2 LEU A1030 6636 6266 5485 804 612 -62 C
ATOM 1883 N THR A1031 55.916 -25.267 -2.051 1.00 42.84 N
ANISOU 1883 N THR A1031 6247 5156 4875 963 691 -275 N
ATOM 1884 CA THR A1031 55.040 -26.352 -1.570 1.00 43.38 C
ANISOU 1884 CA THR A1031 6478 5038 4967 934 738 -369 C
ATOM 1885 C THR A1031 54.383 -25.957 -0.230 1.00 46.87 C
ANISOU 1885 C THR A1031 6885 5418 5505 850 683 -347 C
ATOM 1886 O THR A1031 53.167 -26.114 -0.089 1.00 46.50 O
ANISOU 1886 O THR A1031 6897 5274 5498 720 663 -438 O
ATOM 1887 CB THR A1031 55.825 -27.678 -1.426 1.00 49.96 C
ANISOU 1887 CB THR A1031 7457 5780 5745 1111 875 -364 C
ATOM 1888 OG1 THR A1031 56.426 -28.027 -2.674 1.00 48.53 O
ANISOU 1888 OG1 THR A1031 7306 5662 5471 1193 927 -387 O
ATOM 1889 CG2 THR A1031 54.953 -28.829 -0.924 1.00 47.09 C
ANISOU 1889 CG2 THR A1031 7303 5181 5407 1069 973 -462 C
ATOM 1890 N LYS A1032 55.183 -25.428 0.735 1.00 43.04 N
ANISOU 1890 N LYS A1032 6289 5016 5049 917 659 -239 N
ATOM 1891 CA LYS A1032 54.683 -24.987 2.051 1.00 42.14 C
ANISOU 1891 CA LYS A1032 6129 4867 5015 853 605 -213 C
ATOM 1892 C LYS A1032 53.739 -23.800 1.905 1.00 46.01 C
ANISOU 1892 C LYS A1032 6533 5386 5564 680 501 -232 C
ATOM 1893 O LYS A1032 52.777 -23.704 2.667 1.00 47.37 O
ANISOU 1893 O LYS A1032 6724 5477 5797 592 464 -261 O
ATOM 1894 CB LYS A1032 55.829 -24.640 3.020 1.00 43.59 C
ANISOU 1894 CB LYS A1032 6187 5186 5189 966 599 -117 C
ATOM 1895 CG LYS A1032 56.491 -25.870 3.623 1.00 45.78 C
ANISOU 1895 CG LYS A1032 6568 5427 5400 1178 702 -82 C
ATOM 1896 CD LYS A1032 57.951 -25.618 3.965 1.00 51.14 C
ANISOU 1896 CD LYS A1032 7082 6343 6006 1337 702 -5 C
ATOM 1897 CE LYS A1032 58.560 -26.808 4.667 1.00 53.57 C
ANISOU 1897 CE LYS A1032 7495 6638 6220 1601 805 48 C
ATOM 1898 NZ LYS A1032 60.046 -26.767 4.637 1.00 62.73 N
ANISOU 1898 NZ LYS A1032 8493 8075 7268 1794 820 102 N
ATOM 1899 N MET A1033 53.992 -22.917 0.925 1.00 41.02 N
ANISOU 1899 N MET A1033 5819 4864 4902 650 468 -211 N
ATOM 1900 CA MET A1033 53.141 -21.752 0.659 1.00 40.33 C
ANISOU 1900 CA MET A1033 5675 4805 4843 534 393 -209 C
ATOM 1901 C MET A1033 51.776 -22.182 0.123 1.00 45.46 C
ANISOU 1901 C MET A1033 6403 5401 5470 468 366 -317 C
ATOM 1902 O MET A1033 50.757 -21.637 0.555 1.00 44.24 O
ANISOU 1902 O MET A1033 6222 5234 5354 384 304 -337 O
ATOM 1903 CB MET A1033 53.803 -20.790 -0.332 1.00 42.60 C
ANISOU 1903 CB MET A1033 5893 5207 5085 546 405 -146 C
ATOM 1904 CG MET A1033 54.890 -19.958 0.278 1.00 45.68 C
ANISOU 1904 CG MET A1033 6169 5673 5515 534 426 -67 C
ATOM 1905 SD MET A1033 55.945 -19.249 -0.995 1.00 50.63 S
ANISOU 1905 SD MET A1033 6743 6421 6075 557 500 -8 S
ATOM 1906 CE MET A1033 54.991 -17.892 -1.464 1.00 46.89 C
ANISOU 1906 CE MET A1033 6297 5906 5612 472 484 32 C
ATOM 1907 N ARG A1034 51.768 -23.155 -0.821 1.00 43.25 N
ANISOU 1907 N ARG A1034 6207 5109 5116 504 417 -399 N
ATOM 1908 CA ARG A1034 50.565 -23.713 -1.436 1.00 43.58 C
ANISOU 1908 CA ARG A1034 6307 5138 5113 425 406 -546 C
ATOM 1909 C ARG A1034 49.705 -24.389 -0.366 1.00 48.17 C
ANISOU 1909 C ARG A1034 6951 5585 5768 330 425 -626 C
ATOM 1910 O ARG A1034 48.492 -24.178 -0.348 1.00 48.92 O
ANISOU 1910 O ARG A1034 7010 5712 5865 221 370 -715 O
ATOM 1911 CB ARG A1034 50.944 -24.710 -2.539 1.00 45.48 C
ANISOU 1911 CB ARG A1034 6637 5380 5264 478 482 -631 C
ATOM 1912 CG ARG A1034 49.836 -24.941 -3.554 1.00 57.64 C
ANISOU 1912 CG ARG A1034 8182 7001 6718 395 454 -795 C
ATOM 1913 CD ARG A1034 50.177 -26.059 -4.524 1.00 62.88 C
ANISOU 1913 CD ARG A1034 8953 7640 7296 426 546 -909 C
ATOM 1914 NE ARG A1034 49.248 -27.187 -4.408 1.00 69.95 N
ANISOU 1914 NE ARG A1034 9949 8433 8195 287 612 -1114 N
ATOM 1915 CZ ARG A1034 48.143 -27.335 -5.132 1.00 83.36 C
ANISOU 1915 CZ ARG A1034 11603 10254 9817 167 573 -1303 C
ATOM 1916 NH1 ARG A1034 47.807 -26.425 -6.039 1.00 66.57 N
ANISOU 1916 NH1 ARG A1034 9340 8366 7587 210 460 -1291 N
ATOM 1917 NH2 ARG A1034 47.362 -28.393 -4.951 1.00 72.77 N
ANISOU 1917 NH2 ARG A1034 10353 8809 8487 5 661 -1511 N
ATOM 1918 N ALA A1035 50.346 -25.157 0.551 1.00 43.71 N
ANISOU 1918 N ALA A1035 6471 4885 5249 389 508 -585 N
ATOM 1919 CA ALA A1035 49.689 -25.869 1.647 1.00 42.72 C
ANISOU 1919 CA ALA A1035 6439 4604 5190 324 564 -635 C
ATOM 1920 C ALA A1035 49.073 -24.883 2.644 1.00 45.54 C
ANISOU 1920 C ALA A1035 6689 4993 5621 255 467 -583 C
ATOM 1921 O ALA A1035 47.924 -25.073 3.026 1.00 45.62 O
ANISOU 1921 O ALA A1035 6717 4951 5664 132 463 -676 O
ATOM 1922 CB ALA A1035 50.672 -26.804 2.343 1.00 43.38 C
ANISOU 1922 CB ALA A1035 6646 4562 5275 468 685 -564 C
ATOM 1923 N ALA A1036 49.797 -23.805 3.012 1.00 41.45 N
ANISOU 1923 N ALA A1036 6056 4569 5125 318 398 -451 N
ATOM 1924 CA ALA A1036 49.285 -22.765 3.925 1.00 39.90 C
ANISOU 1924 CA ALA A1036 5765 4400 4994 257 314 -402 C
ATOM 1925 C ALA A1036 48.088 -22.018 3.296 1.00 42.87 C
ANISOU 1925 C ALA A1036 6081 4856 5353 162 233 -462 C
ATOM 1926 O ALA A1036 47.082 -21.831 3.967 1.00 42.39 O
ANISOU 1926 O ALA A1036 6000 4773 5333 83 196 -499 O
ATOM 1927 CB ALA A1036 50.389 -21.783 4.295 1.00 39.64 C
ANISOU 1927 CB ALA A1036 5629 4456 4977 321 284 -280 C
ATOM 1928 N ALA A1037 48.189 -21.645 2.006 1.00 39.54 N
ANISOU 1928 N ALA A1037 5630 4541 4852 191 213 -470 N
ATOM 1929 CA ALA A1037 47.152 -20.947 1.240 1.00 39.73 C
ANISOU 1929 CA ALA A1037 5595 4687 4814 161 143 -513 C
ATOM 1930 C ALA A1037 45.881 -21.803 1.080 1.00 45.69 C
ANISOU 1930 C ALA A1037 6364 5460 5537 61 139 -690 C
ATOM 1931 O ALA A1037 44.785 -21.291 1.313 1.00 45.61 O
ANISOU 1931 O ALA A1037 6284 5527 5519 11 74 -730 O
ATOM 1932 CB ALA A1037 47.695 -20.548 -0.126 1.00 40.89 C
ANISOU 1932 CB ALA A1037 5729 4945 4862 247 147 -476 C
ATOM 1933 N LEU A1038 46.026 -23.107 0.714 1.00 43.44 N
ANISOU 1933 N LEU A1038 6171 5105 5231 24 222 -804 N
ATOM 1934 CA LEU A1038 44.899 -24.029 0.565 1.00 44.50 C
ANISOU 1934 CA LEU A1038 6329 5240 5340 -115 255 -1008 C
ATOM 1935 C LEU A1038 44.252 -24.331 1.920 1.00 49.82 C
ANISOU 1935 C LEU A1038 7031 5784 6115 -219 287 -1033 C
ATOM 1936 O LEU A1038 43.045 -24.557 1.966 1.00 51.64 O
ANISOU 1936 O LEU A1038 7214 6076 6331 -354 278 -1185 O
ATOM 1937 CB LEU A1038 45.291 -25.336 -0.143 1.00 45.84 C
ANISOU 1937 CB LEU A1038 6624 5327 5466 -139 372 -1129 C
ATOM 1938 CG LEU A1038 45.598 -25.260 -1.660 1.00 51.30 C
ANISOU 1938 CG LEU A1038 7284 6178 6029 -71 346 -1173 C
ATOM 1939 CD1 LEU A1038 46.033 -26.616 -2.194 1.00 52.68 C
ANISOU 1939 CD1 LEU A1038 7608 6232 6174 -93 482 -1291 C
ATOM 1940 CD2 LEU A1038 44.407 -24.725 -2.470 1.00 53.04 C
ANISOU 1940 CD2 LEU A1038 7363 6653 6136 -124 245 -1302 C
ATOM 1941 N ASP A1039 45.039 -24.313 3.012 1.00 45.21 N
ANISOU 1941 N ASP A1039 6509 5050 5619 -152 326 -893 N
ATOM 1942 CA ASP A1039 44.545 -24.502 4.368 1.00 45.33 C
ANISOU 1942 CA ASP A1039 6556 4945 5722 -216 358 -885 C
ATOM 1943 C ASP A1039 43.689 -23.295 4.761 1.00 49.70 C
ANISOU 1943 C ASP A1039 6966 5625 6291 -249 234 -855 C
ATOM 1944 O ASP A1039 42.553 -23.471 5.209 1.00 50.89 O
ANISOU 1944 O ASP A1039 7090 5782 6463 -369 236 -956 O
ATOM 1945 CB ASP A1039 45.704 -24.704 5.361 1.00 47.23 C
ANISOU 1945 CB ASP A1039 6879 5050 6017 -92 417 -734 C
ATOM 1946 CG ASP A1039 45.241 -25.013 6.774 1.00 64.24 C
ANISOU 1946 CG ASP A1039 9087 7079 8244 -132 466 -717 C
ATOM 1947 OD1 ASP A1039 44.718 -26.131 6.998 1.00 67.52 O
ANISOU 1947 OD1 ASP A1039 9637 7344 8673 -214 598 -817 O
ATOM 1948 OD2 ASP A1039 45.393 -24.136 7.655 1.00 70.79 O
ANISOU 1948 OD2 ASP A1039 9832 7952 9114 -89 387 -611 O
ATOM 1949 N ALA A1040 44.223 -22.075 4.548 1.00 44.99 N
ANISOU 1949 N ALA A1040 6286 5127 5679 -146 144 -723 N
ATOM 1950 CA ALA A1040 43.553 -20.802 4.818 1.00 44.22 C
ANISOU 1950 CA ALA A1040 6083 5135 5585 -138 46 -670 C
ATOM 1951 C ALA A1040 42.245 -20.644 3.991 1.00 50.56 C
ANISOU 1951 C ALA A1040 6798 6120 6294 -185 -12 -799 C
ATOM 1952 O ALA A1040 41.264 -20.101 4.496 1.00 50.65 O
ANISOU 1952 O ALA A1040 6735 6201 6309 -215 -65 -817 O
ATOM 1953 CB ALA A1040 44.504 -19.658 4.522 1.00 44.09 C
ANISOU 1953 CB ALA A1040 6037 5156 5559 -27 13 -520 C
ATOM 1954 N GLN A1041 42.223 -21.170 2.748 1.00 48.08 N
ANISOU 1954 N GLN A1041 6482 5905 5881 -185 0 -900 N
ATOM 1955 CA GLN A1041 41.068 -21.137 1.853 1.00 48.78 C
ANISOU 1955 CA GLN A1041 6465 6224 5846 -217 -56 -1050 C
ATOM 1956 C GLN A1041 39.884 -21.966 2.403 1.00 54.51 C
ANISOU 1956 C GLN A1041 7155 6963 6595 -402 -24 -1246 C
ATOM 1957 O GLN A1041 38.731 -21.670 2.077 1.00 54.82 O
ANISOU 1957 O GLN A1041 7056 7232 6542 -432 -91 -1361 O
ATOM 1958 CB GLN A1041 41.478 -21.650 0.461 1.00 50.77 C
ANISOU 1958 CB GLN A1041 6735 6570 5987 -183 -36 -1128 C
ATOM 1959 CG GLN A1041 40.408 -21.438 -0.614 1.00 57.71 C
ANISOU 1959 CG GLN A1041 7476 7757 6693 -168 -111 -1272 C
ATOM 1960 CD GLN A1041 40.824 -21.864 -1.996 1.00 68.07 C
ANISOU 1960 CD GLN A1041 8801 9183 7879 -115 -98 -1342 C
ATOM 1961 OE1 GLN A1041 41.504 -22.878 -2.200 1.00 65.23 O
ANISOU 1961 OE1 GLN A1041 8551 8674 7558 -175 -8 -1396 O
ATOM 1962 NE2 GLN A1041 40.354 -21.128 -2.989 1.00 54.48 N
ANISOU 1962 NE2 GLN A1041 6970 7745 5987 16 -181 -1350 N
ATOM 1963 N LYS A1042 40.170 -22.991 3.237 1.00 51.50 N
ANISOU 1963 N LYS A1042 6897 6348 6323 -513 90 -1281 N
ATOM 1964 CA LYS A1042 39.165 -23.892 3.815 1.00 52.22 C
ANISOU 1964 CA LYS A1042 6995 6393 6452 -713 171 -1464 C
ATOM 1965 C LYS A1042 38.522 -23.330 5.100 1.00 54.51 C
ANISOU 1965 C LYS A1042 7233 6659 6819 -737 137 -1399 C
ATOM 1966 O LYS A1042 37.508 -23.859 5.559 1.00 55.09 O
ANISOU 1966 O LYS A1042 7269 6755 6908 -904 187 -1553 O
ATOM 1967 CB LYS A1042 39.802 -25.262 4.117 1.00 55.24 C
ANISOU 1967 CB LYS A1042 7582 6499 6908 -793 348 -1508 C
ATOM 1968 CG LYS A1042 40.237 -26.054 2.892 1.00 64.94 C
ANISOU 1968 CG LYS A1042 8879 7734 8060 -811 414 -1626 C
ATOM 1969 CD LYS A1042 41.169 -27.171 3.330 1.00 78.55 C
ANISOU 1969 CD LYS A1042 10839 9149 9856 -798 592 -1583 C
ATOM 1970 CE LYS A1042 41.914 -27.830 2.196 1.00 90.58 C
ANISOU 1970 CE LYS A1042 12457 10649 11311 -753 658 -1639 C
ATOM 1971 NZ LYS A1042 43.084 -28.603 2.696 1.00 96.48 N
ANISOU 1971 NZ LYS A1042 13424 11120 12113 -638 806 -1516 N
ATOM 1972 N ALA A1043 39.107 -22.266 5.671 1.00 49.36 N
ANISOU 1972 N ALA A1043 6578 5966 6212 -585 65 -1186 N
ATOM 1973 CA ALA A1043 38.662 -21.651 6.924 1.00 47.54 C
ANISOU 1973 CA ALA A1043 6313 5698 6054 -584 33 -1105 C
ATOM 1974 C ALA A1043 37.340 -20.896 6.816 1.00 52.88 C
ANISOU 1974 C ALA A1043 6821 6615 6658 -597 -62 -1177 C
ATOM 1975 O ALA A1043 36.987 -20.381 5.752 1.00 54.07 O
ANISOU 1975 O ALA A1043 6869 6988 6686 -523 -140 -1214 O
ATOM 1976 CB ALA A1043 39.730 -20.703 7.436 1.00 46.13 C
ANISOU 1976 CB ALA A1043 6170 5430 5926 -431 -10 -888 C
ATOM 1977 N THR A1044 36.622 -20.816 7.946 1.00 49.33 N
ANISOU 1977 N THR A1044 6342 6133 6269 -666 -52 -1188 N
ATOM 1978 CA THR A1044 35.411 -20.020 8.076 1.00 49.68 C
ANISOU 1978 CA THR A1044 6226 6401 6249 -650 -139 -1231 C
ATOM 1979 C THR A1044 35.718 -19.009 9.189 1.00 53.09 C
ANISOU 1979 C THR A1044 6692 6722 6757 -538 -177 -1040 C
ATOM 1980 O THR A1044 35.433 -19.274 10.363 1.00 51.39 O
ANISOU 1980 O THR A1044 6504 6395 6627 -616 -131 -1039 O
ATOM 1981 CB THR A1044 34.151 -20.863 8.282 1.00 53.81 C
ANISOU 1981 CB THR A1044 6659 7029 6756 -857 -82 -1459 C
ATOM 1982 OG1 THR A1044 34.069 -21.823 7.230 1.00 55.78 O
ANISOU 1982 OG1 THR A1044 6900 7353 6941 -978 -28 -1648 O
ATOM 1983 CG2 THR A1044 32.892 -20.016 8.269 1.00 50.20 C
ANISOU 1983 CG2 THR A1044 6001 6871 6201 -813 -183 -1514 C
ATOM 1984 N PRO A1045 36.395 -17.879 8.835 1.00 49.96 N
ANISOU 1984 N PRO A1045 6313 6337 6334 -364 -240 -880 N
ATOM 1985 CA PRO A1045 36.735 -16.874 9.854 1.00 48.20 C
ANISOU 1985 CA PRO A1045 6129 6004 6181 -281 -260 -724 C
ATOM 1986 C PRO A1045 35.478 -16.268 10.508 1.00 51.76 C
ANISOU 1986 C PRO A1045 6484 6575 6608 -269 -303 -750 C
ATOM 1987 O PRO A1045 34.395 -16.355 9.908 1.00 51.27 O
ANISOU 1987 O PRO A1045 6298 6743 6441 -274 -340 -868 O
ATOM 1988 CB PRO A1045 37.532 -15.835 9.057 1.00 49.89 C
ANISOU 1988 CB PRO A1045 6380 6231 6347 -128 -288 -592 C
ATOM 1989 CG PRO A1045 37.058 -15.961 7.664 1.00 55.45 C
ANISOU 1989 CG PRO A1045 7016 7138 6914 -79 -318 -672 C
ATOM 1990 CD PRO A1045 36.829 -17.437 7.489 1.00 51.82 C
ANISOU 1990 CD PRO A1045 6540 6683 6466 -245 -277 -845 C
ATOM 1991 N PRO A1046 35.590 -15.668 11.730 1.00 47.92 N
ANISOU 1991 N PRO A1046 6039 5966 6204 -248 -299 -654 N
ATOM 1992 CA PRO A1046 34.390 -15.136 12.413 1.00 47.84 C
ANISOU 1992 CA PRO A1046 5942 6065 6171 -230 -332 -678 C
ATOM 1993 C PRO A1046 33.513 -14.172 11.592 1.00 52.02 C
ANISOU 1993 C PRO A1046 6373 6836 6557 -75 -399 -674 C
ATOM 1994 O PRO A1046 32.294 -14.179 11.773 1.00 53.44 O
ANISOU 1994 O PRO A1046 6427 7207 6673 -83 -427 -766 O
ATOM 1995 CB PRO A1046 34.972 -14.434 13.638 1.00 48.63 C
ANISOU 1995 CB PRO A1046 6127 5983 6365 -193 -320 -551 C
ATOM 1996 CG PRO A1046 36.225 -15.186 13.939 1.00 52.33 C
ANISOU 1996 CG PRO A1046 6694 6267 6920 -260 -266 -520 C
ATOM 1997 CD PRO A1046 36.790 -15.537 12.592 1.00 48.46 C
ANISOU 1997 CD PRO A1046 6217 5818 6378 -245 -263 -541 C
ATOM 1998 N LYS A1047 34.100 -13.394 10.666 1.00 47.64 N
ANISOU 1998 N LYS A1047 5872 6294 5936 74 -412 -573 N
ATOM 1999 CA LYS A1047 33.338 -12.472 9.813 1.00 47.80 C
ANISOU 1999 CA LYS A1047 5829 6542 5792 275 -455 -542 C
ATOM 2000 C LYS A1047 32.481 -13.198 8.760 1.00 53.57 C
ANISOU 2000 C LYS A1047 6398 7580 6377 262 -503 -708 C
ATOM 2001 O LYS A1047 31.529 -12.603 8.243 1.00 54.76 O
ANISOU 2001 O LYS A1047 6440 8004 6364 429 -552 -722 O
ATOM 2002 CB LYS A1047 34.268 -11.490 9.105 1.00 48.65 C
ANISOU 2002 CB LYS A1047 6069 6547 5868 434 -421 -380 C
ATOM 2003 CG LYS A1047 34.821 -10.421 10.019 1.00 51.74 C
ANISOU 2003 CG LYS A1047 6595 6714 6351 482 -367 -237 C
ATOM 2004 CD LYS A1047 35.566 -9.393 9.218 1.00 50.94 C
ANISOU 2004 CD LYS A1047 6628 6530 6198 633 -302 -95 C
ATOM 2005 CE LYS A1047 36.573 -8.714 10.078 1.00 52.17 C
ANISOU 2005 CE LYS A1047 6921 6412 6491 564 -223 -6 C
ATOM 2006 NZ LYS A1047 37.177 -7.565 9.370 1.00 71.05 N
ANISOU 2006 NZ LYS A1047 9463 8699 8834 694 -121 127 N
ATOM 2007 N LEU A1048 32.808 -14.465 8.438 1.00 49.76 N
ANISOU 2007 N LEU A1048 5899 7070 5937 75 -480 -841 N
ATOM 2008 CA LEU A1048 32.066 -15.213 7.416 1.00 51.24 C
ANISOU 2008 CA LEU A1048 5933 7547 5986 23 -513 -1035 C
ATOM 2009 C LEU A1048 31.114 -16.275 7.999 1.00 56.65 C
ANISOU 2009 C LEU A1048 6497 8320 6708 -215 -487 -1253 C
ATOM 2010 O LEU A1048 30.348 -16.875 7.247 1.00 57.82 O
ANISOU 2010 O LEU A1048 6490 8741 6739 -298 -505 -1457 O
ATOM 2011 CB LEU A1048 33.044 -15.864 6.420 1.00 51.02 C
ANISOU 2011 CB LEU A1048 5981 7449 5954 -17 -485 -1057 C
ATOM 2012 CG LEU A1048 33.885 -14.918 5.565 1.00 54.55 C
ANISOU 2012 CG LEU A1048 6526 7865 6334 203 -494 -876 C
ATOM 2013 CD1 LEU A1048 34.826 -15.695 4.708 1.00 54.68 C
ANISOU 2013 CD1 LEU A1048 6610 7806 6360 137 -459 -912 C
ATOM 2014 CD2 LEU A1048 33.015 -14.012 4.698 1.00 56.94 C
ANISOU 2014 CD2 LEU A1048 6724 8494 6419 446 -559 -854 C
ATOM 2015 N GLU A1049 31.141 -16.472 9.328 1.00 53.58 N
ANISOU 2015 N GLU A1049 6174 7716 6470 -327 -435 -1218 N
ATOM 2016 CA GLU A1049 30.319 -17.420 10.088 1.00 54.55 C
ANISOU 2016 CA GLU A1049 6223 7852 6651 -559 -373 -1392 C
ATOM 2017 C GLU A1049 28.840 -17.451 9.708 1.00 61.73 C
ANISOU 2017 C GLU A1049 6884 9161 7409 -597 -419 -1594 C
ATOM 2018 O GLU A1049 28.298 -18.538 9.487 1.00 63.47 O
ANISOU 2018 O GLU A1049 7016 9480 7618 -831 -357 -1827 O
ATOM 2019 CB GLU A1049 30.379 -17.063 11.561 1.00 54.62 C
ANISOU 2019 CB GLU A1049 6315 7650 6788 -562 -342 -1270 C
ATOM 2020 CG GLU A1049 31.419 -17.809 12.355 1.00 64.65 C
ANISOU 2020 CG GLU A1049 7780 8562 8220 -663 -247 -1194 C
ATOM 2021 CD GLU A1049 31.601 -17.177 13.718 1.00 76.20 C
ANISOU 2021 CD GLU A1049 9313 9862 9776 -610 -241 -1054 C
ATOM 2022 OE1 GLU A1049 32.720 -17.284 14.267 1.00 74.45 O
ANISOU 2022 OE1 GLU A1049 9242 9391 9653 -595 -200 -936 O
ATOM 2023 OE2 GLU A1049 30.657 -16.507 14.200 1.00 55.61 O
ANISOU 2023 OE2 GLU A1049 6600 7401 7130 -563 -282 -1063 O
ATOM 2024 N ASP A1050 28.175 -16.278 9.708 1.00 58.94 N
ANISOU 2024 N ASP A1050 6420 9036 6937 -373 -510 -1514 N
ATOM 2025 CA ASP A1050 26.735 -16.182 9.447 1.00 61.23 C
ANISOU 2025 CA ASP A1050 6445 9760 7060 -364 -564 -1694 C
ATOM 2026 C ASP A1050 26.455 -15.684 8.018 1.00 66.29 C
ANISOU 2026 C ASP A1050 6949 10771 7464 -144 -661 -1725 C
ATOM 2027 O ASP A1050 25.439 -15.032 7.770 1.00 67.69 O
ANISOU 2027 O ASP A1050 6932 11330 7456 35 -736 -1763 O
ATOM 2028 CB ASP A1050 26.055 -15.278 10.504 1.00 63.15 C
ANISOU 2028 CB ASP A1050 6645 10040 7308 -241 -588 -1593 C
ATOM 2029 CG ASP A1050 26.335 -15.660 11.953 1.00 74.27 C
ANISOU 2029 CG ASP A1050 8189 11100 8928 -420 -497 -1544 C
ATOM 2030 OD1 ASP A1050 26.064 -16.830 12.328 1.00 75.49 O
ANISOU 2030 OD1 ASP A1050 8319 11201 9165 -706 -405 -1719 O
ATOM 2031 OD2 ASP A1050 26.808 -14.787 12.716 1.00 79.44 O
ANISOU 2031 OD2 ASP A1050 8983 11542 9659 -274 -504 -1336 O
ATOM 2032 N LYS A1051 27.344 -16.030 7.077 1.00 62.24 N
ANISOU 2032 N LYS A1051 6536 10170 6944 -143 -653 -1712 N
ATOM 2033 CA LYS A1051 27.208 -15.654 5.674 1.00 63.29 C
ANISOU 2033 CA LYS A1051 6565 10633 6850 67 -732 -1735 C
ATOM 2034 C LYS A1051 26.832 -16.866 4.844 1.00 70.07 C
ANISOU 2034 C LYS A1051 7264 11734 7626 -165 -723 -2041 C
ATOM 2035 O LYS A1051 27.331 -17.966 5.093 1.00 69.67 O
ANISOU 2035 O LYS A1051 7315 11423 7735 -454 -627 -2150 O
ATOM 2036 CB LYS A1051 28.497 -15.002 5.133 1.00 63.18 C
ANISOU 2036 CB LYS A1051 6782 10361 6863 267 -724 -1486 C
ATOM 2037 CG LYS A1051 28.842 -13.677 5.800 1.00 67.60 C
ANISOU 2037 CG LYS A1051 7498 10712 7474 503 -717 -1205 C
ATOM 2038 CD LYS A1051 28.146 -12.479 5.162 1.00 70.97 C
ANISOU 2038 CD LYS A1051 7849 11457 7660 869 -776 -1102 C
ATOM 2039 CE LYS A1051 28.427 -11.222 5.947 1.00 73.20 C
ANISOU 2039 CE LYS A1051 8316 11487 8011 1064 -733 -847 C
ATOM 2040 NZ LYS A1051 27.983 -10.003 5.223 1.00 80.90 N
ANISOU 2040 NZ LYS A1051 9293 12698 8749 1462 -749 -703 N
ATOM 2041 N SER A1052 25.936 -16.656 3.868 1.00 69.25 N
ANISOU 2041 N SER A1052 6913 12141 7257 -25 -813 -2186 N
ATOM 2042 CA SER A1052 25.445 -17.664 2.931 1.00 71.58 C
ANISOU 2042 CA SER A1052 7007 12773 7418 -220 -821 -2512 C
ATOM 2043 C SER A1052 26.610 -18.226 2.088 1.00 74.37 C
ANISOU 2043 C SER A1052 7543 12893 7822 -275 -778 -2493 C
ATOM 2044 O SER A1052 27.522 -17.463 1.774 1.00 72.37 O
ANISOU 2044 O SER A1052 7473 12447 7575 -24 -798 -2223 O
ATOM 2045 CB SER A1052 24.378 -17.044 2.029 1.00 78.21 C
ANISOU 2045 CB SER A1052 7549 14243 7925 45 -949 -2613 C
ATOM 2046 OG SER A1052 24.079 -17.845 0.897 1.00 91.25 O
ANISOU 2046 OG SER A1052 9006 16261 9405 -89 -973 -2916 O
ATOM 2047 N PRO A1053 26.613 -19.533 1.709 1.00 72.07 N
ANISOU 2047 N PRO A1053 7215 12605 7565 -603 -703 -2776 N
ATOM 2048 CA PRO A1053 27.732 -20.067 0.902 1.00 71.21 C
ANISOU 2048 CA PRO A1053 7287 12275 7495 -635 -657 -2754 C
ATOM 2049 C PRO A1053 27.905 -19.370 -0.453 1.00 75.78 C
ANISOU 2049 C PRO A1053 7798 13169 7827 -316 -767 -2684 C
ATOM 2050 O PRO A1053 29.035 -19.236 -0.923 1.00 73.73 O
ANISOU 2050 O PRO A1053 7742 12658 7615 -206 -745 -2507 O
ATOM 2051 CB PRO A1053 27.358 -21.540 0.703 1.00 74.92 C
ANISOU 2051 CB PRO A1053 7685 12787 7995 -1040 -549 -3125 C
ATOM 2052 CG PRO A1053 26.396 -21.850 1.796 1.00 79.98 C
ANISOU 2052 CG PRO A1053 8214 13454 8722 -1269 -489 -3266 C
ATOM 2053 CD PRO A1053 25.625 -20.589 2.012 1.00 75.71 C
ANISOU 2053 CD PRO A1053 7487 13245 8033 -971 -632 -3135 C
ATOM 2054 N ASP A1054 26.796 -18.920 -1.074 1.00 75.13 N
ANISOU 2054 N ASP A1054 7427 13649 7469 -152 -879 -2816 N
ATOM 2055 CA ASP A1054 26.836 -18.232 -2.364 1.00 76.62 C
ANISOU 2055 CA ASP A1054 7540 14192 7381 195 -979 -2747 C
ATOM 2056 C ASP A1054 26.734 -16.692 -2.196 1.00 79.17 C
ANISOU 2056 C ASP A1054 7911 14571 7601 636 -1044 -2413 C
ATOM 2057 O ASP A1054 26.387 -15.992 -3.146 1.00 81.02 O
ANISOU 2057 O ASP A1054 8037 15194 7551 979 -1125 -2360 O
ATOM 2058 CB ASP A1054 25.745 -18.778 -3.316 1.00 82.50 C
ANISOU 2058 CB ASP A1054 7931 15577 7840 126 -1055 -3126 C
ATOM 2059 CG ASP A1054 24.305 -18.561 -2.884 1.00 97.14 C
ANISOU 2059 CG ASP A1054 9465 17895 9547 126 -1122 -3303 C
ATOM 2060 OD1 ASP A1054 24.059 -18.421 -1.657 1.00 95.40 O
ANISOU 2060 OD1 ASP A1054 9296 17439 9514 22 -1076 -3223 O
ATOM 2061 OD2 ASP A1054 23.415 -18.578 -3.764 1.00107.75 O
ANISOU 2061 OD2 ASP A1054 10493 19866 10581 223 -1219 -3540 O
ATOM 2062 N SER A1055 27.077 -16.168 -1.005 1.00 72.54 N
ANISOU 2062 N SER A1055 7252 13328 6981 640 -993 -2184 N
ATOM 2063 CA SER A1055 27.092 -14.723 -0.759 1.00 71.14 C
ANISOU 2063 CA SER A1055 7178 13111 6742 1025 -1014 -1866 C
ATOM 2064 C SER A1055 28.392 -14.132 -1.349 1.00 74.53 C
ANISOU 2064 C SER A1055 7887 13227 7205 1225 -963 -1586 C
ATOM 2065 O SER A1055 29.398 -14.853 -1.381 1.00 72.67 O
ANISOU 2065 O SER A1055 7802 12660 7151 1004 -901 -1598 O
ATOM 2066 CB SER A1055 26.968 -14.416 0.732 1.00 70.06 C
ANISOU 2066 CB SER A1055 7128 12668 6824 928 -970 -1757 C
ATOM 2067 OG SER A1055 28.113 -14.823 1.463 1.00 70.37 O
ANISOU 2067 OG SER A1055 7420 12153 7163 704 -876 -1651 O
ATOM 2068 N PRO A1056 28.408 -12.855 -1.832 1.00 71.75 N
ANISOU 2068 N PRO A1056 7616 12970 6677 1642 -970 -1335 N
ATOM 2069 CA PRO A1056 29.652 -12.301 -2.417 1.00 69.90 C
ANISOU 2069 CA PRO A1056 7651 12431 6477 1803 -892 -1081 C
ATOM 2070 C PRO A1056 30.860 -12.294 -1.462 1.00 68.66 C
ANISOU 2070 C PRO A1056 7759 11674 6656 1597 -789 -921 C
ATOM 2071 O PRO A1056 31.982 -12.472 -1.928 1.00 67.62 O
ANISOU 2071 O PRO A1056 7786 11301 6604 1550 -730 -841 O
ATOM 2072 CB PRO A1056 29.262 -10.872 -2.820 1.00 73.28 C
ANISOU 2072 CB PRO A1056 8138 13034 6670 2276 -880 -840 C
ATOM 2073 CG PRO A1056 28.000 -10.575 -2.075 1.00 79.02 C
ANISOU 2073 CG PRO A1056 8683 14018 7323 2343 -940 -910 C
ATOM 2074 CD PRO A1056 27.296 -11.882 -1.913 1.00 75.15 C
ANISOU 2074 CD PRO A1056 7906 13794 6853 1997 -1027 -1272 C
ATOM 2075 N GLU A1057 30.637 -12.125 -0.147 1.00 62.42 N
ANISOU 2075 N GLU A1057 6997 10675 6043 1476 -771 -888 N
ATOM 2076 CA GLU A1057 31.690 -12.123 0.881 1.00 58.85 C
ANISOU 2076 CA GLU A1057 6759 9712 5888 1284 -686 -761 C
ATOM 2077 C GLU A1057 32.410 -13.472 0.910 1.00 63.11 C
ANISOU 2077 C GLU A1057 7314 10073 6594 957 -666 -915 C
ATOM 2078 O GLU A1057 33.643 -13.515 0.908 1.00 61.73 O
ANISOU 2078 O GLU A1057 7319 9579 6557 901 -597 -795 O
ATOM 2079 CB GLU A1057 31.116 -11.798 2.274 1.00 58.84 C
ANISOU 2079 CB GLU A1057 6742 9605 6011 1217 -685 -743 C
ATOM 2080 CG GLU A1057 30.489 -10.419 2.396 1.00 68.38 C
ANISOU 2080 CG GLU A1057 7980 10922 7078 1548 -679 -570 C
ATOM 2081 CD GLU A1057 29.007 -10.293 2.085 1.00 93.28 C
ANISOU 2081 CD GLU A1057 10882 14578 9981 1724 -771 -696 C
ATOM 2082 OE1 GLU A1057 28.465 -11.123 1.318 1.00 82.89 O
ANISOU 2082 OE1 GLU A1057 9348 13622 8524 1653 -847 -919 O
ATOM 2083 OE2 GLU A1057 28.392 -9.328 2.592 1.00 95.26 O
ANISOU 2083 OE2 GLU A1057 11149 14881 10162 1946 -760 -577 O
ATOM 2084 N MET A1058 31.635 -14.570 0.904 1.00 61.56 N
ANISOU 2084 N MET A1058 6928 10093 6370 745 -711 -1187 N
ATOM 2085 CA MET A1058 32.148 -15.940 0.881 1.00 61.19 C
ANISOU 2085 CA MET A1058 6903 9893 6453 441 -667 -1360 C
ATOM 2086 C MET A1058 32.866 -16.233 -0.438 1.00 62.55 C
ANISOU 2086 C MET A1058 7121 10122 6522 507 -660 -1370 C
ATOM 2087 O MET A1058 33.929 -16.845 -0.420 1.00 60.09 O
ANISOU 2087 O MET A1058 6960 9517 6356 378 -592 -1340 O
ATOM 2088 CB MET A1058 31.007 -16.948 1.097 1.00 65.68 C
ANISOU 2088 CB MET A1058 7262 10703 6989 198 -687 -1669 C
ATOM 2089 CG MET A1058 30.658 -17.148 2.552 1.00 69.28 C
ANISOU 2089 CG MET A1058 7734 10958 7632 15 -645 -1682 C
ATOM 2090 SD MET A1058 31.774 -18.285 3.399 1.00 72.49 S
ANISOU 2090 SD MET A1058 8358 10868 8317 -280 -514 -1687 S
ATOM 2091 CE MET A1058 30.701 -18.876 4.674 1.00 69.64 C
ANISOU 2091 CE MET A1058 7900 10506 8054 -526 -468 -1851 C
ATOM 2092 N LYS A1059 32.301 -15.761 -1.567 1.00 59.75 N
ANISOU 2092 N LYS A1059 6639 10160 5903 737 -729 -1401 N
ATOM 2093 CA LYS A1059 32.834 -15.953 -2.918 1.00 59.84 C
ANISOU 2093 CA LYS A1059 6669 10299 5767 842 -732 -1418 C
ATOM 2094 C LYS A1059 34.175 -15.235 -3.125 1.00 59.68 C
ANISOU 2094 C LYS A1059 6895 9954 5828 996 -657 -1128 C
ATOM 2095 O LYS A1059 35.110 -15.861 -3.627 1.00 58.18 O
ANISOU 2095 O LYS A1059 6797 9614 5695 902 -611 -1146 O
ATOM 2096 CB LYS A1059 31.819 -15.494 -3.974 1.00 65.56 C
ANISOU 2096 CB LYS A1059 7188 11562 6160 1103 -826 -1498 C
ATOM 2097 CG LYS A1059 30.637 -16.446 -4.146 1.00 84.20 C
ANISOU 2097 CG LYS A1059 9265 14327 8400 905 -895 -1864 C
ATOM 2098 CD LYS A1059 30.132 -16.451 -5.591 1.00100.31 C
ANISOU 2098 CD LYS A1059 11119 16887 10106 1101 -976 -2004 C
ATOM 2099 CE LYS A1059 28.895 -15.608 -5.805 1.00115.26 C
ANISOU 2099 CE LYS A1059 12794 19284 11715 1413 -1074 -2001 C
ATOM 2100 NZ LYS A1059 27.648 -16.387 -5.583 1.00125.18 N
ANISOU 2100 NZ LYS A1059 13733 20941 12888 1187 -1140 -2360 N
ATOM 2101 N ASP A1060 34.273 -13.940 -2.733 1.00 54.72 N
ANISOU 2101 N ASP A1060 6374 9214 5203 1218 -630 -876 N
ATOM 2102 CA ASP A1060 35.495 -13.124 -2.856 1.00 52.95 C
ANISOU 2102 CA ASP A1060 6383 8679 5056 1342 -531 -610 C
ATOM 2103 C ASP A1060 36.627 -13.694 -2.008 1.00 52.36 C
ANISOU 2103 C ASP A1060 6436 8195 5261 1078 -464 -588 C
ATOM 2104 O ASP A1060 37.782 -13.643 -2.427 1.00 51.78 O
ANISOU 2104 O ASP A1060 6495 7938 5241 1084 -394 -483 O
ATOM 2105 CB ASP A1060 35.238 -11.657 -2.449 1.00 55.40 C
ANISOU 2105 CB ASP A1060 6793 8928 5327 1591 -487 -380 C
ATOM 2106 CG ASP A1060 34.343 -10.846 -3.376 1.00 72.11 C
ANISOU 2106 CG ASP A1060 8844 11419 7136 1954 -518 -321 C
ATOM 2107 OD1 ASP A1060 34.015 -11.344 -4.484 1.00 75.01 O
ANISOU 2107 OD1 ASP A1060 9082 12122 7295 2039 -580 -446 O
ATOM 2108 OD2 ASP A1060 33.981 -9.707 -3.000 1.00 78.60 O
ANISOU 2108 OD2 ASP A1060 9748 12206 7910 2171 -473 -151 O
ATOM 2109 N PHE A1061 36.294 -14.244 -0.824 1.00 45.71 N
ANISOU 2109 N PHE A1061 5548 7236 4582 862 -482 -688 N
ATOM 2110 CA PHE A1061 37.262 -14.863 0.066 1.00 43.00 C
ANISOU 2110 CA PHE A1061 5309 6550 4477 640 -423 -677 C
ATOM 2111 C PHE A1061 37.900 -16.089 -0.606 1.00 47.39 C
ANISOU 2111 C PHE A1061 5876 7083 5046 503 -400 -808 C
ATOM 2112 O PHE A1061 39.122 -16.178 -0.646 1.00 46.11 O
ANISOU 2112 O PHE A1061 5838 6697 4982 479 -334 -708 O
ATOM 2113 CB PHE A1061 36.613 -15.240 1.408 1.00 43.52 C
ANISOU 2113 CB PHE A1061 5320 6542 4675 468 -441 -764 C
ATOM 2114 CG PHE A1061 37.567 -15.783 2.450 1.00 42.25 C
ANISOU 2114 CG PHE A1061 5271 6046 4735 290 -378 -728 C
ATOM 2115 CD1 PHE A1061 38.412 -14.930 3.157 1.00 42.58 C
ANISOU 2115 CD1 PHE A1061 5429 5858 4890 338 -333 -540 C
ATOM 2116 CD2 PHE A1061 37.597 -17.142 2.749 1.00 43.30 C
ANISOU 2116 CD2 PHE A1061 5397 6105 4950 82 -348 -889 C
ATOM 2117 CE1 PHE A1061 39.269 -15.427 4.144 1.00 41.62 C
ANISOU 2117 CE1 PHE A1061 5383 5489 4943 199 -286 -516 C
ATOM 2118 CE2 PHE A1061 38.459 -17.639 3.739 1.00 44.49 C
ANISOU 2118 CE2 PHE A1061 5656 5971 5275 -31 -283 -837 C
ATOM 2119 CZ PHE A1061 39.290 -16.777 4.427 1.00 40.56 C
ANISOU 2119 CZ PHE A1061 5241 5299 4871 38 -265 -653 C
ATOM 2120 N ARG A1062 37.087 -16.995 -1.170 1.00 46.17 N
ANISOU 2120 N ARG A1062 5589 7172 4781 418 -443 -1039 N
ATOM 2121 CA ARG A1062 37.589 -18.202 -1.842 1.00 47.15 C
ANISOU 2121 CA ARG A1062 5735 7275 4904 282 -405 -1191 C
ATOM 2122 C ARG A1062 38.357 -17.860 -3.126 1.00 52.33 C
ANISOU 2122 C ARG A1062 6447 8002 5434 460 -395 -1096 C
ATOM 2123 O ARG A1062 39.415 -18.454 -3.353 1.00 51.19 O
ANISOU 2123 O ARG A1062 6412 7672 5368 397 -329 -1078 O
ATOM 2124 CB ARG A1062 36.457 -19.185 -2.173 1.00 49.77 C
ANISOU 2124 CB ARG A1062 5905 7871 5135 123 -438 -1495 C
ATOM 2125 CG ARG A1062 35.431 -19.369 -1.078 1.00 62.38 C
ANISOU 2125 CG ARG A1062 7410 9481 6809 -32 -448 -1603 C
ATOM 2126 CD ARG A1062 35.492 -20.738 -0.482 1.00 75.18 C
ANISOU 2126 CD ARG A1062 9094 10892 8579 -325 -349 -1780 C
ATOM 2127 NE ARG A1062 36.207 -20.769 0.793 1.00 85.71 N
ANISOU 2127 NE ARG A1062 10585 11852 10129 -378 -281 -1618 N
ATOM 2128 CZ ARG A1062 35.626 -20.652 1.983 1.00 97.78 C
ANISOU 2128 CZ ARG A1062 12088 13308 11754 -465 -273 -1616 C
ATOM 2129 NH1 ARG A1062 34.316 -20.453 2.072 1.00 90.01 N
ANISOU 2129 NH1 ARG A1062 10923 12597 10679 -510 -328 -1761 N
ATOM 2130 NH2 ARG A1062 36.351 -20.717 3.091 1.00 77.32 N
ANISOU 2130 NH2 ARG A1062 9640 10400 9338 -494 -211 -1472 N
ATOM 2131 N HIS A1063 37.827 -16.904 -3.948 1.00 50.86 N
ANISOU 2131 N HIS A1063 6192 8089 5042 703 -449 -1026 N
ATOM 2132 CA AHIS A1063 38.448 -16.484 -5.209 0.50 51.78 C
ANISOU 2132 CA AHIS A1063 6366 8300 5009 905 -429 -921 C
ATOM 2133 CA BHIS A1063 38.442 -16.479 -5.209 0.50 51.39 C
ANISOU 2133 CA BHIS A1063 6315 8252 4958 906 -429 -921 C
ATOM 2134 C HIS A1063 39.793 -15.799 -4.972 1.00 53.16 C
ANISOU 2134 C HIS A1063 6730 8149 5320 962 -332 -667 C
ATOM 2135 O HIS A1063 40.716 -15.987 -5.764 1.00 54.01 O
ANISOU 2135 O HIS A1063 6913 8207 5401 999 -280 -621 O
ATOM 2136 CB AHIS A1063 37.516 -15.569 -6.027 0.50 54.90 C
ANISOU 2136 CB AHIS A1063 6661 9062 5135 1190 -492 -881 C
ATOM 2137 CB BHIS A1063 37.502 -15.555 -6.008 0.50 54.10 C
ANISOU 2137 CB BHIS A1063 6559 8962 5036 1190 -493 -881 C
ATOM 2138 CG AHIS A1063 36.249 -16.232 -6.478 0.50 60.53 C
ANISOU 2138 CG AHIS A1063 7144 10189 5663 1152 -593 -1158 C
ATOM 2139 CG BHIS A1063 38.007 -15.211 -7.378 0.50 58.65 C
ANISOU 2139 CG BHIS A1063 7186 9678 5420 1417 -467 -789 C
ATOM 2140 ND1AHIS A1063 35.031 -15.580 -6.398 0.50 63.82 N
ANISOU 2140 ND1AHIS A1063 7411 10921 5915 1315 -670 -1177 N
ATOM 2141 ND1BHIS A1063 38.342 -16.194 -8.293 0.50 61.16 N
ANISOU 2141 ND1BHIS A1063 7465 10113 5659 1343 -475 -954 N
ATOM 2142 CD2AHIS A1063 36.045 -17.478 -6.968 0.50 63.47 C
ANISOU 2142 CD2AHIS A1063 7413 10711 5992 957 -616 -1437 C
ATOM 2143 CD2BHIS A1063 38.213 -14.000 -7.943 0.50 61.13 C
ANISOU 2143 CD2BHIS A1063 7602 10020 5603 1716 -415 -549 C
ATOM 2144 CE1AHIS A1063 34.132 -16.440 -6.851 0.50 65.14 C
ANISOU 2144 CE1AHIS A1063 7361 11450 5938 1206 -746 -1476 C
ATOM 2145 CE1BHIS A1063 38.749 -15.553 -9.375 0.50 61.79 C
ANISOU 2145 CE1BHIS A1063 7610 10304 5563 1601 -443 -806 C
ATOM 2146 NE2AHIS A1063 34.694 -17.596 -7.202 0.50 65.39 N
ANISOU 2146 NE2AHIS A1063 7421 11383 6043 975 -710 -1649 N
ATOM 2147 NE2BHIS A1063 38.688 -14.231 -9.213 0.50 62.20 N
ANISOU 2147 NE2BHIS A1063 7756 10300 5577 1833 -398 -556 N
ATOM 2148 N GLY A1064 39.904 -15.040 -3.883 1.00 47.10 N
ANISOU 2148 N GLY A1064 6027 7174 4693 952 -303 -524 N
ATOM 2149 CA GLY A1064 41.146 -14.369 -3.514 1.00 45.63 C
ANISOU 2149 CA GLY A1064 5997 6694 4647 960 -203 -320 C
ATOM 2150 C GLY A1064 42.275 -15.371 -3.334 1.00 49.73 C
ANISOU 2150 C GLY A1064 6563 7021 5310 783 -158 -369 C
ATOM 2151 O GLY A1064 43.407 -15.128 -3.765 1.00 48.88 O
ANISOU 2151 O GLY A1064 6544 6804 5223 822 -80 -255 O
ATOM 2152 N PHE A1065 41.960 -16.534 -2.733 1.00 46.64 N
ANISOU 2152 N PHE A1065 6117 6598 5005 598 -193 -542 N
ATOM 2153 CA PHE A1065 42.925 -17.610 -2.554 1.00 46.26 C
ANISOU 2153 CA PHE A1065 6128 6380 5070 465 -139 -595 C
ATOM 2154 C PHE A1065 43.217 -18.326 -3.870 1.00 52.45 C
ANISOU 2154 C PHE A1065 6913 7289 5726 501 -125 -687 C
ATOM 2155 O PHE A1065 44.343 -18.767 -4.061 1.00 53.09 O
ANISOU 2155 O PHE A1065 7071 7241 5860 488 -59 -645 O
ATOM 2156 CB PHE A1065 42.455 -18.605 -1.493 1.00 47.43 C
ANISOU 2156 CB PHE A1065 6257 6426 5337 278 -144 -735 C
ATOM 2157 CG PHE A1065 42.648 -18.085 -0.097 1.00 47.35 C
ANISOU 2157 CG PHE A1065 6276 6233 5481 235 -134 -624 C
ATOM 2158 CD1 PHE A1065 43.922 -18.003 0.463 1.00 49.23 C
ANISOU 2158 CD1 PHE A1065 6591 6278 5836 225 -74 -506 C
ATOM 2159 CD2 PHE A1065 41.565 -17.634 0.651 1.00 49.02 C
ANISOU 2159 CD2 PHE A1065 6422 6498 5705 213 -187 -646 C
ATOM 2160 CE1 PHE A1065 44.104 -17.492 1.748 1.00 48.70 C
ANISOU 2160 CE1 PHE A1065 6534 6077 5892 186 -69 -423 C
ATOM 2161 CE2 PHE A1065 41.749 -17.110 1.931 1.00 50.15 C
ANISOU 2161 CE2 PHE A1065 6594 6480 5980 179 -177 -549 C
ATOM 2162 CZ PHE A1065 43.015 -17.045 2.474 1.00 47.35 C
ANISOU 2162 CZ PHE A1065 6315 5938 5737 162 -120 -443 C
ATOM 2163 N ASP A1066 42.234 -18.423 -4.784 1.00 50.85 N
ANISOU 2163 N ASP A1066 6617 7361 5343 558 -187 -818 N
ATOM 2164 CA ASP A1066 42.414 -19.055 -6.102 1.00 52.06 C
ANISOU 2164 CA ASP A1066 6759 7675 5347 600 -181 -927 C
ATOM 2165 C ASP A1066 43.418 -18.283 -6.950 1.00 55.92 C
ANISOU 2165 C ASP A1066 7328 8152 5768 785 -130 -732 C
ATOM 2166 O ASP A1066 44.169 -18.898 -7.705 1.00 57.36 O
ANISOU 2166 O ASP A1066 7556 8325 5913 789 -85 -766 O
ATOM 2167 CB ASP A1066 41.080 -19.165 -6.859 1.00 55.96 C
ANISOU 2167 CB ASP A1066 7101 8529 5632 640 -270 -1115 C
ATOM 2168 CG ASP A1066 40.143 -20.232 -6.334 1.00 71.33 C
ANISOU 2168 CG ASP A1066 8959 10523 7621 406 -291 -1381 C
ATOM 2169 OD1 ASP A1066 40.626 -21.342 -6.011 1.00 71.93 O
ANISOU 2169 OD1 ASP A1066 9118 10391 7819 224 -215 -1486 O
ATOM 2170 OD2 ASP A1066 38.917 -19.978 -6.297 1.00 82.93 O
ANISOU 2170 OD2 ASP A1066 10278 12247 8986 413 -369 -1491 O
ATOM 2171 N ILE A1067 43.435 -16.945 -6.823 1.00 51.04 N
ANISOU 2171 N ILE A1067 6742 7520 5133 933 -117 -529 N
ATOM 2172 CA ILE A1067 44.363 -16.089 -7.559 1.00 51.01 C
ANISOU 2172 CA ILE A1067 6835 7474 5072 1094 -32 -331 C
ATOM 2173 C ILE A1067 45.790 -16.301 -7.016 1.00 54.70 C
ANISOU 2173 C ILE A1067 7388 7668 5728 977 60 -247 C
ATOM 2174 O ILE A1067 46.712 -16.459 -7.812 1.00 55.60 O
ANISOU 2174 O ILE A1067 7550 7774 5800 1025 126 -201 O
ATOM 2175 CB ILE A1067 43.923 -14.591 -7.523 1.00 54.15 C
ANISOU 2175 CB ILE A1067 7276 7902 5398 1280 -5 -144 C
ATOM 2176 CG1 ILE A1067 42.537 -14.403 -8.189 1.00 56.09 C
ANISOU 2176 CG1 ILE A1067 7417 8488 5409 1454 -99 -224 C
ATOM 2177 CG2 ILE A1067 44.976 -13.681 -8.187 1.00 54.18 C
ANISOU 2177 CG2 ILE A1067 7417 7803 5368 1413 132 69 C
ATOM 2178 CD1 ILE A1067 41.744 -13.189 -7.714 1.00 64.15 C
ANISOU 2178 CD1 ILE A1067 8454 9533 6386 1605 -99 -94 C
ATOM 2179 N LEU A1068 45.961 -16.333 -5.676 1.00 50.37 N
ANISOU 2179 N LEU A1068 6843 6927 5369 835 61 -234 N
ATOM 2180 CA LEU A1068 47.269 -16.496 -5.029 1.00 48.74 C
ANISOU 2180 CA LEU A1068 6684 6513 5322 739 136 -166 C
ATOM 2181 C LEU A1068 47.824 -17.921 -5.195 1.00 53.17 C
ANISOU 2181 C LEU A1068 7247 7048 5907 664 145 -292 C
ATOM 2182 O LEU A1068 49.021 -18.063 -5.469 1.00 51.97 O
ANISOU 2182 O LEU A1068 7129 6837 5778 680 218 -230 O
ATOM 2183 CB LEU A1068 47.222 -16.100 -3.540 1.00 47.19 C
ANISOU 2183 CB LEU A1068 6481 6160 5290 633 129 -126 C
ATOM 2184 CG LEU A1068 46.772 -14.669 -3.204 1.00 51.63 C
ANISOU 2184 CG LEU A1068 7070 6697 5850 696 147 0 C
ATOM 2185 CD1 LEU A1068 46.911 -14.388 -1.721 1.00 50.30 C
ANISOU 2185 CD1 LEU A1068 6894 6370 5848 574 147 21 C
ATOM 2186 CD2 LEU A1068 47.517 -13.612 -4.024 1.00 54.14 C
ANISOU 2186 CD2 LEU A1068 7471 6994 6105 803 263 158 C
ATOM 2187 N VAL A1069 46.967 -18.967 -5.046 1.00 51.41 N
ANISOU 2187 N VAL A1069 6993 6868 5671 582 89 -473 N
ATOM 2188 CA VAL A1069 47.368 -20.375 -5.243 1.00 52.02 C
ANISOU 2188 CA VAL A1069 7111 6895 5759 514 126 -607 C
ATOM 2189 C VAL A1069 47.816 -20.551 -6.700 1.00 56.61 C
ANISOU 2189 C VAL A1069 7710 7607 6193 618 155 -623 C
ATOM 2190 O VAL A1069 48.855 -21.169 -6.939 1.00 56.88 O
ANISOU 2190 O VAL A1069 7802 7563 6247 632 225 -612 O
ATOM 2191 CB VAL A1069 46.279 -21.412 -4.829 1.00 56.36 C
ANISOU 2191 CB VAL A1069 7644 7446 6323 375 98 -815 C
ATOM 2192 CG1 VAL A1069 46.654 -22.831 -5.267 1.00 56.82 C
ANISOU 2192 CG1 VAL A1069 7783 7442 6365 317 172 -964 C
ATOM 2193 CG2 VAL A1069 46.044 -21.376 -3.323 1.00 54.73 C
ANISOU 2193 CG2 VAL A1069 7442 7080 6272 279 94 -784 C
ATOM 2194 N GLY A1070 47.073 -19.941 -7.630 1.00 53.54 N
ANISOU 2194 N GLY A1070 7269 7428 5643 717 103 -633 N
ATOM 2195 CA GLY A1070 47.381 -19.943 -9.056 1.00 54.42 C
ANISOU 2195 CA GLY A1070 7391 7702 5584 846 123 -636 C
ATOM 2196 C GLY A1070 48.764 -19.397 -9.368 1.00 57.93 C
ANISOU 2196 C GLY A1070 7901 8053 6055 934 217 -446 C
ATOM 2197 O GLY A1070 49.478 -19.959 -10.205 1.00 58.42 O
ANISOU 2197 O GLY A1070 7998 8148 6051 980 267 -471 O
ATOM 2198 N GLN A1071 49.165 -18.315 -8.677 1.00 53.01 N
ANISOU 2198 N GLN A1071 7294 7316 5533 941 254 -269 N
ATOM 2199 CA GLN A1071 50.479 -17.713 -8.869 1.00 53.03 C
ANISOU 2199 CA GLN A1071 7341 7233 5573 982 363 -106 C
ATOM 2200 C GLN A1071 51.578 -18.638 -8.315 1.00 57.22 C
ANISOU 2200 C GLN A1071 7873 7643 6225 893 406 -140 C
ATOM 2201 O GLN A1071 52.617 -18.793 -8.964 1.00 58.29 O
ANISOU 2201 O GLN A1071 8026 7795 6325 945 484 -92 O
ATOM 2202 CB GLN A1071 50.557 -16.308 -8.243 1.00 53.74 C
ANISOU 2202 CB GLN A1071 7452 7230 5737 981 411 58 C
ATOM 2203 CG GLN A1071 51.792 -15.511 -8.686 1.00 69.81 C
ANISOU 2203 CG GLN A1071 9538 9210 7778 1014 554 214 C
ATOM 2204 CD GLN A1071 51.951 -15.429 -10.196 1.00 85.05 C
ANISOU 2204 CD GLN A1071 11515 11277 9525 1172 608 256 C
ATOM 2205 OE1 GLN A1071 51.060 -14.969 -10.915 1.00 84.67 O
ANISOU 2205 OE1 GLN A1071 11497 11354 9321 1316 583 281 O
ATOM 2206 NE2 GLN A1071 53.091 -15.872 -10.709 1.00 69.88 N
ANISOU 2206 NE2 GLN A1071 9593 9358 7600 1168 684 267 N
ATOM 2207 N ILE A1072 51.330 -19.279 -7.147 1.00 51.87 N
ANISOU 2207 N ILE A1072 7180 6858 5670 783 364 -220 N
ATOM 2208 CA ILE A1072 52.257 -20.229 -6.525 1.00 50.54 C
ANISOU 2208 CA ILE A1072 7025 6586 5593 742 408 -248 C
ATOM 2209 C ILE A1072 52.436 -21.416 -7.476 1.00 55.85 C
ANISOU 2209 C ILE A1072 7750 7303 6167 792 438 -362 C
ATOM 2210 O ILE A1072 53.569 -21.844 -7.692 1.00 55.76 O
ANISOU 2210 O ILE A1072 7757 7275 6153 848 511 -326 O
ATOM 2211 CB ILE A1072 51.786 -20.665 -5.096 1.00 51.87 C
ANISOU 2211 CB ILE A1072 7188 6631 5888 641 368 -301 C
ATOM 2212 CG1 ILE A1072 51.917 -19.505 -4.079 1.00 50.58 C
ANISOU 2212 CG1 ILE A1072 6972 6419 5828 593 356 -185 C
ATOM 2213 CG2 ILE A1072 52.534 -21.925 -4.590 1.00 51.63 C
ANISOU 2213 CG2 ILE A1072 7206 6505 5906 648 425 -348 C
ATOM 2214 CD1 ILE A1072 50.920 -19.566 -2.885 1.00 49.85 C
ANISOU 2214 CD1 ILE A1072 6869 6251 5821 505 289 -236 C
ATOM 2215 N ASP A1073 51.323 -21.905 -8.067 1.00 54.57 N
ANISOU 2215 N ASP A1073 7603 7217 5913 772 386 -511 N
ATOM 2216 CA ASP A1073 51.284 -23.043 -9.003 1.00 56.54 C
ANISOU 2216 CA ASP A1073 7910 7515 6059 791 417 -664 C
ATOM 2217 C ASP A1073 52.129 -22.787 -10.245 1.00 62.54 C
ANISOU 2217 C ASP A1073 8677 8388 6698 923 466 -592 C
ATOM 2218 O ASP A1073 52.818 -23.702 -10.694 1.00 63.14 O
ANISOU 2218 O ASP A1073 8815 8434 6742 961 535 -646 O
ATOM 2219 CB ASP A1073 49.835 -23.393 -9.408 1.00 59.14 C
ANISOU 2219 CB ASP A1073 8212 7962 6295 718 346 -859 C
ATOM 2220 CG ASP A1073 49.027 -24.106 -8.329 1.00 64.14 C
ANISOU 2220 CG ASP A1073 8862 8471 7036 560 336 -990 C
ATOM 2221 OD1 ASP A1073 49.619 -24.490 -7.298 1.00 63.26 O
ANISOU 2221 OD1 ASP A1073 8812 8162 7061 528 392 -931 O
ATOM 2222 OD2 ASP A1073 47.801 -24.280 -8.520 1.00 67.45 O
ANISOU 2222 OD2 ASP A1073 9226 9010 7391 474 277 -1154 O
ATOM 2223 N ASP A1074 52.103 -21.545 -10.774 1.00 60.10 N
ANISOU 2223 N ASP A1074 8323 8194 6320 1004 450 -461 N
ATOM 2224 CA ASP A1074 52.895 -21.143 -11.937 1.00 61.27 C
ANISOU 2224 CA ASP A1074 8484 8445 6350 1134 515 -366 C
ATOM 2225 C ASP A1074 54.383 -21.154 -11.604 1.00 64.77 C
ANISOU 2225 C ASP A1074 8933 8790 6886 1143 613 -250 C
ATOM 2226 O ASP A1074 55.183 -21.589 -12.429 1.00 66.15 O
ANISOU 2226 O ASP A1074 9132 9018 6982 1224 680 -248 O
ATOM 2227 CB ASP A1074 52.480 -19.747 -12.442 1.00 63.85 C
ANISOU 2227 CB ASP A1074 8793 8879 6589 1226 509 -228 C
ATOM 2228 CG ASP A1074 51.069 -19.648 -12.982 1.00 77.61 C
ANISOU 2228 CG ASP A1074 10504 10801 8181 1280 411 -329 C
ATOM 2229 OD1 ASP A1074 50.508 -20.695 -13.376 1.00 79.99 O
ANISOU 2229 OD1 ASP A1074 10789 11199 8405 1246 359 -531 O
ATOM 2230 OD2 ASP A1074 50.526 -18.522 -13.016 1.00 85.21 O
ANISOU 2230 OD2 ASP A1074 11460 11821 9095 1360 399 -214 O
ATOM 2231 N ALA A1075 54.747 -20.684 -10.394 1.00 59.58 N
ANISOU 2231 N ALA A1075 8238 8019 6382 1063 621 -166 N
ATOM 2232 CA ALA A1075 56.128 -20.636 -9.913 1.00 58.48 C
ANISOU 2232 CA ALA A1075 8060 7835 6324 1059 704 -77 C
ATOM 2233 C ALA A1075 56.637 -22.040 -9.605 1.00 61.83 C
ANISOU 2233 C ALA A1075 8516 8209 6768 1086 724 -169 C
ATOM 2234 O ALA A1075 57.805 -22.331 -9.865 1.00 61.60 O
ANISOU 2234 O ALA A1075 8467 8222 6715 1159 802 -127 O
ATOM 2235 CB ALA A1075 56.226 -19.747 -8.682 1.00 57.92 C
ANISOU 2235 CB ALA A1075 7927 7687 6391 958 696 4 C
ATOM 2236 N LEU A1076 55.751 -22.913 -9.080 1.00 58.41 N
ANISOU 2236 N LEU A1076 8141 7685 6368 1035 671 -295 N
ATOM 2237 CA LEU A1076 56.049 -24.306 -8.730 1.00 58.94 C
ANISOU 2237 CA LEU A1076 8292 7654 6449 1067 719 -387 C
ATOM 2238 C LEU A1076 56.324 -25.135 -9.994 1.00 65.95 C
ANISOU 2238 C LEU A1076 9260 8594 7207 1156 779 -471 C
ATOM 2239 O LEU A1076 57.215 -25.987 -9.985 1.00 66.96 O
ANISOU 2239 O LEU A1076 9445 8677 7319 1250 864 -475 O
ATOM 2240 CB LEU A1076 54.886 -24.895 -7.915 1.00 58.34 C
ANISOU 2240 CB LEU A1076 8276 7450 6439 959 675 -505 C
ATOM 2241 CG LEU A1076 55.115 -26.184 -7.113 1.00 63.50 C
ANISOU 2241 CG LEU A1076 9046 7939 7142 980 753 -568 C
ATOM 2242 CD1 LEU A1076 56.431 -26.164 -6.324 1.00 63.71 C
ANISOU 2242 CD1 LEU A1076 9031 7961 7215 1093 804 -431 C
ATOM 2243 CD2 LEU A1076 53.962 -26.426 -6.159 1.00 64.81 C
ANISOU 2243 CD2 LEU A1076 9253 7981 7390 847 718 -657 C
ATOM 2244 N LYS A1077 55.589 -24.845 -11.088 1.00 63.09 N
ANISOU 2244 N LYS A1077 8895 8344 6733 1149 737 -533 N
ATOM 2245 CA LYS A1077 55.738 -25.483 -12.394 1.00 63.97 C
ANISOU 2245 CA LYS A1077 9068 8541 6698 1229 781 -625 C
ATOM 2246 C LYS A1077 57.132 -25.177 -12.949 1.00 67.88 C
ANISOU 2246 C LYS A1077 9531 9112 7149 1360 862 -485 C
ATOM 2247 O LYS A1077 57.782 -26.060 -13.519 1.00 68.56 O
ANISOU 2247 O LYS A1077 9686 9197 7167 1451 939 -536 O
ATOM 2248 CB LYS A1077 54.637 -24.985 -13.352 1.00 67.19 C
ANISOU 2248 CB LYS A1077 9441 9111 6976 1213 702 -703 C
ATOM 2249 CG LYS A1077 54.667 -25.639 -14.734 1.00 86.43 C
ANISOU 2249 CG LYS A1077 11930 11670 9240 1288 735 -828 C
ATOM 2250 CD LYS A1077 53.808 -24.883 -15.739 1.00 99.31 C
ANISOU 2250 CD LYS A1077 13496 13530 10708 1331 656 -856 C
ATOM 2251 CE LYS A1077 54.274 -25.070 -17.166 1.00111.92 C
ANISOU 2251 CE LYS A1077 15116 15286 12121 1469 702 -874 C
ATOM 2252 NZ LYS A1077 54.018 -26.445 -17.672 1.00123.79 N
ANISOU 2252 NZ LYS A1077 16698 16790 13545 1426 732 -1123 N
ATOM 2253 N LEU A1078 57.593 -23.927 -12.751 1.00 63.04 N
ANISOU 2253 N LEU A1078 8818 8559 6577 1359 859 -318 N
ATOM 2254 CA LEU A1078 58.899 -23.453 -13.206 1.00 62.89 C
ANISOU 2254 CA LEU A1078 8742 8627 6526 1442 950 -187 C
ATOM 2255 C LEU A1078 60.019 -24.068 -12.366 1.00 66.62 C
ANISOU 2255 C LEU A1078 9183 9058 7074 1482 1010 -159 C
ATOM 2256 O LEU A1078 61.018 -24.521 -12.932 1.00 67.23 O
ANISOU 2256 O LEU A1078 9256 9209 7079 1595 1093 -139 O
ATOM 2257 CB LEU A1078 58.962 -21.911 -13.188 1.00 62.08 C
ANISOU 2257 CB LEU A1078 8562 8571 6453 1392 960 -39 C
ATOM 2258 CG LEU A1078 58.029 -21.203 -14.190 1.00 66.31 C
ANISOU 2258 CG LEU A1078 9139 9188 6869 1429 931 -23 C
ATOM 2259 CD1 LEU A1078 57.757 -19.784 -13.769 1.00 65.52 C
ANISOU 2259 CD1 LEU A1078 9009 9055 6830 1367 940 107 C
ATOM 2260 CD2 LEU A1078 58.580 -21.252 -15.612 1.00 68.95 C
ANISOU 2260 CD2 LEU A1078 9503 9653 7043 1559 1011 9 C
ATOM 2261 N ALA A1079 59.829 -24.131 -11.028 1.00 62.08 N
ANISOU 2261 N ALA A1079 8583 8382 6623 1411 969 -160 N
ATOM 2262 CA ALA A1079 60.781 -24.736 -10.090 1.00 61.89 C
ANISOU 2262 CA ALA A1079 8522 8343 6648 1480 1016 -133 C
ATOM 2263 C ALA A1079 61.034 -26.203 -10.455 1.00 67.28 C
ANISOU 2263 C ALA A1079 9341 8966 7254 1621 1084 -219 C
ATOM 2264 O ALA A1079 62.186 -26.642 -10.444 1.00 68.31 O
ANISOU 2264 O ALA A1079 9440 9172 7341 1763 1162 -173 O
ATOM 2265 CB ALA A1079 60.262 -24.623 -8.665 1.00 61.33 C
ANISOU 2265 CB ALA A1079 8430 8171 6702 1390 953 -134 C
ATOM 2266 N ASN A1080 59.962 -26.935 -10.843 1.00 63.61 N
ANISOU 2266 N ASN A1080 9026 8382 6761 1579 1067 -355 N
ATOM 2267 CA ASN A1080 60.007 -28.336 -11.270 1.00 64.60 C
ANISOU 2267 CA ASN A1080 9325 8407 6814 1676 1157 -470 C
ATOM 2268 C ASN A1080 60.774 -28.521 -12.594 1.00 70.61 C
ANISOU 2268 C ASN A1080 10096 9294 7439 1803 1224 -468 C
ATOM 2269 O ASN A1080 61.237 -29.628 -12.873 1.00 72.16 O
ANISOU 2269 O ASN A1080 10420 9427 7570 1933 1328 -523 O
ATOM 2270 CB ASN A1080 58.594 -28.902 -11.402 1.00 63.46 C
ANISOU 2270 CB ASN A1080 9310 8129 6674 1540 1129 -649 C
ATOM 2271 CG ASN A1080 58.079 -29.527 -10.136 1.00 81.51 C
ANISOU 2271 CG ASN A1080 11686 10218 9067 1478 1147 -690 C
ATOM 2272 OD1 ASN A1080 57.153 -29.020 -9.495 1.00 71.61 O
ANISOU 2272 OD1 ASN A1080 10381 8933 7895 1331 1060 -708 O
ATOM 2273 ND2 ASN A1080 58.657 -30.661 -9.757 1.00 77.20 N
ANISOU 2273 ND2 ASN A1080 11292 9530 8511 1605 1277 -700 N
ATOM 2274 N GLU A1081 60.911 -27.443 -13.395 1.00 66.77 N
ANISOU 2274 N GLU A1081 9491 8972 6904 1776 1184 -398 N
ATOM 2275 CA GLU A1081 61.638 -27.424 -14.668 1.00 67.33 C
ANISOU 2275 CA GLU A1081 9554 9185 6843 1891 1247 -375 C
ATOM 2276 C GLU A1081 63.097 -26.962 -14.453 1.00 72.21 C
ANISOU 2276 C GLU A1081 10032 9936 7468 1986 1315 -223 C
ATOM 2277 O GLU A1081 63.840 -26.801 -15.423 1.00 73.63 O
ANISOU 2277 O GLU A1081 10179 10251 7547 2077 1381 -181 O
ATOM 2278 CB GLU A1081 60.927 -26.509 -15.682 1.00 68.62 C
ANISOU 2278 CB GLU A1081 9682 9459 6931 1827 1187 -376 C
ATOM 2279 CG GLU A1081 59.598 -27.050 -16.191 1.00 81.20 C
ANISOU 2279 CG GLU A1081 11380 11015 8458 1761 1127 -561 C
ATOM 2280 CD GLU A1081 58.617 -26.030 -16.741 1.00106.16 C
ANISOU 2280 CD GLU A1081 14483 14297 11557 1702 1035 -556 C
ATOM 2281 OE1 GLU A1081 57.403 -26.340 -16.771 1.00100.23 O
ANISOU 2281 OE1 GLU A1081 13765 13535 10782 1612 960 -710 O
ATOM 2282 OE2 GLU A1081 59.052 -24.925 -17.141 1.00103.62 O
ANISOU 2282 OE2 GLU A1081 14084 14087 11199 1750 1051 -400 O
ATOM 2283 N GLY A1082 63.479 -26.743 -13.192 1.00 67.84 N
ANISOU 2283 N GLY A1082 9385 9368 7024 1959 1300 -155 N
ATOM 2284 CA GLY A1082 64.819 -26.317 -12.802 1.00 67.97 C
ANISOU 2284 CA GLY A1082 9229 9549 7046 2024 1357 -45 C
ATOM 2285 C GLY A1082 65.164 -24.863 -13.074 1.00 72.13 C
ANISOU 2285 C GLY A1082 9596 10208 7601 1898 1362 50 C
ATOM 2286 O GLY A1082 66.314 -24.467 -12.862 1.00 72.57 O
ANISOU 2286 O GLY A1082 9487 10427 7658 1913 1423 115 O
ATOM 2287 N LYS A1083 64.176 -24.050 -13.534 1.00 67.85 N
ANISOU 2287 N LYS A1083 9102 9606 7072 1776 1313 54 N
ATOM 2288 CA LYS A1083 64.338 -22.618 -13.846 1.00 67.36 C
ANISOU 2288 CA LYS A1083 8950 9613 7031 1660 1349 154 C
ATOM 2289 C LYS A1083 64.186 -21.797 -12.554 1.00 70.09 C
ANISOU 2289 C LYS A1083 9200 9910 7523 1504 1307 186 C
ATOM 2290 O LYS A1083 63.110 -21.263 -12.289 1.00 68.77 O
ANISOU 2290 O LYS A1083 9092 9626 7410 1410 1233 181 O
ATOM 2291 CB LYS A1083 63.318 -22.163 -14.916 1.00 69.42 C
ANISOU 2291 CB LYS A1083 9325 9838 7214 1652 1324 156 C
ATOM 2292 CG LYS A1083 63.223 -23.044 -16.157 1.00 79.31 C
ANISOU 2292 CG LYS A1083 10681 11142 8311 1796 1342 88 C
ATOM 2293 CD LYS A1083 61.941 -22.753 -16.920 1.00 89.60 C
ANISOU 2293 CD LYS A1083 12081 12433 9530 1792 1273 47 C
ATOM 2294 CE LYS A1083 61.912 -23.399 -18.283 1.00101.30 C
ANISOU 2294 CE LYS A1083 13644 14010 10835 1926 1299 -25 C
ATOM 2295 NZ LYS A1083 60.719 -22.974 -19.060 1.00110.02 N
ANISOU 2295 NZ LYS A1083 14805 15174 11823 1943 1231 -60 N
ATOM 2296 N VAL A1084 65.264 -21.718 -11.750 1.00 67.02 N
ANISOU 2296 N VAL A1084 8652 9634 7180 1487 1352 207 N
ATOM 2297 CA VAL A1084 65.308 -21.056 -10.438 1.00 66.21 C
ANISOU 2297 CA VAL A1084 8431 9524 7200 1346 1318 213 C
ATOM 2298 C VAL A1084 64.859 -19.579 -10.522 1.00 69.81 C
ANISOU 2298 C VAL A1084 8887 9916 7724 1157 1352 271 C
ATOM 2299 O VAL A1084 63.886 -19.213 -9.855 1.00 68.94 O
ANISOU 2299 O VAL A1084 8829 9670 7695 1070 1271 262 O
ATOM 2300 CB VAL A1084 66.696 -21.173 -9.738 1.00 71.03 C
ANISOU 2300 CB VAL A1084 8833 10348 7807 1374 1372 207 C
ATOM 2301 CG1 VAL A1084 66.595 -20.814 -8.256 1.00 69.97 C
ANISOU 2301 CG1 VAL A1084 8590 10215 7779 1264 1307 181 C
ATOM 2302 CG2 VAL A1084 67.293 -22.565 -9.900 1.00 71.74 C
ANISOU 2302 CG2 VAL A1084 8945 10518 7793 1615 1381 178 C
ATOM 2303 N LYS A1085 65.568 -18.747 -11.317 1.00 66.27 N
ANISOU 2303 N LYS A1085 8391 9552 7235 1103 1488 333 N
ATOM 2304 CA LYS A1085 65.304 -17.311 -11.492 1.00 65.38 C
ANISOU 2304 CA LYS A1085 8312 9357 7172 939 1579 403 C
ATOM 2305 C LYS A1085 63.868 -17.039 -11.967 1.00 67.66 C
ANISOU 2305 C LYS A1085 8794 9478 7437 981 1512 441 C
ATOM 2306 O LYS A1085 63.233 -16.122 -11.446 1.00 66.79 O
ANISOU 2306 O LYS A1085 8724 9249 7403 867 1512 474 O
ATOM 2307 CB LYS A1085 66.314 -16.682 -12.461 1.00 68.62 C
ANISOU 2307 CB LYS A1085 8679 9875 7519 905 1768 465 C
ATOM 2308 CG LYS A1085 67.714 -16.547 -11.875 1.00 80.40 C
ANISOU 2308 CG LYS A1085 9938 11566 9047 798 1859 415 C
ATOM 2309 CD LYS A1085 68.713 -16.127 -12.939 1.00 92.69 C
ANISOU 2309 CD LYS A1085 11448 13245 10524 777 2053 462 C
ATOM 2310 CE LYS A1085 70.137 -16.476 -12.586 1.00100.01 C
ANISOU 2310 CE LYS A1085 12117 14451 11431 754 2111 388 C
ATOM 2311 NZ LYS A1085 71.043 -16.306 -13.754 1.00104.36 N
ANISOU 2311 NZ LYS A1085 12631 15135 11884 773 2288 430 N
ATOM 2312 N GLU A1086 63.354 -17.852 -12.914 1.00 63.60 N
ANISOU 2312 N GLU A1086 8386 8973 6805 1147 1454 423 N
ATOM 2313 CA GLU A1086 61.991 -17.735 -13.441 1.00 62.98 C
ANISOU 2313 CA GLU A1086 8455 8810 6666 1211 1376 430 C
ATOM 2314 C GLU A1086 60.957 -18.087 -12.369 1.00 63.86 C
ANISOU 2314 C GLU A1086 8579 8817 6866 1161 1224 352 C
ATOM 2315 O GLU A1086 59.930 -17.415 -12.282 1.00 62.99 O
ANISOU 2315 O GLU A1086 8538 8634 6762 1138 1181 379 O
ATOM 2316 CB GLU A1086 61.792 -18.620 -14.682 1.00 65.40 C
ANISOU 2316 CB GLU A1086 8840 9197 6812 1382 1354 389 C
ATOM 2317 CG GLU A1086 62.360 -18.023 -15.957 1.00 79.62 C
ANISOU 2317 CG GLU A1086 10679 11084 8492 1456 1500 490 C
ATOM 2318 CD GLU A1086 61.661 -18.511 -17.208 1.00108.06 C
ANISOU 2318 CD GLU A1086 14388 14758 11912 1624 1458 462 C
ATOM 2319 OE1 GLU A1086 62.146 -19.494 -17.814 1.00106.06 O
ANISOU 2319 OE1 GLU A1086 14133 14591 11575 1722 1455 389 O
ATOM 2320 OE2 GLU A1086 60.612 -17.929 -17.568 1.00105.84 O
ANISOU 2320 OE2 GLU A1086 14189 14463 11560 1670 1429 504 O
ATOM 2321 N ALA A1087 61.244 -19.123 -11.545 1.00 58.74 N
ANISOU 2321 N ALA A1087 7870 8169 6278 1162 1156 265 N
ATOM 2322 CA ALA A1087 60.394 -19.552 -10.429 1.00 56.63 C
ANISOU 2322 CA ALA A1087 7616 7799 6102 1111 1035 193 C
ATOM 2323 C ALA A1087 60.413 -18.512 -9.310 1.00 59.15 C
ANISOU 2323 C ALA A1087 7861 8063 6549 963 1040 241 C
ATOM 2324 O ALA A1087 59.409 -18.350 -8.622 1.00 57.96 O
ANISOU 2324 O ALA A1087 7746 7816 6460 908 953 216 O
ATOM 2325 CB ALA A1087 60.850 -20.898 -9.899 1.00 57.04 C
ANISOU 2325 CB ALA A1087 7653 7856 6162 1183 1007 112 C
ATOM 2326 N GLN A1088 61.552 -17.800 -9.140 1.00 55.71 N
ANISOU 2326 N GLN A1088 7317 7702 6149 886 1150 292 N
ATOM 2327 CA GLN A1088 61.724 -16.731 -8.152 1.00 54.86 C
ANISOU 2327 CA GLN A1088 7131 7557 6155 717 1186 315 C
ATOM 2328 C GLN A1088 61.002 -15.469 -8.607 1.00 60.70 C
ANISOU 2328 C GLN A1088 7985 8182 6898 655 1249 396 C
ATOM 2329 O GLN A1088 60.439 -14.767 -7.769 1.00 61.42 O
ANISOU 2329 O GLN A1088 8090 8170 7075 554 1222 400 O
ATOM 2330 CB GLN A1088 63.208 -16.427 -7.899 1.00 56.85 C
ANISOU 2330 CB GLN A1088 7214 7961 6426 634 1302 309 C
ATOM 2331 CG GLN A1088 63.919 -17.462 -7.048 1.00 60.22 C
ANISOU 2331 CG GLN A1088 7501 8525 6856 702 1238 235 C
ATOM 2332 CD GLN A1088 65.416 -17.314 -7.095 1.00 73.89 C
ANISOU 2332 CD GLN A1088 9042 10479 8555 668 1350 219 C
ATOM 2333 OE1 GLN A1088 66.033 -17.258 -8.161 1.00 72.28 O
ANISOU 2333 OE1 GLN A1088 8837 10355 8273 712 1453 253 O
ATOM 2334 NE2 GLN A1088 66.042 -17.319 -5.935 1.00 64.10 N
ANISOU 2334 NE2 GLN A1088 7622 9376 7357 604 1330 156 N
ATOM 2335 N ALA A1089 61.015 -15.178 -9.925 1.00 58.27 N
ANISOU 2335 N ALA A1089 7769 7891 6480 739 1340 470 N
ATOM 2336 CA ALA A1089 60.331 -14.013 -10.500 1.00 58.48 C
ANISOU 2336 CA ALA A1089 7936 7816 6469 745 1424 573 C
ATOM 2337 C ALA A1089 58.810 -14.176 -10.403 1.00 60.60 C
ANISOU 2337 C ALA A1089 8297 8026 6703 838 1276 557 C
ATOM 2338 O ALA A1089 58.124 -13.209 -10.071 1.00 60.42 O
ANISOU 2338 O ALA A1089 8350 7896 6710 806 1300 616 O
ATOM 2339 CB ALA A1089 60.750 -13.806 -11.949 1.00 60.64 C
ANISOU 2339 CB ALA A1089 8284 8150 6605 853 1558 659 C
ATOM 2340 N ALA A1090 58.299 -15.402 -10.657 1.00 56.43 N
ANISOU 2340 N ALA A1090 7761 7570 6111 945 1135 464 N
ATOM 2341 CA ALA A1090 56.874 -15.750 -10.588 1.00 55.98 C
ANISOU 2341 CA ALA A1090 7755 7502 6011 1010 991 404 C
ATOM 2342 C ALA A1090 56.367 -15.782 -9.135 1.00 60.44 C
ANISOU 2342 C ALA A1090 8273 7971 6720 891 897 348 C
ATOM 2343 O ALA A1090 55.209 -15.432 -8.893 1.00 60.27 O
ANISOU 2343 O ALA A1090 8293 7917 6691 905 824 344 O
ATOM 2344 CB ALA A1090 56.623 -17.087 -11.259 1.00 56.65 C
ANISOU 2344 CB ALA A1090 7842 7685 5998 1108 905 288 C
ATOM 2345 N ALA A1091 57.217 -16.204 -8.173 1.00 56.61 N
ANISOU 2345 N ALA A1091 7695 7467 6349 794 899 308 N
ATOM 2346 CA ALA A1091 56.841 -16.212 -6.758 1.00 55.32 C
ANISOU 2346 CA ALA A1091 7484 7224 6313 691 822 263 C
ATOM 2347 C ALA A1091 56.796 -14.767 -6.239 1.00 59.16 C
ANISOU 2347 C ALA A1091 7980 7626 6871 584 897 343 C
ATOM 2348 O ALA A1091 55.920 -14.426 -5.446 1.00 58.71 O
ANISOU 2348 O ALA A1091 7942 7491 6876 540 830 331 O
ATOM 2349 CB ALA A1091 57.816 -17.054 -5.949 1.00 55.73 C
ANISOU 2349 CB ALA A1091 7433 7316 6427 662 814 207 C
ATOM 2350 N GLU A1092 57.695 -13.907 -6.761 1.00 55.98 N
ANISOU 2350 N GLU A1092 7582 7231 6455 542 1054 420 N
ATOM 2351 CA GLU A1092 57.804 -12.481 -6.450 1.00 55.72 C
ANISOU 2351 CA GLU A1092 7596 7092 6484 425 1187 493 C
ATOM 2352 C GLU A1092 56.562 -11.711 -6.920 1.00 57.98 C
ANISOU 2352 C GLU A1092 8041 7285 6703 526 1193 578 C
ATOM 2353 O GLU A1092 56.311 -10.615 -6.426 1.00 58.43 O
ANISOU 2353 O GLU A1092 8168 7214 6819 450 1277 630 O
ATOM 2354 CB GLU A1092 59.081 -11.897 -7.096 1.00 58.81 C
ANISOU 2354 CB GLU A1092 7970 7517 6857 355 1385 544 C
ATOM 2355 CG GLU A1092 59.603 -10.603 -6.478 1.00 71.52 C
ANISOU 2355 CG GLU A1092 9582 9024 8567 150 1554 560 C
ATOM 2356 CD GLU A1092 59.988 -10.612 -5.006 1.00 94.07 C
ANISOU 2356 CD GLU A1092 12284 11907 11552 -25 1498 447 C
ATOM 2357 OE1 GLU A1092 60.140 -11.711 -4.422 1.00 83.73 O
ANISOU 2357 OE1 GLU A1092 10840 10722 10252 19 1345 364 O
ATOM 2358 OE2 GLU A1092 60.148 -9.507 -4.438 1.00 90.03 O
ANISOU 2358 OE2 GLU A1092 11796 11290 11122 -201 1623 439 O
ATOM 2359 N GLN A1093 55.770 -12.294 -7.845 1.00 52.84 N
ANISOU 2359 N GLN A1093 7444 6714 5919 705 1106 582 N
ATOM 2360 CA GLN A1093 54.526 -11.702 -8.352 1.00 52.32 C
ANISOU 2360 CA GLN A1093 7498 6636 5746 852 1087 651 C
ATOM 2361 C GLN A1093 53.472 -11.531 -7.233 1.00 54.73 C
ANISOU 2361 C GLN A1093 7790 6876 6130 809 973 608 C
ATOM 2362 O GLN A1093 52.529 -10.758 -7.400 1.00 54.36 O
ANISOU 2362 O GLN A1093 7839 6802 6014 915 986 680 O
ATOM 2363 CB GLN A1093 53.950 -12.543 -9.497 1.00 53.56 C
ANISOU 2363 CB GLN A1093 7661 6958 5731 1034 994 614 C
ATOM 2364 CG GLN A1093 54.722 -12.424 -10.809 1.00 57.56 C
ANISOU 2364 CG GLN A1093 8223 7533 6116 1133 1125 694 C
ATOM 2365 CD GLN A1093 54.513 -11.075 -11.441 1.00 69.18 C
ANISOU 2365 CD GLN A1093 9852 8940 7495 1244 1293 865 C
ATOM 2366 OE1 GLN A1093 53.438 -10.768 -11.961 1.00 67.32 O
ANISOU 2366 OE1 GLN A1093 9692 8774 7114 1433 1253 914 O
ATOM 2367 NE2 GLN A1093 55.515 -10.217 -11.346 1.00 54.74 N
ANISOU 2367 NE2 GLN A1093 8078 6978 5744 1130 1497 955 N
ATOM 2368 N LEU A1094 53.659 -12.222 -6.089 1.00 50.01 N
ANISOU 2368 N LEU A1094 7080 6259 5663 673 874 500 N
ATOM 2369 CA LEU A1094 52.782 -12.123 -4.922 1.00 49.19 C
ANISOU 2369 CA LEU A1094 6954 6091 5645 614 775 453 C
ATOM 2370 C LEU A1094 52.987 -10.786 -4.204 1.00 53.09 C
ANISOU 2370 C LEU A1094 7505 6435 6230 511 897 527 C
ATOM 2371 O LEU A1094 52.154 -10.390 -3.395 1.00 52.36 O
ANISOU 2371 O LEU A1094 7434 6278 6184 495 846 521 O
ATOM 2372 CB LEU A1094 53.012 -13.287 -3.953 1.00 48.11 C
ANISOU 2372 CB LEU A1094 6700 5975 5604 521 659 330 C
ATOM 2373 CG LEU A1094 52.607 -14.662 -4.452 1.00 53.32 C
ANISOU 2373 CG LEU A1094 7334 6733 6191 597 552 232 C
ATOM 2374 CD1 LEU A1094 53.327 -15.718 -3.687 1.00 53.21 C
ANISOU 2374 CD1 LEU A1094 7247 6713 6257 532 521 154 C
ATOM 2375 CD2 LEU A1094 51.090 -14.879 -4.357 1.00 55.47 C
ANISOU 2375 CD2 LEU A1094 7619 7036 6421 640 435 169 C
ATOM 2376 N LYS A1095 54.090 -10.093 -4.520 1.00 50.82 N
ANISOU 2376 N LYS A1095 7248 6096 5966 432 1073 586 N
ATOM 2377 CA LYS A1095 54.438 -8.794 -3.960 1.00 51.03 C
ANISOU 2377 CA LYS A1095 7346 5965 6078 297 1240 635 C
ATOM 2378 C LYS A1095 53.900 -7.652 -4.838 1.00 55.30 C
ANISOU 2378 C LYS A1095 8098 6396 6516 431 1401 785 C
ATOM 2379 O LYS A1095 54.004 -6.499 -4.422 1.00 57.20 O
ANISOU 2379 O LYS A1095 8451 6464 6818 337 1567 834 O
ATOM 2380 CB LYS A1095 55.959 -8.667 -3.744 1.00 54.20 C
ANISOU 2380 CB LYS A1095 7651 6383 6560 103 1367 587 C
ATOM 2381 CG LYS A1095 56.447 -9.345 -2.463 1.00 64.58 C
ANISOU 2381 CG LYS A1095 8775 7780 7982 -35 1247 452 C
ATOM 2382 CD LYS A1095 57.846 -8.886 -2.089 1.00 74.12 C
ANISOU 2382 CD LYS A1095 9875 9025 9262 -247 1393 391 C
ATOM 2383 CE LYS A1095 58.214 -9.279 -0.679 1.00 85.44 C
ANISOU 2383 CE LYS A1095 11129 10548 10784 -368 1286 263 C
ATOM 2384 NZ LYS A1095 59.568 -8.787 -0.301 1.00 92.87 N
ANISOU 2384 NZ LYS A1095 11927 11585 11773 -582 1424 172 N
ATOM 2385 N THR A1096 53.276 -7.955 -6.011 1.00 49.89 N
ANISOU 2385 N THR A1096 7478 5813 5666 662 1361 853 N
ATOM 2386 CA THR A1096 52.657 -6.907 -6.845 1.00 51.03 C
ANISOU 2386 CA THR A1096 7830 5885 5674 856 1508 1013 C
ATOM 2387 C THR A1096 51.543 -6.207 -6.054 1.00 55.19 C
ANISOU 2387 C THR A1096 8438 6313 6218 910 1481 1044 C
ATOM 2388 O THR A1096 50.971 -6.810 -5.135 1.00 53.69 O
ANISOU 2388 O THR A1096 8120 6175 6103 848 1293 932 O
ATOM 2389 CB THR A1096 52.091 -7.446 -8.178 1.00 54.78 C
ANISOU 2389 CB THR A1096 8324 6554 5938 1120 1434 1059 C
ATOM 2390 OG1 THR A1096 51.048 -8.388 -7.932 1.00 51.12 O
ANISOU 2390 OG1 THR A1096 7733 6258 5432 1196 1187 946 O
ATOM 2391 CG2 THR A1096 53.160 -7.999 -9.116 1.00 51.65 C
ANISOU 2391 CG2 THR A1096 7885 6243 5498 1103 1494 1054 C
ATOM 2392 N THR A1097 51.234 -4.946 -6.410 1.00 52.67 N
ANISOU 2392 N THR A1097 8344 5844 5824 1038 1683 1199 N
ATOM 2393 CA THR A1097 50.193 -4.149 -5.754 1.00 52.32 C
ANISOU 2393 CA THR A1097 8408 5696 5777 1126 1692 1249 C
ATOM 2394 C THR A1097 48.873 -4.938 -5.675 1.00 55.07 C
ANISOU 2394 C THR A1097 8627 6272 6023 1306 1424 1187 C
ATOM 2395 O THR A1097 48.261 -4.976 -4.606 1.00 53.10 O
ANISOU 2395 O THR A1097 8318 5999 5860 1241 1316 1117 O
ATOM 2396 CB THR A1097 50.004 -2.803 -6.462 1.00 59.16 C
ANISOU 2396 CB THR A1097 9571 6383 6525 1315 1970 1452 C
ATOM 2397 OG1 THR A1097 51.276 -2.305 -6.847 1.00 61.40 O
ANISOU 2397 OG1 THR A1097 9956 6534 6839 1193 2214 1508 O
ATOM 2398 CG2 THR A1097 49.349 -1.781 -5.573 1.00 59.37 C
ANISOU 2398 CG2 THR A1097 9745 6176 6637 1267 2089 1486 C
ATOM 2399 N ARG A1098 48.488 -5.608 -6.786 1.00 52.79 N
ANISOU 2399 N ARG A1098 8281 6221 5554 1507 1321 1190 N
ATOM 2400 CA ARG A1098 47.273 -6.410 -6.912 1.00 52.70 C
ANISOU 2400 CA ARG A1098 8128 6473 5423 1658 1084 1100 C
ATOM 2401 C ARG A1098 47.265 -7.571 -5.924 1.00 56.86 C
ANISOU 2401 C ARG A1098 8445 7051 6108 1427 881 902 C
ATOM 2402 O ARG A1098 46.306 -7.697 -5.158 1.00 56.33 O
ANISOU 2402 O ARG A1098 8306 7035 6061 1430 755 834 O
ATOM 2403 CB ARG A1098 47.106 -6.938 -8.344 1.00 53.89 C
ANISOU 2403 CB ARG A1098 8251 6876 5349 1877 1038 1112 C
ATOM 2404 CG ARG A1098 45.645 -7.114 -8.740 1.00 70.37 C
ANISOU 2404 CG ARG A1098 10257 9251 7229 2126 876 1072 C
ATOM 2405 CD ARG A1098 45.412 -8.378 -9.551 1.00 84.64 C
ANISOU 2405 CD ARG A1098 11887 11357 8916 2152 701 912 C
ATOM 2406 NE ARG A1098 43.982 -8.665 -9.712 1.00 91.40 N
ANISOU 2406 NE ARG A1098 12612 12523 9591 2325 533 817 N
ATOM 2407 CZ ARG A1098 43.485 -9.849 -10.060 1.00101.99 C
ANISOU 2407 CZ ARG A1098 13763 14137 10852 2287 356 611 C
ATOM 2408 NH1 ARG A1098 44.294 -10.880 -10.283 1.00 82.51 N
ANISOU 2408 NH1 ARG A1098 11238 11643 8469 2104 328 494 N
ATOM 2409 NH2 ARG A1098 42.174 -10.014 -10.181 1.00 90.15 N
ANISOU 2409 NH2 ARG A1098 12127 12945 9180 2428 218 508 N
ATOM 2410 N ASN A1099 48.343 -8.386 -5.908 1.00 53.21 N
ANISOU 2410 N ASN A1099 7894 6573 5751 1242 865 817 N
ATOM 2411 CA ASN A1099 48.439 -9.554 -5.027 1.00 51.19 C
ANISOU 2411 CA ASN A1099 7470 6352 5629 1055 703 648 C
ATOM 2412 C ASN A1099 48.681 -9.170 -3.568 1.00 53.26 C
ANISOU 2412 C ASN A1099 7719 6437 6082 864 719 624 C
ATOM 2413 O ASN A1099 48.217 -9.894 -2.685 1.00 51.14 O
ANISOU 2413 O ASN A1099 7343 6201 5889 780 578 512 O
ATOM 2414 CB ASN A1099 49.480 -10.542 -5.527 1.00 50.04 C
ANISOU 2414 CB ASN A1099 7250 6259 5502 973 694 580 C
ATOM 2415 CG ASN A1099 49.019 -11.264 -6.777 1.00 64.02 C
ANISOU 2415 CG ASN A1099 8992 8242 7090 1134 620 537 C
ATOM 2416 OD1 ASN A1099 47.830 -11.578 -6.951 1.00 55.63 O
ANISOU 2416 OD1 ASN A1099 7878 7336 5922 1234 496 465 O
ATOM 2417 ND2 ASN A1099 49.941 -11.506 -7.696 1.00 52.11 N
ANISOU 2417 ND2 ASN A1099 7506 6766 5529 1160 698 566 N
ATOM 2418 N ALA A1100 49.343 -8.020 -3.307 1.00 50.68 N
ANISOU 2418 N ALA A1100 7508 5925 5825 794 901 721 N
ATOM 2419 CA ALA A1100 49.519 -7.513 -1.939 1.00 49.11 C
ANISOU 2419 CA ALA A1100 7302 5571 5788 615 929 687 C
ATOM 2420 C ALA A1100 48.160 -7.002 -1.424 1.00 54.02 C
ANISOU 2420 C ALA A1100 7973 6176 6375 728 870 711 C
ATOM 2421 O ALA A1100 47.837 -7.227 -0.257 1.00 52.56 O
ANISOU 2421 O ALA A1100 7708 5967 6296 618 773 628 O
ATOM 2422 CB ALA A1100 50.571 -6.420 -1.893 1.00 50.68 C
ANISOU 2422 CB ALA A1100 7614 5586 6055 489 1164 754 C
ATOM 2423 N TYR A1101 47.330 -6.392 -2.319 1.00 52.89 N
ANISOU 2423 N TYR A1101 7952 6079 6063 974 920 826 N
ATOM 2424 CA TYR A1101 45.978 -5.946 -1.975 1.00 53.63 C
ANISOU 2424 CA TYR A1101 8080 6215 6084 1135 859 855 C
ATOM 2425 C TYR A1101 45.112 -7.159 -1.636 1.00 52.66 C
ANISOU 2425 C TYR A1101 7756 6305 5946 1125 619 706 C
ATOM 2426 O TYR A1101 44.413 -7.118 -0.622 1.00 51.43 O
ANISOU 2426 O TYR A1101 7554 6135 5853 1085 541 656 O
ATOM 2427 CB TYR A1101 45.320 -5.100 -3.093 1.00 59.47 C
ANISOU 2427 CB TYR A1101 8981 7009 6605 1450 967 1016 C
ATOM 2428 CG TYR A1101 43.833 -4.886 -2.872 1.00 64.98 C
ANISOU 2428 CG TYR A1101 9658 7850 7181 1663 865 1026 C
ATOM 2429 CD1 TYR A1101 43.372 -3.959 -1.938 1.00 68.04 C
ANISOU 2429 CD1 TYR A1101 10154 8070 7628 1674 941 1081 C
ATOM 2430 CD2 TYR A1101 42.888 -5.660 -3.543 1.00 66.72 C
ANISOU 2430 CD2 TYR A1101 9732 8396 7224 1837 691 958 C
ATOM 2431 CE1 TYR A1101 42.009 -3.807 -1.678 1.00 70.20 C
ANISOU 2431 CE1 TYR A1101 10387 8501 7787 1875 841 1083 C
ATOM 2432 CE2 TYR A1101 41.523 -5.526 -3.283 1.00 68.53 C
ANISOU 2432 CE2 TYR A1101 9897 8806 7335 2016 587 940 C
ATOM 2433 CZ TYR A1101 41.087 -4.591 -2.355 1.00 78.79 C
ANISOU 2433 CZ TYR A1101 11305 9939 8694 2047 662 1013 C
ATOM 2434 OH TYR A1101 39.740 -4.432 -2.112 1.00 82.70 O
ANISOU 2434 OH TYR A1101 11730 10635 9060 2244 565 1000 O
ATOM 2435 N ILE A1102 45.166 -8.234 -2.477 1.00 46.85 N
ANISOU 2435 N ILE A1102 6913 5756 5130 1150 520 628 N
ATOM 2436 CA ILE A1102 44.415 -9.483 -2.271 1.00 44.95 C
ANISOU 2436 CA ILE A1102 6500 5704 4876 1107 327 461 C
ATOM 2437 C ILE A1102 44.773 -10.077 -0.897 1.00 46.91 C
ANISOU 2437 C ILE A1102 6671 5824 5328 867 271 362 C
ATOM 2438 O ILE A1102 43.865 -10.448 -0.166 1.00 46.67 O
ANISOU 2438 O ILE A1102 6559 5850 5323 833 165 275 O
ATOM 2439 CB ILE A1102 44.596 -10.518 -3.428 1.00 48.20 C
ANISOU 2439 CB ILE A1102 6840 6300 5174 1148 270 382 C
ATOM 2440 CG1 ILE A1102 44.065 -9.958 -4.774 1.00 50.42 C
ANISOU 2440 CG1 ILE A1102 7176 6767 5213 1424 303 470 C
ATOM 2441 CG2 ILE A1102 43.916 -11.865 -3.101 1.00 46.54 C
ANISOU 2441 CG2 ILE A1102 6473 6229 4980 1040 111 182 C
ATOM 2442 CD1 ILE A1102 44.650 -10.615 -6.030 1.00 56.57 C
ANISOU 2442 CD1 ILE A1102 7944 7669 5882 1475 315 446 C
ATOM 2443 N GLN A1103 46.066 -10.117 -0.526 1.00 43.13 N
ANISOU 2443 N GLN A1103 6213 5195 4980 716 349 376 N
ATOM 2444 CA GLN A1103 46.499 -10.619 0.783 1.00 41.26 C
ANISOU 2444 CA GLN A1103 5903 4864 4909 527 306 296 C
ATOM 2445 C GLN A1103 45.916 -9.766 1.929 1.00 45.69 C
ANISOU 2445 C GLN A1103 6494 5322 5543 494 312 319 C
ATOM 2446 O GLN A1103 45.296 -10.330 2.831 1.00 44.71 O
ANISOU 2446 O GLN A1103 6293 5221 5473 436 209 236 O
ATOM 2447 CB GLN A1103 48.029 -10.673 0.881 1.00 42.04 C
ANISOU 2447 CB GLN A1103 5998 4879 5097 404 397 308 C
ATOM 2448 CG GLN A1103 48.516 -10.846 2.318 1.00 48.89 C
ANISOU 2448 CG GLN A1103 6795 5671 6109 243 372 246 C
ATOM 2449 CD GLN A1103 49.890 -11.413 2.504 1.00 57.64 C
ANISOU 2449 CD GLN A1103 7831 6796 7274 146 404 208 C
ATOM 2450 OE1 GLN A1103 50.349 -11.604 3.637 1.00 54.12 O
ANISOU 2450 OE1 GLN A1103 7312 6333 6917 45 382 157 O
ATOM 2451 NE2 GLN A1103 50.569 -11.711 1.418 1.00 42.89 N
ANISOU 2451 NE2 GLN A1103 5970 4986 5340 194 453 231 N
ATOM 2452 N LYS A1104 46.117 -8.425 1.884 1.00 43.29 N
ANISOU 2452 N LYS A1104 6319 4893 5236 532 452 431 N
ATOM 2453 CA LYS A1104 45.629 -7.453 2.872 1.00 42.73 C
ANISOU 2453 CA LYS A1104 6314 4698 5224 513 494 462 C
ATOM 2454 C LYS A1104 44.114 -7.623 3.093 1.00 46.06 C
ANISOU 2454 C LYS A1104 6691 5239 5569 643 370 437 C
ATOM 2455 O LYS A1104 43.671 -7.679 4.241 1.00 45.19 O
ANISOU 2455 O LYS A1104 6533 5092 5543 564 310 382 O
ATOM 2456 CB LYS A1104 45.964 -6.019 2.417 1.00 47.17 C
ANISOU 2456 CB LYS A1104 7069 5100 5753 575 702 595 C
ATOM 2457 CG LYS A1104 46.091 -5.021 3.562 1.00 69.35 C
ANISOU 2457 CG LYS A1104 9959 7714 8674 456 802 597 C
ATOM 2458 CD LYS A1104 45.752 -3.588 3.131 1.00 84.17 C
ANISOU 2458 CD LYS A1104 12073 9428 10479 597 1005 738 C
ATOM 2459 CE LYS A1104 46.047 -2.535 4.187 1.00 92.93 C
ANISOU 2459 CE LYS A1104 13291 10310 11710 440 1150 720 C
ATOM 2460 NZ LYS A1104 45.089 -2.563 5.328 1.00 97.03 N
ANISOU 2460 NZ LYS A1104 13750 10849 12266 450 1024 664 N
ATOM 2461 N TYR A1105 43.338 -7.768 1.992 1.00 43.77 N
ANISOU 2461 N TYR A1105 6396 5124 5111 838 329 463 N
ATOM 2462 CA TYR A1105 41.888 -7.992 2.002 1.00 43.55 C
ANISOU 2462 CA TYR A1105 6286 5286 4974 971 208 416 C
ATOM 2463 C TYR A1105 41.550 -9.298 2.748 1.00 46.67 C
ANISOU 2463 C TYR A1105 6516 5763 5455 805 61 248 C
ATOM 2464 O TYR A1105 40.783 -9.256 3.714 1.00 47.09 O
ANISOU 2464 O TYR A1105 6521 5817 5554 771 6 205 O
ATOM 2465 CB TYR A1105 41.306 -8.015 0.557 1.00 46.02 C
ANISOU 2465 CB TYR A1105 6592 5830 5065 1206 191 449 C
ATOM 2466 CG TYR A1105 39.892 -8.561 0.498 1.00 48.74 C
ANISOU 2466 CG TYR A1105 6780 6453 5284 1299 41 338 C
ATOM 2467 CD1 TYR A1105 38.807 -7.788 0.906 1.00 51.26 C
ANISOU 2467 CD1 TYR A1105 7105 6844 5527 1456 31 382 C
ATOM 2468 CD2 TYR A1105 39.645 -9.872 0.094 1.00 50.09 C
ANISOU 2468 CD2 TYR A1105 6794 6821 5418 1214 -77 170 C
ATOM 2469 CE1 TYR A1105 37.513 -8.311 0.928 1.00 52.97 C
ANISOU 2469 CE1 TYR A1105 7145 7353 5630 1517 -106 257 C
ATOM 2470 CE2 TYR A1105 38.353 -10.403 0.103 1.00 51.91 C
ANISOU 2470 CE2 TYR A1105 6861 7322 5542 1248 -199 30 C
ATOM 2471 CZ TYR A1105 37.288 -9.617 0.518 1.00 62.67 C
ANISOU 2471 CZ TYR A1105 8201 8785 6825 1399 -219 72 C
ATOM 2472 OH TYR A1105 36.011 -10.132 0.520 1.00 67.41 O
ANISOU 2472 OH TYR A1105 8610 9692 7310 1425 -337 -83 O
ATOM 2473 N LEU A1106 42.110 -10.451 2.290 1.00 41.61 N
ANISOU 2473 N LEU A1106 5805 5177 4828 711 18 159 N
ATOM 2474 CA LEU A1106 41.867 -11.774 2.882 1.00 40.17 C
ANISOU 2474 CA LEU A1106 5509 5038 4717 561 -78 7 C
ATOM 2475 C LEU A1106 42.243 -11.825 4.366 1.00 42.11 C
ANISOU 2475 C LEU A1106 5755 5111 5132 411 -72 -3 C
ATOM 2476 O LEU A1106 41.502 -12.412 5.152 1.00 42.62 O
ANISOU 2476 O LEU A1106 5752 5205 5236 342 -138 -92 O
ATOM 2477 CB LEU A1106 42.605 -12.888 2.123 1.00 40.24 C
ANISOU 2477 CB LEU A1106 5494 5082 4714 503 -80 -63 C
ATOM 2478 CG LEU A1106 42.188 -13.137 0.659 1.00 46.30 C
ANISOU 2478 CG LEU A1106 6232 6058 5301 631 -105 -100 C
ATOM 2479 CD1 LEU A1106 43.089 -14.167 -0.002 1.00 45.75 C
ANISOU 2479 CD1 LEU A1106 6168 5979 5235 570 -84 -156 C
ATOM 2480 CD2 LEU A1106 40.723 -13.529 0.543 1.00 49.24 C
ANISOU 2480 CD2 LEU A1106 6488 6653 5569 657 -203 -235 C
ATOM 2481 N ARG A 224 43.367 -11.195 4.750 1.00 46.97 N
ANISOU 2481 N ARG A 224 5937 7863 4048 -104 840 103 N
ATOM 2482 CA ARG A 224 43.826 -11.139 6.134 1.00 44.24 C
ANISOU 2482 CA ARG A 224 5621 7306 3882 -144 829 158 C
ATOM 2483 C ARG A 224 42.850 -10.323 6.986 1.00 47.34 C
ANISOU 2483 C ARG A 224 6067 7629 4290 -107 736 215 C
ATOM 2484 O ARG A 224 42.573 -10.714 8.117 1.00 46.29 O
ANISOU 2484 O ARG A 224 5930 7374 4283 -133 712 168 O
ATOM 2485 CB ARG A 224 45.246 -10.567 6.224 1.00 42.09 C
ANISOU 2485 CB ARG A 224 5374 6961 3657 -180 876 303 C
ATOM 2486 CG ARG A 224 46.307 -11.517 5.687 1.00 46.29 C
ANISOU 2486 CG ARG A 224 5839 7540 4209 -209 973 241 C
ATOM 2487 CD ARG A 224 47.700 -10.955 5.831 1.00 49.60 C
ANISOU 2487 CD ARG A 224 6259 7919 4670 -254 1018 376 C
ATOM 2488 NE ARG A 224 48.236 -11.157 7.173 1.00 53.83 N
ANISOU 2488 NE ARG A 224 6776 8312 5363 -287 1014 396 N
ATOM 2489 CZ ARG A 224 49.525 -11.328 7.443 1.00 62.40 C
ANISOU 2489 CZ ARG A 224 7809 9393 6507 -321 1071 445 C
ATOM 2490 NH1 ARG A 224 50.418 -11.337 6.464 1.00 49.91 N
ANISOU 2490 NH1 ARG A 224 6188 7930 4846 -334 1141 476 N
ATOM 2491 NH2 ARG A 224 49.930 -11.503 8.695 1.00 49.03 N
ANISOU 2491 NH2 ARG A 224 6091 7596 4940 -338 1059 463 N
ATOM 2492 N GLY A 225 42.302 -9.243 6.414 1.00 43.57 N
ANISOU 2492 N GLY A 225 5642 7237 3674 -34 691 313 N
ATOM 2493 CA GLY A 225 41.318 -8.385 7.068 1.00 42.44 C
ANISOU 2493 CA GLY A 225 5559 7050 3515 32 610 376 C
ATOM 2494 C GLY A 225 40.014 -9.106 7.337 1.00 46.36 C
ANISOU 2494 C GLY A 225 5983 7634 3997 53 558 218 C
ATOM 2495 O GLY A 225 39.408 -8.923 8.393 1.00 44.88 O
ANISOU 2495 O GLY A 225 5815 7347 3889 61 505 217 O
ATOM 2496 N VAL A 226 39.596 -9.970 6.398 1.00 44.53 N
ANISOU 2496 N VAL A 226 5663 7594 3662 47 580 72 N
ATOM 2497 CA VAL A 226 38.376 -10.783 6.495 1.00 43.99 C
ANISOU 2497 CA VAL A 226 5508 7647 3558 32 548 -112 C
ATOM 2498 C VAL A 226 38.534 -11.808 7.648 1.00 46.87 C
ANISOU 2498 C VAL A 226 5861 7828 4119 -70 580 -218 C
ATOM 2499 O VAL A 226 37.536 -12.180 8.274 1.00 46.44 O
ANISOU 2499 O VAL A 226 5773 7785 4088 -89 543 -318 O
ATOM 2500 CB VAL A 226 38.030 -11.462 5.125 1.00 48.23 C
ANISOU 2500 CB VAL A 226 5955 8442 3927 23 581 -256 C
ATOM 2501 CG1 VAL A 226 36.844 -12.408 5.246 1.00 48.46 C
ANISOU 2501 CG1 VAL A 226 5889 8602 3922 -34 564 -473 C
ATOM 2502 CG2 VAL A 226 37.754 -10.422 4.043 1.00 48.83 C
ANISOU 2502 CG2 VAL A 226 6043 8719 3793 148 544 -139 C
ATOM 2503 N GLY A 227 39.776 -12.211 7.938 1.00 42.54 N
ANISOU 2503 N GLY A 227 5342 7123 3700 -125 651 -183 N
ATOM 2504 CA GLY A 227 40.070 -13.181 8.992 1.00 41.27 C
ANISOU 2504 CA GLY A 227 5181 6787 3714 -194 696 -257 C
ATOM 2505 C GLY A 227 40.129 -12.652 10.409 1.00 44.41 C
ANISOU 2505 C GLY A 227 5627 7003 4245 -187 645 -155 C
ATOM 2506 O GLY A 227 40.191 -13.437 11.357 1.00 44.97 O
ANISOU 2506 O GLY A 227 5696 6943 4446 -231 675 -215 O
ATOM 2507 N LYS A 228 40.132 -11.325 10.563 1.00 40.13 N
ANISOU 2507 N LYS A 228 5138 6445 3665 -132 579 0 N
ATOM 2508 CA LYS A 228 40.231 -10.609 11.832 1.00 38.98 C
ANISOU 2508 CA LYS A 228 5050 6136 3626 -127 531 106 C
ATOM 2509 C LYS A 228 38.994 -10.793 12.714 1.00 43.55 C
ANISOU 2509 C LYS A 228 5615 6697 4235 -115 472 30 C
ATOM 2510 O LYS A 228 37.897 -11.027 12.198 1.00 45.05 O
ANISOU 2510 O LYS A 228 5758 7040 4320 -89 445 -69 O
ATOM 2511 CB LYS A 228 40.452 -9.113 11.530 1.00 42.17 C
ANISOU 2511 CB LYS A 228 5536 6535 3951 -73 497 277 C
ATOM 2512 CG LYS A 228 41.873 -8.570 11.771 1.00 48.19 C
ANISOU 2512 CG LYS A 228 6347 7179 4786 -128 539 405 C
ATOM 2513 CD LYS A 228 43.005 -9.378 11.152 1.00 56.73 C
ANISOU 2513 CD LYS A 228 7369 8307 5879 -178 622 374 C
ATOM 2514 CE LYS A 228 44.176 -8.489 10.818 1.00 69.14 C
ANISOU 2514 CE LYS A 228 8986 9849 7437 -218 660 516 C
ATOM 2515 NZ LYS A 228 45.305 -9.263 10.249 1.00 77.18 N
ANISOU 2515 NZ LYS A 228 9932 10929 8463 -258 742 488 N
ATOM 2516 N VAL A 229 39.171 -10.695 14.053 1.00 39.26 N
ANISOU 2516 N VAL A 229 5102 5988 3828 -138 452 73 N
ATOM 2517 CA VAL A 229 38.079 -10.833 15.029 1.00 38.14 C
ANISOU 2517 CA VAL A 229 4951 5814 3727 -130 400 13 C
ATOM 2518 C VAL A 229 37.199 -9.565 14.979 1.00 42.32 C
ANISOU 2518 C VAL A 229 5524 6404 4151 -38 316 93 C
ATOM 2519 O VAL A 229 37.715 -8.460 15.173 1.00 40.12 O
ANISOU 2519 O VAL A 229 5329 6038 3875 -5 298 237 O
ATOM 2520 CB VAL A 229 38.581 -11.135 16.462 1.00 41.43 C
ANISOU 2520 CB VAL A 229 5387 6046 4309 -174 408 39 C
ATOM 2521 CG1 VAL A 229 37.416 -11.202 17.450 1.00 40.73 C
ANISOU 2521 CG1 VAL A 229 5291 5932 4251 -164 354 -15 C
ATOM 2522 CG2 VAL A 229 39.376 -12.435 16.505 1.00 41.28 C
ANISOU 2522 CG2 VAL A 229 5333 5972 4378 -230 501 -34 C
ATOM 2523 N PRO A 230 35.877 -9.688 14.698 1.00 41.04 N
ANISOU 2523 N PRO A 230 5307 6399 3886 8 273 1 N
ATOM 2524 CA PRO A 230 35.046 -8.476 14.597 1.00 41.84 C
ANISOU 2524 CA PRO A 230 5450 6577 3871 133 201 89 C
ATOM 2525 C PRO A 230 34.502 -7.984 15.944 1.00 46.68 C
ANISOU 2525 C PRO A 230 6104 7071 4561 161 148 125 C
ATOM 2526 O PRO A 230 34.630 -8.676 16.961 1.00 44.16 O
ANISOU 2526 O PRO A 230 5764 6636 4379 79 160 66 O
ATOM 2527 CB PRO A 230 33.916 -8.912 13.659 1.00 44.17 C
ANISOU 2527 CB PRO A 230 5640 7140 4004 173 181 -37 C
ATOM 2528 CG PRO A 230 33.791 -10.389 13.869 1.00 47.46 C
ANISOU 2528 CG PRO A 230 5969 7565 4499 39 230 -222 C
ATOM 2529 CD PRO A 230 35.086 -10.909 14.427 1.00 42.21 C
ANISOU 2529 CD PRO A 230 5356 6677 4007 -51 297 -189 C
ATOM 2530 N ARG A 231 33.880 -6.778 15.926 1.00 46.70 N
ANISOU 2530 N ARG A 231 6173 7105 4466 293 95 226 N
ATOM 2531 CA ARG A 231 33.217 -6.132 17.070 1.00 47.70 C
ANISOU 2531 CA ARG A 231 6349 7144 4633 351 42 266 C
ATOM 2532 C ARG A 231 32.158 -7.045 17.698 1.00 52.52 C
ANISOU 2532 C ARG A 231 6842 7850 5264 318 12 113 C
ATOM 2533 O ARG A 231 32.090 -7.097 18.916 1.00 50.97 O
ANISOU 2533 O ARG A 231 6665 7522 5181 284 -4 109 O
ATOM 2534 CB ARG A 231 32.544 -4.800 16.652 1.00 50.36 C
ANISOU 2534 CB ARG A 231 6771 7543 4819 532 5 385 C
ATOM 2535 CG ARG A 231 33.049 -3.545 17.374 1.00 59.03 C
ANISOU 2535 CG ARG A 231 8043 8408 5977 566 13 539 C
ATOM 2536 CD ARG A 231 33.028 -3.672 18.886 1.00 64.55 C
ANISOU 2536 CD ARG A 231 8751 8952 6823 501 -11 506 C
ATOM 2537 NE ARG A 231 32.115 -2.728 19.531 1.00 69.02 N
ANISOU 2537 NE ARG A 231 9394 9492 7338 639 -53 561 N
ATOM 2538 CZ ARG A 231 31.234 -3.070 20.465 1.00 78.99 C
ANISOU 2538 CZ ARG A 231 10590 10790 8634 656 -101 481 C
ATOM 2539 NH1 ARG A 231 31.112 -4.336 20.843 1.00 61.39 N
ANISOU 2539 NH1 ARG A 231 8224 8615 6486 538 -106 345 N
ATOM 2540 NH2 ARG A 231 30.456 -2.148 21.021 1.00 66.42 N
ANISOU 2540 NH2 ARG A 231 9076 9173 6987 797 -133 538 N
ATOM 2541 N LYS A 232 31.347 -7.768 16.866 1.00 51.73 N
ANISOU 2541 N LYS A 232 6618 7988 5049 314 10 -20 N
ATOM 2542 CA LYS A 232 30.290 -8.721 17.283 1.00 52.37 C
ANISOU 2542 CA LYS A 232 6576 8196 5127 252 -2 -191 C
ATOM 2543 C LYS A 232 30.724 -9.628 18.450 1.00 55.12 C
ANISOU 2543 C LYS A 232 6930 8343 5668 110 41 -252 C
ATOM 2544 O LYS A 232 29.933 -9.913 19.349 1.00 55.36 O
ANISOU 2544 O LYS A 232 6920 8379 5735 87 20 -320 O
ATOM 2545 CB LYS A 232 29.893 -9.633 16.107 1.00 56.64 C
ANISOU 2545 CB LYS A 232 6995 8979 5548 195 27 -344 C
ATOM 2546 CG LYS A 232 28.937 -9.030 15.097 1.00 81.68 C
ANISOU 2546 CG LYS A 232 10093 12450 8491 336 -29 -344 C
ATOM 2547 CD LYS A 232 28.794 -9.921 13.855 1.00 96.72 C
ANISOU 2547 CD LYS A 232 11880 14596 10274 261 6 -497 C
ATOM 2548 CE LYS A 232 29.936 -9.792 12.865 1.00110.08 C
ANISOU 2548 CE LYS A 232 13634 16249 11941 270 51 -418 C
ATOM 2549 NZ LYS A 232 29.840 -10.796 11.771 1.00120.14 N
ANISOU 2549 NZ LYS A 232 14796 17743 13109 177 94 -588 N
ATOM 2550 N LYS A 233 31.982 -10.084 18.407 1.00 50.59 N
ANISOU 2550 N LYS A 233 6407 7608 5207 28 105 -222 N
ATOM 2551 CA LYS A 233 32.597 -10.996 19.367 1.00 48.85 C
ANISOU 2551 CA LYS A 233 6200 7204 5156 -83 160 -259 C
ATOM 2552 C LYS A 233 32.945 -10.353 20.702 1.00 49.60 C
ANISOU 2552 C LYS A 233 6370 7114 5364 -58 126 -147 C
ATOM 2553 O LYS A 233 33.162 -11.080 21.668 1.00 47.92 O
ANISOU 2553 O LYS A 233 6154 6780 5271 -126 158 -182 O
ATOM 2554 CB LYS A 233 33.855 -11.591 18.742 1.00 51.43 C
ANISOU 2554 CB LYS A 233 6546 7459 5535 -144 240 -253 C
ATOM 2555 CG LYS A 233 33.688 -13.048 18.391 1.00 61.27 C
ANISOU 2555 CG LYS A 233 7734 8749 6797 -248 324 -422 C
ATOM 2556 CD LYS A 233 32.752 -13.303 17.214 1.00 63.04 C
ANISOU 2556 CD LYS A 233 7875 9219 6859 -257 319 -551 C
ATOM 2557 CE LYS A 233 31.805 -14.409 17.593 1.00 62.75 C
ANISOU 2557 CE LYS A 233 7780 9223 6838 -373 371 -740 C
ATOM 2558 NZ LYS A 233 31.350 -15.172 16.418 1.00 65.82 N
ANISOU 2558 NZ LYS A 233 8081 9848 7080 -428 396 -900 N
ATOM 2559 N VAL A 234 33.022 -9.006 20.752 1.00 46.00 N
ANISOU 2559 N VAL A 234 5987 6630 4861 39 70 -15 N
ATOM 2560 CA VAL A 234 33.314 -8.228 21.954 1.00 44.91 C
ANISOU 2560 CA VAL A 234 5929 6327 4808 59 38 85 C
ATOM 2561 C VAL A 234 31.985 -7.623 22.433 1.00 52.15 C
ANISOU 2561 C VAL A 234 6840 7321 5655 154 -29 72 C
ATOM 2562 O VAL A 234 31.471 -6.691 21.806 1.00 53.72 O
ANISOU 2562 O VAL A 234 7072 7612 5727 273 -65 128 O
ATOM 2563 CB VAL A 234 34.420 -7.172 21.700 1.00 48.07 C
ANISOU 2563 CB VAL A 234 6434 6619 5210 78 46 231 C
ATOM 2564 CG1 VAL A 234 34.623 -6.273 22.923 1.00 47.30 C
ANISOU 2564 CG1 VAL A 234 6425 6365 5180 87 15 316 C
ATOM 2565 CG2 VAL A 234 35.734 -7.845 21.308 1.00 47.33 C
ANISOU 2565 CG2 VAL A 234 6322 6476 5183 -15 112 237 C
ATOM 2566 N ASN A 235 31.396 -8.198 23.500 1.00 48.40 N
ANISOU 2566 N ASN A 235 6319 6820 5250 113 -39 -2 N
ATOM 2567 CA ASN A 235 30.094 -7.755 24.002 1.00 48.11 C
ANISOU 2567 CA ASN A 235 6256 6878 5146 197 -98 -30 C
ATOM 2568 C ASN A 235 30.276 -6.798 25.186 1.00 51.09 C
ANISOU 2568 C ASN A 235 6734 7092 5588 245 -132 71 C
ATOM 2569 O ASN A 235 30.470 -7.222 26.327 1.00 48.85 O
ANISOU 2569 O ASN A 235 6448 6696 5418 174 -124 53 O
ATOM 2570 CB ASN A 235 29.218 -8.968 24.366 1.00 48.00 C
ANISOU 2570 CB ASN A 235 6126 6963 5150 112 -79 -186 C
ATOM 2571 CG ASN A 235 27.728 -8.731 24.293 1.00 65.98 C
ANISOU 2571 CG ASN A 235 8317 9458 7295 192 -131 -258 C
ATOM 2572 OD1 ASN A 235 27.187 -7.756 24.825 1.00 67.41 O
ANISOU 2572 OD1 ASN A 235 8534 9647 7430 315 -189 -189 O
ATOM 2573 ND2 ASN A 235 27.019 -9.659 23.684 1.00 54.65 N
ANISOU 2573 ND2 ASN A 235 6762 8211 5793 118 -106 -407 N
ATOM 2574 N VAL A 236 30.219 -5.493 24.893 1.00 49.67 N
ANISOU 2574 N VAL A 236 6650 6895 5325 367 -162 178 N
ATOM 2575 CA VAL A 236 30.403 -4.445 25.888 1.00 49.71 C
ANISOU 2575 CA VAL A 236 6777 6737 5375 412 -183 270 C
ATOM 2576 C VAL A 236 29.167 -4.349 26.832 1.00 52.26 C
ANISOU 2576 C VAL A 236 7060 7119 5677 483 -230 218 C
ATOM 2577 O VAL A 236 29.335 -4.013 28.002 1.00 52.19 O
ANISOU 2577 O VAL A 236 7107 6972 5751 461 -239 242 O
ATOM 2578 CB VAL A 236 30.786 -3.089 25.221 1.00 55.53 C
ANISOU 2578 CB VAL A 236 7662 7407 6030 513 -173 401 C
ATOM 2579 CG1 VAL A 236 29.576 -2.339 24.670 1.00 57.01 C
ANISOU 2579 CG1 VAL A 236 7863 7745 6052 708 -206 425 C
ATOM 2580 CG2 VAL A 236 31.574 -2.208 26.175 1.00 55.43 C
ANISOU 2580 CG2 VAL A 236 7792 7169 6100 475 -161 485 C
ATOM 2581 N LYS A 237 27.960 -4.699 26.349 1.00 47.42 N
ANISOU 2581 N LYS A 237 6337 6729 4952 557 -256 137 N
ATOM 2582 CA LYS A 237 26.737 -4.631 27.150 1.00 46.41 C
ANISOU 2582 CA LYS A 237 6150 6699 4785 627 -298 81 C
ATOM 2583 C LYS A 237 26.753 -5.657 28.276 1.00 48.59 C
ANISOU 2583 C LYS A 237 6357 6913 5192 481 -283 -8 C
ATOM 2584 O LYS A 237 26.421 -5.307 29.411 1.00 47.24 O
ANISOU 2584 O LYS A 237 6216 6672 5062 508 -306 5 O
ATOM 2585 CB LYS A 237 25.479 -4.808 26.285 1.00 49.24 C
ANISOU 2585 CB LYS A 237 6378 7357 4975 724 -327 3 C
ATOM 2586 CG LYS A 237 25.185 -3.611 25.390 1.00 62.49 C
ANISOU 2586 CG LYS A 237 8129 9121 6494 931 -349 109 C
ATOM 2587 CD LYS A 237 23.839 -3.742 24.685 1.00 72.95 C
ANISOU 2587 CD LYS A 237 9298 10788 7630 1051 -387 31 C
ATOM 2588 CE LYS A 237 23.834 -3.111 23.317 1.00 82.80 C
ANISOU 2588 CE LYS A 237 10574 12173 8714 1204 -390 109 C
ATOM 2589 NZ LYS A 237 24.449 -4.002 22.296 1.00 93.36 N
ANISOU 2589 NZ LYS A 237 11844 13572 10057 1064 -356 48 N
ATOM 2590 N VAL A 238 27.153 -6.909 27.972 1.00 45.00 N
ANISOU 2590 N VAL A 238 5825 6475 4798 335 -235 -91 N
ATOM 2591 CA VAL A 238 27.207 -7.996 28.959 1.00 44.19 C
ANISOU 2591 CA VAL A 238 5674 6303 4815 201 -199 -167 C
ATOM 2592 C VAL A 238 28.356 -7.732 29.939 1.00 47.60 C
ANISOU 2592 C VAL A 238 6206 6500 5379 162 -188 -72 C
ATOM 2593 O VAL A 238 28.187 -8.005 31.136 1.00 46.88 O
ANISOU 2593 O VAL A 238 6109 6344 5360 126 -188 -88 O
ATOM 2594 CB VAL A 238 27.275 -9.398 28.294 1.00 48.06 C
ANISOU 2594 CB VAL A 238 6077 6861 5322 69 -131 -283 C
ATOM 2595 CG1 VAL A 238 27.469 -10.512 29.325 1.00 46.80 C
ANISOU 2595 CG1 VAL A 238 5907 6585 5292 -58 -70 -338 C
ATOM 2596 CG2 VAL A 238 26.009 -9.655 27.479 1.00 48.96 C
ANISOU 2596 CG2 VAL A 238 6071 7243 5291 86 -145 -402 C
ATOM 2597 N PHE A 239 29.483 -7.132 29.456 1.00 43.65 N
ANISOU 2597 N PHE A 239 5794 5895 4896 171 -180 26 N
ATOM 2598 CA PHE A 239 30.603 -6.775 30.332 1.00 42.33 C
ANISOU 2598 CA PHE A 239 5708 5544 4832 125 -173 110 C
ATOM 2599 C PHE A 239 30.160 -5.668 31.315 1.00 45.95 C
ANISOU 2599 C PHE A 239 6241 5941 5276 202 -222 156 C
ATOM 2600 O PHE A 239 30.468 -5.772 32.500 1.00 45.58 O
ANISOU 2600 O PHE A 239 6205 5801 5311 153 -224 164 O
ATOM 2601 CB PHE A 239 31.874 -6.348 29.550 1.00 43.97 C
ANISOU 2601 CB PHE A 239 5981 5679 5046 99 -147 192 C
ATOM 2602 CG PHE A 239 33.002 -5.961 30.481 1.00 44.69 C
ANISOU 2602 CG PHE A 239 6133 5620 5227 36 -140 263 C
ATOM 2603 CD1 PHE A 239 33.830 -6.930 31.036 1.00 47.03 C
ANISOU 2603 CD1 PHE A 239 6374 5875 5619 -52 -103 251 C
ATOM 2604 CD2 PHE A 239 33.160 -4.639 30.899 1.00 46.16 C
ANISOU 2604 CD2 PHE A 239 6432 5716 5393 69 -166 334 C
ATOM 2605 CE1 PHE A 239 34.812 -6.582 31.971 1.00 47.43 C
ANISOU 2605 CE1 PHE A 239 6455 5833 5733 -105 -103 308 C
ATOM 2606 CE2 PHE A 239 34.136 -4.295 31.837 1.00 48.15 C
ANISOU 2606 CE2 PHE A 239 6724 5856 5715 -10 -160 377 C
ATOM 2607 CZ PHE A 239 34.968 -5.265 32.354 1.00 46.06 C
ANISOU 2607 CZ PHE A 239 6378 5589 5535 -97 -135 363 C
ATOM 2608 N ILE A 240 29.442 -4.629 30.828 1.00 42.37 N
ANISOU 2608 N ILE A 240 5843 5543 4713 331 -256 189 N
ATOM 2609 CA ILE A 240 28.942 -3.536 31.666 1.00 42.43 C
ANISOU 2609 CA ILE A 240 5939 5488 4693 426 -290 230 C
ATOM 2610 C ILE A 240 28.018 -4.092 32.774 1.00 45.43 C
ANISOU 2610 C ILE A 240 6233 5928 5100 423 -314 151 C
ATOM 2611 O ILE A 240 28.216 -3.748 33.944 1.00 43.97 O
ANISOU 2611 O ILE A 240 6100 5634 4975 403 -324 170 O
ATOM 2612 CB ILE A 240 28.250 -2.436 30.822 1.00 46.87 C
ANISOU 2612 CB ILE A 240 6578 6115 5117 598 -307 283 C
ATOM 2613 CG1 ILE A 240 29.315 -1.556 30.100 1.00 48.36 C
ANISOU 2613 CG1 ILE A 240 6910 6169 5294 594 -271 389 C
ATOM 2614 CG2 ILE A 240 27.277 -1.572 31.673 1.00 47.07 C
ANISOU 2614 CG2 ILE A 240 6661 6132 5090 734 -340 293 C
ATOM 2615 CD1 ILE A 240 28.735 -0.511 29.004 1.00 55.32 C
ANISOU 2615 CD1 ILE A 240 7879 7119 6021 778 -267 462 C
ATOM 2616 N ILE A 241 27.056 -4.976 32.410 1.00 41.60 N
ANISOU 2616 N ILE A 241 5615 5623 4567 423 -316 55 N
ATOM 2617 CA ILE A 241 26.117 -5.585 33.360 1.00 41.07 C
ANISOU 2617 CA ILE A 241 5457 5635 4515 403 -326 -28 C
ATOM 2618 C ILE A 241 26.894 -6.380 34.426 1.00 45.37 C
ANISOU 2618 C ILE A 241 5999 6040 5198 268 -293 -34 C
ATOM 2619 O ILE A 241 26.579 -6.224 35.612 1.00 46.03 O
ANISOU 2619 O ILE A 241 6092 6086 5312 277 -310 -36 O
ATOM 2620 CB ILE A 241 25.022 -6.439 32.655 1.00 44.41 C
ANISOU 2620 CB ILE A 241 5733 6289 4853 391 -320 -144 C
ATOM 2621 CG1 ILE A 241 24.089 -5.545 31.813 1.00 45.52 C
ANISOU 2621 CG1 ILE A 241 5856 6611 4828 563 -365 -133 C
ATOM 2622 CG2 ILE A 241 24.201 -7.273 33.662 1.00 44.76 C
ANISOU 2622 CG2 ILE A 241 5681 6397 4929 318 -307 -240 C
ATOM 2623 CD1 ILE A 241 23.385 -6.254 30.692 1.00 50.05 C
ANISOU 2623 CD1 ILE A 241 6291 7430 5297 544 -357 -233 C
ATOM 2624 N ILE A 242 27.928 -7.167 34.033 1.00 41.45 N
ANISOU 2624 N ILE A 242 5497 5476 4776 162 -244 -26 N
ATOM 2625 CA ILE A 242 28.704 -7.934 35.021 1.00 40.71 C
ANISOU 2625 CA ILE A 242 5401 5268 4799 65 -205 -16 C
ATOM 2626 C ILE A 242 29.516 -6.956 35.905 1.00 44.85 C
ANISOU 2626 C ILE A 242 6017 5661 5364 82 -237 74 C
ATOM 2627 O ILE A 242 29.536 -7.140 37.122 1.00 44.02 O
ANISOU 2627 O ILE A 242 5906 5511 5309 57 -239 75 O
ATOM 2628 CB ILE A 242 29.543 -9.131 34.467 1.00 43.17 C
ANISOU 2628 CB ILE A 242 5682 5548 5174 -30 -133 -33 C
ATOM 2629 CG1 ILE A 242 29.865 -10.123 35.615 1.00 42.86 C
ANISOU 2629 CG1 ILE A 242 5623 5432 5229 -97 -82 -39 C
ATOM 2630 CG2 ILE A 242 30.790 -8.711 33.676 1.00 43.33 C
ANISOU 2630 CG2 ILE A 242 5755 5504 5205 -36 -126 44 C
ATOM 2631 CD1 ILE A 242 30.161 -11.591 35.251 1.00 45.95 C
ANISOU 2631 CD1 ILE A 242 5983 5804 5672 -177 15 -88 C
ATOM 2632 N ALA A 243 30.064 -5.869 35.314 1.00 41.78 N
ANISOU 2632 N ALA A 243 5715 5220 4938 121 -257 141 N
ATOM 2633 CA ALA A 243 30.782 -4.833 36.063 1.00 40.96 C
ANISOU 2633 CA ALA A 243 5711 4996 4857 115 -276 207 C
ATOM 2634 C ALA A 243 29.847 -4.191 37.110 1.00 46.51 C
ANISOU 2634 C ALA A 243 6445 5695 5530 187 -315 189 C
ATOM 2635 O ALA A 243 30.243 -4.042 38.262 1.00 46.74 O
ANISOU 2635 O ALA A 243 6495 5656 5606 145 -323 200 O
ATOM 2636 CB ALA A 243 31.339 -3.776 35.113 1.00 41.51 C
ANISOU 2636 CB ALA A 243 5883 5010 4877 138 -271 272 C
ATOM 2637 N VAL A 244 28.587 -3.893 36.718 1.00 43.57 N
ANISOU 2637 N VAL A 244 6063 5422 5072 299 -338 156 N
ATOM 2638 CA VAL A 244 27.531 -3.273 37.536 1.00 43.15 C
ANISOU 2638 CA VAL A 244 6030 5395 4968 399 -373 134 C
ATOM 2639 C VAL A 244 27.147 -4.196 38.705 1.00 45.86 C
ANISOU 2639 C VAL A 244 6279 5779 5369 339 -372 76 C
ATOM 2640 O VAL A 244 26.949 -3.697 39.804 1.00 46.63 O
ANISOU 2640 O VAL A 244 6415 5831 5473 363 -392 78 O
ATOM 2641 CB VAL A 244 26.306 -2.886 36.641 1.00 47.89 C
ANISOU 2641 CB VAL A 244 6609 6142 5444 548 -393 114 C
ATOM 2642 CG1 VAL A 244 25.007 -2.705 37.433 1.00 47.72 C
ANISOU 2642 CG1 VAL A 244 6540 6225 5366 646 -423 63 C
ATOM 2643 CG2 VAL A 244 26.608 -1.635 35.816 1.00 48.71 C
ANISOU 2643 CG2 VAL A 244 6859 6169 5479 650 -389 197 C
ATOM 2644 N PHE A 245 27.048 -5.513 38.482 1.00 40.98 N
ANISOU 2644 N PHE A 245 5550 5235 4787 259 -340 24 N
ATOM 2645 CA PHE A 245 26.686 -6.459 39.537 1.00 40.09 C
ANISOU 2645 CA PHE A 245 5362 5147 4725 197 -319 -24 C
ATOM 2646 C PHE A 245 27.766 -6.523 40.608 1.00 44.49 C
ANISOU 2646 C PHE A 245 5959 5578 5367 133 -310 30 C
ATOM 2647 O PHE A 245 27.434 -6.571 41.792 1.00 45.10 O
ANISOU 2647 O PHE A 245 6025 5653 5457 134 -319 20 O
ATOM 2648 CB PHE A 245 26.421 -7.873 38.963 1.00 41.43 C
ANISOU 2648 CB PHE A 245 5433 5393 4913 114 -262 -92 C
ATOM 2649 CG PHE A 245 24.975 -8.162 38.635 1.00 42.78 C
ANISOU 2649 CG PHE A 245 5513 5742 5001 139 -265 -187 C
ATOM 2650 CD1 PHE A 245 24.389 -7.650 37.481 1.00 45.68 C
ANISOU 2650 CD1 PHE A 245 5856 6237 5264 219 -295 -211 C
ATOM 2651 CD2 PHE A 245 24.202 -8.959 39.470 1.00 45.13 C
ANISOU 2651 CD2 PHE A 245 5739 6096 5312 83 -234 -254 C
ATOM 2652 CE1 PHE A 245 23.046 -7.921 37.173 1.00 47.18 C
ANISOU 2652 CE1 PHE A 245 5933 6635 5357 242 -301 -308 C
ATOM 2653 CE2 PHE A 245 22.858 -9.232 39.160 1.00 48.56 C
ANISOU 2653 CE2 PHE A 245 6070 6724 5658 87 -232 -356 C
ATOM 2654 CZ PHE A 245 22.296 -8.723 38.004 1.00 46.72 C
ANISOU 2654 CZ PHE A 245 5794 6641 5314 165 -269 -386 C
ATOM 2655 N PHE A 246 29.051 -6.504 40.195 1.00 40.44 N
ANISOU 2655 N PHE A 246 5484 4984 4899 80 -293 87 N
ATOM 2656 CA PHE A 246 30.207 -6.570 41.092 1.00 39.33 C
ANISOU 2656 CA PHE A 246 5359 4764 4819 20 -285 139 C
ATOM 2657 C PHE A 246 30.405 -5.286 41.888 1.00 42.42 C
ANISOU 2657 C PHE A 246 5833 5098 5187 40 -331 164 C
ATOM 2658 O PHE A 246 30.731 -5.361 43.077 1.00 41.51 O
ANISOU 2658 O PHE A 246 5705 4969 5097 11 -338 172 O
ATOM 2659 CB PHE A 246 31.495 -6.899 40.314 1.00 41.08 C
ANISOU 2659 CB PHE A 246 5580 4951 5079 -38 -252 185 C
ATOM 2660 CG PHE A 246 31.664 -8.363 39.970 1.00 42.79 C
ANISOU 2660 CG PHE A 246 5725 5192 5341 -74 -186 169 C
ATOM 2661 CD1 PHE A 246 31.864 -9.308 40.961 1.00 46.59 C
ANISOU 2661 CD1 PHE A 246 6167 5664 5873 -95 -147 178 C
ATOM 2662 CD2 PHE A 246 31.680 -8.788 38.652 1.00 44.64 C
ANISOU 2662 CD2 PHE A 246 5945 5451 5564 -83 -154 147 C
ATOM 2663 CE1 PHE A 246 32.063 -10.653 40.642 1.00 47.39 C
ANISOU 2663 CE1 PHE A 246 6233 5758 6016 -120 -66 169 C
ATOM 2664 CE2 PHE A 246 31.833 -10.136 38.341 1.00 47.15 C
ANISOU 2664 CE2 PHE A 246 6219 5773 5924 -121 -79 122 C
ATOM 2665 CZ PHE A 246 32.005 -11.062 39.336 1.00 45.11 C
ANISOU 2665 CZ PHE A 246 5938 5482 5719 -138 -30 133 C
ATOM 2666 N ILE A 247 30.237 -4.118 41.236 1.00 39.75 N
ANISOU 2666 N ILE A 247 5587 4721 4793 91 -352 176 N
ATOM 2667 CA ILE A 247 30.442 -2.803 41.852 1.00 40.28 C
ANISOU 2667 CA ILE A 247 5768 4702 4833 102 -375 192 C
ATOM 2668 C ILE A 247 29.239 -2.407 42.707 1.00 46.49 C
ANISOU 2668 C ILE A 247 6570 5517 5578 193 -403 151 C
ATOM 2669 O ILE A 247 29.418 -2.073 43.876 1.00 46.46 O
ANISOU 2669 O ILE A 247 6589 5479 5585 166 -416 140 O
ATOM 2670 CB ILE A 247 30.754 -1.697 40.782 1.00 43.59 C
ANISOU 2670 CB ILE A 247 6313 5043 5206 127 -364 232 C
ATOM 2671 CG1 ILE A 247 32.048 -1.988 39.993 1.00 43.79 C
ANISOU 2671 CG1 ILE A 247 6323 5045 5268 23 -334 273 C
ATOM 2672 CG2 ILE A 247 30.789 -0.274 41.397 1.00 43.74 C
ANISOU 2672 CG2 ILE A 247 6485 4947 5189 144 -367 237 C
ATOM 2673 CD1 ILE A 247 32.080 -1.315 38.569 1.00 51.14 C
ANISOU 2673 CD1 ILE A 247 7340 5942 6147 66 -312 312 C
ATOM 2674 N CYS A 248 28.033 -2.408 42.118 1.00 44.91 N
ANISOU 2674 N CYS A 248 6349 5397 5320 303 -412 123 N
ATOM 2675 CA CYS A 248 26.806 -1.923 42.752 1.00 45.67 C
ANISOU 2675 CA CYS A 248 6455 5543 5356 415 -437 85 C
ATOM 2676 C CYS A 248 26.077 -2.939 43.605 1.00 47.07 C
ANISOU 2676 C CYS A 248 6506 5829 5552 395 -440 31 C
ATOM 2677 O CYS A 248 25.541 -2.537 44.631 1.00 47.78 O
ANISOU 2677 O CYS A 248 6610 5923 5619 440 -457 9 O
ATOM 2678 CB CYS A 248 25.857 -1.363 41.696 1.00 47.72 C
ANISOU 2678 CB CYS A 248 6742 5871 5519 561 -445 86 C
ATOM 2679 SG CYS A 248 26.608 -0.140 40.593 1.00 52.98 S
ANISOU 2679 SG CYS A 248 7581 6400 6147 603 -424 163 S
ATOM 2680 N PHE A 249 25.946 -4.203 43.166 1.00 40.83 N
ANISOU 2680 N PHE A 249 5600 5122 4792 335 -414 5 N
ATOM 2681 CA PHE A 249 25.077 -5.122 43.892 1.00 39.97 C
ANISOU 2681 CA PHE A 249 5386 5115 4688 315 -400 -51 C
ATOM 2682 C PHE A 249 25.747 -6.128 44.816 1.00 43.25 C
ANISOU 2682 C PHE A 249 5761 5486 5185 208 -364 -37 C
ATOM 2683 O PHE A 249 25.130 -6.464 45.825 1.00 42.28 O
ANISOU 2683 O PHE A 249 5596 5410 5059 207 -358 -65 O
ATOM 2684 CB PHE A 249 24.162 -5.871 42.915 1.00 41.83 C
ANISOU 2684 CB PHE A 249 5521 5493 4879 319 -380 -113 C
ATOM 2685 CG PHE A 249 23.331 -4.958 42.038 1.00 43.76 C
ANISOU 2685 CG PHE A 249 5779 5833 5016 453 -417 -126 C
ATOM 2686 CD1 PHE A 249 22.603 -3.905 42.591 1.00 46.95 C
ANISOU 2686 CD1 PHE A 249 6228 6263 5348 587 -454 -125 C
ATOM 2687 CD2 PHE A 249 23.291 -5.138 40.663 1.00 45.62 C
ANISOU 2687 CD2 PHE A 249 5985 6136 5211 461 -409 -135 C
ATOM 2688 CE1 PHE A 249 21.861 -3.046 41.782 1.00 48.19 C
ANISOU 2688 CE1 PHE A 249 6407 6510 5393 744 -480 -120 C
ATOM 2689 CE2 PHE A 249 22.550 -4.277 39.853 1.00 49.61 C
ANISOU 2689 CE2 PHE A 249 6502 6746 5600 609 -441 -132 C
ATOM 2690 CZ PHE A 249 21.830 -3.245 40.422 1.00 48.25 C
ANISOU 2690 CZ PHE A 249 6379 6599 5356 758 -475 -120 C
ATOM 2691 N VAL A 250 26.957 -6.624 44.493 1.00 39.78 N
ANISOU 2691 N VAL A 250 5333 4971 4810 132 -335 11 N
ATOM 2692 CA VAL A 250 27.627 -7.651 45.303 1.00 39.31 C
ANISOU 2692 CA VAL A 250 5236 4882 4817 61 -291 40 C
ATOM 2693 C VAL A 250 27.921 -7.152 46.744 1.00 43.32 C
ANISOU 2693 C VAL A 250 5769 5368 5324 69 -321 66 C
ATOM 2694 O VAL A 250 27.573 -7.891 47.666 1.00 42.47 O
ANISOU 2694 O VAL A 250 5616 5293 5230 56 -293 61 O
ATOM 2695 CB VAL A 250 28.887 -8.263 44.612 1.00 42.31 C
ANISOU 2695 CB VAL A 250 5617 5207 5252 4 -251 90 C
ATOM 2696 CG1 VAL A 250 29.783 -8.997 45.600 1.00 41.22 C
ANISOU 2696 CG1 VAL A 250 5458 5041 5164 -30 -216 145 C
ATOM 2697 CG2 VAL A 250 28.470 -9.209 43.497 1.00 42.41 C
ANISOU 2697 CG2 VAL A 250 5589 5251 5272 -23 -197 47 C
ATOM 2698 N PRO A 251 28.492 -5.943 46.993 1.00 40.73 N
ANISOU 2698 N PRO A 251 5513 4988 4973 82 -369 87 N
ATOM 2699 CA PRO A 251 28.765 -5.551 48.391 1.00 40.31 C
ANISOU 2699 CA PRO A 251 5473 4933 4911 73 -393 95 C
ATOM 2700 C PRO A 251 27.509 -5.475 49.276 1.00 41.79 C
ANISOU 2700 C PRO A 251 5642 5178 5059 131 -405 47 C
ATOM 2701 O PRO A 251 27.522 -5.992 50.402 1.00 40.39 O
ANISOU 2701 O PRO A 251 5422 5037 4888 115 -393 56 O
ATOM 2702 CB PRO A 251 29.451 -4.183 48.254 1.00 42.70 C
ANISOU 2702 CB PRO A 251 5875 5162 5187 60 -428 101 C
ATOM 2703 CG PRO A 251 29.997 -4.162 46.857 1.00 47.11 C
ANISOU 2703 CG PRO A 251 6456 5681 5764 38 -412 128 C
ATOM 2704 CD PRO A 251 28.996 -4.921 46.045 1.00 42.39 C
ANISOU 2704 CD PRO A 251 5806 5137 5165 89 -391 103 C
ATOM 2705 N PHE A 252 26.423 -4.885 48.762 1.00 38.13 N
ANISOU 2705 N PHE A 252 5201 4740 4545 208 -423 1 N
ATOM 2706 CA PHE A 252 25.159 -4.744 49.501 1.00 37.80 C
ANISOU 2706 CA PHE A 252 5131 4778 4452 275 -435 -50 C
ATOM 2707 C PHE A 252 24.566 -6.090 49.898 1.00 39.40 C
ANISOU 2707 C PHE A 252 5228 5067 4676 233 -388 -68 C
ATOM 2708 O PHE A 252 24.110 -6.238 51.030 1.00 38.43 O
ANISOU 2708 O PHE A 252 5076 4989 4535 241 -384 -83 O
ATOM 2709 CB PHE A 252 24.120 -3.936 48.694 1.00 40.15 C
ANISOU 2709 CB PHE A 252 5459 5118 4678 388 -458 -88 C
ATOM 2710 CG PHE A 252 22.791 -3.752 49.398 1.00 41.66 C
ANISOU 2710 CG PHE A 252 5606 5419 4803 474 -469 -143 C
ATOM 2711 CD1 PHE A 252 22.677 -2.909 50.496 1.00 44.40 C
ANISOU 2711 CD1 PHE A 252 6016 5735 5118 524 -492 -153 C
ATOM 2712 CD2 PHE A 252 21.658 -4.441 48.972 1.00 43.25 C
ANISOU 2712 CD2 PHE A 252 5697 5769 4966 494 -452 -194 C
ATOM 2713 CE1 PHE A 252 21.456 -2.761 51.160 1.00 45.90 C
ANISOU 2713 CE1 PHE A 252 6159 6038 5242 610 -499 -204 C
ATOM 2714 CE2 PHE A 252 20.443 -4.303 49.644 1.00 46.18 C
ANISOU 2714 CE2 PHE A 252 6010 6268 5268 567 -460 -247 C
ATOM 2715 CZ PHE A 252 20.346 -3.450 50.722 1.00 44.72 C
ANISOU 2715 CZ PHE A 252 5890 6047 5054 635 -484 -247 C
ATOM 2716 N HIS A 253 24.577 -7.065 48.983 1.00 35.77 N
ANISOU 2716 N HIS A 253 4718 4623 4249 182 -342 -72 N
ATOM 2717 CA HIS A 253 23.995 -8.376 49.242 1.00 35.69 C
ANISOU 2717 CA HIS A 253 4630 4671 4259 121 -274 -99 C
ATOM 2718 C HIS A 253 24.830 -9.204 50.219 1.00 42.48 C
ANISOU 2718 C HIS A 253 5493 5472 5175 68 -226 -35 C
ATOM 2719 O HIS A 253 24.265 -10.033 50.930 1.00 42.69 O
ANISOU 2719 O HIS A 253 5481 5536 5204 37 -170 -47 O
ATOM 2720 CB HIS A 253 23.705 -9.103 47.933 1.00 35.70 C
ANISOU 2720 CB HIS A 253 4591 4704 4269 75 -230 -139 C
ATOM 2721 CG HIS A 253 22.549 -8.470 47.223 1.00 38.48 C
ANISOU 2721 CG HIS A 253 4905 5180 4538 140 -269 -210 C
ATOM 2722 ND1 HIS A 253 22.735 -7.437 46.328 1.00 39.84 N
ANISOU 2722 ND1 HIS A 253 5126 5340 4672 220 -325 -196 N
ATOM 2723 CD2 HIS A 253 21.221 -8.644 47.410 1.00 39.89 C
ANISOU 2723 CD2 HIS A 253 5000 5506 4652 152 -261 -288 C
ATOM 2724 CE1 HIS A 253 21.526 -7.067 45.940 1.00 39.01 C
ANISOU 2724 CE1 HIS A 253 4964 5379 4477 295 -349 -258 C
ATOM 2725 NE2 HIS A 253 20.584 -7.769 46.556 1.00 39.68 N
ANISOU 2725 NE2 HIS A 253 4958 5577 4541 253 -315 -321 N
ATOM 2726 N PHE A 254 26.141 -8.917 50.322 1.00 41.35 N
ANISOU 2726 N PHE A 254 5394 5255 5064 64 -246 34 N
ATOM 2727 CA PHE A 254 27.064 -9.514 51.295 1.00 41.26 C
ANISOU 2727 CA PHE A 254 5377 5218 5082 45 -215 107 C
ATOM 2728 C PHE A 254 26.787 -8.947 52.705 1.00 43.89 C
ANISOU 2728 C PHE A 254 5708 5599 5369 78 -254 105 C
ATOM 2729 O PHE A 254 26.765 -9.691 53.685 1.00 43.43 O
ANISOU 2729 O PHE A 254 5624 5567 5311 75 -210 141 O
ATOM 2730 CB PHE A 254 28.516 -9.211 50.877 1.00 43.51 C
ANISOU 2730 CB PHE A 254 5687 5453 5393 32 -237 166 C
ATOM 2731 CG PHE A 254 29.202 -10.207 49.967 1.00 46.28 C
ANISOU 2731 CG PHE A 254 6029 5760 5797 4 -170 205 C
ATOM 2732 CD1 PHE A 254 28.466 -11.105 49.204 1.00 50.90 C
ANISOU 2732 CD1 PHE A 254 6605 6331 6406 -22 -102 165 C
ATOM 2733 CD2 PHE A 254 30.583 -10.236 49.860 1.00 50.11 C
ANISOU 2733 CD2 PHE A 254 6511 6228 6300 -1 -171 273 C
ATOM 2734 CE1 PHE A 254 29.106 -12.029 48.368 1.00 52.39 C
ANISOU 2734 CE1 PHE A 254 6798 6466 6641 -47 -30 193 C
ATOM 2735 CE2 PHE A 254 31.220 -11.165 49.030 1.00 53.50 C
ANISOU 2735 CE2 PHE A 254 6935 6619 6773 -10 -103 310 C
ATOM 2736 CZ PHE A 254 30.478 -12.056 48.292 1.00 51.57 C
ANISOU 2736 CZ PHE A 254 6699 6338 6558 -30 -30 270 C
ATOM 2737 N ALA A 255 26.542 -7.625 52.785 1.00 40.25 N
ANISOU 2737 N ALA A 255 5285 5144 4862 115 -328 63 N
ATOM 2738 CA ALA A 255 26.300 -6.858 54.007 1.00 40.15 C
ANISOU 2738 CA ALA A 255 5288 5169 4797 147 -370 42 C
ATOM 2739 C ALA A 255 24.877 -7.029 54.597 1.00 44.77 C
ANISOU 2739 C ALA A 255 5836 5833 5341 187 -357 -11 C
ATOM 2740 O ALA A 255 24.670 -6.784 55.795 1.00 43.90 O
ANISOU 2740 O ALA A 255 5720 5768 5191 208 -371 -17 O
ATOM 2741 CB ALA A 255 26.548 -5.383 53.720 1.00 40.83 C
ANISOU 2741 CB ALA A 255 5458 5204 4851 169 -433 10 C
ATOM 2742 N ARG A 256 23.916 -7.441 53.753 1.00 41.34 N
ANISOU 2742 N ARG A 256 5368 5434 4907 193 -330 -55 N
ATOM 2743 CA ARG A 256 22.497 -7.543 54.070 1.00 40.71 C
ANISOU 2743 CA ARG A 256 5234 5459 4775 224 -317 -119 C
ATOM 2744 C ARG A 256 22.097 -8.595 55.113 1.00 43.89 C
ANISOU 2744 C ARG A 256 5582 5914 5180 178 -251 -108 C
ATOM 2745 O ARG A 256 21.434 -8.199 56.069 1.00 43.24 O
ANISOU 2745 O ARG A 256 5482 5904 5043 220 -269 -136 O
ATOM 2746 CB ARG A 256 21.648 -7.737 52.800 1.00 38.64 C
ANISOU 2746 CB ARG A 256 4928 5255 4498 227 -304 -177 C
ATOM 2747 CG ARG A 256 20.700 -6.564 52.548 1.00 42.53 C
ANISOU 2747 CG ARG A 256 5426 5827 4908 341 -363 -235 C
ATOM 2748 CD ARG A 256 19.615 -6.448 53.619 1.00 44.33 C
ANISOU 2748 CD ARG A 256 5601 6173 5071 386 -362 -282 C
ATOM 2749 NE ARG A 256 18.928 -5.158 53.610 1.00 40.66 N
ANISOU 2749 NE ARG A 256 5168 5756 4523 529 -419 -319 N
ATOM 2750 CZ ARG A 256 18.194 -4.694 54.615 1.00 52.38 C
ANISOU 2750 CZ ARG A 256 6640 7318 5946 601 -432 -352 C
ATOM 2751 NH1 ARG A 256 18.055 -5.402 55.729 1.00 37.43 N
ANISOU 2751 NH1 ARG A 256 4693 5466 4061 534 -396 -352 N
ATOM 2752 NH2 ARG A 256 17.606 -3.511 54.522 1.00 45.57 N
ANISOU 2752 NH2 ARG A 256 5824 6484 5005 750 -472 -380 N
ATOM 2753 N ILE A 257 22.412 -9.903 54.935 1.00 40.58 N
ANISOU 2753 N ILE A 257 5145 5457 4815 99 -165 -69 N
ATOM 2754 CA ILE A 257 21.952 -10.932 55.894 1.00 40.87 C
ANISOU 2754 CA ILE A 257 5152 5528 4850 55 -80 -52 C
ATOM 2755 C ILE A 257 22.375 -10.586 57.353 1.00 44.12 C
ANISOU 2755 C ILE A 257 5577 5958 5229 103 -108 3 C
ATOM 2756 O ILE A 257 21.469 -10.519 58.182 1.00 44.91 O
ANISOU 2756 O ILE A 257 5642 6143 5277 115 -100 -33 O
ATOM 2757 CB ILE A 257 22.297 -12.405 55.522 1.00 44.34 C
ANISOU 2757 CB ILE A 257 5605 5887 5353 -29 39 -9 C
ATOM 2758 CG1 ILE A 257 21.715 -12.773 54.131 1.00 44.76 C
ANISOU 2758 CG1 ILE A 257 5633 5952 5422 -97 74 -91 C
ATOM 2759 CG2 ILE A 257 21.765 -13.379 56.600 1.00 45.68 C
ANISOU 2759 CG2 ILE A 257 5771 6074 5512 -68 141 20 C
ATOM 2760 CD1 ILE A 257 22.382 -13.988 53.422 1.00 49.99 C
ANISOU 2760 CD1 ILE A 257 6339 6499 6155 -170 179 -56 C
ATOM 2761 N PRO A 258 23.656 -10.311 57.716 1.00 38.94 N
ANISOU 2761 N PRO A 258 4958 5251 4587 128 -143 77 N
ATOM 2762 CA PRO A 258 23.939 -9.984 59.128 1.00 38.62 C
ANISOU 2762 CA PRO A 258 4914 5266 4495 167 -170 112 C
ATOM 2763 C PRO A 258 23.141 -8.766 59.638 1.00 41.80 C
ANISOU 2763 C PRO A 258 5315 5737 4829 215 -245 29 C
ATOM 2764 O PRO A 258 22.724 -8.766 60.796 1.00 41.97 O
ANISOU 2764 O PRO A 258 5315 5833 4798 237 -239 28 O
ATOM 2765 CB PRO A 258 25.456 -9.731 59.155 1.00 39.92 C
ANISOU 2765 CB PRO A 258 5101 5394 4674 175 -209 180 C
ATOM 2766 CG PRO A 258 25.865 -9.591 57.765 1.00 43.78 C
ANISOU 2766 CG PRO A 258 5614 5804 5217 150 -221 167 C
ATOM 2767 CD PRO A 258 24.899 -10.341 56.918 1.00 39.33 C
ANISOU 2767 CD PRO A 258 5039 5218 4688 117 -155 128 C
ATOM 2768 N TYR A 259 22.887 -7.765 58.768 1.00 37.32 N
ANISOU 2768 N TYR A 259 4779 5145 4258 242 -305 -36 N
ATOM 2769 CA TYR A 259 22.125 -6.560 59.107 1.00 36.70 C
ANISOU 2769 CA TYR A 259 4722 5111 4113 312 -364 -112 C
ATOM 2770 C TYR A 259 20.630 -6.878 59.314 1.00 42.05 C
ANISOU 2770 C TYR A 259 5332 5899 4746 339 -330 -169 C
ATOM 2771 O TYR A 259 20.003 -6.295 60.202 1.00 42.79 O
ANISOU 2771 O TYR A 259 5419 6065 4773 396 -352 -210 O
ATOM 2772 CB TYR A 259 22.302 -5.448 58.050 1.00 36.37 C
ANISOU 2772 CB TYR A 259 4752 4996 4073 352 -419 -148 C
ATOM 2773 CG TYR A 259 21.533 -4.194 58.412 1.00 37.29 C
ANISOU 2773 CG TYR A 259 4916 5137 4115 448 -462 -218 C
ATOM 2774 CD1 TYR A 259 21.811 -3.501 59.589 1.00 39.21 C
ANISOU 2774 CD1 TYR A 259 5202 5383 4312 464 -489 -236 C
ATOM 2775 CD2 TYR A 259 20.438 -3.780 57.658 1.00 37.84 C
ANISOU 2775 CD2 TYR A 259 4978 5252 4147 534 -469 -270 C
ATOM 2776 CE1 TYR A 259 21.066 -2.387 59.968 1.00 38.92 C
ANISOU 2776 CE1 TYR A 259 5223 5359 4205 561 -514 -305 C
ATOM 2777 CE2 TYR A 259 19.689 -2.659 58.023 1.00 39.35 C
ANISOU 2777 CE2 TYR A 259 5219 5469 4261 652 -497 -326 C
ATOM 2778 CZ TYR A 259 20.017 -1.959 59.177 1.00 44.59 C
ANISOU 2778 CZ TYR A 259 5948 6105 4891 665 -515 -344 C
ATOM 2779 OH TYR A 259 19.309 -0.857 59.577 1.00 41.50 O
ANISOU 2779 OH TYR A 259 5623 5722 4422 787 -531 -403 O
ATOM 2780 N THR A 260 20.069 -7.788 58.500 1.00 39.13 N
ANISOU 2780 N THR A 260 4908 5554 4405 289 -274 -181 N
ATOM 2781 CA THR A 260 18.672 -8.235 58.606 1.00 39.87 C
ANISOU 2781 CA THR A 260 4916 5779 4452 281 -229 -245 C
ATOM 2782 C THR A 260 18.500 -8.998 59.925 1.00 44.42 C
ANISOU 2782 C THR A 260 5464 6400 5012 239 -167 -212 C
ATOM 2783 O THR A 260 17.521 -8.757 60.632 1.00 44.80 O
ANISOU 2783 O THR A 260 5463 6568 4992 273 -167 -262 O
ATOM 2784 CB THR A 260 18.272 -9.062 57.379 1.00 44.45 C
ANISOU 2784 CB THR A 260 5449 6375 5065 205 -175 -276 C
ATOM 2785 OG1 THR A 260 18.372 -8.217 56.235 1.00 40.10 O
ANISOU 2785 OG1 THR A 260 4924 5802 4509 267 -240 -302 O
ATOM 2786 CG2 THR A 260 16.847 -9.621 57.477 1.00 43.87 C
ANISOU 2786 CG2 THR A 260 5270 6464 4934 163 -120 -357 C
ATOM 2787 N LEU A 261 19.487 -9.855 60.278 1.00 40.94 N
ANISOU 2787 N LEU A 261 5058 5871 4626 183 -115 -120 N
ATOM 2788 CA LEU A 261 19.516 -10.633 61.523 1.00 41.78 C
ANISOU 2788 CA LEU A 261 5156 6003 4714 159 -47 -59 C
ATOM 2789 C LEU A 261 19.490 -9.729 62.781 1.00 46.65 C
ANISOU 2789 C LEU A 261 5774 6695 5257 237 -112 -66 C
ATOM 2790 O LEU A 261 18.888 -10.103 63.791 1.00 47.44 O
ANISOU 2790 O LEU A 261 5841 6878 5308 233 -65 -60 O
ATOM 2791 CB LEU A 261 20.757 -11.547 61.571 1.00 41.44 C
ANISOU 2791 CB LEU A 261 5162 5851 4731 129 11 56 C
ATOM 2792 CG LEU A 261 20.792 -12.760 60.619 1.00 45.81 C
ANISOU 2792 CG LEU A 261 5733 6316 5356 44 117 74 C
ATOM 2793 CD1 LEU A 261 22.076 -13.544 60.804 1.00 46.46 C
ANISOU 2793 CD1 LEU A 261 5872 6295 5483 57 170 199 C
ATOM 2794 CD2 LEU A 261 19.607 -13.688 60.831 1.00 46.48 C
ANISOU 2794 CD2 LEU A 261 5787 6447 5425 -42 233 35 C
ATOM 2795 N SER A 262 20.133 -8.545 62.701 1.00 41.95 N
ANISOU 2795 N SER A 262 5224 6067 4650 297 -210 -84 N
ATOM 2796 CA SER A 262 20.211 -7.570 63.790 1.00 41.22 C
ANISOU 2796 CA SER A 262 5149 6029 4485 359 -272 -110 C
ATOM 2797 C SER A 262 18.898 -6.802 63.959 1.00 44.90 C
ANISOU 2797 C SER A 262 5591 6587 4883 426 -296 -208 C
ATOM 2798 O SER A 262 18.603 -6.346 65.059 1.00 45.31 O
ANISOU 2798 O SER A 262 5638 6713 4864 470 -312 -233 O
ATOM 2799 CB SER A 262 21.370 -6.595 63.559 1.00 42.87 C
ANISOU 2799 CB SER A 262 5427 6157 4704 372 -348 -108 C
ATOM 2800 OG SER A 262 21.117 -5.644 62.536 1.00 47.00 O
ANISOU 2800 OG SER A 262 6000 6619 5239 406 -395 -173 O
ATOM 2801 N GLN A 263 18.133 -6.645 62.867 1.00 41.52 N
ANISOU 2801 N GLN A 263 5142 6168 4464 445 -299 -264 N
ATOM 2802 CA GLN A 263 16.853 -5.928 62.804 1.00 41.02 C
ANISOU 2802 CA GLN A 263 5043 6215 4328 534 -320 -354 C
ATOM 2803 C GLN A 263 15.675 -6.744 63.346 1.00 45.80 C
ANISOU 2803 C GLN A 263 5540 6976 4887 501 -252 -382 C
ATOM 2804 O GLN A 263 14.759 -6.164 63.948 1.00 45.93 O
ANISOU 2804 O GLN A 263 5519 7113 4819 582 -266 -442 O
ATOM 2805 CB GLN A 263 16.534 -5.555 61.339 1.00 41.50 C
ANISOU 2805 CB GLN A 263 5107 6258 4402 573 -345 -392 C
ATOM 2806 CG GLN A 263 17.265 -4.336 60.782 1.00 37.86 C
ANISOU 2806 CG GLN A 263 4764 5667 3954 644 -412 -391 C
ATOM 2807 CD GLN A 263 16.833 -4.045 59.357 1.00 48.33 C
ANISOU 2807 CD GLN A 263 6085 6997 5279 696 -426 -417 C
ATOM 2808 OE1 GLN A 263 16.965 -4.882 58.454 1.00 42.79 O
ANISOU 2808 OE1 GLN A 263 5340 6289 4631 616 -397 -397 O
ATOM 2809 NE2 GLN A 263 16.327 -2.844 59.107 1.00 33.55 N
ANISOU 2809 NE2 GLN A 263 4269 5137 3341 841 -465 -460 N
ATOM 2810 N THR A 264 15.667 -8.071 63.077 1.00 43.42 N
ANISOU 2810 N THR A 264 5192 6669 4636 380 -168 -344 N
ATOM 2811 CA THR A 264 14.552 -8.970 63.402 1.00 44.81 C
ANISOU 2811 CA THR A 264 5271 6980 4775 307 -80 -377 C
ATOM 2812 C THR A 264 14.647 -9.583 64.815 1.00 52.15 C
ANISOU 2812 C THR A 264 6202 7931 5680 272 -20 -318 C
ATOM 2813 O THR A 264 13.619 -9.997 65.344 1.00 53.12 O
ANISOU 2813 O THR A 264 6248 8190 5745 239 39 -358 O
ATOM 2814 CB THR A 264 14.400 -10.042 62.321 1.00 51.99 C
ANISOU 2814 CB THR A 264 6147 7862 5744 180 -2 -384 C
ATOM 2815 OG1 THR A 264 15.593 -10.815 62.243 1.00 53.08 O
ANISOU 2815 OG1 THR A 264 6369 7830 5971 116 41 -285 O
ATOM 2816 CG2 THR A 264 14.083 -9.444 60.951 1.00 48.99 C
ANISOU 2816 CG2 THR A 264 5737 7519 5359 220 -58 -455 C
ATOM 2817 N ARG A 265 15.850 -9.626 65.426 1.00 50.15 N
ANISOU 2817 N ARG A 265 6028 7569 5460 283 -34 -226 N
ATOM 2818 CA ARG A 265 16.074 -10.082 66.808 1.00 50.99 C
ANISOU 2818 CA ARG A 265 6140 7708 5526 279 12 -156 C
ATOM 2819 C ARG A 265 17.018 -9.124 67.502 1.00 55.23 C
ANISOU 2819 C ARG A 265 6731 8220 6033 363 -80 -131 C
ATOM 2820 O ARG A 265 17.922 -8.594 66.859 1.00 53.65 O
ANISOU 2820 O ARG A 265 6584 7921 5879 380 -144 -122 O
ATOM 2821 CB ARG A 265 16.660 -11.510 66.887 1.00 53.01 C
ANISOU 2821 CB ARG A 265 6429 7875 5838 188 128 -46 C
ATOM 2822 CG ARG A 265 15.740 -12.668 66.515 1.00 65.16 C
ANISOU 2822 CG ARG A 265 7931 9432 7394 68 258 -69 C
ATOM 2823 CD ARG A 265 14.636 -12.970 67.522 1.00 76.75 C
ANISOU 2823 CD ARG A 265 9340 11040 8780 37 330 -93 C
ATOM 2824 NE ARG A 265 15.075 -13.470 68.834 1.00 79.31 N
ANISOU 2824 NE ARG A 265 9709 11354 9070 60 388 21 N
ATOM 2825 CZ ARG A 265 15.439 -14.726 69.100 1.00 84.28 C
ANISOU 2825 CZ ARG A 265 10402 11889 9731 -8 525 129 C
ATOM 2826 NH1 ARG A 265 15.549 -15.617 68.121 1.00 70.00 N
ANISOU 2826 NH1 ARG A 265 8633 9963 8000 -113 622 131 N
ATOM 2827 NH2 ARG A 265 15.741 -15.086 70.340 1.00 59.85 N
ANISOU 2827 NH2 ARG A 265 7342 8814 6583 40 573 237 N
ATOM 2828 N ASP A 266 16.841 -8.919 68.812 1.00 54.02 N
ANISOU 2828 N ASP A 266 6562 8164 5798 403 -82 -125 N
ATOM 2829 CA ASP A 266 17.729 -8.056 69.588 1.00 54.95 C
ANISOU 2829 CA ASP A 266 6722 8285 5870 462 -161 -117 C
ATOM 2830 C ASP A 266 18.860 -8.946 70.117 1.00 58.38 C
ANISOU 2830 C ASP A 266 7173 8692 6319 433 -118 14 C
ATOM 2831 O ASP A 266 18.900 -9.275 71.300 1.00 59.42 O
ANISOU 2831 O ASP A 266 7283 8914 6379 452 -86 66 O
ATOM 2832 CB ASP A 266 16.942 -7.341 70.702 1.00 58.67 C
ANISOU 2832 CB ASP A 266 7166 8893 6235 527 -183 -187 C
ATOM 2833 CG ASP A 266 17.652 -6.140 71.292 1.00 79.41 C
ANISOU 2833 CG ASP A 266 9846 11519 8807 582 -273 -234 C
ATOM 2834 OD1 ASP A 266 18.144 -5.291 70.503 1.00 82.11 O
ANISOU 2834 OD1 ASP A 266 10252 11760 9186 596 -336 -282 O
ATOM 2835 OD2 ASP A 266 17.673 -6.016 72.542 1.00 87.26 O
ANISOU 2835 OD2 ASP A 266 10824 12618 9714 607 -274 -232 O
ATOM 2836 N VAL A 267 19.754 -9.360 69.197 1.00 53.25 N
ANISOU 2836 N VAL A 267 6556 7925 5753 399 -114 72 N
ATOM 2837 CA VAL A 267 20.837 -10.333 69.380 1.00 52.38 C
ANISOU 2837 CA VAL A 267 6461 7773 5667 389 -60 206 C
ATOM 2838 C VAL A 267 22.255 -9.687 69.380 1.00 52.62 C
ANISOU 2838 C VAL A 267 6508 7794 5689 414 -149 229 C
ATOM 2839 O VAL A 267 23.175 -10.239 69.985 1.00 51.24 O
ANISOU 2839 O VAL A 267 6323 7664 5482 442 -127 335 O
ATOM 2840 CB VAL A 267 20.673 -11.407 68.249 1.00 56.04 C
ANISOU 2840 CB VAL A 267 6947 8117 6229 326 33 245 C
ATOM 2841 CG1 VAL A 267 22.001 -11.931 67.722 1.00 55.77 C
ANISOU 2841 CG1 VAL A 267 6950 7988 6253 331 47 345 C
ATOM 2842 CG2 VAL A 267 19.788 -12.556 68.709 1.00 56.64 C
ANISOU 2842 CG2 VAL A 267 7014 8212 6292 282 168 286 C
ATOM 2843 N PHE A 268 22.433 -8.559 68.696 1.00 47.87 N
ANISOU 2843 N PHE A 268 5933 7146 5110 405 -238 135 N
ATOM 2844 CA PHE A 268 23.745 -7.931 68.609 1.00 47.26 C
ANISOU 2844 CA PHE A 268 5871 7060 5026 397 -312 140 C
ATOM 2845 C PHE A 268 23.928 -6.814 69.606 1.00 54.07 C
ANISOU 2845 C PHE A 268 6733 8020 5791 410 -386 63 C
ATOM 2846 O PHE A 268 22.956 -6.153 69.975 1.00 54.99 O
ANISOU 2846 O PHE A 268 6865 8165 5866 435 -400 -27 O
ATOM 2847 CB PHE A 268 23.967 -7.366 67.195 1.00 47.59 C
ANISOU 2847 CB PHE A 268 5960 6971 5151 363 -351 87 C
ATOM 2848 CG PHE A 268 24.161 -8.389 66.097 1.00 48.10 C
ANISOU 2848 CG PHE A 268 6026 6938 5310 337 -289 158 C
ATOM 2849 CD1 PHE A 268 23.069 -9.003 65.493 1.00 49.48 C
ANISOU 2849 CD1 PHE A 268 6198 7070 5531 323 -224 141 C
ATOM 2850 CD2 PHE A 268 25.433 -8.702 65.633 1.00 49.75 C
ANISOU 2850 CD2 PHE A 268 6236 7110 5555 321 -293 229 C
ATOM 2851 CE1 PHE A 268 23.244 -9.918 64.454 1.00 49.50 C
ANISOU 2851 CE1 PHE A 268 6211 6979 5616 285 -161 189 C
ATOM 2852 CE2 PHE A 268 25.608 -9.625 64.593 1.00 51.46 C
ANISOU 2852 CE2 PHE A 268 6466 7230 5858 302 -230 287 C
ATOM 2853 CZ PHE A 268 24.511 -10.222 64.008 1.00 48.65 C
ANISOU 2853 CZ PHE A 268 6120 6817 5550 280 -163 263 C
ATOM 2854 N ASP A 269 25.199 -6.569 69.992 1.00 52.11 N
ANISOU 2854 N ASP A 269 6467 7834 5500 390 -430 88 N
ATOM 2855 CA ASP A 269 25.659 -5.439 70.799 1.00 53.69 C
ANISOU 2855 CA ASP A 269 6671 8124 5605 367 -502 -4 C
ATOM 2856 C ASP A 269 25.416 -4.138 70.041 1.00 59.54 C
ANISOU 2856 C ASP A 269 7505 8739 6380 329 -550 -136 C
ATOM 2857 O ASP A 269 25.424 -4.152 68.812 1.00 58.36 O
ANISOU 2857 O ASP A 269 7396 8455 6323 315 -543 -130 O
ATOM 2858 CB ASP A 269 27.169 -5.573 71.070 1.00 56.48 C
ANISOU 2858 CB ASP A 269 6968 8581 5912 333 -533 53 C
ATOM 2859 CG ASP A 269 27.544 -5.990 72.467 1.00 70.84 C
ANISOU 2859 CG ASP A 269 8702 10608 7604 375 -530 110 C
ATOM 2860 OD1 ASP A 269 26.629 -6.301 73.260 1.00 73.11 O
ANISOU 2860 OD1 ASP A 269 8982 10949 7848 430 -494 123 O
ATOM 2861 OD2 ASP A 269 28.754 -6.013 72.771 1.00 78.23 O
ANISOU 2861 OD2 ASP A 269 9573 11675 8476 355 -564 143 O
ATOM 2862 N CYS A 270 25.272 -3.020 70.756 1.00 59.84 N
ANISOU 2862 N CYS A 270 7585 8815 6337 316 -590 -251 N
ATOM 2863 CA CYS A 270 25.034 -1.684 70.214 1.00 61.83 C
ANISOU 2863 CA CYS A 270 7954 8936 6602 295 -618 -378 C
ATOM 2864 C CYS A 270 26.033 -1.316 69.092 1.00 59.13 C
ANISOU 2864 C CYS A 270 7664 8475 6328 215 -638 -379 C
ATOM 2865 O CYS A 270 25.612 -0.962 67.986 1.00 57.39 O
ANISOU 2865 O CYS A 270 7522 8102 6180 235 -629 -398 O
ATOM 2866 CB CYS A 270 25.065 -0.653 71.339 1.00 66.70 C
ANISOU 2866 CB CYS A 270 8611 9625 7107 274 -645 -496 C
ATOM 2867 SG CYS A 270 24.651 1.029 70.812 1.00 73.58 S
ANISOU 2867 SG CYS A 270 9667 10306 7981 272 -651 -653 S
ATOM 2868 N THR A 271 27.342 -1.429 69.374 1.00 52.67 N
ANISOU 2868 N THR A 271 6789 7746 5477 130 -662 -353 N
ATOM 2869 CA THR A 271 28.417 -1.098 68.438 1.00 50.81 C
ANISOU 2869 CA THR A 271 6583 7434 5289 36 -678 -356 C
ATOM 2870 C THR A 271 28.461 -2.084 67.278 1.00 51.16 C
ANISOU 2870 C THR A 271 6597 7399 5442 71 -650 -241 C
ATOM 2871 O THR A 271 28.828 -1.682 66.176 1.00 50.43 O
ANISOU 2871 O THR A 271 6566 7180 5413 24 -652 -255 O
ATOM 2872 CB THR A 271 29.778 -1.001 69.146 1.00 55.99 C
ANISOU 2872 CB THR A 271 7157 8259 5858 -64 -710 -367 C
ATOM 2873 OG1 THR A 271 30.081 -2.237 69.790 1.00 61.21 O
ANISOU 2873 OG1 THR A 271 7678 9098 6480 0 -702 -243 O
ATOM 2874 CG2 THR A 271 29.835 0.139 70.144 1.00 52.15 C
ANISOU 2874 CG2 THR A 271 6720 7831 5263 -138 -735 -514 C
ATOM 2875 N ALA A 272 28.091 -3.360 67.518 1.00 46.05 N
ANISOU 2875 N ALA A 272 5865 6819 4812 148 -613 -132 N
ATOM 2876 CA ALA A 272 28.027 -4.393 66.482 1.00 44.48 C
ANISOU 2876 CA ALA A 272 5647 6541 4712 178 -569 -33 C
ATOM 2877 C ALA A 272 26.891 -4.065 65.511 1.00 48.14 C
ANISOU 2877 C ALA A 272 6189 6856 5244 209 -555 -83 C
ATOM 2878 O ALA A 272 27.106 -4.073 64.299 1.00 47.63 O
ANISOU 2878 O ALA A 272 6160 6684 5255 189 -550 -71 O
ATOM 2879 CB ALA A 272 27.824 -5.763 67.108 1.00 45.02 C
ANISOU 2879 CB ALA A 272 5634 6702 4770 244 -514 84 C
ATOM 2880 N GLU A 273 25.708 -3.705 66.061 1.00 44.62 N
ANISOU 2880 N GLU A 273 5766 6428 4759 265 -551 -145 N
ATOM 2881 CA GLU A 273 24.498 -3.290 65.352 1.00 44.53 C
ANISOU 2881 CA GLU A 273 5811 6332 4777 322 -542 -202 C
ATOM 2882 C GLU A 273 24.768 -2.047 64.491 1.00 48.38 C
ANISOU 2882 C GLU A 273 6413 6687 5283 305 -574 -274 C
ATOM 2883 O GLU A 273 24.447 -2.044 63.300 1.00 47.66 O
ANISOU 2883 O GLU A 273 6353 6505 5250 329 -564 -265 O
ATOM 2884 CB GLU A 273 23.406 -2.970 66.382 1.00 46.83 C
ANISOU 2884 CB GLU A 273 6096 6707 4992 387 -538 -262 C
ATOM 2885 CG GLU A 273 22.141 -3.808 66.315 1.00 61.33 C
ANISOU 2885 CG GLU A 273 7872 8589 6839 444 -490 -244 C
ATOM 2886 CD GLU A 273 21.200 -3.561 67.487 1.00 90.92 C
ANISOU 2886 CD GLU A 273 11597 12450 10500 503 -484 -296 C
ATOM 2887 OE1 GLU A 273 20.919 -2.376 67.790 1.00 93.26 O
ANISOU 2887 OE1 GLU A 273 11963 12731 10741 548 -517 -388 O
ATOM 2888 OE2 GLU A 273 20.758 -4.550 68.116 1.00 79.03 O
ANISOU 2888 OE2 GLU A 273 10011 11040 8977 502 -435 -243 O
ATOM 2889 N ASN A 274 25.373 -0.999 65.105 1.00 44.89 N
ANISOU 2889 N ASN A 274 6037 6237 4783 258 -605 -345 N
ATOM 2890 CA ASN A 274 25.704 0.271 64.461 1.00 44.69 C
ANISOU 2890 CA ASN A 274 6150 6069 4762 225 -617 -418 C
ATOM 2891 C ASN A 274 26.669 0.070 63.300 1.00 48.30 C
ANISOU 2891 C ASN A 274 6612 6446 5291 152 -617 -364 C
ATOM 2892 O ASN A 274 26.453 0.659 62.242 1.00 49.08 O
ANISOU 2892 O ASN A 274 6809 6411 5427 175 -608 -380 O
ATOM 2893 CB ASN A 274 26.280 1.263 65.473 1.00 44.81 C
ANISOU 2893 CB ASN A 274 6227 6105 4695 152 -634 -513 C
ATOM 2894 CG ASN A 274 25.283 1.807 66.474 1.00 61.07 C
ANISOU 2894 CG ASN A 274 8323 8203 6676 232 -629 -593 C
ATOM 2895 OD1 ASN A 274 24.065 1.726 66.307 1.00 58.59 O
ANISOU 2895 OD1 ASN A 274 8014 7881 6366 356 -613 -591 O
ATOM 2896 ND2 ASN A 274 25.784 2.385 67.541 1.00 55.32 N
ANISOU 2896 ND2 ASN A 274 7616 7536 5866 159 -641 -672 N
ATOM 2897 N THR A 275 27.689 -0.804 63.470 1.00 43.57 N
ANISOU 2897 N THR A 275 5907 5942 4706 82 -622 -292 N
ATOM 2898 CA THR A 275 28.664 -1.131 62.425 1.00 42.65 C
ANISOU 2898 CA THR A 275 5775 5778 4653 17 -619 -233 C
ATOM 2899 C THR A 275 27.922 -1.771 61.236 1.00 46.39 C
ANISOU 2899 C THR A 275 6247 6171 5206 90 -592 -180 C
ATOM 2900 O THR A 275 28.138 -1.348 60.099 1.00 46.86 O
ANISOU 2900 O THR A 275 6375 6120 5309 71 -589 -183 O
ATOM 2901 CB THR A 275 29.778 -2.016 62.997 1.00 45.36 C
ANISOU 2901 CB THR A 275 5989 6271 4975 -33 -625 -160 C
ATOM 2902 OG1 THR A 275 30.461 -1.265 63.999 1.00 45.10 O
ANISOU 2902 OG1 THR A 275 5952 6332 4852 -113 -655 -231 O
ATOM 2903 CG2 THR A 275 30.778 -2.473 61.944 1.00 40.44 C
ANISOU 2903 CG2 THR A 275 5334 5620 4412 -83 -616 -93 C
ATOM 2904 N LEU A 276 27.013 -2.735 61.509 1.00 41.10 N
ANISOU 2904 N LEU A 276 5506 5564 4546 163 -567 -141 N
ATOM 2905 CA LEU A 276 26.199 -3.396 60.481 1.00 40.01 C
ANISOU 2905 CA LEU A 276 5352 5382 4468 214 -535 -111 C
ATOM 2906 C LEU A 276 25.345 -2.370 59.733 1.00 41.35 C
ANISOU 2906 C LEU A 276 5618 5465 4630 275 -547 -180 C
ATOM 2907 O LEU A 276 25.210 -2.469 58.520 1.00 40.54 O
ANISOU 2907 O LEU A 276 5531 5301 4572 289 -537 -164 O
ATOM 2908 CB LEU A 276 25.306 -4.518 61.074 1.00 40.00 C
ANISOU 2908 CB LEU A 276 5264 5471 4461 256 -493 -78 C
ATOM 2909 CG LEU A 276 26.019 -5.740 61.652 1.00 44.36 C
ANISOU 2909 CG LEU A 276 5738 6092 5027 227 -454 16 C
ATOM 2910 CD1 LEU A 276 25.049 -6.638 62.383 1.00 44.76 C
ANISOU 2910 CD1 LEU A 276 5734 6214 5057 263 -400 38 C
ATOM 2911 CD2 LEU A 276 26.791 -6.506 60.591 1.00 45.48 C
ANISOU 2911 CD2 LEU A 276 5867 6171 5243 194 -423 84 C
ATOM 2912 N PHE A 277 24.833 -1.355 60.441 1.00 37.97 N
ANISOU 2912 N PHE A 277 5258 5033 4137 321 -566 -253 N
ATOM 2913 CA PHE A 277 24.046 -0.281 59.829 1.00 37.48 C
ANISOU 2913 CA PHE A 277 5305 4886 4050 412 -569 -310 C
ATOM 2914 C PHE A 277 24.906 0.572 58.879 1.00 42.44 C
ANISOU 2914 C PHE A 277 6054 5368 4703 366 -571 -312 C
ATOM 2915 O PHE A 277 24.504 0.769 57.739 1.00 42.07 O
ANISOU 2915 O PHE A 277 6050 5260 4675 427 -562 -298 O
ATOM 2916 CB PHE A 277 23.381 0.613 60.894 1.00 38.98 C
ANISOU 2916 CB PHE A 277 5556 5096 4159 481 -575 -388 C
ATOM 2917 CG PHE A 277 22.726 1.851 60.318 1.00 40.06 C
ANISOU 2917 CG PHE A 277 5838 5124 4259 593 -566 -440 C
ATOM 2918 CD1 PHE A 277 21.531 1.763 59.609 1.00 41.47 C
ANISOU 2918 CD1 PHE A 277 5991 5343 4421 731 -558 -436 C
ATOM 2919 CD2 PHE A 277 23.311 3.105 60.473 1.00 41.93 C
ANISOU 2919 CD2 PHE A 277 6240 5223 4468 563 -557 -494 C
ATOM 2920 CE1 PHE A 277 20.933 2.903 59.072 1.00 41.97 C
ANISOU 2920 CE1 PHE A 277 6192 5319 4438 869 -544 -468 C
ATOM 2921 CE2 PHE A 277 22.708 4.245 59.940 1.00 44.30 C
ANISOU 2921 CE2 PHE A 277 6702 5400 4731 687 -531 -530 C
ATOM 2922 CZ PHE A 277 21.529 4.133 59.237 1.00 41.82 C
ANISOU 2922 CZ PHE A 277 6360 5134 4397 854 -526 -508 C
ATOM 2923 N TYR A 278 26.077 1.067 59.348 1.00 40.00 N
ANISOU 2923 N TYR A 278 5794 5020 4384 251 -580 -332 N
ATOM 2924 CA TYR A 278 26.971 1.916 58.558 1.00 40.54 C
ANISOU 2924 CA TYR A 278 5983 4952 4470 176 -570 -342 C
ATOM 2925 C TYR A 278 27.422 1.224 57.266 1.00 44.13 C
ANISOU 2925 C TYR A 278 6389 5385 4995 151 -564 -265 C
ATOM 2926 O TYR A 278 27.419 1.860 56.215 1.00 44.21 O
ANISOU 2926 O TYR A 278 6505 5276 5018 172 -547 -260 O
ATOM 2927 CB TYR A 278 28.189 2.388 59.378 1.00 42.30 C
ANISOU 2927 CB TYR A 278 6225 5187 4659 24 -577 -387 C
ATOM 2928 CG TYR A 278 27.839 3.187 60.618 1.00 45.28 C
ANISOU 2928 CG TYR A 278 6668 5578 4960 29 -577 -481 C
ATOM 2929 CD1 TYR A 278 27.004 4.300 60.547 1.00 48.27 C
ANISOU 2929 CD1 TYR A 278 7213 5826 5302 123 -549 -546 C
ATOM 2930 CD2 TYR A 278 28.396 2.870 61.853 1.00 46.45 C
ANISOU 2930 CD2 TYR A 278 6717 5871 5060 -53 -601 -505 C
ATOM 2931 CE1 TYR A 278 26.689 5.046 61.685 1.00 50.08 C
ANISOU 2931 CE1 TYR A 278 7514 6059 5457 130 -540 -640 C
ATOM 2932 CE2 TYR A 278 28.088 3.606 62.998 1.00 48.42 C
ANISOU 2932 CE2 TYR A 278 7024 6142 5230 -56 -599 -601 C
ATOM 2933 CZ TYR A 278 27.234 4.694 62.911 1.00 59.00 C
ANISOU 2933 CZ TYR A 278 8537 7339 6543 31 -567 -673 C
ATOM 2934 OH TYR A 278 26.946 5.431 64.041 1.00 64.06 O
ANISOU 2934 OH TYR A 278 9245 7992 7103 29 -558 -776 O
ATOM 2935 N VAL A 279 27.752 -0.074 57.339 1.00 40.28 N
ANISOU 2935 N VAL A 279 5752 5005 4546 119 -569 -202 N
ATOM 2936 CA VAL A 279 28.170 -0.895 56.201 1.00 39.20 C
ANISOU 2936 CA VAL A 279 5559 4861 4476 97 -555 -132 C
ATOM 2937 C VAL A 279 27.006 -1.027 55.196 1.00 42.98 C
ANISOU 2937 C VAL A 279 6050 5312 4968 205 -543 -129 C
ATOM 2938 O VAL A 279 27.223 -0.810 54.004 1.00 43.00 O
ANISOU 2938 O VAL A 279 6101 5242 4996 206 -534 -108 O
ATOM 2939 CB VAL A 279 28.687 -2.281 56.673 1.00 42.77 C
ANISOU 2939 CB VAL A 279 5867 5429 4955 60 -547 -67 C
ATOM 2940 CG1 VAL A 279 28.918 -3.222 55.499 1.00 41.81 C
ANISOU 2940 CG1 VAL A 279 5693 5291 4900 58 -518 -4 C
ATOM 2941 CG2 VAL A 279 29.960 -2.144 57.507 1.00 43.02 C
ANISOU 2941 CG2 VAL A 279 5866 5523 4957 -38 -563 -62 C
ATOM 2942 N LYS A 280 25.778 -1.356 55.670 1.00 39.03 N
ANISOU 2942 N LYS A 280 5500 4889 4440 294 -541 -153 N
ATOM 2943 CA LYS A 280 24.627 -1.514 54.783 1.00 38.25 C
ANISOU 2943 CA LYS A 280 5384 4815 4334 391 -531 -162 C
ATOM 2944 C LYS A 280 24.261 -0.164 54.145 1.00 45.20 C
ANISOU 2944 C LYS A 280 6403 5602 5169 485 -539 -191 C
ATOM 2945 O LYS A 280 23.926 -0.128 52.957 1.00 46.75 O
ANISOU 2945 O LYS A 280 6611 5787 5366 540 -533 -174 O
ATOM 2946 CB LYS A 280 23.432 -2.191 55.492 1.00 39.37 C
ANISOU 2946 CB LYS A 280 5427 5088 4446 447 -521 -189 C
ATOM 2947 CG LYS A 280 22.342 -1.271 56.005 1.00 48.63 C
ANISOU 2947 CG LYS A 280 6647 6292 5539 568 -535 -250 C
ATOM 2948 CD LYS A 280 21.146 -1.184 55.064 1.00 43.59 C
ANISOU 2948 CD LYS A 280 5981 5721 4859 687 -532 -272 C
ATOM 2949 CE LYS A 280 20.583 0.211 55.156 1.00 39.84 C
ANISOU 2949 CE LYS A 280 5627 5204 4307 831 -544 -311 C
ATOM 2950 NZ LYS A 280 19.110 0.238 55.222 1.00 34.79 N
ANISOU 2950 NZ LYS A 280 4913 4719 3588 973 -543 -352 N
ATOM 2951 N GLU A 281 24.360 0.933 54.915 1.00 41.43 N
ANISOU 2951 N GLU A 281 6040 5054 4646 503 -543 -233 N
ATOM 2952 CA GLU A 281 24.072 2.281 54.446 1.00 41.98 C
ANISOU 2952 CA GLU A 281 6279 5002 4668 599 -530 -256 C
ATOM 2953 C GLU A 281 25.050 2.667 53.307 1.00 46.07 C
ANISOU 2953 C GLU A 281 6891 5391 5223 531 -513 -214 C
ATOM 2954 O GLU A 281 24.604 3.103 52.247 1.00 46.04 O
ANISOU 2954 O GLU A 281 6957 5340 5196 635 -498 -190 O
ATOM 2955 CB GLU A 281 24.139 3.256 55.632 1.00 44.09 C
ANISOU 2955 CB GLU A 281 6658 5208 4887 597 -523 -320 C
ATOM 2956 CG GLU A 281 23.353 4.542 55.464 1.00 57.44 C
ANISOU 2956 CG GLU A 281 8523 6794 6507 756 -493 -352 C
ATOM 2957 CD GLU A 281 21.862 4.482 55.162 1.00 72.18 C
ANISOU 2957 CD GLU A 281 10339 8770 8314 963 -497 -353 C
ATOM 2958 OE1 GLU A 281 21.360 5.452 54.549 1.00 67.06 O
ANISOU 2958 OE1 GLU A 281 9834 8037 7611 1119 -468 -347 O
ATOM 2959 OE2 GLU A 281 21.196 3.490 55.537 1.00 54.40 O
ANISOU 2959 OE2 GLU A 281 7911 6695 6062 974 -522 -359 O
ATOM 2960 N SER A 282 26.362 2.417 53.503 1.00 42.25 N
ANISOU 2960 N SER A 282 6388 4878 4786 364 -514 -200 N
ATOM 2961 CA SER A 282 27.435 2.665 52.532 1.00 41.71 C
ANISOU 2961 CA SER A 282 6382 4712 4753 269 -496 -163 C
ATOM 2962 C SER A 282 27.236 1.879 51.225 1.00 45.37 C
ANISOU 2962 C SER A 282 6768 5217 5252 311 -496 -104 C
ATOM 2963 O SER A 282 27.390 2.444 50.142 1.00 45.42 O
ANISOU 2963 O SER A 282 6874 5133 5252 339 -474 -76 O
ATOM 2964 CB SER A 282 28.787 2.274 53.129 1.00 43.67 C
ANISOU 2964 CB SER A 282 6564 4995 5034 90 -504 -162 C
ATOM 2965 OG SER A 282 29.123 3.038 54.275 1.00 50.91 O
ANISOU 2965 OG SER A 282 7544 5892 5908 23 -503 -229 O
ATOM 2966 N THR A 283 26.928 0.568 51.338 1.00 41.01 N
ANISOU 2966 N THR A 283 6049 4799 4733 308 -511 -87 N
ATOM 2967 CA THR A 283 26.768 -0.353 50.214 1.00 40.23 C
ANISOU 2967 CA THR A 283 5862 4755 4668 322 -504 -48 C
ATOM 2968 C THR A 283 25.433 -0.098 49.491 1.00 46.43 C
ANISOU 2968 C THR A 283 6658 5586 5399 474 -506 -64 C
ATOM 2969 O THR A 283 25.333 -0.377 48.292 1.00 46.47 O
ANISOU 2969 O THR A 283 6642 5610 5407 499 -498 -40 O
ATOM 2970 CB THR A 283 26.947 -1.814 50.679 1.00 45.72 C
ANISOU 2970 CB THR A 283 6403 5556 5414 255 -499 -32 C
ATOM 2971 OG1 THR A 283 26.080 -2.090 51.781 1.00 48.34 O
ANISOU 2971 OG1 THR A 283 6679 5970 5718 299 -505 -66 O
ATOM 2972 CG2 THR A 283 28.393 -2.128 51.094 1.00 41.06 C
ANISOU 2972 CG2 THR A 283 5788 4948 4866 131 -495 4 C
ATOM 2973 N LEU A 284 24.426 0.458 50.205 1.00 44.37 N
ANISOU 2973 N LEU A 284 6424 5358 5076 584 -515 -107 N
ATOM 2974 CA LEU A 284 23.123 0.837 49.643 1.00 44.78 C
ANISOU 2974 CA LEU A 284 6481 5483 5052 756 -518 -123 C
ATOM 2975 C LEU A 284 23.316 1.993 48.683 1.00 51.60 C
ANISOU 2975 C LEU A 284 7509 6221 5874 843 -501 -89 C
ATOM 2976 O LEU A 284 22.592 2.088 47.691 1.00 52.93 O
ANISOU 2976 O LEU A 284 7664 6460 5987 969 -501 -73 O
ATOM 2977 CB LEU A 284 22.129 1.232 50.760 1.00 45.16 C
ANISOU 2977 CB LEU A 284 6525 5595 5038 857 -527 -174 C
ATOM 2978 CG LEU A 284 20.691 1.640 50.360 1.00 49.24 C
ANISOU 2978 CG LEU A 284 7022 6231 5454 1058 -532 -196 C
ATOM 2979 CD1 LEU A 284 19.880 0.440 49.898 1.00 48.19 C
ANISOU 2979 CD1 LEU A 284 6691 6308 5313 1048 -540 -219 C
ATOM 2980 CD2 LEU A 284 19.988 2.308 51.514 1.00 49.91 C
ANISOU 2980 CD2 LEU A 284 7153 6331 5479 1161 -532 -241 C
ATOM 2981 N TRP A 285 24.287 2.878 48.980 1.00 49.22 N
ANISOU 2981 N TRP A 285 7364 5744 5592 772 -480 -79 N
ATOM 2982 CA TRP A 285 24.603 4.026 48.136 1.00 50.76 C
ANISOU 2982 CA TRP A 285 7751 5782 5754 829 -442 -41 C
ATOM 2983 C TRP A 285 25.212 3.554 46.805 1.00 53.55 C
ANISOU 2983 C TRP A 285 8067 6137 6140 774 -437 16 C
ATOM 2984 O TRP A 285 24.894 4.125 45.766 1.00 53.67 O
ANISOU 2984 O TRP A 285 8170 6119 6101 894 -415 58 O
ATOM 2985 CB TRP A 285 25.531 5.016 48.854 1.00 50.73 C
ANISOU 2985 CB TRP A 285 7922 5591 5763 723 -407 -63 C
ATOM 2986 CG TRP A 285 25.857 6.202 48.006 1.00 53.67 C
ANISOU 2986 CG TRP A 285 8515 5776 6100 766 -346 -24 C
ATOM 2987 CD1 TRP A 285 25.067 7.293 47.783 1.00 58.19 C
ANISOU 2987 CD1 TRP A 285 9266 6253 6591 961 -302 -10 C
ATOM 2988 CD2 TRP A 285 27.007 6.357 47.162 1.00 53.95 C
ANISOU 2988 CD2 TRP A 285 8617 5707 6175 631 -314 19 C
ATOM 2989 NE1 TRP A 285 25.679 8.146 46.896 1.00 59.18 N
ANISOU 2989 NE1 TRP A 285 9585 6196 6704 947 -236 42 N
ATOM 2990 CE2 TRP A 285 26.870 7.594 46.492 1.00 59.79 C
ANISOU 2990 CE2 TRP A 285 9592 6271 6856 736 -244 57 C
ATOM 2991 CE3 TRP A 285 28.155 5.580 46.923 1.00 54.39 C
ANISOU 2991 CE3 TRP A 285 8558 5803 6303 436 -331 32 C
ATOM 2992 CZ2 TRP A 285 27.844 8.079 45.608 1.00 59.58 C
ANISOU 2992 CZ2 TRP A 285 9692 6102 6844 632 -188 104 C
ATOM 2993 CZ3 TRP A 285 29.124 6.065 46.053 1.00 56.46 C
ANISOU 2993 CZ3 TRP A 285 8930 5944 6578 338 -283 73 C
ATOM 2994 CH2 TRP A 285 28.963 7.297 45.403 1.00 58.51 C
ANISOU 2994 CH2 TRP A 285 9424 6025 6781 425 -212 107 C
ATOM 2995 N LEU A 286 26.057 2.508 46.836 1.00 49.39 N
ANISOU 2995 N LEU A 286 7414 5659 5693 608 -452 20 N
ATOM 2996 CA LEU A 286 26.653 1.910 45.633 1.00 49.43 C
ANISOU 2996 CA LEU A 286 7367 5682 5733 549 -444 66 C
ATOM 2997 C LEU A 286 25.572 1.336 44.731 1.00 53.85 C
ANISOU 2997 C LEU A 286 7823 6389 6247 673 -459 66 C
ATOM 2998 O LEU A 286 25.653 1.434 43.509 1.00 53.29 O
ANISOU 2998 O LEU A 286 7774 6320 6152 711 -446 105 O
ATOM 2999 CB LEU A 286 27.639 0.794 46.013 1.00 48.56 C
ANISOU 2999 CB LEU A 286 7130 5613 5708 377 -452 67 C
ATOM 3000 CG LEU A 286 29.029 1.220 46.462 1.00 53.32 C
ANISOU 3000 CG LEU A 286 7800 6113 6346 226 -437 75 C
ATOM 3001 CD1 LEU A 286 29.748 0.060 47.129 1.00 52.36 C
ANISOU 3001 CD1 LEU A 286 7530 6081 6284 112 -451 74 C
ATOM 3002 CD2 LEU A 286 29.843 1.781 45.301 1.00 54.93 C
ANISOU 3002 CD2 LEU A 286 8099 6220 6552 175 -404 120 C
ATOM 3003 N THR A 287 24.560 0.732 45.362 1.00 51.56 N
ANISOU 3003 N THR A 287 7412 6239 5938 725 -482 18 N
ATOM 3004 CA THR A 287 23.377 0.123 44.767 1.00 52.18 C
ANISOU 3004 CA THR A 287 7363 6503 5961 821 -495 -11 C
ATOM 3005 C THR A 287 22.594 1.194 43.953 1.00 58.21 C
ANISOU 3005 C THR A 287 8220 7286 6612 1026 -494 15 C
ATOM 3006 O THR A 287 22.090 0.887 42.872 1.00 58.04 O
ANISOU 3006 O THR A 287 8125 7393 6535 1092 -500 19 O
ATOM 3007 CB THR A 287 22.583 -0.522 45.929 1.00 60.50 C
ANISOU 3007 CB THR A 287 8298 7675 7017 811 -508 -71 C
ATOM 3008 OG1 THR A 287 22.824 -1.924 45.968 1.00 59.33 O
ANISOU 3008 OG1 THR A 287 8012 7595 6938 671 -496 -91 O
ATOM 3009 CG2 THR A 287 21.109 -0.242 45.894 1.00 61.29 C
ANISOU 3009 CG2 THR A 287 8342 7937 7010 980 -524 -111 C
ATOM 3010 N SER A 288 22.546 2.447 44.471 1.00 56.50 N
ANISOU 3010 N SER A 288 8173 6938 6356 1125 -480 32 N
ATOM 3011 CA SER A 288 21.851 3.617 43.919 1.00 57.98 C
ANISOU 3011 CA SER A 288 8496 7104 6432 1348 -462 71 C
ATOM 3012 C SER A 288 22.561 4.217 42.688 1.00 63.81 C
ANISOU 3012 C SER A 288 9370 7717 7156 1364 -426 149 C
ATOM 3013 O SER A 288 21.930 4.963 41.936 1.00 64.41 O
ANISOU 3013 O SER A 288 9531 7815 7126 1567 -408 197 O
ATOM 3014 CB SER A 288 21.688 4.685 44.997 1.00 62.18 C
ANISOU 3014 CB SER A 288 9189 7498 6939 1424 -438 58 C
ATOM 3015 OG SER A 288 20.998 4.181 46.132 1.00 67.67 O
ANISOU 3015 OG SER A 288 9760 8316 7638 1418 -468 -12 O
ATOM 3016 N LEU A 289 23.857 3.885 42.478 1.00 60.85 N
ANISOU 3016 N LEU A 289 9014 7228 6878 1162 -413 168 N
ATOM 3017 CA LEU A 289 24.643 4.310 41.309 1.00 61.34 C
ANISOU 3017 CA LEU A 289 9187 7182 6935 1140 -375 239 C
ATOM 3018 C LEU A 289 24.080 3.685 40.051 1.00 67.06 C
ANISOU 3018 C LEU A 289 9784 8095 7601 1227 -396 257 C
ATOM 3019 O LEU A 289 24.089 4.321 39.004 1.00 67.28 O
ANISOU 3019 O LEU A 289 9917 8087 7558 1335 -367 326 O
ATOM 3020 CB LEU A 289 26.121 3.912 41.449 1.00 60.26 C
ANISOU 3020 CB LEU A 289 9049 6935 6911 895 -362 241 C
ATOM 3021 CG LEU A 289 27.098 4.983 41.881 1.00 65.26 C
ANISOU 3021 CG LEU A 289 9889 7337 7569 801 -309 259 C
ATOM 3022 CD1 LEU A 289 26.892 5.335 43.314 1.00 65.75 C
ANISOU 3022 CD1 LEU A 289 9987 7350 7644 778 -316 198 C
ATOM 3023 CD2 LEU A 289 28.510 4.494 41.727 1.00 66.34 C
ANISOU 3023 CD2 LEU A 289 9987 7430 7790 579 -298 268 C
ATOM 3024 N ASN A 290 23.586 2.436 40.162 1.00 64.89 N
ANISOU 3024 N ASN A 290 9289 8020 7346 1173 -439 192 N
ATOM 3025 CA ASN A 290 22.975 1.655 39.085 1.00 65.60 C
ANISOU 3025 CA ASN A 290 9224 8325 7378 1219 -459 176 C
ATOM 3026 C ASN A 290 21.893 2.472 38.368 1.00 72.20 C
ANISOU 3026 C ASN A 290 10097 9279 8056 1477 -462 210 C
ATOM 3027 O ASN A 290 21.887 2.508 37.144 1.00 71.60 O
ANISOU 3027 O ASN A 290 10009 9283 7912 1541 -457 249 O
ATOM 3028 CB ASN A 290 22.394 0.352 39.652 1.00 65.43 C
ANISOU 3028 CB ASN A 290 8989 8480 7392 1123 -487 81 C
ATOM 3029 CG ASN A 290 21.511 -0.404 38.698 1.00 87.21 C
ANISOU 3029 CG ASN A 290 11578 11490 10067 1167 -503 33 C
ATOM 3030 OD1 ASN A 290 21.946 -0.837 37.629 1.00 81.20 O
ANISOU 3030 OD1 ASN A 290 10782 10760 9309 1108 -492 42 O
ATOM 3031 ND2 ASN A 290 20.259 -0.605 39.086 1.00 79.29 N
ANISOU 3031 ND2 ASN A 290 10455 10690 8983 1259 -526 -31 N
ATOM 3032 N ALA A 291 21.025 3.167 39.135 1.00 71.45 N
ANISOU 3032 N ALA A 291 10054 9199 7897 1637 -467 203 N
ATOM 3033 CA ALA A 291 19.955 4.026 38.620 1.00 73.80 C
ANISOU 3033 CA ALA A 291 10396 9614 8032 1922 -464 245 C
ATOM 3034 C ALA A 291 20.518 5.179 37.760 1.00 81.50 C
ANISOU 3034 C ALA A 291 11608 10401 8958 2039 -408 362 C
ATOM 3035 O ALA A 291 19.828 5.662 36.865 1.00 82.36 O
ANISOU 3035 O ALA A 291 11733 10636 8924 2267 -402 419 O
ATOM 3036 CB ALA A 291 19.136 4.581 39.776 1.00 74.89 C
ANISOU 3036 CB ALA A 291 10569 9756 8130 2054 -467 215 C
ATOM 3037 N CYS A 292 21.780 5.586 38.018 1.00 79.92 N
ANISOU 3037 N CYS A 292 11584 9915 8868 1877 -363 397 N
ATOM 3038 CA CYS A 292 22.498 6.642 37.295 1.00 82.03 C
ANISOU 3038 CA CYS A 292 12096 9962 9110 1926 -291 502 C
ATOM 3039 C CYS A 292 23.448 6.025 36.231 1.00 89.47 C
ANISOU 3039 C CYS A 292 12983 10909 10101 1764 -288 529 C
ATOM 3040 O CYS A 292 23.870 6.728 35.315 1.00 90.23 O
ANISOU 3040 O CYS A 292 13239 10893 10149 1824 -232 622 O
ATOM 3041 CB CYS A 292 23.264 7.534 38.272 1.00 82.17 C
ANISOU 3041 CB CYS A 292 12341 9676 9204 1830 -231 506 C
ATOM 3042 SG CYS A 292 22.354 7.953 39.787 1.00 86.10 S
ANISOU 3042 SG CYS A 292 12866 10168 9682 1942 -241 439 S
ATOM 3043 N LEU A 293 23.785 4.720 36.366 1.00 87.61 N
ANISOU 3043 N LEU A 293 12534 10797 9959 1566 -338 452 N
ATOM 3044 CA LEU A 293 24.682 3.995 35.460 1.00 88.03 C
ANISOU 3044 CA LEU A 293 12515 10866 10065 1406 -335 462 C
ATOM 3045 C LEU A 293 23.923 3.309 34.321 1.00 95.81 C
ANISOU 3045 C LEU A 293 13329 12120 10953 1500 -369 447 C
ATOM 3046 O LEU A 293 24.321 3.472 33.168 1.00 96.47 O
ANISOU 3046 O LEU A 293 13455 12207 10992 1521 -344 508 O
ATOM 3047 CB LEU A 293 25.534 2.933 36.206 1.00 86.31 C
ANISOU 3047 CB LEU A 293 12179 10616 9997 1147 -354 391 C
ATOM 3048 CG LEU A 293 26.653 3.393 37.158 1.00 90.44 C
ANISOU 3048 CG LEU A 293 12834 10907 10623 990 -323 399 C
ATOM 3049 CD1 LEU A 293 27.310 2.204 37.813 1.00 88.85 C
ANISOU 3049 CD1 LEU A 293 12478 10741 10540 786 -348 337 C
ATOM 3050 CD2 LEU A 293 27.717 4.212 36.443 1.00 93.69 C
ANISOU 3050 CD2 LEU A 293 13426 11137 11036 934 -260 479 C
ATOM 3051 N ASN A 294 22.838 2.552 34.644 1.00 93.96 N
ANISOU 3051 N ASN A 294 12899 12122 10678 1545 -420 359 N
ATOM 3052 CA ASN A 294 21.993 1.771 33.725 1.00 94.92 C
ANISOU 3052 CA ASN A 294 12822 12544 10701 1602 -454 307 C
ATOM 3053 C ASN A 294 21.751 2.413 32.342 1.00103.05 C
ANISOU 3053 C ASN A 294 13906 13668 11579 1792 -441 391 C
ATOM 3054 O ASN A 294 21.903 1.674 31.367 1.00102.56 O
ANISOU 3054 O ASN A 294 13727 13747 11494 1722 -449 363 O
ATOM 3055 CB ASN A 294 20.646 1.423 34.347 1.00 95.00 C
ANISOU 3055 CB ASN A 294 12671 12787 10640 1692 -496 220 C
ATOM 3056 CG ASN A 294 20.534 0.025 34.909 1.00116.57 C
ANISOU 3056 CG ASN A 294 15209 15619 13463 1480 -514 97 C
ATOM 3057 OD1 ASN A 294 21.380 -0.850 34.676 1.00112.29 O
ANISOU 3057 OD1 ASN A 294 14628 15011 13027 1280 -497 70 O
ATOM 3058 ND2 ASN A 294 19.470 -0.223 35.660 1.00106.21 N
ANISOU 3058 ND2 ASN A 294 13777 14471 12107 1528 -540 22 N
ATOM 3059 N PRO A 295 21.426 3.732 32.178 1.00103.07 N
ANISOU 3059 N PRO A 295 14091 13596 11474 2032 -412 497 N
ATOM 3060 CA PRO A 295 21.212 4.259 30.816 1.00105.08 C
ANISOU 3060 CA PRO A 295 14394 13959 11574 2224 -394 589 C
ATOM 3061 C PRO A 295 22.444 4.185 29.886 1.00110.29 C
ANISOU 3061 C PRO A 295 15140 14475 12289 2085 -352 650 C
ATOM 3062 O PRO A 295 22.261 4.280 28.671 1.00110.76 O
ANISOU 3062 O PRO A 295 15180 14681 12225 2202 -347 702 O
ATOM 3063 CB PRO A 295 20.795 5.710 31.067 1.00108.41 C
ANISOU 3063 CB PRO A 295 15044 14249 11900 2493 -348 700 C
ATOM 3064 CG PRO A 295 20.251 5.715 32.452 1.00112.10 C
ANISOU 3064 CG PRO A 295 15483 14689 12420 2488 -371 627 C
ATOM 3065 CD PRO A 295 21.156 4.785 33.182 1.00105.39 C
ANISOU 3065 CD PRO A 295 14560 13719 11765 2161 -387 538 C
ATOM 3066 N PHE A 296 23.671 3.957 30.431 1.00106.84 N
ANISOU 3066 N PHE A 296 14777 13789 12027 1837 -325 637 N
ATOM 3067 CA PHE A 296 24.915 3.845 29.647 1.00106.86 C
ANISOU 3067 CA PHE A 296 14847 13662 12091 1684 -283 686 C
ATOM 3068 C PHE A 296 25.023 2.510 28.873 1.00111.83 C
ANISOU 3068 C PHE A 296 15254 14504 12734 1554 -318 605 C
ATOM 3069 O PHE A 296 25.963 2.333 28.092 1.00111.22 O
ANISOU 3069 O PHE A 296 15206 14367 12684 1452 -285 641 O
ATOM 3070 CB PHE A 296 26.157 4.069 30.523 1.00107.56 C
ANISOU 3070 CB PHE A 296 15066 13459 12343 1471 -243 692 C
ATOM 3071 CG PHE A 296 26.415 5.528 30.817 1.00110.29 C
ANISOU 3071 CG PHE A 296 15692 13548 12664 1561 -172 790 C
ATOM 3072 CD1 PHE A 296 27.238 6.286 29.993 1.00113.94 C
ANISOU 3072 CD1 PHE A 296 16341 13850 13102 1550 -95 895 C
ATOM 3073 CD2 PHE A 296 25.821 6.150 31.911 1.00112.91 C
ANISOU 3073 CD2 PHE A 296 16113 13794 12995 1653 -171 775 C
ATOM 3074 CE1 PHE A 296 27.469 7.637 30.261 1.00116.30 C
ANISOU 3074 CE1 PHE A 296 16923 13888 13376 1616 -8 980 C
ATOM 3075 CE2 PHE A 296 26.049 7.504 32.175 1.00117.00 C
ANISOU 3075 CE2 PHE A 296 16913 14054 13488 1730 -88 856 C
ATOM 3076 CZ PHE A 296 26.873 8.237 31.350 1.00115.99 C
ANISOU 3076 CZ PHE A 296 16980 13753 13338 1705 -2 957 C
ATOM 3077 N ILE A 297 24.040 1.602 29.053 1.00109.53 N
ANISOU 3077 N ILE A 297 14745 14459 12410 1558 -374 491 N
ATOM 3078 CA ILE A 297 23.930 0.328 28.331 1.00109.52 C
ANISOU 3078 CA ILE A 297 14536 14676 12401 1442 -396 392 C
ATOM 3079 C ILE A 297 23.373 0.650 26.914 1.00116.53 C
ANISOU 3079 C ILE A 297 15393 15784 13099 1624 -400 437 C
ATOM 3080 O ILE A 297 23.639 -0.084 25.958 1.00115.85 O
ANISOU 3080 O ILE A 297 15212 15812 12993 1535 -395 399 O
ATOM 3081 CB ILE A 297 23.062 -0.691 29.149 1.00111.98 C
ANISOU 3081 CB ILE A 297 14649 15157 12740 1367 -436 249 C
ATOM 3082 CG1 ILE A 297 23.813 -1.134 30.428 1.00110.84 C
ANISOU 3082 CG1 ILE A 297 14534 14795 12785 1172 -423 215 C
ATOM 3083 CG2 ILE A 297 22.643 -1.922 28.320 1.00112.72 C
ANISOU 3083 CG2 ILE A 297 14531 15519 12780 1278 -449 129 C
ATOM 3084 CD1 ILE A 297 22.949 -1.508 31.628 1.00117.38 C
ANISOU 3084 CD1 ILE A 297 15271 15693 13636 1166 -451 132 C
ATOM 3085 N TYR A 298 22.654 1.786 26.789 1.00116.08 N
ANISOU 3085 N TYR A 298 15430 15777 12898 1888 -403 527 N
ATOM 3086 CA TYR A 298 22.063 2.284 25.547 1.00118.39 C
ANISOU 3086 CA TYR A 298 15713 16285 12985 2116 -405 597 C
ATOM 3087 C TYR A 298 22.790 3.529 25.007 1.00125.20 C
ANISOU 3087 C TYR A 298 16845 16912 13813 2237 -335 774 C
ATOM 3088 O TYR A 298 22.685 3.810 23.811 1.00126.39 O
ANISOU 3088 O TYR A 298 17005 17198 13822 2367 -321 846 O
ATOM 3089 CB TYR A 298 20.582 2.618 25.769 1.00120.93 C
ANISOU 3089 CB TYR A 298 15939 16869 13139 2366 -449 579 C
ATOM 3090 N PHE A 299 23.507 4.275 25.880 1.00122.53 N
ANISOU 3090 N PHE A 299 16727 16232 13595 2189 -285 841 N
ATOM 3091 CA PHE A 299 24.219 5.511 25.532 1.00124.16 C
ANISOU 3091 CA PHE A 299 17221 16171 13782 2272 -198 1000 C
ATOM 3092 C PHE A 299 25.380 5.311 24.552 1.00129.65 C
ANISOU 3092 C PHE A 299 17960 16788 14515 2119 -154 1046 C
ATOM 3093 O PHE A 299 25.708 6.247 23.818 1.00130.50 O
ANISOU 3093 O PHE A 299 18266 16781 14538 2238 -82 1184 O
ATOM 3094 CB PHE A 299 24.747 6.217 26.790 1.00125.61 C
ANISOU 3094 CB PHE A 299 17608 16019 14098 2191 -152 1020 C
ATOM 3095 CG PHE A 299 23.744 7.006 27.604 1.00128.44 C
ANISOU 3095 CG PHE A 299 18056 16358 14387 2416 -151 1042 C
ATOM 3096 CD1 PHE A 299 22.569 7.481 27.027 1.00133.61 C
ANISOU 3096 CD1 PHE A 299 18692 17233 14839 2741 -162 1102 C
ATOM 3097 CD2 PHE A 299 24.003 7.330 28.930 1.00130.10 C
ANISOU 3097 CD2 PHE A 299 18374 16337 14720 2318 -133 1006 C
ATOM 3098 CE1 PHE A 299 21.653 8.225 27.777 1.00135.72 C
ANISOU 3098 CE1 PHE A 299 19045 17487 15036 2969 -154 1126 C
ATOM 3099 CE2 PHE A 299 23.094 8.084 29.674 1.00134.09 C
ANISOU 3099 CE2 PHE A 299 18974 16817 15158 2532 -124 1024 C
ATOM 3100 CZ PHE A 299 21.925 8.527 29.093 1.00134.05 C
ANISOU 3100 CZ PHE A 299 18949 17025 14957 2862 -133 1086 C
ATOM 3101 N PHE A 300 26.006 4.119 24.540 1.00126.30 N
ANISOU 3101 N PHE A 300 17364 16416 14210 1866 -186 937 N
ATOM 3102 CA PHE A 300 27.122 3.852 23.635 1.00126.63 C
ANISOU 3102 CA PHE A 300 17428 16399 14286 1720 -144 971 C
ATOM 3103 C PHE A 300 26.669 2.993 22.441 1.00132.31 C
ANISOU 3103 C PHE A 300 17946 17438 14889 1759 -182 918 C
ATOM 3104 O PHE A 300 26.887 1.777 22.407 1.00130.40 O
ANISOU 3104 O PHE A 300 17523 17299 14725 1574 -212 797 O
ATOM 3105 CB PHE A 300 28.315 3.235 24.382 1.00126.71 C
ANISOU 3105 CB PHE A 300 17421 16223 14502 1426 -132 907 C
ATOM 3106 CG PHE A 300 28.952 4.181 25.374 1.00128.31 C
ANISOU 3106 CG PHE A 300 17836 16118 14798 1365 -80 965 C
ATOM 3107 CD1 PHE A 300 29.710 5.266 24.941 1.00132.48 C
ANISOU 3107 CD1 PHE A 300 18598 16436 15301 1370 10 1089 C
ATOM 3108 CD2 PHE A 300 28.804 3.983 26.741 1.00129.40 C
ANISOU 3108 CD2 PHE A 300 17944 16180 15041 1291 -112 889 C
ATOM 3109 CE1 PHE A 300 30.296 6.142 25.860 1.00133.53 C
ANISOU 3109 CE1 PHE A 300 18933 16289 15514 1288 68 1124 C
ATOM 3110 CE2 PHE A 300 29.399 4.855 27.659 1.00132.32 C
ANISOU 3110 CE2 PHE A 300 18506 16283 15487 1221 -63 927 C
ATOM 3111 CZ PHE A 300 30.136 5.931 27.212 1.00131.59 C
ANISOU 3111 CZ PHE A 300 18645 15984 15368 1213 29 1037 C
ATOM 3112 N LEU A 301 26.017 3.668 21.468 1.00132.14 N
ANISOU 3112 N LEU A 301 17969 17572 14667 2011 -174 1012 N
ATOM 3113 CA LEU A 301 25.501 3.145 20.195 1.00133.40 C
ANISOU 3113 CA LEU A 301 17962 18061 14663 2100 -204 985 C
ATOM 3114 C LEU A 301 25.249 4.306 19.202 1.00140.26 C
ANISOU 3114 C LEU A 301 18992 18971 15330 2383 -157 1161 C
ATOM 3115 O LEU A 301 25.149 5.465 19.618 1.00140.55 O
ANISOU 3115 O LEU A 301 19251 18813 15340 2547 -108 1287 O
ATOM 3116 CB LEU A 301 24.228 2.291 20.386 1.00133.49 C
ANISOU 3116 CB LEU A 301 17708 18412 14599 2139 -290 832 C
ATOM 3117 CG LEU A 301 24.424 0.767 20.311 1.00136.84 C
ANISOU 3117 CG LEU A 301 17908 18965 15119 1877 -321 652 C
ATOM 3118 CD1 LEU A 301 23.305 0.035 21.023 1.00136.73 C
ANISOU 3118 CD1 LEU A 301 17688 19171 15093 1857 -384 496 C
ATOM 3119 CD2 LEU A 301 24.539 0.279 18.866 1.00140.26 C
ANISOU 3119 CD2 LEU A 301 18242 19620 15432 1868 -315 631 C
ATOM 3120 N CYS A 302 25.157 3.973 17.892 1.00138.51 N
ANISOU 3120 N CYS A 302 18667 18999 14963 2439 -164 1169 N
ATOM 3121 CA CYS A 302 24.991 4.878 16.744 1.00140.88 C
ANISOU 3121 CA CYS A 302 19088 19388 15053 2697 -118 1334 C
ATOM 3122 C CYS A 302 23.810 5.861 16.876 1.00147.39 C
ANISOU 3122 C CYS A 302 19995 20311 15697 3055 -121 1440 C
ATOM 3123 O CYS A 302 23.914 6.979 16.364 1.00148.80 O
ANISOU 3123 O CYS A 302 20411 20358 15768 3265 -40 1629 O
ATOM 3124 CB CYS A 302 24.877 4.077 15.451 1.00141.70 C
ANISOU 3124 CB CYS A 302 18980 19839 15020 2685 -155 1267 C
ATOM 3125 N LYS A 303 22.698 5.447 17.524 1.00144.11 N
ANISOU 3125 N LYS A 303 19388 20130 15239 3131 -203 1325 N
ATOM 3126 CA LYS A 303 21.486 6.261 17.706 1.00145.87 C
ANISOU 3126 CA LYS A 303 19643 20503 15279 3483 -216 1406 C
ATOM 3127 C LYS A 303 21.750 7.556 18.497 1.00150.11 C
ANISOU 3127 C LYS A 303 20512 20639 15883 3606 -128 1556 C
ATOM 3128 O LYS A 303 21.160 8.589 18.179 1.00151.62 O
ANISOU 3128 O LYS A 303 20854 20860 15897 3946 -83 1709 O
ATOM 3129 CB LYS A 303 20.392 5.443 18.407 1.00147.94 C
ANISOU 3129 CB LYS A 303 19620 21068 15523 3465 -317 1225 C
ATOM 3130 N SER A 304 22.634 7.493 19.511 1.00145.04 N
ANISOU 3130 N SER A 304 19988 19634 15487 3334 -97 1510 N
ATOM 3131 CA SER A 304 22.995 8.624 20.375 1.00145.13 C
ANISOU 3131 CA SER A 304 20310 19247 15585 3381 -8 1615 C
ATOM 3132 C SER A 304 24.310 9.308 19.927 1.00148.92 C
ANISOU 3132 C SER A 304 21074 19373 16136 3265 112 1745 C
ATOM 3133 O SER A 304 24.697 10.325 20.513 1.00149.00 O
ANISOU 3133 O SER A 304 21376 19037 16202 3292 209 1839 O
ATOM 3134 CB SER A 304 23.113 8.155 21.823 1.00146.43 C
ANISOU 3134 CB SER A 304 20413 19267 15957 3155 -50 1473 C
ATOM 3135 OG SER A 304 21.936 7.487 22.249 1.00154.28 O
ANISOU 3135 OG SER A 304 21157 20575 16886 3249 -149 1354 O
ATOM 3136 N PHE A 305 24.970 8.755 18.872 1.00144.84 N
ANISOU 3136 N PHE A 305 20471 18955 15608 3132 113 1744 N
ATOM 3137 CA PHE A 305 26.236 9.202 18.272 1.00169.72 C
ANISOU 3137 CA PHE A 305 23830 21845 18810 2992 218 1850 C
ATOM 3138 C PHE A 305 27.374 9.157 19.291 1.00186.95 C
ANISOU 3138 C PHE A 305 26112 23681 21238 2661 257 1787 C
ATOM 3139 O PHE A 305 27.709 8.084 19.788 1.00142.06 O
ANISOU 3139 O PHE A 305 20216 18061 15699 2414 181 1632 O
ATOM 3140 CB PHE A 305 26.119 10.606 17.651 1.00174.25 C
ANISOU 3140 CB PHE A 305 24721 22265 19220 3279 343 2073 C
TER 3141 PHE A 305
HETATM 3142 O2B 6AD A1201 16.181 1.025 59.445 1.00 46.32 O
HETATM 3143 PB 6AD A1201 16.569 0.984 57.870 1.00 44.17 P
HETATM 3144 O3B 6AD A1201 18.003 0.277 57.772 1.00 44.38 O
HETATM 3145 O1B 6AD A1201 16.571 2.339 57.263 1.00 44.13 O
HETATM 3146 O3A 6AD A1201 15.481 -0.035 57.297 1.00 42.76 O
HETATM 3147 PA 6AD A1201 15.599 -0.994 55.991 1.00 39.70 P
HETATM 3148 O2A 6AD A1201 15.940 -2.388 56.356 1.00 36.90 O
HETATM 3149 O1A 6AD A1201 16.343 -0.306 54.904 1.00 40.02 O
HETATM 3150 O5' 6AD A1201 14.034 -1.053 55.675 1.00 37.87 O
HETATM 3151 C5' 6AD A1201 13.267 0.075 55.188 1.00 37.83 C
HETATM 3152 C4' 6AD A1201 11.889 -0.406 54.659 1.00 37.65 C
HETATM 3153 O4' 6AD A1201 12.011 -1.113 53.382 1.00 38.41 O
HETATM 3154 C3' 6AD A1201 11.197 -1.374 55.631 1.00 38.94 C
HETATM 3155 O3' 6AD A1201 9.769 -1.226 55.606 1.00 42.59 O
HETATM 3156 C2' 6AD A1201 11.582 -2.723 55.107 1.00 39.20 C
HETATM 3157 O2' 6AD A1201 10.634 -3.727 55.422 1.00 41.16 O
HETATM 3158 C1' 6AD A1201 11.687 -2.525 53.603 1.00 40.30 C
HETATM 3159 N9 6AD A1201 12.703 -3.449 53.002 1.00 43.64 N
HETATM 3160 C8 6AD A1201 13.886 -3.813 53.502 1.00 43.83 C
HETATM 3161 N7 6AD A1201 14.434 -4.713 52.697 1.00 46.33 N
HETATM 3162 C5 6AD A1201 13.612 -4.895 51.659 1.00 49.95 C
HETATM 3163 C4 6AD A1201 12.518 -4.136 51.880 1.00 47.93 C
HETATM 3164 N3 6AD A1201 11.505 -4.135 50.996 1.00 49.08 N
HETATM 3165 C2 6AD A1201 11.566 -4.903 49.892 1.00 51.58 C
HETATM 3166 S1 6AD A1201 10.191 -4.864 48.788 1.00 51.59 S
HETATM 3167 C11 6AD A1201 10.293 -6.409 47.909 1.00 51.19 C
HETATM 3168 N1 6AD A1201 12.677 -5.636 49.644 1.00 51.89 N
HETATM 3169 C6 6AD A1201 13.688 -5.642 50.532 1.00 49.64 C
HETATM 3170 N6 6AD A1201 14.761 -6.416 50.348 1.00 46.28 N
HETATM 3171 C1 CLR A1202 4.661 -1.470 27.470 1.00 90.56 C
HETATM 3172 C2 CLR A1202 5.076 -1.713 26.003 1.00 91.39 C
HETATM 3173 C3 CLR A1202 6.413 -1.027 25.618 1.00 91.71 C
HETATM 3174 C4 CLR A1202 7.539 -1.301 26.655 1.00 90.66 C
HETATM 3175 C5 CLR A1202 7.061 -0.983 28.055 1.00 89.72 C
HETATM 3176 C6 CLR A1202 7.755 -0.073 28.787 1.00 89.45 C
HETATM 3177 C7 CLR A1202 7.395 0.351 30.190 1.00 89.11 C
HETATM 3178 C8 CLR A1202 6.469 -0.694 30.870 1.00 88.75 C
HETATM 3179 C9 CLR A1202 5.276 -1.001 29.875 1.00 88.95 C
HETATM 3180 C10 CLR A1202 5.780 -1.699 28.548 1.00 89.10 C
HETATM 3181 C11 CLR A1202 3.992 -1.621 30.505 1.00 89.37 C
HETATM 3182 C12 CLR A1202 3.654 -1.098 31.917 1.00 88.90 C
HETATM 3183 C13 CLR A1202 4.844 -1.183 32.908 1.00 87.72 C
HETATM 3184 C14 CLR A1202 5.940 -0.237 32.269 1.00 87.63 C
HETATM 3185 C15 CLR A1202 6.908 0.063 33.410 1.00 87.03 C
HETATM 3186 C16 CLR A1202 5.975 0.220 34.619 1.00 86.76 C
HETATM 3187 C17 CLR A1202 4.583 -0.384 34.242 1.00 86.90 C
HETATM 3188 C18 CLR A1202 5.276 -2.691 33.158 1.00 87.14 C
HETATM 3189 C19 CLR A1202 6.052 -3.229 28.748 1.00 87.74 C
HETATM 3190 C20 CLR A1202 3.780 -1.006 35.438 1.00 86.51 C
HETATM 3191 C21 CLR A1202 2.373 -1.502 35.048 1.00 87.63 C
HETATM 3192 C22 CLR A1202 3.558 0.014 36.572 1.00 84.94 C
HETATM 3193 C23 CLR A1202 3.770 -0.697 37.899 1.00 84.30 C
HETATM 3194 C24 CLR A1202 3.008 -0.005 39.027 1.00 83.71 C
HETATM 3195 C25 CLR A1202 3.292 -0.651 40.397 1.00 83.27 C
HETATM 3196 C26 CLR A1202 2.279 -0.089 41.396 1.00 83.89 C
HETATM 3197 C27 CLR A1202 3.195 -2.190 40.370 1.00 82.31 C
HETATM 3198 O1 CLR A1202 6.737 -1.671 24.432 1.00 92.79 O
HETATM 3199 C10 OLC A1203 1.405 2.085 47.435 1.00 69.84 C
HETATM 3200 C9 OLC A1203 0.157 2.006 48.319 1.00 70.83 C
HETATM 3201 C8 OLC A1203 0.317 1.202 49.614 1.00 71.94 C
HETATM 3202 C24 OLC A1203 0.641 4.786 61.399 1.00 95.82 C
HETATM 3203 C7 OLC A1203 0.215 2.146 50.818 1.00 72.79 C
HETATM 3204 C6 OLC A1203 0.247 1.321 52.104 1.00 74.22 C
HETATM 3205 C5 OLC A1203 0.061 2.231 53.325 1.00 75.46 C
HETATM 3206 C4 OLC A1203 -0.732 1.465 54.383 1.00 77.30 C
HETATM 3207 C3 OLC A1203 -0.491 2.068 55.762 1.00 80.90 C
HETATM 3208 C2 OLC A1203 -1.491 1.463 56.748 1.00 84.54 C
HETATM 3209 C21 OLC A1203 -0.122 3.096 59.730 1.00 93.21 C
HETATM 3210 C1 OLC A1203 -0.936 1.526 58.174 1.00 88.60 C
HETATM 3211 C22 OLC A1203 -0.515 4.371 60.479 1.00 95.09 C
HETATM 3212 O19 OLC A1203 -0.380 0.544 58.667 1.00 89.86 O
HETATM 3213 O25 OLC A1203 0.508 4.151 62.677 1.00 95.55 O
HETATM 3214 O23 OLC A1203 -0.774 5.415 59.531 1.00 96.08 O
HETATM 3215 O20 OLC A1203 -1.178 2.699 58.836 1.00 91.24 O
HETATM 3216 C10 OLC A1204 33.729 -0.058 49.991 1.00 67.31 C
HETATM 3217 C9 OLC A1204 32.335 -0.409 50.522 1.00 66.74 C
HETATM 3218 C8 OLC A1204 32.293 -0.849 51.984 1.00 66.46 C
HETATM 3219 C24 OLC A1204 31.801 2.446 64.454 1.00 86.95 C
HETATM 3220 C7 OLC A1204 32.021 0.378 52.855 1.00 67.76 C
HETATM 3221 C6 OLC A1204 31.627 -0.043 54.274 1.00 68.82 C
HETATM 3222 C5 OLC A1204 32.646 0.490 55.295 1.00 70.24 C
HETATM 3223 C4 OLC A1204 32.155 1.797 55.940 1.00 71.82 C
HETATM 3224 C3 OLC A1204 31.546 1.500 57.313 1.00 73.07 C
HETATM 3225 C2 OLC A1204 32.204 2.374 58.386 1.00 75.15 C
HETATM 3226 C21 OLC A1204 31.928 2.558 61.925 1.00 83.05 C
HETATM 3227 C1 OLC A1204 32.234 1.665 59.752 1.00 77.84 C
HETATM 3228 C22 OLC A1204 32.713 2.282 63.220 1.00 85.38 C
HETATM 3229 O19 OLC A1204 31.857 0.498 59.873 1.00 77.77 O
HETATM 3230 O25 OLC A1204 30.968 1.291 64.664 1.00 86.73 O
HETATM 3231 O23 OLC A1204 33.283 0.968 63.193 1.00 85.58 O
HETATM 3232 O20 OLC A1204 32.774 2.410 60.771 1.00 80.73 O
HETATM 3233 C8 OLC A1205 35.845 3.699 51.669 1.00 95.08 C
HETATM 3234 C24 OLC A1205 31.156 6.294 61.917 1.00 91.02 C
HETATM 3235 C7 OLC A1205 35.281 5.124 51.685 1.00 95.07 C
HETATM 3236 C6 OLC A1205 33.796 5.081 52.057 1.00 95.41 C
HETATM 3237 C5 OLC A1205 33.571 5.763 53.412 1.00 95.51 C
HETATM 3238 C4 OLC A1205 32.118 5.570 53.867 1.00 95.07 C
HETATM 3239 C3 OLC A1205 31.968 6.039 55.319 1.00 94.90 C
HETATM 3240 C2 OLC A1205 30.734 5.389 55.956 1.00 95.12 C
HETATM 3241 C21 OLC A1205 31.129 5.929 59.430 1.00 93.88 C
HETATM 3242 C1 OLC A1205 30.308 6.136 57.228 1.00 95.81 C
HETATM 3243 C22 OLC A1205 30.265 6.187 60.673 1.00 92.34 C
HETATM 3244 O19 OLC A1205 29.908 7.300 57.171 1.00 97.02 O
HETATM 3245 O25 OLC A1205 30.396 6.766 63.038 1.00 90.27 O
HETATM 3246 O23 OLC A1205 29.523 7.399 60.497 1.00 92.55 O
HETATM 3247 O20 OLC A1205 30.319 5.383 58.370 1.00 95.27 O
HETATM 3248 C1 PEG A1206 37.717 -25.210 -0.301 1.00 65.43 C
HETATM 3249 O1 PEG A1206 38.051 -24.761 -1.624 1.00 65.19 O
HETATM 3250 C2 PEG A1206 36.948 -24.100 0.448 1.00 64.32 C
HETATM 3251 O2 PEG A1206 35.552 -24.416 0.634 1.00 63.77 O
HETATM 3252 C3 PEG A1206 34.784 -24.082 -0.541 1.00 62.99 C
HETATM 3253 C4 PEG A1206 33.280 -24.143 -0.267 1.00 61.04 C
HETATM 3254 O4 PEG A1206 32.593 -24.196 -1.527 1.00 59.57 O
HETATM 3255 O HOH A1301 33.071 -10.021 24.852 1.00 69.66 O
HETATM 3256 O HOH A1302 37.935 -12.632 30.598 1.00 63.54 O
HETATM 3257 O HOH A1303 25.778 -13.648 50.587 1.00 80.46 O
HETATM 3258 O HOH A1304 25.272 -16.609 49.716 1.00 71.55 O
HETATM 3259 O HOH A1305 20.378 -18.193 47.913 1.00 62.82 O
HETATM 3260 O HOH A1306 12.326 -18.226 53.361 1.00 74.57 O
HETATM 3261 O HOH A1307 13.531 -10.151 20.227 1.00 58.09 O
HETATM 3262 O HOH A1308 16.914 -11.552 20.316 1.00 76.08 O
HETATM 3263 O HOH A1309 35.430 -24.194 7.203 1.00 59.75 O
HETATM 3264 O HOH A1310 -0.853 -6.777 63.295 1.00 72.51 O
HETATM 3265 O HOH A1311 0.195 -10.131 48.439 1.00 63.23 O
HETATM 3266 O HOH A1312 30.687 -4.784 71.086 1.00 69.29 O
HETATM 3267 O HOH A1313 27.198 9.313 61.699 1.00 56.27 O
HETATM 3268 O HOH A1314 27.377 3.946 71.301 1.00 65.66 O
HETATM 3269 O HOH A1315 31.970 -25.006 -4.000 1.00 62.62 O
HETATM 3270 O HOH A1316 36.786 -13.020 10.564 1.00 37.59 O
HETATM 3271 O HOH A1317 26.789 -2.452 46.967 1.00 46.06 O
HETATM 3272 O HOH A1318 29.268 -6.947 57.334 1.00 46.46 O
HETATM 3273 O HOH A1319 17.077 -4.916 51.514 1.00 42.49 O
HETATM 3274 O HOH A1320 24.545 -11.354 53.314 1.00 45.37 O
HETATM 3275 O HOH A1321 42.954 -14.520 6.211 1.00 42.48 O
HETATM 3276 O HOH A1322 14.921 3.455 55.141 1.00 52.02 O
HETATM 3277 O HOH A1323 32.286 -13.599 21.828 1.00 44.21 O
HETATM 3278 O HOH A1324 22.677 4.961 52.088 1.00 45.76 O
HETATM 3279 O HOH A1325 20.558 -6.887 67.138 1.00 45.71 O
HETATM 3280 O HOH A1326 21.981 7.395 56.692 1.00 49.40 O
HETATM 3281 O HOH A1327 31.162 -6.849 14.077 1.00 47.40 O
HETATM 3282 O HOH A1328 7.519 -5.584 57.243 1.00 47.23 O
HETATM 3283 O HOH A1329 18.261 4.467 65.643 1.00 41.30 O
HETATM 3284 O HOH A1330 20.162 -17.238 50.454 1.00 61.11 O
HETATM 3285 O HOH A1331 15.897 -0.989 61.183 1.00 42.30 O
HETATM 3286 O HOH A1332 27.994 -4.668 22.667 1.00 60.70 O
HETATM 3287 O HOH A1333 20.829 -19.244 45.463 1.00 57.64 O
HETATM 3288 O HOH A1334 27.508 7.475 37.291 1.00 68.16 O
HETATM 3289 O HOH A1335 28.194 -2.258 72.608 1.00 56.52 O
HETATM 3290 O HOH A1336 18.396 2.223 61.008 1.00 48.50 O
HETATM 3291 O HOH A1337 25.987 -4.984 57.426 1.00 43.31 O
HETATM 3292 O HOH A1338 43.813 -13.511 8.580 1.00 45.03 O
HETATM 3293 O HOH A1339 1.608 -8.663 63.854 1.00 60.19 O
HETATM 3294 O HOH A1340 70.080 -23.444 -0.138 1.00 82.32 O
HETATM 3295 O HOH A1341 19.105 -9.881 54.023 1.00 41.09 O
HETATM 3296 O HOH A1342 18.600 -0.678 62.167 1.00 56.43 O
HETATM 3297 O HOH A1343 34.318 -19.892 4.747 1.00 69.16 O
HETATM 3298 O HOH A1344 15.501 -12.049 35.704 1.00 51.11 O
HETATM 3299 O HOH A1345 12.715 -17.353 55.888 1.00 69.46 O
HETATM 3300 O HOH A1346 62.761 -29.796 -2.340 1.00 68.77 O
HETATM 3301 O HOH A1347 27.865 -2.606 18.663 1.00 66.59 O
HETATM 3302 O HOH A1348 17.686 -7.141 50.221 1.00 44.89 O
HETATM 3303 O HOH A1349 14.067 -12.368 38.224 1.00 62.31 O
CONECT 19 2867
CONECT 647 1235
CONECT 1235 647
CONECT 2867 19
CONECT 3142 3143
CONECT 3143 3142 3144 3145 3146
CONECT 3144 3143
CONECT 3145 3143
CONECT 3146 3143 3147
CONECT 3147 3146 3148 3149 3150
CONECT 3148 3147
CONECT 3149 3147
CONECT 3150 3147 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153 3154
CONECT 3153 3152 3158
CONECT 3154 3152 3155 3156
CONECT 3155 3154
CONECT 3156 3154 3157 3158
CONECT 3157 3156
CONECT 3158 3153 3156 3159
CONECT 3159 3158 3160 3163
CONECT 3160 3159 3161
CONECT 3161 3160 3162
CONECT 3162 3161 3163 3169
CONECT 3163 3159 3162 3164
CONECT 3164 3163 3165
CONECT 3165 3164 3166 3168
CONECT 3166 3165 3167
CONECT 3167 3166
CONECT 3168 3165 3169
CONECT 3169 3162 3168 3170
CONECT 3170 3169
CONECT 3171 3172 3180
CONECT 3172 3171 3173
CONECT 3173 3172 3174 3198
CONECT 3174 3173 3175
CONECT 3175 3174 3176 3180
CONECT 3176 3175 3177
CONECT 3177 3176 3178
CONECT 3178 3177 3179 3184
CONECT 3179 3178 3180 3181
CONECT 3180 3171 3175 3179 3189
CONECT 3181 3179 3182
CONECT 3182 3181 3183
CONECT 3183 3182 3184 3187 3188
CONECT 3184 3178 3183 3185
CONECT 3185 3184 3186
CONECT 3186 3185 3187
CONECT 3187 3183 3186 3190
CONECT 3188 3183
CONECT 3189 3180
CONECT 3190 3187 3191 3192
CONECT 3191 3190
CONECT 3192 3190 3193
CONECT 3193 3192 3194
CONECT 3194 3193 3195
CONECT 3195 3194 3196 3197
CONECT 3196 3195
CONECT 3197 3195
CONECT 3198 3173
CONECT 3199 3200
CONECT 3200 3199 3201
CONECT 3201 3200 3203
CONECT 3202 3211 3213
CONECT 3203 3201 3204
CONECT 3204 3203 3205
CONECT 3205 3204 3206
CONECT 3206 3205 3207
CONECT 3207 3206 3208
CONECT 3208 3207 3210
CONECT 3209 3211 3215
CONECT 3210 3208 3212 3215
CONECT 3211 3202 3209 3214
CONECT 3212 3210
CONECT 3213 3202
CONECT 3214 3211
CONECT 3215 3209 3210
CONECT 3216 3217
CONECT 3217 3216 3218
CONECT 3218 3217 3220
CONECT 3219 3228 3230
CONECT 3220 3218 3221
CONECT 3221 3220 3222
CONECT 3222 3221 3223
CONECT 3223 3222 3224
CONECT 3224 3223 3225
CONECT 3225 3224 3227
CONECT 3226 3228 3232
CONECT 3227 3225 3229 3232
CONECT 3228 3219 3226 3231
CONECT 3229 3227
CONECT 3230 3219
CONECT 3231 3228
CONECT 3232 3226 3227
CONECT 3233 3235
CONECT 3234 3243 3245
CONECT 3235 3233 3236
CONECT 3236 3235 3237
CONECT 3237 3236 3238
CONECT 3238 3237 3239
CONECT 3239 3238 3240
CONECT 3240 3239 3242
CONECT 3241 3243 3247
CONECT 3242 3240 3244 3247
CONECT 3243 3234 3241 3246
CONECT 3244 3242
CONECT 3245 3234
CONECT 3246 3243
CONECT 3247 3241 3242
CONECT 3248 3249 3250
CONECT 3249 3248
CONECT 3250 3248 3251
CONECT 3251 3250 3252
CONECT 3252 3251 3253
CONECT 3253 3252 3254
CONECT 3254 3253
MASTER 421 0 6 18 0 0 15 6 3295 1 117 36
END