HEADER MEMBRANE PROTEIN 25-MAR-14 4PY0
TITLE CRYSTAL STRUCTURE OF P2Y12 RECEPTOR IN COMPLEX WITH 2MESATP
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, 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, PARTIAL AGONIST-BOUND, G-PROTEIN COUPLED
KEYWDS 2 RECEPTOR (GPCR), MEMBRANE PROTEIN, SIGNALING PROTEIN-NUCLEOTIDE
KEYWDS 3 COMPLEX, PSI-BIOLOGY, GPCR NETWORK, STRUCTURAL GENOMICS, SIGNALING
KEYWDS 4 MEMBRANE 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 4 16-AUG-17 4PY0 1 SOURCE REMARK
REVDAT 3 03-SEP-14 4PY0 1 REMARK
REVDAT 2 28-MAY-14 4PY0 1 JRNL
REVDAT 1 30-APR-14 4PY0 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. 3.10 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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 8273
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 422
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.33
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2293
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2277
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2178
REMARK 3 BIN R VALUE (WORKING SET) : 0.2248
REMARK 3 BIN FREE R VALUE : 0.2876
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.02
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 115
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 : 3046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 87.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.89220
REMARK 3 B22 (A**2) : -0.33710
REMARK 3 B33 (A**2) : -2.55520
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.60830
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.653
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.498
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.864
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3190 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4341 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1448 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 56 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 458 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3190 ; 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 : 447 ; 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 : 3707 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.87
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.68
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.24
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): -13.485 -10.127 -0.115
REMARK 3 T TENSOR
REMARK 3 T11: 0.7049 T22: 0.2790
REMARK 3 T33: 0.3761 T12: 0.0947
REMARK 3 T13: -0.1688 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 1.5617 L22: 0.9639
REMARK 3 L33: 0.0491 L12: 0.2137
REMARK 3 L13: 0.3302 L23: -0.2873
REMARK 3 S TENSOR
REMARK 3 S11: -0.1393 S12: -0.5087 S13: 0.2083
REMARK 3 S21: 0.5340 S22: -0.1158 S23: -0.3719
REMARK 3 S31: -0.1519 S32: -0.2820 S33: 0.2551
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.502 -25.972 -43.415
REMARK 3 T TENSOR
REMARK 3 T11: -0.0281 T22: 0.0338
REMARK 3 T33: 0.1848 T12: 0.0543
REMARK 3 T13: 0.1481 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 0.8698 L22: 1.5112
REMARK 3 L33: 7.1701 L12: 0.4498
REMARK 3 L13: 1.6070 L23: 0.9282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: -0.0124 S13: 0.1509
REMARK 3 S21: 0.4882 S22: -0.2147 S23: -0.2456
REMARK 3 S31: -0.3026 S32: -0.3963 S33: 0.2731
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PY0 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_1000085360.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 6
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8273
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.22200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.92200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4PXZ AND 1M6T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35-40% PEG 400, 0.15-0.20M AMMONIUM
REMARK 280 TARTRATE, 4% V/V MPD, 0.1M SODIUM CITRATE, PH 6.0, LIPIDIC CUBIC
REMARK 280 PHASE (LCP), TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 37.82500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.82500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 LEU A 87
REMARK 465 GLY A 88
REMARK 465 PRO A 129
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 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 165 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 168 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 ASN A 171 CG OD1 ND2
REMARK 470 GLU A 181 CD OE1 OE2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1015 CG CD CE NZ
REMARK 470 GLU A1018 CG CD OE1 OE2
REMARK 470 LYS A1019 CG CD CE NZ
REMARK 470 GLN A1025 CG CD OE1 NE2
REMARK 470 LYS A1027 CG CD CE NZ
REMARK 470 LEU A1030 CG CD1 CD2
REMARK 470 LYS A1032 CG CD CE NZ
REMARK 470 ARG A1034 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1038 CG CD1 CD2
REMARK 470 ASP A1050 CG OD1 OD2
REMARK 470 ASP A1073 CG OD1 OD2
REMARK 470 LEU A1076 CG CD1 CD2
REMARK 470 LYS A1077 CG CD CE NZ
REMARK 470 GLN A1103 CG CD OE1 NE2
REMARK 470 LYS A 232 CG CD CE NZ
REMARK 470 LEU A 293 CG CD1 CD2
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 -73.65 -117.39
REMARK 500 VAL A 172 97.12 -69.09
REMARK 500 THR A1009 32.22 -82.58
REMARK 500 LEU A1010 -35.93 -143.08
REMARK 500 ASP A1050 39.90 -91.94
REMARK 500 LYS A 303 52.00 -99.39
REMARK 500 SER A 304 -34.29 -155.02
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 1202
REMARK 610 OLC A 1203
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6AT A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC 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 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: 4PXZ RELATED DB: PDB
DBREF 4PY0 A 2 223 UNP Q9H244 P2Y12_HUMAN 2 223
DBREF 4PY0 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 4PY0 A 224 342 UNP Q9H244 P2Y12_HUMAN 224 342
SEQADV 4PY0 ASP A -9 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 TYR A -8 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 LYS A -7 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ASP A -6 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ASP A -5 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ASP A -4 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ASP A -3 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 GLY A -2 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ALA A -1 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 PRO A 0 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 4PY0 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 4PY0 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 4PY0 ASN A 294 UNP Q9H244 ASP 294 ENGINEERED MUTATION
SEQADV 4PY0 GLY A 343 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 ARG A 344 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 PRO A 345 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 LEU A 346 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 GLU A 347 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 VAL A 348 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 LEU A 349 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 PHE A 350 UNP Q9H244 EXPRESSION TAG
SEQADV 4PY0 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 6AT A1201 33
HET OLC A1202 16
HET OLC A1203 16
HETNAM 6AT 2-(METHYLSULFANYL)ADENOSINE 5'-(TETRAHYDROGEN
HETNAM 2 6AT TRIPHOSPHATE)
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN 6AT 2-METHYLTHIO-ADENOSINE-5'-TRIPHOSPHATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 6AT C11 H18 N5 O13 P3 S
FORMUL 3 OLC 2(C21 H40 O4)
FORMUL 5 HOH *(H2 O)
HELIX 1 1 ILE A 23 PHE A 51 1 29
HELIX 2 2 SER A 57 LYS A 86 1 30
HELIX 3 3 GLY A 90 VAL A 99 1 10
HELIX 4 4 VAL A 99 ARG A 128 1 30
HELIX 5 5 LYS A 136 LEU A 162 1 27
HELIX 6 6 LYS A 174 LYS A 179 5 6
HELIX 7 7 SER A 180 ALA A 1020 1 64
HELIX 8 8 ASN A 1022 ALA A 1043 1 22
HELIX 9 9 PRO A 1045 GLU A 1049 5 5
HELIX 10 10 SER A 1055 GLY A 1082 1 28
HELIX 11 11 VAL A 1084 GLU A 1092 1 9
HELIX 12 12 GLN A 1093 LYS A 1095 5 3
HELIX 13 13 THR A 1096 LYS A 228 1 16
HELIX 14 14 ASN A 235 PHE A 249 1 15
HELIX 15 15 PHE A 249 PHE A 254 1 6
HELIX 16 16 ALA A 255 ARG A 265 1 11
HELIX 17 17 ASP A 269 LEU A 289 1 21
HELIX 18 18 ASN A 290 ASN A 294 5 5
HELIX 19 19 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 20 ARG A 93 CYS A 97 SER A 101 VAL A 102
SITE 2 AC1 20 TYR A 105 SER A 156 ASN A 159 LYS A 173
SITE 3 AC1 20 LYS A 174 CYS A 175 SER A 176 LYS A 179
SITE 4 AC1 20 HIS A 187 VAL A 190 ASN A 191 CYS A 194
SITE 5 AC1 20 ARG A 256 TYR A 259 GLN A 263 LYS A 280
SITE 1 AC2 3 THR A 275 TYR A 278 OLC A1203
SITE 1 AC3 7 ASP A 20 ILE A 23 PHE A 28 TYR A 278
SITE 2 AC3 7 SER A 282 TRP A 285 OLC A1202
CRYST1 75.650 65.110 100.740 90.00 95.50 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013219 0.000000 0.001273 0.00000
SCALE2 0.000000 0.015359 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009972 0.00000
ATOM 1 N SER A 15 -15.725 -8.746 29.913 1.00 95.67 N
ANISOU 1 N SER A 15 13198 13443 9707 1902 2286 -1208 N
ATOM 2 CA SER A 15 -16.635 -8.217 30.925 1.00 97.40 C
ANISOU 2 CA SER A 15 13383 13782 9841 1996 2414 -1320 C
ATOM 3 C SER A 15 -16.069 -6.946 31.579 1.00101.86 C
ANISOU 3 C SER A 15 14012 14329 10363 2077 2362 -1535 C
ATOM 4 O SER A 15 -16.767 -5.931 31.633 1.00102.45 O
ANISOU 4 O SER A 15 14026 14369 10530 2155 2399 -1669 O
ATOM 5 CB SER A 15 -16.932 -9.274 31.985 1.00102.04 C
ANISOU 5 CB SER A 15 13986 14562 10221 1985 2531 -1231 C
ATOM 6 N LEU A 16 -14.809 -7.002 32.067 1.00 97.75 N
ANISOU 6 N LEU A 16 13606 13824 9712 2059 2273 -1569 N
ATOM 7 CA LEU A 16 -14.117 -5.879 32.710 1.00 98.14 C
ANISOU 7 CA LEU A 16 13725 13851 9711 2127 2204 -1767 C
ATOM 8 C LEU A 16 -12.819 -5.523 31.945 1.00 99.33 C
ANISOU 8 C LEU A 16 13939 13840 9963 2081 2024 -1768 C
ATOM 9 O LEU A 16 -12.009 -4.722 32.424 1.00 99.45 O
ANISOU 9 O LEU A 16 14025 13824 9936 2121 1939 -1908 O
ATOM 10 CB LEU A 16 -13.814 -6.224 34.179 1.00 99.78 C
ANISOU 10 CB LEU A 16 14017 14246 9649 2154 2264 -1819 C
ATOM 11 CG LEU A 16 -13.856 -5.052 35.153 1.00106.43 C
ANISOU 11 CG LEU A 16 14890 15134 10413 2260 2282 -2057 C
ATOM 12 CD1 LEU A 16 -14.952 -5.238 36.183 1.00108.59 C
ANISOU 12 CD1 LEU A 16 15122 15601 10537 2320 2465 -2099 C
ATOM 13 CD2 LEU A 16 -12.514 -4.858 35.827 1.00109.16 C
ANISOU 13 CD2 LEU A 16 15365 15496 10615 2254 2167 -2136 C
ATOM 14 N CYS A 17 -12.651 -6.102 30.738 1.00 93.08 N
ANISOU 14 N CYS A 17 13114 12943 9310 1998 1968 -1615 N
ATOM 15 CA CYS A 17 -11.490 -5.895 29.872 1.00 90.86 C
ANISOU 15 CA CYS A 17 12878 12512 9132 1945 1811 -1590 C
ATOM 16 C CYS A 17 -11.520 -4.506 29.230 1.00 95.45 C
ANISOU 16 C CYS A 17 13418 12944 9903 1994 1729 -1715 C
ATOM 17 O CYS A 17 -12.582 -4.029 28.819 1.00 95.24 O
ANISOU 17 O CYS A 17 13295 12884 10007 2028 1782 -1740 O
ATOM 18 CB CYS A 17 -11.404 -6.993 28.814 1.00 88.87 C
ANISOU 18 CB CYS A 17 12600 12212 8956 1843 1792 -1395 C
ATOM 19 SG CYS A 17 -10.025 -6.809 27.649 1.00 90.51 S
ANISOU 19 SG CYS A 17 12855 12246 9288 1773 1616 -1353 S
ATOM 20 N THR A 18 -10.336 -3.874 29.141 1.00 92.29 N
ANISOU 20 N THR A 18 13086 12450 9529 1995 1592 -1785 N
ATOM 21 CA THR A 18 -10.139 -2.553 28.542 1.00 92.27 C
ANISOU 21 CA THR A 18 13051 12295 9714 2035 1488 -1895 C
ATOM 22 C THR A 18 -9.317 -2.702 27.250 1.00 94.37 C
ANISOU 22 C THR A 18 13313 12422 10120 1950 1368 -1774 C
ATOM 23 O THR A 18 -8.299 -3.400 27.233 1.00 92.91 O
ANISOU 23 O THR A 18 13201 12240 9859 1888 1314 -1689 O
ATOM 24 CB THR A 18 -9.525 -1.546 29.552 1.00102.37 C
ANISOU 24 CB THR A 18 14397 13573 10924 2113 1428 -2088 C
ATOM 25 OG1 THR A 18 -9.307 -0.291 28.903 1.00101.74 O
ANISOU 25 OG1 THR A 18 14275 13330 11051 2146 1316 -2180 O
ATOM 26 CG2 THR A 18 -8.224 -2.042 30.208 1.00101.09 C
ANISOU 26 CG2 THR A 18 14357 13451 10600 2075 1355 -2066 C
ATOM 27 N ARG A 19 -9.789 -2.064 26.169 1.00 90.66 N
ANISOU 27 N ARG A 19 12754 11835 9857 1947 1330 -1761 N
ATOM 28 CA ARG A 19 -9.146 -2.100 24.858 1.00 88.92 C
ANISOU 28 CA ARG A 19 12517 11490 9777 1869 1223 -1650 C
ATOM 29 C ARG A 19 -8.568 -0.727 24.519 1.00 93.53 C
ANISOU 29 C ARG A 19 13087 11933 10519 1906 1092 -1750 C
ATOM 30 O ARG A 19 -9.256 0.287 24.661 1.00 94.06 O
ANISOU 30 O ARG A 19 13087 11959 10693 1977 1098 -1862 O
ATOM 31 CB ARG A 19 -10.149 -2.562 23.787 1.00 87.77 C
ANISOU 31 CB ARG A 19 12277 11333 9739 1818 1278 -1524 C
ATOM 32 CG ARG A 19 -9.514 -2.996 22.470 1.00 93.56 C
ANISOU 32 CG ARG A 19 13008 11984 10557 1718 1196 -1382 C
ATOM 33 CD ARG A 19 -10.511 -3.726 21.592 1.00 98.56 C
ANISOU 33 CD ARG A 19 13567 12641 11242 1660 1265 -1253 C
ATOM 34 NE ARG A 19 -10.645 -5.134 21.971 1.00102.84 N
ANISOU 34 NE ARG A 19 14147 13292 11634 1615 1351 -1160 N
ATOM 35 CZ ARG A 19 -11.588 -5.952 21.515 1.00114.03 C
ANISOU 35 CZ ARG A 19 15508 14755 13062 1572 1430 -1055 C
ATOM 36 NH1 ARG A 19 -12.505 -5.511 20.662 1.00 99.32 N
ANISOU 36 NH1 ARG A 19 13551 12843 11344 1566 1435 -1028 N
ATOM 37 NH2 ARG A 19 -11.628 -7.216 21.916 1.00100.34 N
ANISOU 37 NH2 ARG A 19 13807 13113 11203 1533 1499 -972 N
ATOM 38 N ASP A 20 -7.296 -0.702 24.087 1.00 89.75 N
ANISOU 38 N ASP A 20 12664 11375 10062 1859 973 -1708 N
ATOM 39 CA ASP A 20 -6.592 0.524 23.718 1.00 89.92 C
ANISOU 39 CA ASP A 20 12673 11256 10237 1883 834 -1781 C
ATOM 40 C ASP A 20 -7.078 1.001 22.346 1.00 93.26 C
ANISOU 40 C ASP A 20 12991 11573 10871 1846 788 -1699 C
ATOM 41 O ASP A 20 -6.762 0.386 21.322 1.00 91.54 O
ANISOU 41 O ASP A 20 12769 11325 10687 1759 755 -1556 O
ATOM 42 CB ASP A 20 -5.067 0.303 23.733 1.00 91.16 C
ANISOU 42 CB ASP A 20 12922 11373 10343 1842 729 -1748 C
ATOM 43 CG ASP A 20 -4.263 1.575 23.569 1.00102.57 C
ANISOU 43 CG ASP A 20 14363 12682 11929 1878 585 -1837 C
ATOM 44 OD1 ASP A 20 -3.989 1.958 22.411 1.00102.44 O
ANISOU 44 OD1 ASP A 20 14292 12554 12076 1833 500 -1757 O
ATOM 45 OD2 ASP A 20 -3.904 2.186 24.597 1.00109.87 O
ANISOU 45 OD2 ASP A 20 15335 13612 12799 1949 553 -1984 O
ATOM 46 N TYR A 21 -7.877 2.082 22.341 1.00 90.84 N
ANISOU 46 N TYR A 21 12596 11214 10705 1910 789 -1791 N
ATOM 47 CA TYR A 21 -8.431 2.667 21.120 1.00 90.21 C
ANISOU 47 CA TYR A 21 12405 11033 10837 1880 740 -1718 C
ATOM 48 C TYR A 21 -7.677 3.942 20.697 1.00 92.83 C
ANISOU 48 C TYR A 21 12706 11214 11350 1899 585 -1769 C
ATOM 49 O TYR A 21 -8.023 4.531 19.674 1.00 92.16 O
ANISOU 49 O TYR A 21 12525 11037 11453 1873 525 -1706 O
ATOM 50 CB TYR A 21 -9.937 2.958 21.283 1.00 92.84 C
ANISOU 50 CB TYR A 21 12640 11393 11240 1930 838 -1762 C
ATOM 51 CG TYR A 21 -10.811 1.721 21.254 1.00 94.82 C
ANISOU 51 CG TYR A 21 12887 11767 11372 1890 975 -1663 C
ATOM 52 CD1 TYR A 21 -11.047 1.037 20.064 1.00 95.74 C
ANISOU 52 CD1 TYR A 21 12969 11876 11532 1794 972 -1493 C
ATOM 53 CD2 TYR A 21 -11.435 1.257 22.408 1.00 96.74 C
ANISOU 53 CD2 TYR A 21 13155 12135 11466 1948 1107 -1740 C
ATOM 54 CE1 TYR A 21 -11.849 -0.103 20.031 1.00 96.58 C
ANISOU 54 CE1 TYR A 21 13066 12086 11544 1758 1089 -1403 C
ATOM 55 CE2 TYR A 21 -12.248 0.124 22.386 1.00 97.50 C
ANISOU 55 CE2 TYR A 21 13239 12340 11468 1911 1229 -1639 C
ATOM 56 CZ TYR A 21 -12.450 -0.555 21.195 1.00104.33 C
ANISOU 56 CZ TYR A 21 14069 13184 12389 1817 1216 -1472 C
ATOM 57 OH TYR A 21 -13.244 -1.676 21.167 1.00105.43 O
ANISOU 57 OH TYR A 21 14192 13421 12448 1780 1327 -1373 O
ATOM 58 N LYS A 22 -6.624 4.332 21.450 1.00 88.65 N
ANISOU 58 N LYS A 22 12257 10660 10767 1938 514 -1869 N
ATOM 59 CA LYS A 22 -5.800 5.528 21.214 1.00 88.20 C
ANISOU 59 CA LYS A 22 12177 10459 10874 1963 361 -1927 C
ATOM 60 C LYS A 22 -5.121 5.541 19.831 1.00 89.15 C
ANISOU 60 C LYS A 22 12266 10490 11119 1871 257 -1762 C
ATOM 61 O LYS A 22 -4.892 6.622 19.283 1.00 89.03 O
ANISOU 61 O LYS A 22 12177 10347 11303 1881 143 -1769 O
ATOM 62 CB LYS A 22 -4.725 5.672 22.305 1.00 91.32 C
ANISOU 62 CB LYS A 22 12680 10862 11153 2008 310 -2045 C
ATOM 63 CG LYS A 22 -5.278 6.009 23.693 1.00107.29 C
ANISOU 63 CG LYS A 22 14730 12956 13079 2110 382 -2241 C
ATOM 64 CD LYS A 22 -4.202 6.525 24.662 1.00117.36 C
ANISOU 64 CD LYS A 22 16090 14198 14302 2162 287 -2381 C
ATOM 65 CE LYS A 22 -3.364 5.446 25.318 1.00126.11 C
ANISOU 65 CE LYS A 22 17329 15410 15178 2124 307 -2341 C
ATOM 66 NZ LYS A 22 -4.139 4.652 26.310 1.00135.15 N
ANISOU 66 NZ LYS A 22 18522 16728 16101 2151 460 -2390 N
ATOM 67 N ILE A 23 -4.802 4.355 19.276 1.00 83.06 N
ANISOU 67 N ILE A 23 11543 9785 10232 1783 298 -1618 N
ATOM 68 CA ILE A 23 -4.142 4.218 17.972 1.00 80.97 C
ANISOU 68 CA ILE A 23 11256 9459 10050 1690 219 -1462 C
ATOM 69 C ILE A 23 -5.186 3.909 16.874 1.00 82.38 C
ANISOU 69 C ILE A 23 11346 9656 10300 1631 267 -1341 C
ATOM 70 O ILE A 23 -5.143 4.538 15.815 1.00 81.68 O
ANISOU 70 O ILE A 23 11178 9481 10374 1591 181 -1262 O
ATOM 71 CB ILE A 23 -3.006 3.147 18.035 1.00 83.06 C
ANISOU 71 CB ILE A 23 11628 9775 10156 1630 226 -1388 C
ATOM 72 CG1 ILE A 23 -1.928 3.545 19.068 1.00 84.07 C
ANISOU 72 CG1 ILE A 23 11836 9866 10241 1682 152 -1495 C
ATOM 73 CG2 ILE A 23 -2.359 2.903 16.662 1.00 82.45 C
ANISOU 73 CG2 ILE A 23 11526 9656 10144 1530 171 -1226 C
ATOM 74 CD1 ILE A 23 -1.571 2.464 20.052 1.00 91.53 C
ANISOU 74 CD1 ILE A 23 12889 10920 10968 1686 228 -1525 C
ATOM 75 N THR A 24 -6.124 2.972 17.137 1.00 77.36 N
ANISOU 75 N THR A 24 10718 9130 9544 1622 399 -1322 N
ATOM 76 CA THR A 24 -7.162 2.541 16.186 1.00 76.02 C
ANISOU 76 CA THR A 24 10473 8991 9421 1564 452 -1209 C
ATOM 77 C THR A 24 -8.159 3.660 15.801 1.00 78.69 C
ANISOU 77 C THR A 24 10686 9252 9962 1598 418 -1232 C
ATOM 78 O THR A 24 -8.738 3.582 14.717 1.00 77.94 O
ANISOU 78 O THR A 24 10517 9144 9953 1532 406 -1114 O
ATOM 79 CB THR A 24 -7.941 1.322 16.719 1.00 84.43 C
ANISOU 79 CB THR A 24 11571 10185 10321 1561 599 -1199 C
ATOM 80 OG1 THR A 24 -8.587 1.658 17.947 1.00 84.85 O
ANISOU 80 OG1 THR A 24 11620 10277 10344 1659 669 -1338 O
ATOM 81 CG2 THR A 24 -7.065 0.083 16.892 1.00 82.38 C
ANISOU 81 CG2 THR A 24 11419 10000 9881 1512 635 -1149 C
ATOM 82 N GLN A 25 -8.361 4.682 16.667 1.00 74.60 N
ANISOU 82 N GLN A 25 10139 8683 9522 1698 400 -1384 N
ATOM 83 CA GLN A 25 -9.294 5.781 16.386 1.00 74.45 C
ANISOU 83 CA GLN A 25 9992 8579 9715 1738 366 -1418 C
ATOM 84 C GLN A 25 -8.683 6.846 15.449 1.00 76.41 C
ANISOU 84 C GLN A 25 10171 8689 10172 1708 206 -1360 C
ATOM 85 O GLN A 25 -9.417 7.698 14.949 1.00 76.69 O
ANISOU 85 O GLN A 25 10087 8645 10408 1719 160 -1348 O
ATOM 86 CB GLN A 25 -9.810 6.435 17.686 1.00 77.22 C
ANISOU 86 CB GLN A 25 10333 8931 10076 1859 418 -1614 C
ATOM 87 CG GLN A 25 -8.846 7.419 18.358 1.00 88.12 C
ANISOU 87 CG GLN A 25 11744 10224 11515 1928 314 -1754 C
ATOM 88 CD GLN A 25 -9.476 8.125 19.533 1.00102.27 C
ANISOU 88 CD GLN A 25 13512 12013 13332 2047 364 -1957 C
ATOM 89 OE1 GLN A 25 -9.201 7.811 20.694 1.00 97.57 O
ANISOU 89 OE1 GLN A 25 13010 11473 12589 2105 394 -2090 O
ATOM 90 NE2 GLN A 25 -10.318 9.111 19.259 1.00 92.63 N
ANISOU 90 NE2 GLN A 25 12163 10726 12304 2084 370 -1990 N
ATOM 91 N VAL A 26 -7.359 6.805 15.227 1.00 70.91 N
ANISOU 91 N VAL A 26 9542 7964 9438 1670 121 -1319 N
ATOM 92 CA VAL A 26 -6.661 7.765 14.366 1.00 70.10 C
ANISOU 92 CA VAL A 26 9378 7738 9520 1637 -31 -1251 C
ATOM 93 C VAL A 26 -6.156 7.062 13.089 1.00 71.61 C
ANISOU 93 C VAL A 26 9583 7961 9664 1516 -55 -1061 C
ATOM 94 O VAL A 26 -6.332 7.596 11.995 1.00 71.02 O
ANISOU 94 O VAL A 26 9416 7827 9740 1460 -135 -946 O
ATOM 95 CB VAL A 26 -5.502 8.487 15.119 1.00 74.36 C
ANISOU 95 CB VAL A 26 9968 8199 10087 1700 -124 -1368 C
ATOM 96 CG1 VAL A 26 -4.855 9.567 14.253 1.00 74.17 C
ANISOU 96 CG1 VAL A 26 9864 8039 10279 1671 -285 -1293 C
ATOM 97 CG2 VAL A 26 -5.980 9.086 16.441 1.00 75.61 C
ANISOU 97 CG2 VAL A 26 10125 8343 10261 1820 -90 -1574 C
ATOM 98 N LEU A 27 -5.539 5.873 13.237 1.00 66.56 N
ANISOU 98 N LEU A 27 9056 7416 8820 1476 13 -1031 N
ATOM 99 CA LEU A 27 -4.936 5.100 12.150 1.00 64.87 C
ANISOU 99 CA LEU A 27 8870 7239 8538 1368 3 -877 C
ATOM 100 C LEU A 27 -5.962 4.486 11.181 1.00 67.67 C
ANISOU 100 C LEU A 27 9169 7656 8886 1292 60 -758 C
ATOM 101 O LEU A 27 -5.824 4.686 9.973 1.00 66.87 O
ANISOU 101 O LEU A 27 9013 7529 8865 1213 -8 -631 O
ATOM 102 CB LEU A 27 -4.036 3.993 12.734 1.00 64.15 C
ANISOU 102 CB LEU A 27 8908 7223 8242 1359 66 -898 C
ATOM 103 CG LEU A 27 -3.110 3.248 11.772 1.00 67.71 C
ANISOU 103 CG LEU A 27 9402 7701 8623 1260 51 -769 C
ATOM 104 CD1 LEU A 27 -1.886 4.082 11.415 1.00 67.86 C
ANISOU 104 CD1 LEU A 27 9403 7620 8759 1245 -80 -730 C
ATOM 105 CD2 LEU A 27 -2.661 1.946 12.380 1.00 69.69 C
ANISOU 105 CD2 LEU A 27 9766 8032 8682 1256 135 -796 C
ATOM 106 N PHE A 28 -6.953 3.723 11.691 1.00 63.72 N
ANISOU 106 N PHE A 28 8681 7240 8289 1312 180 -793 N
ATOM 107 CA PHE A 28 -7.946 3.044 10.851 1.00 62.77 C
ANISOU 107 CA PHE A 28 8514 7180 8156 1240 236 -686 C
ATOM 108 C PHE A 28 -8.926 4.008 10.131 1.00 66.16 C
ANISOU 108 C PHE A 28 8809 7542 8786 1232 175 -636 C
ATOM 109 O PHE A 28 -9.098 3.804 8.928 1.00 65.33 O
ANISOU 109 O PHE A 28 8662 7450 8708 1138 142 -500 O
ATOM 110 CB PHE A 28 -8.715 1.963 11.625 1.00 64.55 C
ANISOU 110 CB PHE A 28 8785 7509 8233 1264 377 -729 C
ATOM 111 CG PHE A 28 -7.897 0.711 11.848 1.00 65.20 C
ANISOU 111 CG PHE A 28 8980 7669 8124 1229 435 -714 C
ATOM 112 CD1 PHE A 28 -7.700 -0.204 10.819 1.00 67.30 C
ANISOU 112 CD1 PHE A 28 9266 7973 8331 1126 435 -594 C
ATOM 113 CD2 PHE A 28 -7.314 0.452 13.082 1.00 67.59 C
ANISOU 113 CD2 PHE A 28 9365 8006 8308 1296 488 -821 C
ATOM 114 CE1 PHE A 28 -6.929 -1.353 11.022 1.00 67.44 C
ANISOU 114 CE1 PHE A 28 9380 8051 8194 1096 487 -584 C
ATOM 115 CE2 PHE A 28 -6.548 -0.700 13.285 1.00 69.56 C
ANISOU 115 CE2 PHE A 28 9710 8320 8397 1260 535 -797 C
ATOM 116 CZ PHE A 28 -6.360 -1.594 12.253 1.00 66.65 C
ANISOU 116 CZ PHE A 28 9355 7977 7991 1162 534 -680 C
ATOM 117 N PRO A 29 -9.548 5.057 10.752 1.00 62.82 N
ANISOU 117 N PRO A 29 8313 7048 8509 1320 155 -734 N
ATOM 118 CA PRO A 29 -10.446 5.932 9.970 1.00 62.88 C
ANISOU 118 CA PRO A 29 8184 6985 8725 1300 89 -667 C
ATOM 119 C PRO A 29 -9.714 6.689 8.860 1.00 65.41 C
ANISOU 119 C PRO A 29 8451 7229 9175 1232 -55 -550 C
ATOM 120 O PRO A 29 -10.325 6.980 7.834 1.00 65.44 O
ANISOU 120 O PRO A 29 8361 7215 9288 1164 -106 -427 O
ATOM 121 CB PRO A 29 -11.012 6.897 11.018 1.00 66.01 C
ANISOU 121 CB PRO A 29 8523 7310 9246 1420 97 -823 C
ATOM 122 CG PRO A 29 -10.809 6.212 12.319 1.00 70.64 C
ANISOU 122 CG PRO A 29 9220 7975 9644 1491 208 -958 C
ATOM 123 CD PRO A 29 -9.506 5.497 12.159 1.00 65.14 C
ANISOU 123 CD PRO A 29 8639 7322 8791 1437 189 -911 C
ATOM 124 N LEU A 30 -8.407 6.973 9.050 1.00 60.27 N
ANISOU 124 N LEU A 30 7857 6537 8505 1244 -122 -578 N
ATOM 125 CA LEU A 30 -7.552 7.649 8.071 1.00 59.19 C
ANISOU 125 CA LEU A 30 7677 6334 8477 1181 -255 -465 C
ATOM 126 C LEU A 30 -7.265 6.717 6.882 1.00 59.87 C
ANISOU 126 C LEU A 30 7798 6510 8439 1058 -239 -308 C
ATOM 127 O LEU A 30 -7.361 7.150 5.733 1.00 59.44 O
ANISOU 127 O LEU A 30 7665 6435 8484 979 -323 -171 O
ATOM 128 CB LEU A 30 -6.239 8.099 8.738 1.00 59.32 C
ANISOU 128 CB LEU A 30 7756 6290 8495 1235 -315 -548 C
ATOM 129 CG LEU A 30 -5.341 9.026 7.929 1.00 64.17 C
ANISOU 129 CG LEU A 30 8318 6821 9242 1186 -458 -442 C
ATOM 130 CD1 LEU A 30 -5.494 10.463 8.388 1.00 65.75 C
ANISOU 130 CD1 LEU A 30 8409 6879 9693 1254 -571 -498 C
ATOM 131 CD2 LEU A 30 -3.890 8.590 8.026 1.00 65.71 C
ANISOU 131 CD2 LEU A 30 8621 7028 9317 1179 -468 -455 C
ATOM 132 N LEU A 31 -6.921 5.443 7.169 1.00 53.93 N
ANISOU 132 N LEU A 31 7160 5858 7474 1041 -135 -331 N
ATOM 133 CA LEU A 31 -6.626 4.413 6.171 1.00 52.08 C
ANISOU 133 CA LEU A 31 6971 5714 7103 933 -102 -214 C
ATOM 134 C LEU A 31 -7.855 4.081 5.318 1.00 54.04 C
ANISOU 134 C LEU A 31 7154 6015 7364 864 -75 -119 C
ATOM 135 O LEU A 31 -7.720 3.870 4.111 1.00 53.17 O
ANISOU 135 O LEU A 31 7028 5945 7228 761 -110 8 O
ATOM 136 CB LEU A 31 -6.112 3.135 6.855 1.00 51.43 C
ANISOU 136 CB LEU A 31 7016 5710 6814 946 5 -281 C
ATOM 137 CG LEU A 31 -4.635 3.084 7.243 1.00 55.85 C
ANISOU 137 CG LEU A 31 7658 6246 7318 961 -25 -316 C
ATOM 138 CD1 LEU A 31 -4.390 1.988 8.262 1.00 55.67 C
ANISOU 138 CD1 LEU A 31 7745 6288 7119 996 81 -402 C
ATOM 139 CD2 LEU A 31 -3.741 2.866 6.029 1.00 57.61 C
ANISOU 139 CD2 LEU A 31 7882 6482 7524 861 -77 -187 C
ATOM 140 N TYR A 32 -9.049 4.040 5.945 1.00 49.62 N
ANISOU 140 N TYR A 32 6555 5458 6842 918 -14 -181 N
ATOM 141 CA TYR A 32 -10.309 3.740 5.268 1.00 48.81 C
ANISOU 141 CA TYR A 32 6383 5394 6767 860 9 -95 C
ATOM 142 C TYR A 32 -10.823 4.947 4.457 1.00 51.58 C
ANISOU 142 C TYR A 32 6599 5665 7334 830 -111 -4 C
ATOM 143 O TYR A 32 -11.626 4.750 3.544 1.00 50.98 O
ANISOU 143 O TYR A 32 6465 5622 7284 750 -128 110 O
ATOM 144 CB TYR A 32 -11.371 3.251 6.263 1.00 50.27 C
ANISOU 144 CB TYR A 32 6571 5613 6915 929 125 -187 C
ATOM 145 CG TYR A 32 -11.332 1.759 6.524 1.00 51.04 C
ANISOU 145 CG TYR A 32 6772 5818 6805 907 242 -202 C
ATOM 146 CD1 TYR A 32 -11.907 0.859 5.630 1.00 52.62 C
ANISOU 146 CD1 TYR A 32 6969 6090 6936 813 271 -101 C
ATOM 147 CD2 TYR A 32 -10.769 1.250 7.690 1.00 51.43 C
ANISOU 147 CD2 TYR A 32 6914 5894 6732 979 318 -318 C
ATOM 148 CE1 TYR A 32 -11.890 -0.514 5.874 1.00 52.49 C
ANISOU 148 CE1 TYR A 32 7036 6160 6748 793 373 -115 C
ATOM 149 CE2 TYR A 32 -10.754 -0.121 7.949 1.00 51.59 C
ANISOU 149 CE2 TYR A 32 7017 6006 6578 957 420 -322 C
ATOM 150 CZ TYR A 32 -11.319 -0.999 7.038 1.00 58.04 C
ANISOU 150 CZ TYR A 32 7825 6885 7344 865 447 -221 C
ATOM 151 OH TYR A 32 -11.311 -2.351 7.285 1.00 57.58 O
ANISOU 151 OH TYR A 32 7838 6906 7132 844 541 -225 O
ATOM 152 N THR A 33 -10.347 6.180 4.766 1.00 47.62 N
ANISOU 152 N THR A 33 6047 5057 6991 891 -200 -47 N
ATOM 153 CA THR A 33 -10.691 7.400 4.016 1.00 47.66 C
ANISOU 153 CA THR A 33 5916 4970 7224 864 -329 45 C
ATOM 154 C THR A 33 -9.989 7.325 2.649 1.00 50.14 C
ANISOU 154 C THR A 33 6225 5319 7506 743 -414 212 C
ATOM 155 O THR A 33 -10.578 7.700 1.633 1.00 50.15 O
ANISOU 155 O THR A 33 6131 5316 7609 665 -487 348 O
ATOM 156 CB THR A 33 -10.317 8.669 4.813 1.00 54.21 C
ANISOU 156 CB THR A 33 6697 5671 8228 968 -398 -63 C
ATOM 157 OG1 THR A 33 -11.008 8.661 6.059 1.00 53.19 O
ANISOU 157 OG1 THR A 33 6569 5527 8115 1075 -309 -219 O
ATOM 158 CG2 THR A 33 -10.660 9.960 4.070 1.00 53.35 C
ANISOU 158 CG2 THR A 33 6439 5455 8377 940 -544 39 C
ATOM 159 N VAL A 34 -8.740 6.804 2.640 1.00 45.08 N
ANISOU 159 N VAL A 34 5689 4720 6720 725 -398 201 N
ATOM 160 CA VAL A 34 -7.900 6.592 1.456 1.00 43.99 C
ANISOU 160 CA VAL A 34 5567 4633 6516 617 -452 339 C
ATOM 161 C VAL A 34 -8.579 5.553 0.538 1.00 46.49 C
ANISOU 161 C VAL A 34 5898 5066 6700 514 -398 432 C
ATOM 162 O VAL A 34 -8.694 5.799 -0.664 1.00 46.12 O
ANISOU 162 O VAL A 34 5790 5047 6688 414 -472 578 O
ATOM 163 CB VAL A 34 -6.453 6.172 1.858 1.00 47.11 C
ANISOU 163 CB VAL A 34 6073 5041 6787 638 -427 282 C
ATOM 164 CG1 VAL A 34 -5.603 5.823 0.637 1.00 46.35 C
ANISOU 164 CG1 VAL A 34 5998 5013 6601 525 -458 416 C
ATOM 165 CG2 VAL A 34 -5.773 7.260 2.686 1.00 47.47 C
ANISOU 165 CG2 VAL A 34 6095 4964 6978 730 -503 202 C
ATOM 166 N LEU A 35 -9.055 4.422 1.115 1.00 42.09 N
ANISOU 166 N LEU A 35 5418 4576 5999 537 -274 349 N
ATOM 167 CA LEU A 35 -9.742 3.346 0.388 1.00 41.41 C
ANISOU 167 CA LEU A 35 5351 4593 5789 450 -216 414 C
ATOM 168 C LEU A 35 -11.061 3.815 -0.213 1.00 46.07 C
ANISOU 168 C LEU A 35 5825 5166 6512 411 -266 501 C
ATOM 169 O LEU A 35 -11.389 3.418 -1.330 1.00 45.53 O
ANISOU 169 O LEU A 35 5738 5167 6396 304 -293 617 O
ATOM 170 CB LEU A 35 -10.010 2.133 1.292 1.00 40.80 C
ANISOU 170 CB LEU A 35 5369 4573 5559 495 -78 304 C
ATOM 171 CG LEU A 35 -8.822 1.273 1.720 1.00 44.36 C
ANISOU 171 CG LEU A 35 5943 5066 5845 505 -14 240 C
ATOM 172 CD1 LEU A 35 -9.264 0.248 2.721 1.00 44.02 C
ANISOU 172 CD1 LEU A 35 5970 5066 5691 560 110 137 C
ATOM 173 CD2 LEU A 35 -8.187 0.561 0.536 1.00 46.05 C
ANISOU 173 CD2 LEU A 35 6195 5360 5942 391 -22 334 C
ATOM 174 N PHE A 36 -11.819 4.644 0.532 1.00 43.68 N
ANISOU 174 N PHE A 36 5444 4774 6378 498 -280 442 N
ATOM 175 CA PHE A 36 -13.104 5.199 0.101 1.00 44.39 C
ANISOU 175 CA PHE A 36 5410 4827 6630 474 -330 518 C
ATOM 176 C PHE A 36 -12.900 6.185 -1.058 1.00 49.72 C
ANISOU 176 C PHE A 36 5985 5465 7441 391 -479 673 C
ATOM 177 O PHE A 36 -13.701 6.189 -1.992 1.00 49.57 O
ANISOU 177 O PHE A 36 5893 5472 7469 305 -530 798 O
ATOM 178 CB PHE A 36 -13.824 5.872 1.285 1.00 46.68 C
ANISOU 178 CB PHE A 36 5640 5023 7072 598 -299 398 C
ATOM 179 CG PHE A 36 -15.202 6.420 0.997 1.00 48.93 C
ANISOU 179 CG PHE A 36 5792 5259 7542 589 -337 460 C
ATOM 180 CD1 PHE A 36 -16.280 5.567 0.798 1.00 51.78 C
ANISOU 180 CD1 PHE A 36 6146 5684 7842 549 -269 495 C
ATOM 181 CD2 PHE A 36 -15.430 7.790 0.970 1.00 51.80 C
ANISOU 181 CD2 PHE A 36 6027 5501 8153 624 -440 478 C
ATOM 182 CE1 PHE A 36 -17.556 6.076 0.534 1.00 53.54 C
ANISOU 182 CE1 PHE A 36 6241 5855 8248 540 -305 556 C
ATOM 183 CE2 PHE A 36 -16.707 8.298 0.715 1.00 55.46 C
ANISOU 183 CE2 PHE A 36 6358 5909 8804 616 -475 536 C
ATOM 184 CZ PHE A 36 -17.763 7.438 0.508 1.00 53.49 C
ANISOU 184 CZ PHE A 36 6107 5727 8489 575 -405 576 C
ATOM 185 N PHE A 37 -11.807 6.981 -1.011 1.00 47.31 N
ANISOU 185 N PHE A 37 5678 5103 7195 412 -553 674 N
ATOM 186 CA PHE A 37 -11.448 7.962 -2.038 1.00 48.30 C
ANISOU 186 CA PHE A 37 5707 5192 7452 337 -697 828 C
ATOM 187 C PHE A 37 -11.005 7.260 -3.330 1.00 52.72 C
ANISOU 187 C PHE A 37 6313 5878 7841 200 -710 963 C
ATOM 188 O PHE A 37 -11.620 7.484 -4.371 1.00 52.90 O
ANISOU 188 O PHE A 37 6257 5933 7910 103 -781 1108 O
ATOM 189 CB PHE A 37 -10.351 8.919 -1.522 1.00 50.38 C
ANISOU 189 CB PHE A 37 5959 5356 7827 406 -765 781 C
ATOM 190 CG PHE A 37 -9.940 10.018 -2.478 1.00 52.80 C
ANISOU 190 CG PHE A 37 6149 5607 8305 341 -920 941 C
ATOM 191 CD1 PHE A 37 -10.771 11.108 -2.712 1.00 57.07 C
ANISOU 191 CD1 PHE A 37 6538 6055 9092 339 -1021 1014 C
ATOM 192 CD2 PHE A 37 -8.706 9.980 -3.117 1.00 54.62 C
ANISOU 192 CD2 PHE A 37 6414 5874 8465 283 -967 1023 C
ATOM 193 CE1 PHE A 37 -10.387 12.126 -3.590 1.00 58.75 C
ANISOU 193 CE1 PHE A 37 6634 6214 9472 275 -1171 1175 C
ATOM 194 CE2 PHE A 37 -8.320 11.001 -3.992 1.00 58.16 C
ANISOU 194 CE2 PHE A 37 6748 6276 9074 221 -1112 1183 C
ATOM 195 CZ PHE A 37 -9.167 12.062 -4.229 1.00 57.37 C
ANISOU 195 CZ PHE A 37 6497 6087 9215 216 -1216 1262 C
ATOM 196 N VAL A 38 -9.967 6.397 -3.249 1.00 49.07 N
ANISOU 196 N VAL A 38 5975 5488 7181 192 -639 913 N
ATOM 197 CA VAL A 38 -9.401 5.632 -4.370 1.00 48.74 C
ANISOU 197 CA VAL A 38 5991 5571 6958 73 -631 1010 C
ATOM 198 C VAL A 38 -10.488 4.736 -5.003 1.00 52.93 C
ANISOU 198 C VAL A 38 6527 6196 7386 -5 -586 1053 C
ATOM 199 O VAL A 38 -10.678 4.785 -6.221 1.00 52.99 O
ANISOU 199 O VAL A 38 6499 6277 7358 -122 -648 1192 O
ATOM 200 CB VAL A 38 -8.153 4.815 -3.917 1.00 51.81 C
ANISOU 200 CB VAL A 38 6511 6001 7174 102 -544 915 C
ATOM 201 CG1 VAL A 38 -7.756 3.752 -4.942 1.00 51.16 C
ANISOU 201 CG1 VAL A 38 6498 6055 6887 -11 -502 979 C
ATOM 202 CG2 VAL A 38 -6.972 5.737 -3.620 1.00 51.78 C
ANISOU 202 CG2 VAL A 38 6491 5914 7271 150 -614 914 C
ATOM 203 N GLY A 39 -11.193 3.973 -4.162 1.00 49.18 N
ANISOU 203 N GLY A 39 6094 5718 6874 61 -486 937 N
ATOM 204 CA GLY A 39 -12.256 3.052 -4.553 1.00 48.98 C
ANISOU 204 CA GLY A 39 6077 5766 6767 5 -435 958 C
ATOM 205 C GLY A 39 -13.382 3.654 -5.369 1.00 54.09 C
ANISOU 205 C GLY A 39 6602 6402 7546 -67 -533 1093 C
ATOM 206 O GLY A 39 -13.840 3.026 -6.325 1.00 53.98 O
ANISOU 206 O GLY A 39 6594 6479 7436 -173 -544 1177 O
ATOM 207 N LEU A 40 -13.835 4.874 -5.006 1.00 51.27 N
ANISOU 207 N LEU A 40 6132 5931 7419 -12 -608 1113 N
ATOM 208 CA LEU A 40 -14.910 5.570 -5.722 1.00 52.01 C
ANISOU 208 CA LEU A 40 6092 5993 7677 -74 -712 1249 C
ATOM 209 C LEU A 40 -14.462 6.011 -7.113 1.00 56.71 C
ANISOU 209 C LEU A 40 6640 6642 8265 -204 -836 1428 C
ATOM 210 O LEU A 40 -15.276 6.013 -8.036 1.00 56.77 O
ANISOU 210 O LEU A 40 6579 6689 8301 -303 -906 1559 O
ATOM 211 CB LEU A 40 -15.421 6.782 -4.930 1.00 52.76 C
ANISOU 211 CB LEU A 40 6072 5940 8035 26 -758 1211 C
ATOM 212 CG LEU A 40 -16.525 6.523 -3.901 1.00 57.22 C
ANISOU 212 CG LEU A 40 6624 6457 8662 124 -662 1090 C
ATOM 213 CD1 LEU A 40 -16.650 7.689 -2.959 1.00 58.01 C
ANISOU 213 CD1 LEU A 40 6636 6414 8992 241 -690 1010 C
ATOM 214 CD2 LEU A 40 -17.872 6.262 -4.569 1.00 59.74 C
ANISOU 214 CD2 LEU A 40 6871 6802 9025 50 -680 1188 C
ATOM 215 N ILE A 41 -13.173 6.377 -7.260 1.00 53.67 N
ANISOU 215 N ILE A 41 6288 6262 7841 -206 -865 1440 N
ATOM 216 CA ILE A 41 -12.573 6.790 -8.533 1.00 54.23 C
ANISOU 216 CA ILE A 41 6320 6397 7888 -326 -972 1610 C
ATOM 217 C ILE A 41 -12.431 5.549 -9.426 1.00 58.49 C
ANISOU 217 C ILE A 41 6957 7099 8167 -435 -916 1641 C
ATOM 218 O ILE A 41 -12.835 5.584 -10.589 1.00 58.71 O
ANISOU 218 O ILE A 41 6936 7206 8166 -558 -994 1789 O
ATOM 219 CB ILE A 41 -11.213 7.526 -8.309 1.00 57.16 C
ANISOU 219 CB ILE A 41 6693 6716 8311 -284 -1013 1609 C
ATOM 220 CG1 ILE A 41 -11.410 8.831 -7.498 1.00 58.19 C
ANISOU 220 CG1 ILE A 41 6718 6675 8716 -176 -1080 1571 C
ATOM 221 CG2 ILE A 41 -10.491 7.808 -9.641 1.00 58.30 C
ANISOU 221 CG2 ILE A 41 6798 6944 8411 -414 -1112 1795 C
ATOM 222 CD1 ILE A 41 -10.181 9.299 -6.707 1.00 65.15 C
ANISOU 222 CD1 ILE A 41 7639 7482 9634 -84 -1074 1479 C
ATOM 223 N THR A 42 -11.890 4.452 -8.858 1.00 54.88 N
ANISOU 223 N THR A 42 6633 6691 7527 -391 -784 1498 N
ATOM 224 CA THR A 42 -11.660 3.170 -9.527 1.00 54.79 C
ANISOU 224 CA THR A 42 6723 6822 7275 -477 -715 1490 C
ATOM 225 C THR A 42 -12.998 2.563 -9.995 1.00 60.11 C
ANISOU 225 C THR A 42 7370 7543 7924 -544 -719 1530 C
ATOM 226 O THR A 42 -13.098 2.176 -11.159 1.00 60.03 O
ANISOU 226 O THR A 42 7359 7643 7806 -670 -765 1635 O
ATOM 227 CB THR A 42 -10.869 2.227 -8.599 1.00 63.77 C
ANISOU 227 CB THR A 42 7990 7967 8272 -397 -577 1319 C
ATOM 228 OG1 THR A 42 -9.710 2.913 -8.119 1.00 63.90 O
ANISOU 228 OG1 THR A 42 8021 7933 8325 -343 -590 1297 O
ATOM 229 CG2 THR A 42 -10.434 0.945 -9.293 1.00 62.84 C
ANISOU 229 CG2 THR A 42 7971 7982 7921 -479 -502 1296 C
ATOM 230 N ASN A 43 -14.021 2.515 -9.110 1.00 57.58 N
ANISOU 230 N ASN A 43 7025 7144 7707 -462 -676 1453 N
ATOM 231 CA ASN A 43 -15.349 1.982 -9.438 1.00 58.11 C
ANISOU 231 CA ASN A 43 7058 7238 7782 -511 -679 1488 C
ATOM 232 C ASN A 43 -16.127 2.926 -10.356 1.00 63.98 C
ANISOU 232 C ASN A 43 7666 7962 8680 -595 -825 1664 C
ATOM 233 O ASN A 43 -16.951 2.459 -11.145 1.00 63.98 O
ANISOU 233 O ASN A 43 7646 8025 8640 -689 -860 1741 O
ATOM 234 CB ASN A 43 -16.155 1.687 -8.179 1.00 58.59 C
ANISOU 234 CB ASN A 43 7122 7218 7921 -393 -586 1362 C
ATOM 235 CG ASN A 43 -16.364 0.214 -7.939 1.00 81.51 C
ANISOU 235 CG ASN A 43 10124 10195 10652 -399 -472 1271 C
ATOM 236 OD1 ASN A 43 -17.489 -0.288 -7.999 1.00 76.49 O
ANISOU 236 OD1 ASN A 43 9456 9564 10042 -421 -462 1289 O
ATOM 237 ND2 ASN A 43 -15.286 -0.515 -7.666 1.00 72.26 N
ANISOU 237 ND2 ASN A 43 9067 9074 9314 -381 -387 1178 N
ATOM 238 N GLY A 44 -15.853 4.229 -10.248 1.00 61.79 N
ANISOU 238 N GLY A 44 7298 7597 8584 -564 -915 1728 N
ATOM 239 CA GLY A 44 -16.458 5.261 -11.085 1.00 63.17 C
ANISOU 239 CA GLY A 44 7331 7741 8930 -643 -1066 1908 C
ATOM 240 C GLY A 44 -16.049 5.091 -12.534 1.00 68.30 C
ANISOU 240 C GLY A 44 7991 8529 9432 -799 -1145 2060 C
ATOM 241 O GLY A 44 -16.883 5.209 -13.435 1.00 68.78 O
ANISOU 241 O GLY A 44 7974 8627 9533 -905 -1243 2204 O
ATOM 242 N LEU A 45 -14.759 4.765 -12.752 1.00 64.93 N
ANISOU 242 N LEU A 45 7662 8185 8824 -816 -1097 2024 N
ATOM 243 CA LEU A 45 -14.179 4.497 -14.067 1.00 65.43 C
ANISOU 243 CA LEU A 45 7754 8399 8706 -956 -1142 2140 C
ATOM 244 C LEU A 45 -14.608 3.121 -14.570 1.00 70.01 C
ANISOU 244 C LEU A 45 8428 9104 9070 -1029 -1074 2091 C
ATOM 245 O LEU A 45 -14.842 2.958 -15.764 1.00 70.35 O
ANISOU 245 O LEU A 45 8451 9257 9023 -1163 -1148 2215 O
ATOM 246 CB LEU A 45 -12.643 4.580 -14.012 1.00 64.89 C
ANISOU 246 CB LEU A 45 7752 8364 8538 -935 -1101 2105 C
ATOM 247 CG LEU A 45 -12.031 5.976 -13.935 1.00 70.11 C
ANISOU 247 CG LEU A 45 8317 8931 9391 -900 -1197 2194 C
ATOM 248 CD1 LEU A 45 -10.689 5.940 -13.233 1.00 69.36 C
ANISOU 248 CD1 LEU A 45 8303 8810 9241 -815 -1117 2082 C
ATOM 249 CD2 LEU A 45 -11.885 6.595 -15.319 1.00 73.92 C
ANISOU 249 CD2 LEU A 45 8712 9499 9874 -1041 -1332 2416 C
ATOM 250 N ALA A 46 -14.713 2.135 -13.658 1.00 66.49 N
ANISOU 250 N ALA A 46 8079 8638 8545 -943 -938 1913 N
ATOM 251 CA ALA A 46 -15.097 0.758 -13.971 1.00 66.54 C
ANISOU 251 CA ALA A 46 8175 8742 8365 -993 -863 1843 C
ATOM 252 C ALA A 46 -16.544 0.644 -14.460 1.00 72.76 C
ANISOU 252 C ALA A 46 8895 9535 9217 -1061 -932 1925 C
ATOM 253 O ALA A 46 -16.798 -0.108 -15.400 1.00 72.81 O
ANISOU 253 O ALA A 46 8943 9657 9066 -1169 -942 1951 O
ATOM 254 CB ALA A 46 -14.898 -0.127 -12.754 1.00 66.08 C
ANISOU 254 CB ALA A 46 8211 8635 8262 -873 -716 1651 C
ATOM 255 N MET A 47 -17.484 1.381 -13.829 1.00 70.63 N
ANISOU 255 N MET A 47 8519 9138 9179 -999 -979 1959 N
ATOM 256 CA MET A 47 -18.909 1.345 -14.171 1.00 71.61 C
ANISOU 256 CA MET A 47 8564 9245 9400 -1052 -1045 2041 C
ATOM 257 C MET A 47 -19.207 2.024 -15.515 1.00 77.89 C
ANISOU 257 C MET A 47 9271 10105 10218 -1200 -1206 2248 C
ATOM 258 O MET A 47 -19.989 1.477 -16.291 1.00 77.93 O
ANISOU 258 O MET A 47 9267 10177 10165 -1300 -1255 2313 O
ATOM 259 CB MET A 47 -19.760 1.969 -13.058 1.00 73.99 C
ANISOU 259 CB MET A 47 8775 9388 9951 -932 -1032 2004 C
ATOM 260 CG MET A 47 -19.920 1.062 -11.858 1.00 76.67 C
ANISOU 260 CG MET A 47 9191 9689 10252 -817 -880 1824 C
ATOM 261 SD MET A 47 -21.000 1.744 -10.582 1.00 81.17 S
ANISOU 261 SD MET A 47 9651 10092 11096 -683 -854 1778 S
ATOM 262 CE MET A 47 -22.594 1.266 -11.224 1.00 78.74 C
ANISOU 262 CE MET A 47 9276 9807 10837 -780 -913 1883 C
ATOM 263 N ARG A 48 -18.579 3.187 -15.804 1.00 75.99 N
ANISOU 263 N ARG A 48 8965 9849 10060 -1218 -1293 2356 N
ATOM 264 CA ARG A 48 -18.789 3.918 -17.063 1.00 77.58 C
ANISOU 264 CA ARG A 48 9073 10115 10287 -1361 -1453 2571 C
ATOM 265 C ARG A 48 -18.198 3.164 -18.273 1.00 82.86 C
ANISOU 265 C ARG A 48 9834 10980 10669 -1498 -1457 2611 C
ATOM 266 O ARG A 48 -18.591 3.439 -19.407 1.00 83.66 O
ANISOU 266 O ARG A 48 9880 11169 10740 -1636 -1579 2778 O
ATOM 267 CB ARG A 48 -18.230 5.358 -16.994 1.00 78.27 C
ANISOU 267 CB ARG A 48 9049 10119 10572 -1338 -1550 2684 C
ATOM 268 CG ARG A 48 -16.720 5.470 -16.789 1.00 87.94 C
ANISOU 268 CG ARG A 48 10340 11365 11709 -1290 -1494 2626 C
ATOM 269 CD ARG A 48 -16.216 6.890 -16.964 1.00 98.35 C
ANISOU 269 CD ARG A 48 11533 12619 13217 -1301 -1620 2778 C
ATOM 270 NE ARG A 48 -15.970 7.216 -18.371 1.00108.08 N
ANISOU 270 NE ARG A 48 12734 13995 14338 -1462 -1729 2974 N
ATOM 271 CZ ARG A 48 -14.811 7.029 -18.996 1.00121.88 C
ANISOU 271 CZ ARG A 48 14540 15852 15915 -1507 -1709 3000 C
ATOM 272 NH1 ARG A 48 -13.774 6.511 -18.347 1.00107.79 N
ANISOU 272 NH1 ARG A 48 12850 14043 14064 -1404 -1589 2844 N
ATOM 273 NH2 ARG A 48 -14.680 7.355 -20.274 1.00109.54 N
ANISOU 273 NH2 ARG A 48 12941 14431 14250 -1658 -1807 3186 N
ATOM 274 N ILE A 49 -17.270 2.219 -18.026 1.00 79.30 N
ANISOU 274 N ILE A 49 9521 10599 10013 -1462 -1325 2458 N
ATOM 275 CA ILE A 49 -16.627 1.416 -19.067 1.00 79.79 C
ANISOU 275 CA ILE A 49 9676 10843 9797 -1579 -1306 2463 C
ATOM 276 C ILE A 49 -17.381 0.081 -19.244 1.00 84.76 C
ANISOU 276 C ILE A 49 10379 11533 10292 -1619 -1254 2373 C
ATOM 277 O ILE A 49 -17.638 -0.318 -20.382 1.00 85.23 O
ANISOU 277 O ILE A 49 10450 11725 10209 -1757 -1320 2453 O
ATOM 278 CB ILE A 49 -15.103 1.220 -18.755 1.00 81.96 C
ANISOU 278 CB ILE A 49 10048 11157 9936 -1525 -1197 2356 C
ATOM 279 CG1 ILE A 49 -14.291 2.548 -18.883 1.00 82.61 C
ANISOU 279 CG1 ILE A 49 10053 11178 10159 -1489 -1258 2455 C
ATOM 280 CG2 ILE A 49 -14.450 0.072 -19.550 1.00 82.82 C
ANISOU 280 CG2 ILE A 49 10260 11452 9754 -1633 -1151 2327 C
ATOM 281 CD1 ILE A 49 -14.304 3.318 -20.272 1.00 92.39 C
ANISOU 281 CD1 ILE A 49 11176 12481 11446 -1618 -1422 2697 C
ATOM 282 N PHE A 50 -17.747 -0.588 -18.132 1.00 81.31 N
ANISOU 282 N PHE A 50 9988 11002 9905 -1503 -1143 2213 N
ATOM 283 CA PHE A 50 -18.409 -1.893 -18.170 1.00 81.47 C
ANISOU 283 CA PHE A 50 10076 11061 9816 -1526 -1085 2116 C
ATOM 284 C PHE A 50 -19.918 -1.850 -18.445 1.00 86.79 C
ANISOU 284 C PHE A 50 10662 11698 10615 -1579 -1182 2213 C
ATOM 285 O PHE A 50 -20.425 -2.790 -19.056 1.00 86.77 O
ANISOU 285 O PHE A 50 10704 11779 10487 -1664 -1191 2198 O
ATOM 286 CB PHE A 50 -18.150 -2.683 -16.884 1.00 82.12 C
ANISOU 286 CB PHE A 50 10237 11065 9901 -1385 -929 1921 C
ATOM 287 CG PHE A 50 -17.395 -3.957 -17.162 1.00 83.42 C
ANISOU 287 CG PHE A 50 10532 11336 9828 -1412 -828 1790 C
ATOM 288 CD1 PHE A 50 -18.070 -5.155 -17.354 1.00 86.87 C
ANISOU 288 CD1 PHE A 50 11018 11820 10169 -1458 -798 1723 C
ATOM 289 CD2 PHE A 50 -16.012 -3.950 -17.295 1.00 85.37 C
ANISOU 289 CD2 PHE A 50 10845 11632 9959 -1396 -767 1737 C
ATOM 290 CE1 PHE A 50 -17.373 -6.329 -17.643 1.00 87.54 C
ANISOU 290 CE1 PHE A 50 11215 11995 10050 -1484 -708 1597 C
ATOM 291 CE2 PHE A 50 -15.317 -5.123 -17.595 1.00 87.97 C
ANISOU 291 CE2 PHE A 50 11286 12054 10083 -1422 -673 1615 C
ATOM 292 CZ PHE A 50 -16.003 -6.303 -17.773 1.00 86.20 C
ANISOU 292 CZ PHE A 50 11109 11874 9770 -1466 -644 1542 C
ATOM 293 N PHE A 51 -20.639 -0.806 -18.001 1.00 84.13 N
ANISOU 293 N PHE A 51 10203 11235 10529 -1531 -1253 2305 N
ATOM 294 CA PHE A 51 -22.084 -0.742 -18.242 1.00 85.01 C
ANISOU 294 CA PHE A 51 10222 11302 10774 -1581 -1343 2401 C
ATOM 295 C PHE A 51 -22.405 -0.152 -19.631 1.00 90.62 C
ANISOU 295 C PHE A 51 10856 12100 11474 -1743 -1517 2611 C
ATOM 296 O PHE A 51 -23.546 -0.269 -20.089 1.00 91.21 O
ANISOU 296 O PHE A 51 10861 12162 11632 -1813 -1609 2708 O
ATOM 297 CB PHE A 51 -22.811 0.018 -17.121 1.00 86.68 C
ANISOU 297 CB PHE A 51 10333 11335 11268 -1453 -1329 2390 C
ATOM 298 CG PHE A 51 -22.932 -0.794 -15.851 1.00 87.12 C
ANISOU 298 CG PHE A 51 10458 11324 11319 -1319 -1170 2201 C
ATOM 299 CD1 PHE A 51 -24.024 -1.630 -15.643 1.00 90.27 C
ANISOU 299 CD1 PHE A 51 10866 11716 11717 -1326 -1137 2161 C
ATOM 300 CD2 PHE A 51 -21.943 -0.744 -14.875 1.00 88.16 C
ANISOU 300 CD2 PHE A 51 10646 11407 11444 -1192 -1056 2069 C
ATOM 301 CE1 PHE A 51 -24.128 -2.393 -14.476 1.00 90.15 C
ANISOU 301 CE1 PHE A 51 10910 11648 11696 -1208 -991 2000 C
ATOM 302 CE2 PHE A 51 -22.049 -1.507 -13.710 1.00 89.99 C
ANISOU 302 CE2 PHE A 51 10942 11590 11663 -1076 -913 1906 C
ATOM 303 CZ PHE A 51 -23.140 -2.327 -13.519 1.00 88.16 C
ANISOU 303 CZ PHE A 51 10713 11354 11429 -1086 -880 1876 C
ATOM 304 N GLN A 52 -21.395 0.427 -20.315 1.00 87.43 N
ANISOU 304 N GLN A 52 10467 11794 10958 -1808 -1560 2685 N
ATOM 305 CA GLN A 52 -21.543 0.977 -21.665 1.00 88.61 C
ANISOU 305 CA GLN A 52 10553 12053 11062 -1971 -1719 2890 C
ATOM 306 C GLN A 52 -21.210 -0.090 -22.732 1.00 92.25 C
ANISOU 306 C GLN A 52 11130 12714 11208 -2098 -1706 2859 C
ATOM 307 O GLN A 52 -21.400 0.159 -23.926 1.00 93.17 O
ANISOU 307 O GLN A 52 11214 12954 11233 -2247 -1830 3016 O
ATOM 308 CB GLN A 52 -20.689 2.242 -21.851 1.00 90.41 C
ANISOU 308 CB GLN A 52 10702 12262 11386 -1971 -1789 3017 C
ATOM 309 CG GLN A 52 -21.378 3.499 -21.326 1.00107.82 C
ANISOU 309 CG GLN A 52 12753 14286 13928 -1901 -1870 3112 C
ATOM 310 CD GLN A 52 -20.745 4.770 -21.834 1.00130.03 C
ANISOU 310 CD GLN A 52 15454 17097 16855 -1956 -2000 3305 C
ATOM 311 OE1 GLN A 52 -20.808 5.096 -23.025 1.00127.56 O
ANISOU 311 OE1 GLN A 52 15100 16906 16461 -2109 -2127 3486 O
ATOM 312 NE2 GLN A 52 -20.162 5.544 -20.931 1.00121.99 N
ANISOU 312 NE2 GLN A 52 14374 15936 16042 -1835 -1982 3279 N
ATOM 313 N ILE A 53 -20.744 -1.284 -22.294 1.00 87.21 N
ANISOU 313 N ILE A 53 10621 12105 10408 -2040 -1558 2656 N
ATOM 314 CA ILE A 53 -20.433 -2.426 -23.165 1.00 86.96 C
ANISOU 314 CA ILE A 53 10706 12243 10091 -2139 -1523 2581 C
ATOM 315 C ILE A 53 -21.443 -3.561 -22.874 1.00 89.96 C
ANISOU 315 C ILE A 53 11120 12589 10473 -2133 -1494 2483 C
ATOM 316 O ILE A 53 -21.938 -3.675 -21.749 1.00 88.97 O
ANISOU 316 O ILE A 53 10948 12312 10546 -2026 -1459 2442 O
ATOM 317 CB ILE A 53 -18.947 -2.899 -23.086 1.00 89.13 C
ANISOU 317 CB ILE A 53 11097 12592 10175 -2095 -1386 2437 C
ATOM 318 CG1 ILE A 53 -18.563 -3.478 -21.704 1.00 87.80 C
ANISOU 318 CG1 ILE A 53 10984 12292 10082 -1925 -1229 2246 C
ATOM 319 CG2 ILE A 53 -17.984 -1.784 -23.523 1.00 90.40 C
ANISOU 319 CG2 ILE A 53 11220 12812 10316 -2129 -1432 2560 C
ATOM 320 CD1 ILE A 53 -17.595 -4.659 -21.754 1.00 93.32 C
ANISOU 320 CD1 ILE A 53 11821 13070 10568 -1907 -1090 2059 C
ATOM 321 N ARG A 54 -21.758 -4.376 -23.897 1.00 86.47 N
ANISOU 321 N ARG A 54 10752 12287 9817 -2249 -1512 2448 N
ATOM 322 CA ARG A 54 -22.747 -5.459 -23.804 1.00 85.99 C
ANISOU 322 CA ARG A 54 10716 12200 9757 -2261 -1505 2370 C
ATOM 323 C ARG A 54 -22.174 -6.743 -23.165 1.00 87.91 C
ANISOU 323 C ARG A 54 11080 12440 9883 -2180 -1341 2141 C
ATOM 324 O ARG A 54 -20.953 -6.906 -23.078 1.00 86.97 O
ANISOU 324 O ARG A 54 11043 12387 9617 -2156 -1246 2043 O
ATOM 325 CB ARG A 54 -23.342 -5.778 -25.195 1.00 87.73 C
ANISOU 325 CB ARG A 54 10935 12562 9836 -2442 -1643 2471 C
ATOM 326 CG ARG A 54 -23.863 -4.567 -25.987 1.00 98.71 C
ANISOU 326 CG ARG A 54 12203 13972 11329 -2545 -1822 2717 C
ATOM 327 CD ARG A 54 -25.075 -3.887 -25.359 1.00107.28 C
ANISOU 327 CD ARG A 54 13157 14876 12727 -2480 -1886 2818 C
ATOM 328 NE ARG A 54 -25.401 -2.621 -26.020 1.00114.90 N
ANISOU 328 NE ARG A 54 13998 15851 13808 -2578 -2059 3057 N
ATOM 329 CZ ARG A 54 -24.896 -1.438 -25.679 1.00126.34 C
ANISOU 329 CZ ARG A 54 15368 17253 15381 -2542 -2089 3164 C
ATOM 330 NH1 ARG A 54 -24.025 -1.341 -24.681 1.00111.33 N
ANISOU 330 NH1 ARG A 54 13507 15296 13499 -2411 -1958 3050 N
ATOM 331 NH2 ARG A 54 -25.254 -0.343 -26.336 1.00113.01 N
ANISOU 331 NH2 ARG A 54 13558 15572 13808 -2640 -2256 3390 N
ATOM 332 N SER A 55 -23.078 -7.645 -22.715 1.00 83.35 N
ANISOU 332 N SER A 55 10503 11780 9386 -2140 -1312 2065 N
ATOM 333 CA SER A 55 -22.749 -8.928 -22.087 1.00 81.78 C
ANISOU 333 CA SER A 55 10399 11560 9113 -2068 -1173 1865 C
ATOM 334 C SER A 55 -22.760 -10.057 -23.135 1.00 85.35 C
ANISOU 334 C SER A 55 10932 12151 9344 -2192 -1198 1795 C
ATOM 335 O SER A 55 -23.702 -10.853 -23.196 1.00 85.25 O
ANISOU 335 O SER A 55 10917 12116 9360 -2224 -1230 1768 O
ATOM 336 CB SER A 55 -23.720 -9.231 -20.947 1.00 84.79 C
ANISOU 336 CB SER A 55 10728 11783 9703 -1963 -1133 1834 C
ATOM 337 OG SER A 55 -23.663 -8.248 -19.927 1.00 92.82 O
ANISOU 337 OG SER A 55 11686 12677 10905 -1834 -1084 1857 O
ATOM 338 N LYS A 56 -21.704 -10.106 -23.966 1.00 81.49 N
ANISOU 338 N LYS A 56 10513 11808 8640 -2263 -1184 1766 N
ATOM 339 CA LYS A 56 -21.544 -11.097 -25.033 1.00 81.86 C
ANISOU 339 CA LYS A 56 10642 12007 8453 -2383 -1200 1685 C
ATOM 340 C LYS A 56 -20.796 -12.352 -24.553 1.00 84.02 C
ANISOU 340 C LYS A 56 11021 12281 8621 -2315 -1043 1461 C
ATOM 341 O LYS A 56 -20.899 -13.398 -25.198 1.00 84.39 O
ANISOU 341 O LYS A 56 11136 12426 8501 -2395 -1040 1357 O
ATOM 342 CB LYS A 56 -20.813 -10.476 -26.232 1.00 85.50 C
ANISOU 342 CB LYS A 56 11112 12642 8732 -2509 -1276 1789 C
ATOM 343 N SER A 57 -20.048 -12.248 -23.434 1.00 78.31 N
ANISOU 343 N SER A 57 10307 11447 8000 -2169 -918 1386 N
ATOM 344 CA SER A 57 -19.276 -13.355 -22.860 1.00 76.76 C
ANISOU 344 CA SER A 57 10198 11231 7737 -2093 -768 1189 C
ATOM 345 C SER A 57 -19.603 -13.560 -21.373 1.00 78.31 C
ANISOU 345 C SER A 57 10370 11254 8130 -1941 -680 1134 C
ATOM 346 O SER A 57 -20.228 -12.694 -20.754 1.00 77.69 O
ANISOU 346 O SER A 57 10212 11078 8229 -1881 -717 1243 O
ATOM 347 CB SER A 57 -17.779 -13.112 -23.042 1.00 80.00 C
ANISOU 347 CB SER A 57 10661 11721 8014 -2082 -691 1147 C
ATOM 348 OG SER A 57 -17.317 -12.029 -22.252 1.00 87.67 O
ANISOU 348 OG SER A 57 11582 12614 9116 -1994 -679 1237 O
ATOM 349 N ASN A 58 -19.173 -14.709 -20.807 1.00 73.21 N
ANISOU 349 N ASN A 58 9789 10574 7453 -1882 -564 965 N
ATOM 350 CA ASN A 58 -19.383 -15.065 -19.401 1.00 71.26 C
ANISOU 350 CA ASN A 58 9530 10181 7364 -1744 -469 901 C
ATOM 351 C ASN A 58 -18.537 -14.180 -18.480 1.00 72.66 C
ANISOU 351 C ASN A 58 9699 10296 7614 -1631 -399 920 C
ATOM 352 O ASN A 58 -19.023 -13.769 -17.426 1.00 71.69 O
ANISOU 352 O ASN A 58 9522 10059 7660 -1534 -382 960 O
ATOM 353 CB ASN A 58 -19.060 -16.548 -19.152 1.00 71.82 C
ANISOU 353 CB ASN A 58 9672 10245 7372 -1722 -370 723 C
ATOM 354 CG ASN A 58 -19.771 -17.542 -20.050 1.00 96.95 C
ANISOU 354 CG ASN A 58 12873 13488 10476 -1831 -432 673 C
ATOM 355 OD1 ASN A 58 -19.189 -18.548 -20.467 1.00 92.38 O
ANISOU 355 OD1 ASN A 58 12361 12956 9785 -1858 -375 530 O
ATOM 356 ND2 ASN A 58 -21.042 -17.308 -20.358 1.00 89.70 N
ANISOU 356 ND2 ASN A 58 11894 12564 9626 -1894 -550 784 N
ATOM 357 N PHE A 59 -17.282 -13.878 -18.891 1.00 67.99 N
ANISOU 357 N PHE A 59 9157 9782 6894 -1647 -362 890 N
ATOM 358 CA PHE A 59 -16.312 -13.048 -18.164 1.00 66.34 C
ANISOU 358 CA PHE A 59 8947 9527 6732 -1554 -304 903 C
ATOM 359 C PHE A 59 -16.848 -11.631 -17.914 1.00 68.69 C
ANISOU 359 C PHE A 59 9154 9771 7174 -1532 -392 1063 C
ATOM 360 O PHE A 59 -16.595 -11.076 -16.844 1.00 67.39 O
ANISOU 360 O PHE A 59 8967 9506 7133 -1418 -346 1062 O
ATOM 361 CB PHE A 59 -14.975 -12.992 -18.930 1.00 68.41 C
ANISOU 361 CB PHE A 59 9269 9904 6820 -1606 -271 865 C
ATOM 362 CG PHE A 59 -13.952 -11.985 -18.447 1.00 69.43 C
ANISOU 362 CG PHE A 59 9389 10006 6988 -1539 -242 910 C
ATOM 363 CD1 PHE A 59 -13.228 -12.207 -17.281 1.00 71.39 C
ANISOU 363 CD1 PHE A 59 9665 10156 7305 -1413 -135 820 C
ATOM 364 CD2 PHE A 59 -13.681 -10.838 -19.183 1.00 72.34 C
ANISOU 364 CD2 PHE A 59 9717 10448 7320 -1606 -327 1045 C
ATOM 365 CE1 PHE A 59 -12.276 -11.280 -16.843 1.00 71.83 C
ANISOU 365 CE1 PHE A 59 9711 10181 7400 -1353 -118 859 C
ATOM 366 CE2 PHE A 59 -12.727 -9.914 -18.746 1.00 74.64 C
ANISOU 366 CE2 PHE A 59 9994 10707 7660 -1544 -307 1088 C
ATOM 367 CZ PHE A 59 -12.029 -10.143 -17.581 1.00 71.53 C
ANISOU 367 CZ PHE A 59 9630 10209 7337 -1417 -203 991 C
ATOM 368 N ILE A 60 -17.580 -11.057 -18.893 1.00 65.16 N
ANISOU 368 N ILE A 60 8653 9388 6717 -1641 -522 1196 N
ATOM 369 CA ILE A 60 -18.172 -9.722 -18.787 1.00 64.74 C
ANISOU 369 CA ILE A 60 8500 9281 6818 -1634 -621 1358 C
ATOM 370 C ILE A 60 -19.293 -9.751 -17.726 1.00 67.00 C
ANISOU 370 C ILE A 60 8726 9427 7305 -1543 -611 1361 C
ATOM 371 O ILE A 60 -19.329 -8.860 -16.878 1.00 66.22 O
ANISOU 371 O ILE A 60 8571 9229 7362 -1450 -604 1403 O
ATOM 372 CB ILE A 60 -18.645 -9.189 -20.175 1.00 69.26 C
ANISOU 372 CB ILE A 60 9029 9967 7321 -1786 -768 1508 C
ATOM 373 CG1 ILE A 60 -17.424 -8.817 -21.053 1.00 70.04 C
ANISOU 373 CG1 ILE A 60 9160 10187 7263 -1847 -773 1541 C
ATOM 374 CG2 ILE A 60 -19.606 -7.988 -20.043 1.00 70.50 C
ANISOU 374 CG2 ILE A 60 9065 10043 7680 -1787 -885 1677 C
ATOM 375 CD1 ILE A 60 -17.692 -8.682 -22.567 1.00 79.38 C
ANISOU 375 CD1 ILE A 60 10330 11531 8300 -2016 -896 1661 C
ATOM 376 N ILE A 61 -20.156 -10.795 -17.742 1.00 62.66 N
ANISOU 376 N ILE A 61 8188 8867 6752 -1565 -603 1307 N
ATOM 377 CA ILE A 61 -21.267 -10.979 -16.793 1.00 61.60 C
ANISOU 377 CA ILE A 61 7996 8611 6797 -1487 -585 1309 C
ATOM 378 C ILE A 61 -20.727 -11.072 -15.348 1.00 63.15 C
ANISOU 378 C ILE A 61 8215 8709 7069 -1331 -450 1207 C
ATOM 379 O ILE A 61 -21.240 -10.375 -14.470 1.00 62.45 O
ANISOU 379 O ILE A 61 8058 8520 7151 -1243 -444 1250 O
ATOM 380 CB ILE A 61 -22.146 -12.214 -17.167 1.00 65.05 C
ANISOU 380 CB ILE A 61 8449 9068 7200 -1550 -601 1265 C
ATOM 381 CG1 ILE A 61 -22.796 -12.032 -18.561 1.00 66.78 C
ANISOU 381 CG1 ILE A 61 8634 9376 7362 -1703 -752 1381 C
ATOM 382 CG2 ILE A 61 -23.215 -12.501 -16.091 1.00 65.24 C
ANISOU 382 CG2 ILE A 61 8416 8967 7407 -1456 -558 1258 C
ATOM 383 CD1 ILE A 61 -23.294 -13.315 -19.233 1.00 73.98 C
ANISOU 383 CD1 ILE A 61 9591 10350 8168 -1795 -777 1314 C
ATOM 384 N PHE A 62 -19.688 -11.905 -15.117 1.00 58.26 N
ANISOU 384 N PHE A 62 7689 8120 6326 -1300 -346 1073 N
ATOM 385 CA PHE A 62 -19.079 -12.094 -13.797 1.00 56.64 C
ANISOU 385 CA PHE A 62 7516 7835 6171 -1165 -222 976 C
ATOM 386 C PHE A 62 -18.420 -10.813 -13.280 1.00 60.21 C
ANISOU 386 C PHE A 62 7941 8244 6694 -1092 -222 1019 C
ATOM 387 O PHE A 62 -18.505 -10.532 -12.084 1.00 59.30 O
ANISOU 387 O PHE A 62 7800 8032 6698 -976 -166 996 O
ATOM 388 CB PHE A 62 -18.051 -13.239 -13.810 1.00 57.70 C
ANISOU 388 CB PHE A 62 7749 8015 6159 -1164 -126 836 C
ATOM 389 CG PHE A 62 -18.559 -14.615 -14.183 1.00 59.38 C
ANISOU 389 CG PHE A 62 7992 8258 6314 -1223 -115 766 C
ATOM 390 CD1 PHE A 62 -19.809 -15.055 -13.759 1.00 62.63 C
ANISOU 390 CD1 PHE A 62 8350 8606 6838 -1207 -128 789 C
ATOM 391 CD2 PHE A 62 -17.759 -15.496 -14.899 1.00 61.50 C
ANISOU 391 CD2 PHE A 62 8335 8609 6424 -1288 -85 670 C
ATOM 392 CE1 PHE A 62 -20.270 -16.331 -14.093 1.00 63.81 C
ANISOU 392 CE1 PHE A 62 8522 8775 6948 -1261 -125 726 C
ATOM 393 CE2 PHE A 62 -18.218 -16.774 -15.227 1.00 64.68 C
ANISOU 393 CE2 PHE A 62 8761 9029 6785 -1340 -78 595 C
ATOM 394 CZ PHE A 62 -19.469 -17.184 -14.819 1.00 62.96 C
ANISOU 394 CZ PHE A 62 8490 8745 6686 -1326 -102 626 C
ATOM 395 N LEU A 63 -17.784 -10.034 -14.176 1.00 57.10 N
ANISOU 395 N LEU A 63 7548 7919 6227 -1160 -288 1086 N
ATOM 396 CA LEU A 63 -17.123 -8.783 -13.809 1.00 56.60 C
ANISOU 396 CA LEU A 63 7454 7816 6237 -1103 -305 1137 C
ATOM 397 C LEU A 63 -18.141 -7.643 -13.639 1.00 60.62 C
ANISOU 397 C LEU A 63 7849 8253 6931 -1091 -400 1265 C
ATOM 398 O LEU A 63 -17.845 -6.668 -12.946 1.00 60.05 O
ANISOU 398 O LEU A 63 7736 8107 6972 -1012 -404 1289 O
ATOM 399 CB LEU A 63 -16.041 -8.419 -14.835 1.00 57.06 C
ANISOU 399 CB LEU A 63 7547 7978 6156 -1185 -339 1171 C
ATOM 400 CG LEU A 63 -14.773 -7.729 -14.304 1.00 61.47 C
ANISOU 400 CG LEU A 63 8125 8503 6728 -1109 -296 1150 C
ATOM 401 CD1 LEU A 63 -14.194 -8.442 -13.076 1.00 60.60 C
ANISOU 401 CD1 LEU A 63 8078 8321 6626 -988 -166 1005 C
ATOM 402 CD2 LEU A 63 -13.708 -7.672 -15.376 1.00 64.72 C
ANISOU 402 CD2 LEU A 63 8578 9032 6979 -1197 -310 1170 C
ATOM 403 N LYS A 64 -19.346 -7.784 -14.235 1.00 57.55 N
ANISOU 403 N LYS A 64 7406 7877 6583 -1166 -478 1342 N
ATOM 404 CA LYS A 64 -20.451 -6.826 -14.105 1.00 57.79 C
ANISOU 404 CA LYS A 64 7319 7832 6806 -1160 -568 1463 C
ATOM 405 C LYS A 64 -21.103 -6.978 -12.729 1.00 61.32 C
ANISOU 405 C LYS A 64 7736 8161 7402 -1030 -484 1396 C
ATOM 406 O LYS A 64 -21.679 -6.021 -12.209 1.00 61.55 O
ANISOU 406 O LYS A 64 7673 8100 7613 -973 -518 1457 O
ATOM 407 CB LYS A 64 -21.491 -7.037 -15.215 1.00 61.11 C
ANISOU 407 CB LYS A 64 7696 8312 7210 -1293 -681 1568 C
ATOM 408 CG LYS A 64 -21.562 -5.894 -16.214 1.00 73.48 C
ANISOU 408 CG LYS A 64 9182 9911 8826 -1385 -827 1737 C
ATOM 409 CD LYS A 64 -22.288 -6.311 -17.485 1.00 82.60 C
ANISOU 409 CD LYS A 64 10338 11177 9867 -1544 -931 1818 C
ATOM 410 CE LYS A 64 -22.681 -5.123 -18.326 1.00 92.56 C
ANISOU 410 CE LYS A 64 11493 12448 11229 -1634 -1090 2012 C
ATOM 411 NZ LYS A 64 -23.118 -5.526 -19.687 1.00101.44 N
ANISOU 411 NZ LYS A 64 12632 13706 12204 -1799 -1196 2091 N
ATOM 412 N ASN A 65 -21.023 -8.197 -12.156 1.00 56.82 N
ANISOU 412 N ASN A 65 7240 7595 6755 -986 -373 1272 N
ATOM 413 CA ASN A 65 -21.546 -8.543 -10.834 1.00 55.90 C
ANISOU 413 CA ASN A 65 7109 7389 6741 -866 -275 1199 C
ATOM 414 C ASN A 65 -20.541 -8.175 -9.750 1.00 58.52 C
ANISOU 414 C ASN A 65 7479 7672 7082 -744 -184 1112 C
ATOM 415 O ASN A 65 -20.944 -7.785 -8.654 1.00 58.05 O
ANISOU 415 O ASN A 65 7376 7528 7150 -636 -134 1087 O
ATOM 416 CB ASN A 65 -21.867 -10.030 -10.761 1.00 55.97 C
ANISOU 416 CB ASN A 65 7176 7429 6662 -885 -208 1119 C
ATOM 417 CG ASN A 65 -23.212 -10.390 -11.323 1.00 77.86 C
ANISOU 417 CG ASN A 65 9886 10198 9501 -954 -274 1192 C
ATOM 418 OD1 ASN A 65 -24.235 -10.305 -10.642 1.00 73.35 O
ANISOU 418 OD1 ASN A 65 9249 9551 9070 -891 -245 1208 O
ATOM 419 ND2 ASN A 65 -23.236 -10.832 -12.570 1.00 69.68 N
ANISOU 419 ND2 ASN A 65 8867 9246 8363 -1086 -362 1236 N
ATOM 420 N THR A 66 -19.235 -8.316 -10.055 1.00 54.20 N
ANISOU 420 N THR A 66 7014 7182 6399 -761 -161 1062 N
ATOM 421 CA THR A 66 -18.124 -8.007 -9.153 1.00 53.12 C
ANISOU 421 CA THR A 66 6924 7008 6251 -660 -87 980 C
ATOM 422 C THR A 66 -18.056 -6.489 -8.913 1.00 57.05 C
ANISOU 422 C THR A 66 7346 7439 6889 -613 -151 1048 C
ATOM 423 O THR A 66 -17.820 -6.071 -7.780 1.00 56.27 O
ANISOU 423 O THR A 66 7246 7267 6868 -497 -93 986 O
ATOM 424 CB THR A 66 -16.806 -8.573 -9.723 1.00 61.01 C
ANISOU 424 CB THR A 66 8019 8088 7075 -710 -58 926 C
ATOM 425 OG1 THR A 66 -16.972 -9.969 -9.974 1.00 60.72 O
ANISOU 425 OG1 THR A 66 8037 8104 6928 -761 -11 865 O
ATOM 426 CG2 THR A 66 -15.613 -8.373 -8.790 1.00 58.73 C
ANISOU 426 CG2 THR A 66 7785 7759 6770 -609 22 837 C
ATOM 427 N VAL A 67 -18.295 -5.674 -9.965 1.00 54.07 N
ANISOU 427 N VAL A 67 6905 7088 6550 -703 -273 1174 N
ATOM 428 CA VAL A 67 -18.257 -4.212 -9.881 1.00 54.08 C
ANISOU 428 CA VAL A 67 6821 7022 6704 -672 -352 1253 C
ATOM 429 C VAL A 67 -19.438 -3.679 -9.015 1.00 57.76 C
ANISOU 429 C VAL A 67 7193 7380 7372 -586 -348 1260 C
ATOM 430 O VAL A 67 -19.246 -2.690 -8.306 1.00 57.35 O
ANISOU 430 O VAL A 67 7099 7244 7446 -495 -348 1242 O
ATOM 431 CB VAL A 67 -18.154 -3.523 -11.278 1.00 58.83 C
ANISOU 431 CB VAL A 67 7373 7687 7293 -801 -489 1402 C
ATOM 432 CG1 VAL A 67 -19.435 -3.651 -12.098 1.00 59.54 C
ANISOU 432 CG1 VAL A 67 7396 7804 7423 -898 -573 1506 C
ATOM 433 CG2 VAL A 67 -17.721 -2.065 -11.159 1.00 58.99 C
ANISOU 433 CG2 VAL A 67 7316 7640 7459 -765 -564 1475 C
ATOM 434 N ILE A 68 -20.617 -4.351 -9.019 1.00 54.34 N
ANISOU 434 N ILE A 68 6730 6946 6972 -608 -337 1275 N
ATOM 435 CA ILE A 68 -21.738 -3.890 -8.186 1.00 54.51 C
ANISOU 435 CA ILE A 68 6659 6868 7185 -524 -320 1279 C
ATOM 436 C ILE A 68 -21.528 -4.366 -6.724 1.00 57.02 C
ANISOU 436 C ILE A 68 7030 7146 7488 -388 -175 1133 C
ATOM 437 O ILE A 68 -22.043 -3.726 -5.804 1.00 57.13 O
ANISOU 437 O ILE A 68 6982 7076 7650 -288 -144 1105 O
ATOM 438 CB ILE A 68 -23.165 -4.221 -8.732 1.00 58.47 C
ANISOU 438 CB ILE A 68 7084 7368 7765 -594 -374 1370 C
ATOM 439 CG1 ILE A 68 -23.585 -5.690 -8.530 1.00 58.64 C
ANISOU 439 CG1 ILE A 68 7160 7422 7699 -590 -282 1300 C
ATOM 440 CG2 ILE A 68 -23.351 -3.752 -10.179 1.00 59.89 C
ANISOU 440 CG2 ILE A 68 7223 7606 7929 -742 -522 1515 C
ATOM 441 CD1 ILE A 68 -25.086 -5.864 -8.194 1.00 66.91 C
ANISOU 441 CD1 ILE A 68 8112 8395 8914 -542 -259 1326 C
ATOM 442 N SER A 69 -20.751 -5.460 -6.519 1.00 51.58 N
ANISOU 442 N SER A 69 6455 6519 6624 -387 -88 1042 N
ATOM 443 CA SER A 69 -20.423 -5.976 -5.186 1.00 50.12 C
ANISOU 443 CA SER A 69 6329 6311 6405 -271 43 916 C
ATOM 444 C SER A 69 -19.344 -5.101 -4.546 1.00 52.53 C
ANISOU 444 C SER A 69 6660 6576 6723 -190 55 857 C
ATOM 445 O SER A 69 -19.390 -4.867 -3.339 1.00 51.93 O
ANISOU 445 O SER A 69 6587 6450 6696 -75 132 774 O
ATOM 446 CB SER A 69 -19.980 -7.435 -5.250 1.00 53.02 C
ANISOU 446 CB SER A 69 6795 6748 6601 -306 116 851 C
ATOM 447 OG SER A 69 -18.667 -7.590 -5.763 1.00 61.43 O
ANISOU 447 OG SER A 69 7944 7867 7531 -347 108 822 O
ATOM 448 N ASP A 70 -18.390 -4.595 -5.366 1.00 48.34 N
ANISOU 448 N ASP A 70 6146 6072 6149 -251 -24 904 N
ATOM 449 CA ASP A 70 -17.324 -3.688 -4.930 1.00 47.49 C
ANISOU 449 CA ASP A 70 6053 5922 6070 -188 -36 868 C
ATOM 450 C ASP A 70 -17.917 -2.351 -4.483 1.00 51.53 C
ANISOU 450 C ASP A 70 6457 6335 6788 -120 -89 897 C
ATOM 451 O ASP A 70 -17.403 -1.747 -3.546 1.00 50.72 O
ANISOU 451 O ASP A 70 6361 6172 6739 -19 -58 819 O
ATOM 452 CB ASP A 70 -16.294 -3.462 -6.051 1.00 49.22 C
ANISOU 452 CB ASP A 70 6300 6198 6202 -282 -113 933 C
ATOM 453 CG ASP A 70 -15.426 -4.658 -6.405 1.00 59.55 C
ANISOU 453 CG ASP A 70 7720 7596 7312 -332 -53 881 C
ATOM 454 OD1 ASP A 70 -15.200 -5.518 -5.522 1.00 59.71 O
ANISOU 454 OD1 ASP A 70 7808 7614 7264 -271 53 775 O
ATOM 455 OD2 ASP A 70 -14.952 -4.723 -7.560 1.00 65.86 O
ANISOU 455 OD2 ASP A 70 8534 8465 8026 -433 -112 945 O
ATOM 456 N LEU A 71 -19.016 -1.914 -5.138 1.00 48.97 N
ANISOU 456 N LEU A 71 6029 5992 6586 -178 -171 1006 N
ATOM 457 CA LEU A 71 -19.743 -0.678 -4.842 1.00 49.69 C
ANISOU 457 CA LEU A 71 5998 5983 6900 -126 -230 1046 C
ATOM 458 C LEU A 71 -20.335 -0.708 -3.428 1.00 53.65 C
ANISOU 458 C LEU A 71 6485 6421 7479 7 -121 932 C
ATOM 459 O LEU A 71 -20.185 0.269 -2.695 1.00 53.49 O
ANISOU 459 O LEU A 71 6424 6320 7580 101 -122 877 O
ATOM 460 CB LEU A 71 -20.857 -0.450 -5.878 1.00 50.71 C
ANISOU 460 CB LEU A 71 6023 6112 7131 -227 -333 1191 C
ATOM 461 CG LEU A 71 -21.534 0.922 -5.852 1.00 56.48 C
ANISOU 461 CG LEU A 71 6612 6737 8110 -201 -427 1265 C
ATOM 462 CD1 LEU A 71 -20.853 1.878 -6.801 1.00 57.09 C
ANISOU 462 CD1 LEU A 71 6651 6820 8220 -282 -562 1381 C
ATOM 463 CD2 LEU A 71 -22.998 0.809 -6.210 1.00 59.86 C
ANISOU 463 CD2 LEU A 71 6939 7139 8666 -240 -460 1349 C
ATOM 464 N LEU A 72 -20.994 -1.824 -3.049 1.00 50.25 N
ANISOU 464 N LEU A 72 6087 6030 6977 16 -27 893 N
ATOM 465 CA LEU A 72 -21.600 -2.003 -1.723 1.00 50.37 C
ANISOU 465 CA LEU A 72 6091 6007 7042 135 88 793 C
ATOM 466 C LEU A 72 -20.525 -2.061 -0.630 1.00 53.96 C
ANISOU 466 C LEU A 72 6640 6464 7397 234 176 658 C
ATOM 467 O LEU A 72 -20.768 -1.619 0.494 1.00 53.86 O
ANISOU 467 O LEU A 72 6607 6404 7455 347 244 569 O
ATOM 468 CB LEU A 72 -22.464 -3.271 -1.680 1.00 50.33 C
ANISOU 468 CB LEU A 72 6097 6051 6976 107 159 805 C
ATOM 469 CG LEU A 72 -23.788 -3.231 -2.438 1.00 55.82 C
ANISOU 469 CG LEU A 72 6685 6727 7797 33 89 925 C
ATOM 470 CD1 LEU A 72 -24.055 -4.549 -3.134 1.00 55.60 C
ANISOU 470 CD1 LEU A 72 6705 6779 7642 -68 91 971 C
ATOM 471 CD2 LEU A 72 -24.939 -2.874 -1.513 1.00 59.10 C
ANISOU 471 CD2 LEU A 72 7002 7073 8380 126 150 902 C
ATOM 472 N MET A 73 -19.336 -2.591 -0.978 1.00 49.86 N
ANISOU 472 N MET A 73 6224 6002 6718 189 172 642 N
ATOM 473 CA MET A 73 -18.171 -2.707 -0.103 1.00 48.99 C
ANISOU 473 CA MET A 73 6209 5896 6508 264 236 530 C
ATOM 474 C MET A 73 -17.609 -1.313 0.224 1.00 52.52 C
ANISOU 474 C MET A 73 6616 6263 7074 328 174 503 C
ATOM 475 O MET A 73 -17.261 -1.060 1.377 1.00 52.02 O
ANISOU 475 O MET A 73 6580 6165 7017 435 235 393 O
ATOM 476 CB MET A 73 -17.106 -3.589 -0.778 1.00 50.63 C
ANISOU 476 CB MET A 73 6519 6180 6538 184 236 539 C
ATOM 477 CG MET A 73 -15.977 -4.017 0.140 1.00 53.70 C
ANISOU 477 CG MET A 73 7010 6579 6812 252 314 429 C
ATOM 478 SD MET A 73 -15.710 -5.808 0.165 1.00 57.21 S
ANISOU 478 SD MET A 73 7556 7111 7070 209 411 395 S
ATOM 479 CE MET A 73 -15.012 -6.065 -1.464 1.00 53.68 C
ANISOU 479 CE MET A 73 7134 6722 6542 67 325 480 C
ATOM 480 N ILE A 74 -17.536 -0.415 -0.786 1.00 49.13 N
ANISOU 480 N ILE A 74 6120 5805 6743 260 49 606 N
ATOM 481 CA ILE A 74 -17.031 0.960 -0.648 1.00 49.15 C
ANISOU 481 CA ILE A 74 6067 5723 6886 304 -34 604 C
ATOM 482 C ILE A 74 -18.061 1.806 0.136 1.00 53.73 C
ANISOU 482 C ILE A 74 6542 6211 7662 398 -24 561 C
ATOM 483 O ILE A 74 -17.662 2.619 0.972 1.00 53.55 O
ANISOU 483 O ILE A 74 6509 6118 7719 494 -22 470 O
ATOM 484 CB ILE A 74 -16.656 1.572 -2.038 1.00 52.41 C
ANISOU 484 CB ILE A 74 6430 6143 7339 189 -171 749 C
ATOM 485 CG1 ILE A 74 -15.443 0.826 -2.651 1.00 51.87 C
ANISOU 485 CG1 ILE A 74 6470 6159 7078 121 -166 760 C
ATOM 486 CG2 ILE A 74 -16.357 3.082 -1.954 1.00 53.87 C
ANISOU 486 CG2 ILE A 74 6518 6223 7727 228 -276 777 C
ATOM 487 CD1 ILE A 74 -15.366 0.822 -4.189 1.00 58.54 C
ANISOU 487 CD1 ILE A 74 7293 7072 7878 -22 -261 908 C
ATOM 488 N LEU A 75 -19.371 1.565 -0.093 1.00 50.66 N
ANISOU 488 N LEU A 75 6078 5823 7349 372 -13 618 N
ATOM 489 CA LEU A 75 -20.489 2.252 0.571 1.00 51.35 C
ANISOU 489 CA LEU A 75 6054 5827 7628 452 6 586 C
ATOM 490 C LEU A 75 -20.537 1.969 2.087 1.00 55.09 C
ANISOU 490 C LEU A 75 6576 6299 8056 585 145 424 C
ATOM 491 O LEU A 75 -21.150 2.738 2.832 1.00 55.35 O
ANISOU 491 O LEU A 75 6527 6258 8244 676 168 360 O
ATOM 492 CB LEU A 75 -21.818 1.827 -0.084 1.00 51.83 C
ANISOU 492 CB LEU A 75 6038 5905 7749 380 -6 694 C
ATOM 493 CG LEU A 75 -22.561 2.889 -0.903 1.00 57.42 C
ANISOU 493 CG LEU A 75 6604 6543 8668 315 -143 831 C
ATOM 494 CD1 LEU A 75 -21.866 3.172 -2.228 1.00 57.42 C
ANISOU 494 CD1 LEU A 75 6614 6563 8639 211 -276 940 C
ATOM 495 CD2 LEU A 75 -23.977 2.453 -1.185 1.00 60.16 C
ANISOU 495 CD2 LEU A 75 6890 6914 9053 245 -146 928 C
ATOM 496 N THR A 76 -19.884 0.873 2.529 1.00 50.87 N
ANISOU 496 N THR A 76 6169 5847 7312 594 237 359 N
ATOM 497 CA THR A 76 -19.794 0.432 3.924 1.00 50.58 C
ANISOU 497 CA THR A 76 6195 5833 7188 703 369 219 C
ATOM 498 C THR A 76 -18.770 1.280 4.701 1.00 54.22 C
ANISOU 498 C THR A 76 6699 6248 7654 789 355 107 C
ATOM 499 O THR A 76 -19.060 1.698 5.825 1.00 54.35 O
ANISOU 499 O THR A 76 6705 6238 7707 899 425 -11 O
ATOM 500 CB THR A 76 -19.423 -1.068 3.967 1.00 58.49 C
ANISOU 500 CB THR A 76 7305 6940 7979 659 453 222 C
ATOM 501 OG1 THR A 76 -20.420 -1.826 3.281 1.00 58.84 O
ANISOU 501 OG1 THR A 76 7298 7012 8048 634 505 276 O
ATOM 502 CG2 THR A 76 -19.253 -1.601 5.383 1.00 57.37 C
ANISOU 502 CG2 THR A 76 7266 6835 7698 746 556 94 C
ATOM 503 N PHE A 77 -17.584 1.527 4.092 1.00 50.08 N
ANISOU 503 N PHE A 77 6217 5714 7095 737 263 144 N
ATOM 504 CA PHE A 77 -16.436 2.252 4.656 1.00 49.73 C
ANISOU 504 CA PHE A 77 6219 5624 7054 801 230 56 C
ATOM 505 C PHE A 77 -16.785 3.572 5.396 1.00 55.07 C
ANISOU 505 C PHE A 77 6806 6194 7924 905 202 -31 C
ATOM 506 O PHE A 77 -16.236 3.738 6.486 1.00 54.67 O
ANISOU 506 O PHE A 77 6813 6132 7828 998 248 -164 O
ATOM 507 CB PHE A 77 -15.360 2.545 3.588 1.00 50.89 C
ANISOU 507 CB PHE A 77 6386 5764 7186 714 116 147 C
ATOM 508 CG PHE A 77 -14.776 1.372 2.825 1.00 51.24 C
ANISOU 508 CG PHE A 77 6521 5906 7042 615 136 213 C
ATOM 509 CD1 PHE A 77 -14.748 0.096 3.383 1.00 53.49 C
ANISOU 509 CD1 PHE A 77 6900 6267 7156 629 253 154 C
ATOM 510 CD2 PHE A 77 -14.197 1.556 1.575 1.00 52.91 C
ANISOU 510 CD2 PHE A 77 6723 6131 7248 511 39 330 C
ATOM 511 CE1 PHE A 77 -14.210 -0.982 2.676 1.00 53.39 C
ANISOU 511 CE1 PHE A 77 6964 6334 6988 540 270 205 C
ATOM 512 CE2 PHE A 77 -13.652 0.477 0.873 1.00 54.81 C
ANISOU 512 CE2 PHE A 77 7046 6463 7315 423 63 375 C
ATOM 513 CZ PHE A 77 -13.664 -0.784 1.427 1.00 52.20 C
ANISOU 513 CZ PHE A 77 6804 6197 6832 440 178 307 C
ATOM 514 N PRO A 78 -17.655 4.509 4.899 1.00 52.81 N
ANISOU 514 N PRO A 78 6383 5829 7854 895 128 31 N
ATOM 515 CA PRO A 78 -17.909 5.747 5.666 1.00 53.80 C
ANISOU 515 CA PRO A 78 6424 5847 8171 1001 105 -71 C
ATOM 516 C PRO A 78 -18.526 5.502 7.045 1.00 58.79 C
ANISOU 516 C PRO A 78 7074 6497 8765 1119 245 -226 C
ATOM 517 O PRO A 78 -18.229 6.252 7.969 1.00 59.05 O
ANISOU 517 O PRO A 78 7106 6474 8857 1221 252 -363 O
ATOM 518 CB PRO A 78 -18.863 6.539 4.767 1.00 56.35 C
ANISOU 518 CB PRO A 78 6592 6094 8724 952 12 48 C
ATOM 519 CG PRO A 78 -19.480 5.532 3.876 1.00 60.21 C
ANISOU 519 CG PRO A 78 7089 6667 9119 845 31 180 C
ATOM 520 CD PRO A 78 -18.407 4.528 3.627 1.00 54.50 C
ANISOU 520 CD PRO A 78 6508 6042 8157 787 54 194 C
ATOM 521 N PHE A 79 -19.341 4.438 7.189 1.00 55.55 N
ANISOU 521 N PHE A 79 6685 6172 8249 1105 356 -207 N
ATOM 522 CA PHE A 79 -19.976 4.058 8.455 1.00 56.00 C
ANISOU 522 CA PHE A 79 6759 6271 8249 1206 502 -332 C
ATOM 523 C PHE A 79 -18.944 3.475 9.434 1.00 60.00 C
ANISOU 523 C PHE A 79 7408 6846 8542 1259 574 -448 C
ATOM 524 O PHE A 79 -19.133 3.582 10.648 1.00 60.34 O
ANISOU 524 O PHE A 79 7467 6905 8554 1363 668 -585 O
ATOM 525 CB PHE A 79 -21.126 3.066 8.212 1.00 57.57 C
ANISOU 525 CB PHE A 79 6928 6537 8408 1162 586 -250 C
ATOM 526 CG PHE A 79 -22.256 3.646 7.394 1.00 59.69 C
ANISOU 526 CG PHE A 79 7050 6735 8897 1120 522 -145 C
ATOM 527 CD1 PHE A 79 -23.258 4.397 7.996 1.00 63.87 C
ANISOU 527 CD1 PHE A 79 7463 7197 9608 1206 563 -211 C
ATOM 528 CD2 PHE A 79 -22.309 3.458 6.017 1.00 61.25 C
ANISOU 528 CD2 PHE A 79 7220 6932 9122 993 417 20 C
ATOM 529 CE1 PHE A 79 -24.296 4.946 7.238 1.00 65.57 C
ANISOU 529 CE1 PHE A 79 7533 7336 10043 1164 497 -106 C
ATOM 530 CE2 PHE A 79 -23.347 4.007 5.259 1.00 64.85 C
ANISOU 530 CE2 PHE A 79 7537 7322 9783 948 346 127 C
ATOM 531 CZ PHE A 79 -24.334 4.746 5.874 1.00 64.19 C
ANISOU 531 CZ PHE A 79 7334 7161 9892 1033 385 67 C
ATOM 532 N LYS A 80 -17.850 2.882 8.904 1.00 55.63 N
ANISOU 532 N LYS A 80 6954 6335 7848 1186 530 -392 N
ATOM 533 CA LYS A 80 -16.760 2.322 9.702 1.00 54.94 C
ANISOU 533 CA LYS A 80 7000 6304 7571 1221 579 -480 C
ATOM 534 C LYS A 80 -15.798 3.433 10.150 1.00 60.18 C
ANISOU 534 C LYS A 80 7675 6885 8305 1285 498 -578 C
ATOM 535 O LYS A 80 -15.251 3.347 11.248 1.00 60.09 O
ANISOU 535 O LYS A 80 7742 6898 8191 1360 550 -702 O
ATOM 536 CB LYS A 80 -16.007 1.232 8.921 1.00 56.01 C
ANISOU 536 CB LYS A 80 7226 6509 7547 1117 566 -380 C
ATOM 537 CG LYS A 80 -15.115 0.361 9.801 1.00 70.16 C
ANISOU 537 CG LYS A 80 9149 8373 9137 1148 642 -456 C
ATOM 538 CD LYS A 80 -14.459 -0.775 9.029 1.00 79.50 C
ANISOU 538 CD LYS A 80 10406 9627 10176 1048 651 -362 C
ATOM 539 CE LYS A 80 -13.540 -1.604 9.898 1.00 87.83 C
ANISOU 539 CE LYS A 80 11579 10741 11050 1074 718 -427 C
ATOM 540 NZ LYS A 80 -14.284 -2.428 10.892 1.00 94.62 N
ANISOU 540 NZ LYS A 80 12455 11673 11824 1132 847 -481 N
ATOM 541 N ILE A 81 -15.602 4.474 9.306 1.00 57.50 N
ANISOU 541 N ILE A 81 7255 6449 8145 1251 366 -515 N
ATOM 542 CA ILE A 81 -14.718 5.617 9.581 1.00 57.95 C
ANISOU 542 CA ILE A 81 7300 6407 8309 1301 266 -587 C
ATOM 543 C ILE A 81 -15.205 6.377 10.835 1.00 63.49 C
ANISOU 543 C ILE A 81 7963 7061 9098 1433 315 -761 C
ATOM 544 O ILE A 81 -14.379 6.717 11.682 1.00 63.14 O
ANISOU 544 O ILE A 81 7981 6995 9015 1502 303 -885 O
ATOM 545 CB ILE A 81 -14.582 6.551 8.330 1.00 61.26 C
ANISOU 545 CB ILE A 81 7616 6736 8924 1228 115 -455 C
ATOM 546 CG1 ILE A 81 -13.824 5.835 7.187 1.00 60.33 C
ANISOU 546 CG1 ILE A 81 7560 6674 8688 1107 64 -313 C
ATOM 547 CG2 ILE A 81 -13.885 7.884 8.672 1.00 63.00 C
ANISOU 547 CG2 ILE A 81 7781 6830 9325 1294 8 -532 C
ATOM 548 CD1 ILE A 81 -14.109 6.336 5.761 1.00 66.12 C
ANISOU 548 CD1 ILE A 81 8193 7375 9555 1001 -49 -139 C
ATOM 549 N LEU A 82 -16.530 6.601 10.966 1.00 61.57 N
ANISOU 549 N LEU A 82 7622 6807 8966 1468 375 -775 N
ATOM 550 CA LEU A 82 -17.123 7.331 12.099 1.00 63.08 C
ANISOU 550 CA LEU A 82 7762 6956 9248 1593 434 -944 C
ATOM 551 C LEU A 82 -17.188 6.488 13.384 1.00 67.79 C
ANISOU 551 C LEU A 82 8460 7669 9627 1663 589 -1067 C
ATOM 552 O LEU A 82 -16.943 7.027 14.465 1.00 68.09 O
ANISOU 552 O LEU A 82 8525 7693 9653 1763 617 -1234 O
ATOM 553 CB LEU A 82 -18.540 7.861 11.775 1.00 64.17 C
ANISOU 553 CB LEU A 82 7743 7033 9605 1604 442 -910 C
ATOM 554 CG LEU A 82 -18.863 8.306 10.341 1.00 68.71 C
ANISOU 554 CG LEU A 82 8206 7529 10371 1505 313 -733 C
ATOM 555 CD1 LEU A 82 -20.347 8.494 10.154 1.00 69.89 C
ANISOU 555 CD1 LEU A 82 8217 7643 10696 1513 350 -695 C
ATOM 556 CD2 LEU A 82 -18.113 9.565 9.944 1.00 71.44 C
ANISOU 556 CD2 LEU A 82 8500 7748 10897 1508 156 -736 C
ATOM 557 N SER A 83 -17.546 5.189 13.271 1.00 64.27 N
ANISOU 557 N SER A 83 8065 7337 9016 1609 686 -983 N
ATOM 558 CA SER A 83 -17.691 4.281 14.414 1.00 64.56 C
ANISOU 558 CA SER A 83 8187 7496 8849 1662 835 -1067 C
ATOM 559 C SER A 83 -16.352 3.971 15.097 1.00 68.91 C
ANISOU 559 C SER A 83 8880 8093 9211 1680 830 -1142 C
ATOM 560 O SER A 83 -16.306 3.927 16.327 1.00 69.31 O
ANISOU 560 O SER A 83 8984 8203 9149 1764 918 -1275 O
ATOM 561 CB SER A 83 -18.376 2.984 13.994 1.00 67.53 C
ANISOU 561 CB SER A 83 8569 7965 9123 1589 918 -938 C
ATOM 562 OG SER A 83 -17.636 2.291 13.004 1.00 75.65 O
ANISOU 562 OG SER A 83 9664 9017 10061 1480 855 -810 O
ATOM 563 N ASP A 84 -15.275 3.764 14.312 1.00 65.02 N
ANISOU 563 N ASP A 84 8445 7578 8682 1601 729 -1055 N
ATOM 564 CA ASP A 84 -13.937 3.469 14.835 1.00 64.53 C
ANISOU 564 CA ASP A 84 8510 7546 8461 1609 710 -1108 C
ATOM 565 C ASP A 84 -13.277 4.715 15.446 1.00 69.67 C
ANISOU 565 C ASP A 84 9161 8106 9203 1690 629 -1247 C
ATOM 566 O ASP A 84 -12.446 4.578 16.345 1.00 69.37 O
ANISOU 566 O ASP A 84 9223 8103 9031 1733 642 -1343 O
ATOM 567 CB ASP A 84 -13.039 2.883 13.732 1.00 65.01 C
ANISOU 567 CB ASP A 84 8624 7612 8467 1496 637 -966 C
ATOM 568 CG ASP A 84 -13.446 1.502 13.243 1.00 75.76 C
ANISOU 568 CG ASP A 84 10015 9072 9698 1417 718 -851 C
ATOM 569 OD1 ASP A 84 -14.664 1.203 13.240 1.00 77.06 O
ANISOU 569 OD1 ASP A 84 10119 9276 9886 1424 800 -829 O
ATOM 570 OD2 ASP A 84 -12.551 0.732 12.829 1.00 80.90 O
ANISOU 570 OD2 ASP A 84 10743 9755 10239 1347 696 -782 O
ATOM 571 N ALA A 85 -13.654 5.918 14.965 1.00 67.09 N
ANISOU 571 N ALA A 85 8720 7660 9110 1709 539 -1256 N
ATOM 572 CA ALA A 85 -13.122 7.203 15.426 1.00 67.87 C
ANISOU 572 CA ALA A 85 8797 7652 9338 1786 447 -1386 C
ATOM 573 C ALA A 85 -13.622 7.580 16.825 1.00 73.34 C
ANISOU 573 C ALA A 85 9490 8366 10008 1910 537 -1586 C
ATOM 574 O ALA A 85 -12.866 8.182 17.591 1.00 73.66 O
ANISOU 574 O ALA A 85 9582 8374 10033 1977 495 -1725 O
ATOM 575 CB ALA A 85 -13.488 8.302 14.443 1.00 69.03 C
ANISOU 575 CB ALA A 85 8808 7665 9757 1761 323 -1318 C
ATOM 576 N LYS A 86 -14.890 7.252 17.150 1.00 70.36 N
ANISOU 576 N LYS A 86 9054 8047 9633 1940 660 -1602 N
ATOM 577 CA LYS A 86 -15.503 7.568 18.444 1.00 96.32 C
ANISOU 577 CA LYS A 86 12331 11372 12896 2056 767 -1787 C
ATOM 578 C LYS A 86 -14.983 6.648 19.551 1.00122.24 C
ANISOU 578 C LYS A 86 15755 14794 15897 2087 867 -1867 C
ATOM 579 O LYS A 86 -14.790 5.454 19.336 1.00 81.88 O
ANISOU 579 O LYS A 86 10722 9779 10611 2016 911 -1752 O
ATOM 580 CB LYS A 86 -17.039 7.490 18.364 1.00 99.44 C
ANISOU 580 CB LYS A 86 12612 11789 13383 2070 872 -1758 C
ATOM 581 CG LYS A 86 -17.685 8.605 17.536 1.00113.54 C
ANISOU 581 CG LYS A 86 14238 13425 15476 2070 781 -1725 C
ATOM 582 CD LYS A 86 -17.716 9.946 18.270 1.00124.71 C
ANISOU 582 CD LYS A 86 15587 14742 17054 2186 755 -1927 C
ATOM 583 CE LYS A 86 -17.681 11.109 17.312 1.00135.26 C
ANISOU 583 CE LYS A 86 16823 15905 18664 2164 580 -1887 C
ATOM 584 NZ LYS A 86 -17.479 12.398 18.023 1.00146.05 N
ANISOU 584 NZ LYS A 86 18148 17171 20175 2277 537 -2097 N
ATOM 585 N THR A 89 -19.066 2.711 22.812 1.00 85.43 N
ANISOU 585 N THR A 89 11118 10760 10581 2198 1625 -1876 N
ATOM 586 CA THR A 89 -20.114 2.264 21.894 1.00 84.61 C
ANISOU 586 CA THR A 89 10914 10639 10594 2138 1658 -1719 C
ATOM 587 C THR A 89 -21.353 3.176 21.991 1.00 88.89 C
ANISOU 587 C THR A 89 11310 11119 11344 2211 1710 -1795 C
ATOM 588 O THR A 89 -21.541 3.876 22.991 1.00 90.05 O
ANISOU 588 O THR A 89 11443 11276 11495 2316 1764 -1977 O
ATOM 589 CB THR A 89 -20.468 0.774 22.139 1.00 93.36 C
ANISOU 589 CB THR A 89 12066 11896 11511 2093 1779 -1603 C
ATOM 590 OG1 THR A 89 -21.313 0.307 21.087 1.00 92.75 O
ANISOU 590 OG1 THR A 89 11901 11786 11553 2019 1780 -1438 O
ATOM 591 CG2 THR A 89 -21.145 0.524 23.486 1.00 93.52 C
ANISOU 591 CG2 THR A 89 12084 12050 11399 2181 1948 -1705 C
ATOM 592 N GLY A 90 -22.174 3.139 20.944 1.00 83.98 N
ANISOU 592 N GLY A 90 10582 10434 10893 2154 1690 -1657 N
ATOM 593 CA GLY A 90 -23.413 3.901 20.840 1.00 84.50 C
ANISOU 593 CA GLY A 90 10494 10428 11184 2205 1730 -1691 C
ATOM 594 C GLY A 90 -24.379 3.310 19.828 1.00 86.03 C
ANISOU 594 C GLY A 90 10595 10603 11488 2123 1737 -1500 C
ATOM 595 O GLY A 90 -24.151 2.197 19.342 1.00 84.33 O
ANISOU 595 O GLY A 90 10443 10445 11155 2030 1725 -1353 O
ATOM 596 N PRO A 91 -25.461 4.042 19.457 1.00 82.03 N
ANISOU 596 N PRO A 91 9936 10009 11221 2152 1749 -1498 N
ATOM 597 CA PRO A 91 -26.417 3.501 18.470 1.00 80.71 C
ANISOU 597 CA PRO A 91 9676 9818 11170 2070 1746 -1311 C
ATOM 598 C PRO A 91 -25.818 3.313 17.073 1.00 80.94 C
ANISOU 598 C PRO A 91 9726 9776 11250 1944 1582 -1149 C
ATOM 599 O PRO A 91 -26.349 2.516 16.299 1.00 79.80 O
ANISOU 599 O PRO A 91 9552 9650 11117 1858 1578 -986 O
ATOM 600 CB PRO A 91 -27.536 4.547 18.444 1.00 84.16 C
ANISOU 600 CB PRO A 91 9945 10153 11878 2135 1767 -1367 C
ATOM 601 CG PRO A 91 -27.364 5.345 19.694 1.00 90.29 C
ANISOU 601 CG PRO A 91 10735 10951 12622 2266 1849 -1596 C
ATOM 602 CD PRO A 91 -25.893 5.366 19.941 1.00 85.12 C
ANISOU 602 CD PRO A 91 10229 10318 11797 2261 1768 -1669 C
ATOM 603 N LEU A 92 -24.718 4.028 16.754 1.00 75.53 N
ANISOU 603 N LEU A 92 9091 9015 10592 1933 1447 -1193 N
ATOM 604 CA LEU A 92 -24.027 3.910 15.468 1.00 73.29 C
ANISOU 604 CA LEU A 92 8834 8675 10338 1817 1294 -1049 C
ATOM 605 C LEU A 92 -23.272 2.578 15.396 1.00 74.53 C
ANISOU 605 C LEU A 92 9131 8947 10241 1745 1317 -969 C
ATOM 606 O LEU A 92 -23.401 1.873 14.396 1.00 73.16 O
ANISOU 606 O LEU A 92 8955 8782 10061 1640 1273 -812 O
ATOM 607 CB LEU A 92 -23.071 5.097 15.233 1.00 73.29 C
ANISOU 607 CB LEU A 92 8838 8561 10447 1834 1151 -1121 C
ATOM 608 CG LEU A 92 -22.423 5.198 13.842 1.00 76.55 C
ANISOU 608 CG LEU A 92 9259 8909 10919 1717 987 -971 C
ATOM 609 CD1 LEU A 92 -23.365 5.843 12.831 1.00 77.12 C
ANISOU 609 CD1 LEU A 92 9179 8880 11243 1665 907 -851 C
ATOM 610 CD2 LEU A 92 -21.136 5.985 13.906 1.00 78.70 C
ANISOU 610 CD2 LEU A 92 9584 9113 11206 1739 874 -1052 C
ATOM 611 N ARG A 93 -22.509 2.229 16.462 1.00 70.01 N
ANISOU 611 N ARG A 93 8676 8462 9465 1799 1384 -1080 N
ATOM 612 CA ARG A 93 -21.739 0.982 16.569 1.00 68.05 C
ANISOU 612 CA ARG A 93 8557 8319 8979 1743 1413 -1021 C
ATOM 613 C ARG A 93 -22.679 -0.229 16.554 1.00 70.92 C
ANISOU 613 C ARG A 93 8898 8777 9272 1707 1527 -915 C
ATOM 614 O ARG A 93 -22.352 -1.236 15.926 1.00 69.29 O
ANISOU 614 O ARG A 93 8745 8609 8972 1615 1505 -794 O
ATOM 615 CB ARG A 93 -20.868 0.988 17.842 1.00 68.10 C
ANISOU 615 CB ARG A 93 8676 8393 8805 1820 1462 -1170 C
ATOM 616 CG ARG A 93 -19.949 -0.228 18.021 1.00 75.53 C
ANISOU 616 CG ARG A 93 9750 9436 9513 1765 1483 -1114 C
ATOM 617 CD ARG A 93 -18.640 -0.111 17.260 1.00 82.42 C
ANISOU 617 CD ARG A 93 10698 10249 10367 1698 1345 -1074 C
ATOM 618 NE ARG A 93 -17.731 -1.215 17.573 1.00 87.29 N
ANISOU 618 NE ARG A 93 11437 10957 10771 1658 1372 -1040 N
ATOM 619 CZ ARG A 93 -17.597 -2.316 16.839 1.00 98.57 C
ANISOU 619 CZ ARG A 93 12895 12416 12141 1560 1362 -903 C
ATOM 620 NH1 ARG A 93 -18.309 -2.474 15.729 1.00 82.60 N
ANISOU 620 NH1 ARG A 93 10795 10348 10240 1488 1322 -786 N
ATOM 621 NH2 ARG A 93 -16.746 -3.264 17.206 1.00 85.55 N
ANISOU 621 NH2 ARG A 93 11349 10840 10315 1531 1387 -882 N
ATOM 622 N THR A 94 -23.850 -0.113 17.220 1.00 68.25 N
ANISOU 622 N THR A 94 8473 8468 8992 1779 1646 -962 N
ATOM 623 CA THR A 94 -24.890 -1.147 17.279 1.00 68.03 C
ANISOU 623 CA THR A 94 8400 8519 8930 1757 1759 -862 C
ATOM 624 C THR A 94 -25.420 -1.405 15.860 1.00 70.57 C
ANISOU 624 C THR A 94 8648 8771 9395 1650 1671 -693 C
ATOM 625 O THR A 94 -25.579 -2.564 15.477 1.00 69.31 O
ANISOU 625 O THR A 94 8511 8670 9154 1577 1695 -573 O
ATOM 626 CB THR A 94 -26.011 -0.733 18.255 1.00 78.31 C
ANISOU 626 CB THR A 94 9609 9851 10294 1864 1898 -958 C
ATOM 627 OG1 THR A 94 -25.435 -0.303 19.490 1.00 79.34 O
ANISOU 627 OG1 THR A 94 9812 10040 10294 1961 1958 -1131 O
ATOM 628 CG2 THR A 94 -27.008 -1.859 18.522 1.00 77.03 C
ANISOU 628 CG2 THR A 94 9405 9786 10076 1851 2030 -859 C
ATOM 629 N PHE A 95 -25.650 -0.323 15.081 1.00 67.05 N
ANISOU 629 N PHE A 95 8115 8201 9161 1639 1561 -685 N
ATOM 630 CA PHE A 95 -26.116 -0.364 13.693 1.00 66.15 C
ANISOU 630 CA PHE A 95 7928 8015 9192 1535 1457 -530 C
ATOM 631 C PHE A 95 -25.046 -0.984 12.777 1.00 68.74 C
ANISOU 631 C PHE A 95 8359 8354 9404 1427 1350 -441 C
ATOM 632 O PHE A 95 -25.399 -1.753 11.883 1.00 67.56 O
ANISOU 632 O PHE A 95 8197 8217 9255 1330 1317 -304 O
ATOM 633 CB PHE A 95 -26.509 1.051 13.208 1.00 68.59 C
ANISOU 633 CB PHE A 95 8115 8189 9759 1558 1364 -551 C
ATOM 634 CG PHE A 95 -26.527 1.252 11.709 1.00 69.21 C
ANISOU 634 CG PHE A 95 8146 8186 9966 1443 1208 -404 C
ATOM 635 CD1 PHE A 95 -27.588 0.785 10.940 1.00 72.19 C
ANISOU 635 CD1 PHE A 95 8440 8555 10435 1368 1197 -258 C
ATOM 636 CD2 PHE A 95 -25.485 1.911 11.066 1.00 70.52 C
ANISOU 636 CD2 PHE A 95 8347 8286 10160 1408 1070 -406 C
ATOM 637 CE1 PHE A 95 -27.599 0.965 9.554 1.00 72.56 C
ANISOU 637 CE1 PHE A 95 8447 8539 10583 1256 1050 -121 C
ATOM 638 CE2 PHE A 95 -25.497 2.087 9.680 1.00 72.76 C
ANISOU 638 CE2 PHE A 95 8587 8511 10548 1297 929 -263 C
ATOM 639 CZ PHE A 95 -26.552 1.612 8.933 1.00 70.98 C
ANISOU 639 CZ PHE A 95 8285 8287 10398 1221 919 -123 C
ATOM 640 N VAL A 96 -23.754 -0.631 12.989 1.00 65.08 N
ANISOU 640 N VAL A 96 7994 7885 8848 1443 1295 -523 N
ATOM 641 CA VAL A 96 -22.613 -1.143 12.216 1.00 63.61 C
ANISOU 641 CA VAL A 96 7907 7709 8551 1352 1202 -457 C
ATOM 642 C VAL A 96 -22.549 -2.671 12.386 1.00 67.46 C
ANISOU 642 C VAL A 96 8474 8306 8850 1305 1283 -396 C
ATOM 643 O VAL A 96 -22.511 -3.386 11.387 1.00 65.86 O
ANISOU 643 O VAL A 96 8283 8111 8629 1202 1230 -278 O
ATOM 644 CB VAL A 96 -21.278 -0.431 12.588 1.00 67.22 C
ANISOU 644 CB VAL A 96 8446 8136 8958 1394 1139 -566 C
ATOM 645 CG1 VAL A 96 -20.058 -1.205 12.089 1.00 65.62 C
ANISOU 645 CG1 VAL A 96 8365 7975 8591 1318 1092 -517 C
ATOM 646 CG2 VAL A 96 -21.251 0.996 12.050 1.00 67.53 C
ANISOU 646 CG2 VAL A 96 8402 8050 9205 1402 1017 -579 C
ATOM 647 N CYS A 97 -22.622 -3.152 13.646 1.00 65.55 N
ANISOU 647 N CYS A 97 8277 8150 8480 1379 1410 -474 N
ATOM 648 CA CYS A 97 -22.622 -4.568 14.035 1.00 65.28 C
ANISOU 648 CA CYS A 97 8307 8221 8277 1349 1499 -423 C
ATOM 649 C CYS A 97 -23.797 -5.326 13.404 1.00 67.06 C
ANISOU 649 C CYS A 97 8449 8459 8573 1290 1532 -295 C
ATOM 650 O CYS A 97 -23.651 -6.491 13.036 1.00 65.70 O
ANISOU 650 O CYS A 97 8320 8336 8307 1218 1542 -209 O
ATOM 651 CB CYS A 97 -22.660 -4.696 15.557 1.00 67.19 C
ANISOU 651 CB CYS A 97 8588 8549 8393 1449 1627 -531 C
ATOM 652 SG CYS A 97 -21.107 -4.271 16.386 1.00 71.33 S
ANISOU 652 SG CYS A 97 9242 9084 8776 1499 1590 -665 S
ATOM 653 N GLN A 98 -24.959 -4.659 13.304 1.00 63.09 N
ANISOU 653 N GLN A 98 7824 7906 8242 1321 1547 -284 N
ATOM 654 CA GLN A 98 -26.213 -5.219 12.812 1.00 62.44 C
ANISOU 654 CA GLN A 98 7646 7826 8254 1278 1579 -169 C
ATOM 655 C GLN A 98 -26.386 -5.150 11.287 1.00 63.44 C
ANISOU 655 C GLN A 98 7728 7879 8498 1166 1444 -48 C
ATOM 656 O GLN A 98 -26.946 -6.089 10.725 1.00 62.54 O
ANISOU 656 O GLN A 98 7591 7787 8384 1094 1448 62 O
ATOM 657 CB GLN A 98 -27.387 -4.485 13.483 1.00 65.39 C
ANISOU 657 CB GLN A 98 7901 8179 8766 1371 1666 -218 C
ATOM 658 CG GLN A 98 -28.682 -5.280 13.553 1.00 82.07 C
ANISOU 658 CG GLN A 98 9926 10328 10928 1358 1757 -121 C
ATOM 659 CD GLN A 98 -29.709 -4.600 14.420 1.00103.97 C
ANISOU 659 CD GLN A 98 12592 13097 13815 1464 1867 -189 C
ATOM 660 OE1 GLN A 98 -29.669 -4.679 15.652 1.00100.53 O
ANISOU 660 OE1 GLN A 98 12185 12743 13271 1554 1993 -286 O
ATOM 661 NE2 GLN A 98 -30.659 -3.923 13.793 1.00 97.39 N
ANISOU 661 NE2 GLN A 98 11629 12170 13202 1453 1823 -139 N
ATOM 662 N VAL A 99 -25.972 -4.044 10.623 1.00 58.35 N
ANISOU 662 N VAL A 99 7064 7147 7959 1151 1325 -64 N
ATOM 663 CA VAL A 99 -26.232 -3.879 9.188 1.00 57.01 C
ANISOU 663 CA VAL A 99 6841 6916 7905 1044 1196 57 C
ATOM 664 C VAL A 99 -24.953 -3.796 8.307 1.00 58.10 C
ANISOU 664 C VAL A 99 7068 7043 7965 966 1074 77 C
ATOM 665 O VAL A 99 -24.703 -4.743 7.561 1.00 56.53 O
ANISOU 665 O VAL A 99 6924 6887 7669 874 1046 153 O
ATOM 666 CB VAL A 99 -27.173 -2.665 8.907 1.00 61.88 C
ANISOU 666 CB VAL A 99 7316 7434 8763 1071 1147 72 C
ATOM 667 CG1 VAL A 99 -27.601 -2.617 7.442 1.00 61.48 C
ANISOU 667 CG1 VAL A 99 7200 7333 8826 952 1020 220 C
ATOM 668 CG2 VAL A 99 -28.405 -2.683 9.811 1.00 62.89 C
ANISOU 668 CG2 VAL A 99 7351 7571 8975 1159 1278 37 C
ATOM 669 N THR A 100 -24.207 -2.659 8.336 1.00 53.91 N
ANISOU 669 N THR A 100 6542 6450 7490 999 1000 12 N
ATOM 670 CA THR A 100 -23.062 -2.372 7.450 1.00 52.46 C
ANISOU 670 CA THR A 100 6419 6243 7270 930 877 40 C
ATOM 671 C THR A 100 -21.914 -3.401 7.487 1.00 54.13 C
ANISOU 671 C THR A 100 6769 6530 7270 891 897 27 C
ATOM 672 O THR A 100 -21.470 -3.802 6.410 1.00 52.88 O
ANISOU 672 O THR A 100 6643 6379 7069 791 815 105 O
ATOM 673 CB THR A 100 -22.492 -0.968 7.672 1.00 60.72 C
ANISOU 673 CB THR A 100 7443 7209 8420 993 812 -40 C
ATOM 674 OG1 THR A 100 -22.093 -0.815 9.029 1.00 61.31 O
ANISOU 674 OG1 THR A 100 7575 7308 8412 1104 903 -184 O
ATOM 675 CG2 THR A 100 -23.465 0.132 7.273 1.00 60.36 C
ANISOU 675 CG2 THR A 100 7250 7069 8615 1008 754 -7 C
ATOM 676 N SER A 101 -21.430 -3.822 8.680 1.00 49.84 N
ANISOU 676 N SER A 101 6301 6042 6595 966 1001 -69 N
ATOM 677 CA SER A 101 -20.328 -4.796 8.772 1.00 48.19 C
ANISOU 677 CA SER A 101 6215 5895 6200 932 1019 -80 C
ATOM 678 C SER A 101 -20.707 -6.150 8.158 1.00 50.45 C
ANISOU 678 C SER A 101 6515 6237 6418 843 1043 16 C
ATOM 679 O SER A 101 -19.854 -6.780 7.542 1.00 49.17 O
ANISOU 679 O SER A 101 6425 6097 6160 770 1002 46 O
ATOM 680 CB SER A 101 -19.865 -4.985 10.213 1.00 51.93 C
ANISOU 680 CB SER A 101 6757 6415 6558 1029 1119 -194 C
ATOM 681 OG SER A 101 -20.916 -5.436 11.048 1.00 61.83 O
ANISOU 681 OG SER A 101 7965 7717 7810 1083 1237 -204 O
ATOM 682 N VAL A 102 -21.987 -6.562 8.286 1.00 46.95 N
ANISOU 682 N VAL A 102 5994 5808 6035 847 1105 63 N
ATOM 683 CA VAL A 102 -22.538 -7.807 7.727 1.00 46.17 C
ANISOU 683 CA VAL A 102 5889 5752 5901 767 1123 156 C
ATOM 684 C VAL A 102 -22.534 -7.717 6.181 1.00 49.44 C
ANISOU 684 C VAL A 102 6280 6133 6372 651 998 249 C
ATOM 685 O VAL A 102 -22.196 -8.700 5.516 1.00 48.33 O
ANISOU 685 O VAL A 102 6190 6029 6146 567 977 295 O
ATOM 686 CB VAL A 102 -23.958 -8.119 8.287 1.00 50.85 C
ANISOU 686 CB VAL A 102 6392 6361 6569 808 1216 186 C
ATOM 687 CG1 VAL A 102 -24.446 -9.497 7.843 1.00 50.34 C
ANISOU 687 CG1 VAL A 102 6324 6336 6466 730 1236 278 C
ATOM 688 CG2 VAL A 102 -23.995 -8.011 9.811 1.00 51.19 C
ANISOU 688 CG2 VAL A 102 6451 6446 6553 926 1341 91 C
ATOM 689 N ILE A 103 -22.886 -6.528 5.628 1.00 46.32 N
ANISOU 689 N ILE A 103 5808 5671 6119 648 913 273 N
ATOM 690 CA ILE A 103 -22.920 -6.221 4.189 1.00 45.87 C
ANISOU 690 CA ILE A 103 5718 5585 6126 541 784 368 C
ATOM 691 C ILE A 103 -21.495 -6.329 3.608 1.00 48.67 C
ANISOU 691 C ILE A 103 6173 5962 6359 485 722 355 C
ATOM 692 O ILE A 103 -21.327 -6.867 2.510 1.00 47.77 O
ANISOU 692 O ILE A 103 6079 5874 6199 379 658 425 O
ATOM 693 CB ILE A 103 -23.575 -4.821 3.940 1.00 49.83 C
ANISOU 693 CB ILE A 103 6106 6005 6824 565 714 394 C
ATOM 694 CG1 ILE A 103 -25.113 -4.907 4.092 1.00 51.09 C
ANISOU 694 CG1 ILE A 103 6153 6144 7116 579 755 448 C
ATOM 695 CG2 ILE A 103 -23.182 -4.208 2.575 1.00 50.39 C
ANISOU 695 CG2 ILE A 103 6157 6045 6943 467 566 479 C
ATOM 696 CD1 ILE A 103 -25.845 -3.577 4.271 1.00 59.01 C
ANISOU 696 CD1 ILE A 103 7032 7059 8329 635 724 448 C
ATOM 697 N PHE A 104 -20.482 -5.844 4.359 1.00 44.94 N
ANISOU 697 N PHE A 104 5763 5480 5834 557 743 262 N
ATOM 698 CA PHE A 104 -19.071 -5.893 3.970 1.00 43.90 C
ANISOU 698 CA PHE A 104 5722 5361 5597 520 695 242 C
ATOM 699 C PHE A 104 -18.619 -7.341 3.738 1.00 46.81 C
ANISOU 699 C PHE A 104 6173 5799 5814 458 738 252 C
ATOM 700 O PHE A 104 -17.988 -7.613 2.718 1.00 45.95 O
ANISOU 700 O PHE A 104 6098 5709 5652 367 673 296 O
ATOM 701 CB PHE A 104 -18.184 -5.207 5.024 1.00 45.67 C
ANISOU 701 CB PHE A 104 5993 5560 5799 620 721 134 C
ATOM 702 CG PHE A 104 -16.702 -5.264 4.730 1.00 46.50 C
ANISOU 702 CG PHE A 104 6190 5674 5804 590 678 113 C
ATOM 703 CD1 PHE A 104 -16.120 -4.381 3.829 1.00 49.59 C
ANISOU 703 CD1 PHE A 104 6563 6026 6253 543 566 157 C
ATOM 704 CD2 PHE A 104 -15.888 -6.199 5.359 1.00 48.03 C
ANISOU 704 CD2 PHE A 104 6482 5914 5854 608 748 57 C
ATOM 705 CE1 PHE A 104 -14.751 -4.441 3.555 1.00 49.81 C
ANISOU 705 CE1 PHE A 104 6670 6062 6194 515 532 143 C
ATOM 706 CE2 PHE A 104 -14.522 -6.259 5.080 1.00 50.12 C
ANISOU 706 CE2 PHE A 104 6824 6180 6039 579 710 41 C
ATOM 707 CZ PHE A 104 -13.964 -5.381 4.181 1.00 48.15 C
ANISOU 707 CZ PHE A 104 6556 5893 5847 535 606 82 C
ATOM 708 N TYR A 105 -18.948 -8.258 4.675 1.00 43.29 N
ANISOU 708 N TYR A 105 5753 5390 5304 505 846 213 N
ATOM 709 CA TYR A 105 -18.603 -9.678 4.583 1.00 42.44 C
ANISOU 709 CA TYR A 105 5712 5338 5076 453 891 221 C
ATOM 710 C TYR A 105 -19.381 -10.356 3.457 1.00 46.68 C
ANISOU 710 C TYR A 105 6206 5891 5641 352 852 309 C
ATOM 711 O TYR A 105 -18.813 -11.176 2.742 1.00 45.88 O
ANISOU 711 O TYR A 105 6156 5819 5458 272 828 324 O
ATOM 712 CB TYR A 105 -18.862 -10.403 5.914 1.00 43.61 C
ANISOU 712 CB TYR A 105 5880 5520 5169 529 1011 175 C
ATOM 713 CG TYR A 105 -17.923 -10.023 7.039 1.00 44.95 C
ANISOU 713 CG TYR A 105 6113 5691 5274 617 1052 83 C
ATOM 714 CD1 TYR A 105 -16.585 -10.410 7.020 1.00 46.19 C
ANISOU 714 CD1 TYR A 105 6364 5860 5327 598 1040 48 C
ATOM 715 CD2 TYR A 105 -18.391 -9.354 8.165 1.00 46.17 C
ANISOU 715 CD2 TYR A 105 6236 5839 5468 721 1108 26 C
ATOM 716 CE1 TYR A 105 -15.722 -10.080 8.064 1.00 46.86 C
ANISOU 716 CE1 TYR A 105 6508 5945 5353 675 1070 -32 C
ATOM 717 CE2 TYR A 105 -17.537 -9.014 9.212 1.00 46.95 C
ANISOU 717 CE2 TYR A 105 6397 5944 5498 799 1141 -64 C
ATOM 718 CZ TYR A 105 -16.205 -9.386 9.161 1.00 53.75 C
ANISOU 718 CZ TYR A 105 7351 6814 6258 774 1117 -89 C
ATOM 719 OH TYR A 105 -15.369 -9.059 10.199 1.00 54.80 O
ANISOU 719 OH TYR A 105 7546 6951 6326 848 1140 -173 O
ATOM 720 N PHE A 106 -20.669 -9.992 3.291 1.00 44.18 N
ANISOU 720 N PHE A 106 5792 5551 5444 355 842 364 N
ATOM 721 CA PHE A 106 -21.575 -10.500 2.257 1.00 44.52 C
ANISOU 721 CA PHE A 106 5781 5601 5535 261 792 454 C
ATOM 722 C PHE A 106 -20.970 -10.272 0.855 1.00 48.54 C
ANISOU 722 C PHE A 106 6313 6116 6012 155 677 497 C
ATOM 723 O PHE A 106 -20.774 -11.239 0.117 1.00 48.02 O
ANISOU 723 O PHE A 106 6286 6090 5869 70 659 517 O
ATOM 724 CB PHE A 106 -22.955 -9.821 2.411 1.00 47.34 C
ANISOU 724 CB PHE A 106 6020 5914 6051 295 787 503 C
ATOM 725 CG PHE A 106 -23.904 -9.817 1.233 1.00 49.48 C
ANISOU 725 CG PHE A 106 6216 6171 6413 199 696 608 C
ATOM 726 CD1 PHE A 106 -24.712 -10.914 0.966 1.00 52.86 C
ANISOU 726 CD1 PHE A 106 6624 6622 6839 143 711 661 C
ATOM 727 CD2 PHE A 106 -24.065 -8.676 0.455 1.00 52.15 C
ANISOU 727 CD2 PHE A 106 6495 6466 6852 167 591 660 C
ATOM 728 CE1 PHE A 106 -25.617 -10.893 -0.101 1.00 54.37 C
ANISOU 728 CE1 PHE A 106 6744 6798 7115 52 619 758 C
ATOM 729 CE2 PHE A 106 -24.967 -8.657 -0.612 1.00 55.54 C
ANISOU 729 CE2 PHE A 106 6852 6885 7366 74 499 766 C
ATOM 730 CZ PHE A 106 -25.744 -9.762 -0.877 1.00 53.79 C
ANISOU 730 CZ PHE A 106 6618 6690 7132 17 513 812 C
ATOM 731 N THR A 107 -20.603 -9.015 0.532 1.00 45.21 N
ANISOU 731 N THR A 107 5872 5660 5646 163 604 504 N
ATOM 732 CA THR A 107 -20.015 -8.628 -0.757 1.00 44.81 C
ANISOU 732 CA THR A 107 5834 5622 5569 68 495 555 C
ATOM 733 C THR A 107 -18.568 -9.128 -0.924 1.00 47.92 C
ANISOU 733 C THR A 107 6336 6057 5814 42 509 501 C
ATOM 734 O THR A 107 -18.108 -9.262 -2.062 1.00 47.39 O
ANISOU 734 O THR A 107 6293 6028 5687 -55 443 541 O
ATOM 735 CB THR A 107 -20.088 -7.112 -0.956 1.00 51.80 C
ANISOU 735 CB THR A 107 6653 6451 6577 91 414 588 C
ATOM 736 OG1 THR A 107 -19.516 -6.436 0.166 1.00 50.39 O
ANISOU 736 OG1 THR A 107 6501 6236 6410 201 462 500 O
ATOM 737 CG2 THR A 107 -21.500 -6.633 -1.199 1.00 50.76 C
ANISOU 737 CG2 THR A 107 6404 6275 6607 89 376 661 C
ATOM 738 N MET A 108 -17.862 -9.406 0.194 1.00 43.95 N
ANISOU 738 N MET A 108 5895 5550 5253 127 593 413 N
ATOM 739 CA MET A 108 -16.487 -9.914 0.184 1.00 43.04 C
ANISOU 739 CA MET A 108 5877 5463 5013 113 613 359 C
ATOM 740 C MET A 108 -16.444 -11.338 -0.388 1.00 46.44 C
ANISOU 740 C MET A 108 6348 5945 5351 31 638 364 C
ATOM 741 O MET A 108 -15.648 -11.605 -1.291 1.00 45.60 O
ANISOU 741 O MET A 108 6284 5871 5170 -45 599 368 O
ATOM 742 CB MET A 108 -15.882 -9.883 1.600 1.00 45.07 C
ANISOU 742 CB MET A 108 6183 5702 5240 222 695 272 C
ATOM 743 CG MET A 108 -14.431 -10.308 1.656 1.00 48.06 C
ANISOU 743 CG MET A 108 6655 6099 5509 212 713 221 C
ATOM 744 SD MET A 108 -14.006 -10.984 3.273 1.00 52.11 S
ANISOU 744 SD MET A 108 7226 6612 5962 312 823 136 S
ATOM 745 CE MET A 108 -12.448 -11.710 2.908 1.00 48.03 C
ANISOU 745 CE MET A 108 6800 6112 5336 265 824 104 C
ATOM 746 N TYR A 109 -17.315 -12.236 0.122 1.00 42.90 N
ANISOU 746 N TYR A 109 5880 5505 4916 47 702 363 N
ATOM 747 CA TYR A 109 -17.371 -13.630 -0.318 1.00 42.26 C
ANISOU 747 CA TYR A 109 5827 5461 4771 -22 727 362 C
ATOM 748 C TYR A 109 -18.069 -13.765 -1.680 1.00 46.79 C
ANISOU 748 C TYR A 109 6359 6056 5362 -131 644 430 C
ATOM 749 O TYR A 109 -17.858 -14.771 -2.362 1.00 46.12 O
ANISOU 749 O TYR A 109 6307 6006 5211 -206 640 418 O
ATOM 750 CB TYR A 109 -17.990 -14.529 0.761 1.00 42.95 C
ANISOU 750 CB TYR A 109 5901 5545 4874 36 820 346 C
ATOM 751 CG TYR A 109 -17.078 -14.629 1.965 1.00 43.45 C
ANISOU 751 CG TYR A 109 6023 5604 4883 121 896 277 C
ATOM 752 CD1 TYR A 109 -15.941 -15.431 1.938 1.00 44.64 C
ANISOU 752 CD1 TYR A 109 6248 5769 4942 98 921 230 C
ATOM 753 CD2 TYR A 109 -17.298 -13.849 3.096 1.00 44.23 C
ANISOU 753 CD2 TYR A 109 6101 5682 5021 223 936 255 C
ATOM 754 CE1 TYR A 109 -15.061 -15.475 3.017 1.00 44.85 C
ANISOU 754 CE1 TYR A 109 6328 5790 4922 170 977 176 C
ATOM 755 CE2 TYR A 109 -16.420 -13.878 4.178 1.00 44.70 C
ANISOU 755 CE2 TYR A 109 6220 5743 5020 297 994 192 C
ATOM 756 CZ TYR A 109 -15.303 -14.693 4.135 1.00 51.31 C
ANISOU 756 CZ TYR A 109 7131 6594 5770 268 1011 158 C
ATOM 757 OH TYR A 109 -14.455 -14.747 5.215 1.00 51.71 O
ANISOU 757 OH TYR A 109 7238 6645 5766 335 1061 104 O
ATOM 758 N ILE A 110 -18.828 -12.726 -2.108 1.00 43.99 N
ANISOU 758 N ILE A 110 5935 5683 5098 -144 571 498 N
ATOM 759 CA ILE A 110 -19.431 -12.666 -3.442 1.00 44.29 C
ANISOU 759 CA ILE A 110 5933 5746 5151 -254 475 574 C
ATOM 760 C ILE A 110 -18.274 -12.429 -4.425 1.00 48.64 C
ANISOU 760 C ILE A 110 6540 6340 5602 -325 417 567 C
ATOM 761 O ILE A 110 -18.156 -13.157 -5.411 1.00 48.55 O
ANISOU 761 O ILE A 110 6556 6380 5511 -422 384 572 O
ATOM 762 CB ILE A 110 -20.556 -11.589 -3.537 1.00 47.83 C
ANISOU 762 CB ILE A 110 6278 6153 5743 -244 413 658 C
ATOM 763 CG1 ILE A 110 -21.864 -12.123 -2.930 1.00 48.34 C
ANISOU 763 CG1 ILE A 110 6281 6192 5895 -208 465 679 C
ATOM 764 CG2 ILE A 110 -20.789 -11.126 -4.991 1.00 49.06 C
ANISOU 764 CG2 ILE A 110 6400 6337 5902 -361 288 746 C
ATOM 765 CD1 ILE A 110 -22.849 -11.082 -2.528 1.00 54.78 C
ANISOU 765 CD1 ILE A 110 6996 6951 6865 -156 446 732 C
ATOM 766 N SER A 111 -17.391 -11.450 -4.103 1.00 45.09 N
ANISOU 766 N SER A 111 6109 5869 5155 -272 411 549 N
ATOM 767 CA SER A 111 -16.204 -11.083 -4.880 1.00 44.78 C
ANISOU 767 CA SER A 111 6117 5864 5032 -323 367 547 C
ATOM 768 C SER A 111 -15.237 -12.264 -5.021 1.00 47.80 C
ANISOU 768 C SER A 111 6587 6289 5284 -352 427 470 C
ATOM 769 O SER A 111 -14.719 -12.480 -6.114 1.00 47.41 O
ANISOU 769 O SER A 111 6566 6298 5149 -443 388 479 O
ATOM 770 CB SER A 111 -15.488 -9.899 -4.239 1.00 48.53 C
ANISOU 770 CB SER A 111 6591 6292 5558 -242 359 535 C
ATOM 771 OG SER A 111 -16.322 -8.753 -4.193 1.00 58.98 O
ANISOU 771 OG SER A 111 7825 7566 7017 -214 301 599 O
ATOM 772 N ILE A 112 -15.026 -13.043 -3.932 1.00 43.64 N
ANISOU 772 N ILE A 112 6097 5737 4747 -279 522 397 N
ATOM 773 CA ILE A 112 -14.152 -14.226 -3.911 1.00 42.70 C
ANISOU 773 CA ILE A 112 6049 5642 4531 -297 585 322 C
ATOM 774 C ILE A 112 -14.728 -15.302 -4.856 1.00 46.17 C
ANISOU 774 C ILE A 112 6485 6126 4932 -395 569 327 C
ATOM 775 O ILE A 112 -13.990 -15.824 -5.696 1.00 45.77 O
ANISOU 775 O ILE A 112 6479 6119 4791 -465 563 292 O
ATOM 776 CB ILE A 112 -13.939 -14.758 -2.454 1.00 45.25 C
ANISOU 776 CB ILE A 112 6399 5925 4871 -196 681 263 C
ATOM 777 CG1 ILE A 112 -13.135 -13.748 -1.611 1.00 45.36 C
ANISOU 777 CG1 ILE A 112 6433 5902 4901 -109 691 240 C
ATOM 778 CG2 ILE A 112 -13.240 -16.124 -2.441 1.00 45.51 C
ANISOU 778 CG2 ILE A 112 6487 5973 4831 -222 742 198 C
ATOM 779 CD1 ILE A 112 -13.310 -13.861 -0.102 1.00 52.84 C
ANISOU 779 CD1 ILE A 112 7380 6813 5882 -1 765 205 C
ATOM 780 N SER A 113 -16.045 -15.596 -4.731 1.00 42.38 N
ANISOU 780 N SER A 113 5947 5632 4524 -399 560 369 N
ATOM 781 CA SER A 113 -16.766 -16.585 -5.539 1.00 42.27 C
ANISOU 781 CA SER A 113 5918 5648 4493 -486 535 377 C
ATOM 782 C SER A 113 -16.681 -16.272 -7.033 1.00 45.26 C
ANISOU 782 C SER A 113 6299 6089 4810 -600 441 414 C
ATOM 783 O SER A 113 -16.409 -17.179 -7.821 1.00 45.07 O
ANISOU 783 O SER A 113 6308 6110 4708 -679 434 371 O
ATOM 784 CB SER A 113 -18.228 -16.671 -5.111 1.00 46.68 C
ANISOU 784 CB SER A 113 6402 6173 5162 -462 533 434 C
ATOM 785 OG SER A 113 -18.342 -17.063 -3.753 1.00 56.44 O
ANISOU 785 OG SER A 113 7637 7368 6441 -365 626 403 O
ATOM 786 N PHE A 114 -16.883 -14.993 -7.416 1.00 41.22 N
ANISOU 786 N PHE A 114 5749 5582 4332 -611 368 491 N
ATOM 787 CA PHE A 114 -16.817 -14.558 -8.811 1.00 41.25 C
ANISOU 787 CA PHE A 114 5748 5654 4272 -722 272 544 C
ATOM 788 C PHE A 114 -15.377 -14.571 -9.322 1.00 44.52 C
ANISOU 788 C PHE A 114 6231 6120 4563 -752 289 493 C
ATOM 789 O PHE A 114 -15.170 -14.896 -10.490 1.00 44.70 O
ANISOU 789 O PHE A 114 6277 6220 4486 -854 247 492 O
ATOM 790 CB PHE A 114 -17.462 -13.178 -9.010 1.00 43.41 C
ANISOU 790 CB PHE A 114 5945 5909 4639 -726 183 658 C
ATOM 791 CG PHE A 114 -18.964 -13.234 -9.172 1.00 45.51 C
ANISOU 791 CG PHE A 114 6136 6154 5002 -755 131 729 C
ATOM 792 CD1 PHE A 114 -19.538 -13.594 -10.386 1.00 49.28 C
ANISOU 792 CD1 PHE A 114 6603 6692 5430 -875 51 772 C
ATOM 793 CD2 PHE A 114 -19.806 -12.936 -8.108 1.00 47.55 C
ANISOU 793 CD2 PHE A 114 6332 6335 5401 -664 162 752 C
ATOM 794 CE1 PHE A 114 -20.927 -13.660 -10.530 1.00 50.84 C
ANISOU 794 CE1 PHE A 114 6726 6862 5727 -905 -3 844 C
ATOM 795 CE2 PHE A 114 -21.194 -13.000 -8.252 1.00 51.04 C
ANISOU 795 CE2 PHE A 114 6697 6753 5944 -691 117 824 C
ATOM 796 CZ PHE A 114 -21.745 -13.367 -9.460 1.00 49.84 C
ANISOU 796 CZ PHE A 114 6534 6652 5752 -811 31 872 C
ATOM 797 N LEU A 115 -14.385 -14.281 -8.444 1.00 39.97 N
ANISOU 797 N LEU A 115 5691 5505 3991 -664 353 445 N
ATOM 798 CA LEU A 115 -12.960 -14.320 -8.797 1.00 39.25 C
ANISOU 798 CA LEU A 115 5663 5452 3800 -681 379 395 C
ATOM 799 C LEU A 115 -12.537 -15.742 -9.167 1.00 43.32 C
ANISOU 799 C LEU A 115 6233 6005 4222 -730 436 300 C
ATOM 800 O LEU A 115 -11.720 -15.913 -10.067 1.00 43.28 O
ANISOU 800 O LEU A 115 6265 6065 4114 -798 431 273 O
ATOM 801 CB LEU A 115 -12.066 -13.777 -7.669 1.00 38.41 C
ANISOU 801 CB LEU A 115 5579 5282 3735 -572 432 364 C
ATOM 802 CG LEU A 115 -11.820 -12.265 -7.658 1.00 42.93 C
ANISOU 802 CG LEU A 115 6117 5836 4360 -546 370 436 C
ATOM 803 CD1 LEU A 115 -11.360 -11.804 -6.292 1.00 42.37 C
ANISOU 803 CD1 LEU A 115 6054 5684 4359 -424 417 400 C
ATOM 804 CD2 LEU A 115 -10.808 -11.852 -8.715 1.00 45.42 C
ANISOU 804 CD2 LEU A 115 6457 6216 4586 -617 335 457 C
ATOM 805 N GLY A 116 -13.123 -16.733 -8.493 1.00 39.88 N
ANISOU 805 N GLY A 116 5795 5527 3830 -696 488 254 N
ATOM 806 CA GLY A 116 -12.888 -18.150 -8.751 1.00 39.81 C
ANISOU 806 CA GLY A 116 5824 5536 3767 -737 536 164 C
ATOM 807 C GLY A 116 -13.478 -18.587 -10.076 1.00 44.69 C
ANISOU 807 C GLY A 116 6432 6224 4324 -854 471 171 C
ATOM 808 O GLY A 116 -12.840 -19.337 -10.819 1.00 44.35 O
ANISOU 808 O GLY A 116 6431 6230 4190 -918 489 93 O
ATOM 809 N LEU A 117 -14.696 -18.096 -10.389 1.00 42.30 N
ANISOU 809 N LEU A 117 6072 5926 4073 -885 392 262 N
ATOM 810 CA LEU A 117 -15.408 -18.382 -11.638 1.00 43.36 C
ANISOU 810 CA LEU A 117 6190 6128 4156 -1001 310 287 C
ATOM 811 C LEU A 117 -14.705 -17.758 -12.842 1.00 48.56 C
ANISOU 811 C LEU A 117 6875 6885 4690 -1088 257 308 C
ATOM 812 O LEU A 117 -14.678 -18.372 -13.910 1.00 48.60 O
ANISOU 812 O LEU A 117 6906 6968 4593 -1186 229 266 O
ATOM 813 CB LEU A 117 -16.863 -17.889 -11.572 1.00 43.80 C
ANISOU 813 CB LEU A 117 6170 6153 4318 -1005 237 394 C
ATOM 814 CG LEU A 117 -17.866 -18.789 -10.853 1.00 48.24 C
ANISOU 814 CG LEU A 117 6698 6647 4986 -964 269 381 C
ATOM 815 CD1 LEU A 117 -19.208 -18.113 -10.759 1.00 48.79 C
ANISOU 815 CD1 LEU A 117 6686 6693 5157 -981 189 493 C
ATOM 816 CD2 LEU A 117 -18.036 -20.118 -11.574 1.00 51.40 C
ANISOU 816 CD2 LEU A 117 7129 7070 5331 -1029 281 291 C
ATOM 817 N ILE A 118 -14.136 -16.543 -12.663 1.00 45.80 N
ANISOU 817 N ILE A 118 6517 6535 4351 -1052 243 373 N
ATOM 818 CA ILE A 118 -13.384 -15.804 -13.685 1.00 46.47 C
ANISOU 818 CA ILE A 118 6616 6709 4330 -1123 196 413 C
ATOM 819 C ILE A 118 -12.105 -16.603 -14.026 1.00 51.74 C
ANISOU 819 C ILE A 118 7356 7426 4876 -1144 275 295 C
ATOM 820 O ILE A 118 -11.754 -16.711 -15.203 1.00 52.02 O
ANISOU 820 O ILE A 118 7415 7568 4784 -1243 247 284 O
ATOM 821 CB ILE A 118 -13.102 -14.338 -13.219 1.00 49.01 C
ANISOU 821 CB ILE A 118 6902 6992 4727 -1062 166 509 C
ATOM 822 CG1 ILE A 118 -14.381 -13.478 -13.345 1.00 49.77 C
ANISOU 822 CG1 ILE A 118 6917 7068 4927 -1080 65 637 C
ATOM 823 CG2 ILE A 118 -11.946 -13.686 -14.000 1.00 49.92 C
ANISOU 823 CG2 ILE A 118 7042 7186 4741 -1109 152 533 C
ATOM 824 CD1 ILE A 118 -14.460 -12.245 -12.435 1.00 55.51 C
ANISOU 824 CD1 ILE A 118 7592 7704 5795 -980 54 701 C
ATOM 825 N THR A 119 -11.460 -17.208 -13.002 1.00 48.77 N
ANISOU 825 N THR A 119 7012 6976 4542 -1054 373 207 N
ATOM 826 CA THR A 119 -10.254 -18.029 -13.153 1.00 49.14 C
ANISOU 826 CA THR A 119 7118 7045 4507 -1059 457 91 C
ATOM 827 C THR A 119 -10.566 -19.289 -13.984 1.00 55.48 C
ANISOU 827 C THR A 119 7944 7902 5235 -1144 463 -2 C
ATOM 828 O THR A 119 -9.768 -19.636 -14.855 1.00 55.62 O
ANISOU 828 O THR A 119 7997 8002 5133 -1210 482 -64 O
ATOM 829 CB THR A 119 -9.647 -18.386 -11.783 1.00 56.55 C
ANISOU 829 CB THR A 119 8076 7881 5531 -944 546 34 C
ATOM 830 OG1 THR A 119 -9.657 -17.237 -10.939 1.00 56.23 O
ANISOU 830 OG1 THR A 119 8009 7786 5568 -865 528 115 O
ATOM 831 CG2 THR A 119 -8.218 -18.895 -11.892 1.00 55.04 C
ANISOU 831 CG2 THR A 119 7935 7701 5276 -942 626 -66 C
ATOM 832 N ILE A 120 -11.728 -19.947 -13.736 1.00 53.49 N
ANISOU 832 N ILE A 120 7666 7605 5054 -1143 445 -11 N
ATOM 833 CA ILE A 120 -12.164 -21.150 -14.464 1.00 54.63 C
ANISOU 833 CA ILE A 120 7822 7785 5151 -1220 437 -99 C
ATOM 834 C ILE A 120 -12.486 -20.780 -15.924 1.00 61.12 C
ANISOU 834 C ILE A 120 8645 8730 5847 -1344 347 -61 C
ATOM 835 O ILE A 120 -11.969 -21.431 -16.834 1.00 61.54 O
ANISOU 835 O ILE A 120 8737 8862 5782 -1418 363 -157 O
ATOM 836 CB ILE A 120 -13.361 -21.870 -13.762 1.00 57.57 C
ANISOU 836 CB ILE A 120 8155 8072 5649 -1187 428 -93 C
ATOM 837 CG1 ILE A 120 -12.918 -22.509 -12.426 1.00 57.09 C
ANISOU 837 CG1 ILE A 120 8102 7910 5680 -1086 528 -159 C
ATOM 838 CG2 ILE A 120 -14.013 -22.928 -14.681 1.00 59.13 C
ANISOU 838 CG2 ILE A 120 8349 8311 5806 -1285 377 -150 C
ATOM 839 CD1 ILE A 120 -14.059 -22.828 -11.435 1.00 64.05 C
ANISOU 839 CD1 ILE A 120 8932 8702 6702 -1026 529 -114 C
ATOM 840 N ASP A 121 -13.315 -19.732 -16.136 1.00 58.92 N
ANISOU 840 N ASP A 121 8322 8470 5597 -1367 254 78 N
ATOM 841 CA ASP A 121 -13.729 -19.252 -17.458 1.00 60.37 C
ANISOU 841 CA ASP A 121 8496 8770 5673 -1486 152 145 C
ATOM 842 C ASP A 121 -12.522 -18.921 -18.340 1.00 65.68 C
ANISOU 842 C ASP A 121 9209 9555 6189 -1541 170 127 C
ATOM 843 O ASP A 121 -12.469 -19.388 -19.477 1.00 66.33 O
ANISOU 843 O ASP A 121 9320 9752 6132 -1648 140 83 O
ATOM 844 CB ASP A 121 -14.653 -18.026 -17.336 1.00 62.37 C
ANISOU 844 CB ASP A 121 8681 8999 6018 -1483 54 312 C
ATOM 845 CG ASP A 121 -15.136 -17.486 -18.669 1.00 74.91 C
ANISOU 845 CG ASP A 121 10252 10706 7504 -1609 -62 406 C
ATOM 846 OD1 ASP A 121 -16.012 -18.129 -19.288 1.00 76.75 O
ANISOU 846 OD1 ASP A 121 10481 10980 7701 -1693 -126 394 O
ATOM 847 OD2 ASP A 121 -14.628 -16.430 -19.100 1.00 81.19 O
ANISOU 847 OD2 ASP A 121 11036 11555 8256 -1627 -93 495 O
ATOM 848 N ARG A 122 -11.549 -18.155 -17.808 1.00 62.23 N
ANISOU 848 N ARG A 122 8778 9091 5777 -1470 220 157 N
ATOM 849 CA ARG A 122 -10.347 -17.750 -18.541 1.00 62.67 C
ANISOU 849 CA ARG A 122 8863 9246 5701 -1513 244 154 C
ATOM 850 C ARG A 122 -9.382 -18.927 -18.782 1.00 67.21 C
ANISOU 850 C ARG A 122 9498 9850 6187 -1521 350 -14 C
ATOM 851 O ARG A 122 -8.642 -18.897 -19.769 1.00 67.45 O
ANISOU 851 O ARG A 122 9557 9998 6075 -1591 366 -40 O
ATOM 852 CB ARG A 122 -9.633 -16.589 -17.833 1.00 62.05 C
ANISOU 852 CB ARG A 122 8762 9116 5696 -1433 254 247 C
ATOM 853 CG ARG A 122 -10.335 -15.241 -18.024 1.00 73.71 C
ANISOU 853 CG ARG A 122 10176 10612 7217 -1463 138 421 C
ATOM 854 CD ARG A 122 -9.978 -14.593 -19.353 1.00 87.91 C
ANISOU 854 CD ARG A 122 11974 12563 8865 -1581 78 494 C
ATOM 855 NE ARG A 122 -11.139 -13.989 -20.012 1.00 99.76 N
ANISOU 855 NE ARG A 122 13421 14112 10373 -1662 -53 629 N
ATOM 856 CZ ARG A 122 -11.889 -14.604 -20.921 1.00115.94 C
ANISOU 856 CZ ARG A 122 15477 16238 12338 -1762 -109 612 C
ATOM 857 NH1 ARG A 122 -11.620 -15.851 -21.283 1.00104.42 N
ANISOU 857 NH1 ARG A 122 14077 14815 10783 -1789 -44 457 N
ATOM 858 NH2 ARG A 122 -12.917 -13.975 -21.475 1.00103.60 N
ANISOU 858 NH2 ARG A 122 13858 14711 10793 -1836 -235 751 N
ATOM 859 N TYR A 123 -9.407 -19.964 -17.915 1.00 63.61 N
ANISOU 859 N TYR A 123 9057 9293 5819 -1454 421 -125 N
ATOM 860 CA TYR A 123 -8.574 -21.160 -18.082 1.00 63.76 C
ANISOU 860 CA TYR A 123 9122 9320 5786 -1458 517 -290 C
ATOM 861 C TYR A 123 -9.134 -22.041 -19.207 1.00 69.52 C
ANISOU 861 C TYR A 123 9869 10141 6406 -1568 484 -380 C
ATOM 862 O TYR A 123 -8.359 -22.641 -19.953 1.00 69.94 O
ANISOU 862 O TYR A 123 9959 10272 6343 -1618 539 -493 O
ATOM 863 CB TYR A 123 -8.448 -21.963 -16.769 1.00 63.89 C
ANISOU 863 CB TYR A 123 9138 9192 5948 -1352 594 -363 C
ATOM 864 CG TYR A 123 -7.747 -23.294 -16.940 1.00 65.98 C
ANISOU 864 CG TYR A 123 9434 9446 6188 -1363 680 -533 C
ATOM 865 CD1 TYR A 123 -6.384 -23.357 -17.217 1.00 68.02 C
ANISOU 865 CD1 TYR A 123 9723 9736 6384 -1358 763 -606 C
ATOM 866 CD2 TYR A 123 -8.454 -24.490 -16.882 1.00 67.09 C
ANISOU 866 CD2 TYR A 123 9568 9543 6380 -1380 677 -622 C
ATOM 867 CE1 TYR A 123 -5.741 -24.576 -17.419 1.00 69.06 C
ANISOU 867 CE1 TYR A 123 9877 9855 6507 -1369 842 -768 C
ATOM 868 CE2 TYR A 123 -7.821 -25.717 -17.078 1.00 68.36 C
ANISOU 868 CE2 TYR A 123 9750 9689 6536 -1392 750 -783 C
ATOM 869 CZ TYR A 123 -6.462 -25.755 -17.345 1.00 75.36 C
ANISOU 869 CZ TYR A 123 10667 10606 7363 -1386 835 -859 C
ATOM 870 OH TYR A 123 -5.830 -26.958 -17.540 1.00 76.40 O
ANISOU 870 OH TYR A 123 10811 10714 7504 -1395 909 -1024 O
ATOM 871 N GLN A 124 -10.475 -22.117 -19.323 1.00 66.86 N
ANISOU 871 N GLN A 124 9503 9790 6111 -1604 396 -333 N
ATOM 872 CA GLN A 124 -11.167 -22.905 -20.348 1.00 68.20 C
ANISOU 872 CA GLN A 124 9685 10035 6192 -1708 344 -410 C
ATOM 873 C GLN A 124 -10.944 -22.322 -21.754 1.00 73.96 C
ANISOU 873 C GLN A 124 10435 10940 6726 -1828 288 -376 C
ATOM 874 O GLN A 124 -10.986 -23.070 -22.733 1.00 74.78 O
ANISOU 874 O GLN A 124 10569 11135 6708 -1917 276 -483 O
ATOM 875 CB GLN A 124 -12.672 -23.003 -20.043 1.00 69.62 C
ANISOU 875 CB GLN A 124 9820 10147 6484 -1712 255 -342 C
ATOM 876 CG GLN A 124 -12.997 -23.867 -18.828 1.00 84.23 C
ANISOU 876 CG GLN A 124 11652 11847 8505 -1617 313 -401 C
ATOM 877 CD GLN A 124 -14.468 -24.169 -18.710 1.00103.06 C
ANISOU 877 CD GLN A 124 13990 14177 10990 -1633 231 -349 C
ATOM 878 OE1 GLN A 124 -15.254 -23.364 -18.203 1.00 97.99 O
ANISOU 878 OE1 GLN A 124 13301 13488 10442 -1596 180 -211 O
ATOM 879 NE2 GLN A 124 -14.867 -25.352 -19.154 1.00 95.73 N
ANISOU 879 NE2 GLN A 124 13069 13245 10058 -1684 216 -461 N
ATOM 880 N LYS A 125 -10.694 -20.998 -21.848 1.00 70.78 N
ANISOU 880 N LYS A 125 10014 10586 6294 -1829 252 -228 N
ATOM 881 CA LYS A 125 -10.448 -20.295 -23.109 1.00 72.01 C
ANISOU 881 CA LYS A 125 10179 10911 6271 -1940 196 -162 C
ATOM 882 C LYS A 125 -9.001 -20.481 -23.602 1.00 76.69 C
ANISOU 882 C LYS A 125 10817 11594 6728 -1953 300 -260 C
ATOM 883 O LYS A 125 -8.744 -20.283 -24.791 1.00 77.71 O
ANISOU 883 O LYS A 125 10964 11886 6676 -2058 275 -254 O
ATOM 884 CB LYS A 125 -10.782 -18.798 -22.977 1.00 74.26 C
ANISOU 884 CB LYS A 125 10410 11197 6606 -1934 109 49 C
ATOM 885 CG LYS A 125 -12.147 -18.415 -23.554 1.00 89.97 C
ANISOU 885 CG LYS A 125 12360 13229 8594 -2020 -36 169 C
ATOM 886 CD LYS A 125 -13.294 -18.637 -22.568 1.00 99.67 C
ANISOU 886 CD LYS A 125 13551 14310 10010 -1956 -70 186 C
ATOM 887 CE LYS A 125 -14.637 -18.252 -23.136 1.00111.35 C
ANISOU 887 CE LYS A 125 14976 15811 11521 -2029 -215 334 C
ATOM 888 NZ LYS A 125 -15.721 -18.407 -22.130 1.00118.89 N
ANISOU 888 NZ LYS A 125 15886 16619 12666 -1960 -236 352 N
ATOM 889 N THR A 126 -8.067 -20.863 -22.707 1.00 72.37 N
ANISOU 889 N THR A 126 10283 10946 6267 -1851 416 -347 N
ATOM 890 CA THR A 126 -6.664 -21.098 -23.077 1.00 72.61 C
ANISOU 890 CA THR A 126 10349 11042 6197 -1853 525 -446 C
ATOM 891 C THR A 126 -6.482 -22.523 -23.612 1.00 77.72 C
ANISOU 891 C THR A 126 11036 11724 6769 -1898 587 -654 C
ATOM 892 O THR A 126 -5.556 -22.773 -24.385 1.00 78.37 O
ANISOU 892 O THR A 126 11149 11919 6710 -1947 654 -746 O
ATOM 893 CB THR A 126 -5.711 -20.830 -21.900 1.00 80.19 C
ANISOU 893 CB THR A 126 11303 11875 7292 -1729 614 -440 C
ATOM 894 OG1 THR A 126 -6.049 -21.672 -20.798 1.00 79.10 O
ANISOU 894 OG1 THR A 126 11164 11584 7305 -1646 657 -531 O
ATOM 895 CG2 THR A 126 -5.688 -19.367 -21.475 1.00 78.49 C
ANISOU 895 CG2 THR A 126 11048 11625 7151 -1683 555 -250 C
ATOM 896 N THR A 127 -7.369 -23.448 -23.200 1.00 74.25 N
ANISOU 896 N THR A 127 10591 11186 6433 -1879 565 -729 N
ATOM 897 CA THR A 127 -7.343 -24.858 -23.599 1.00 75.03 C
ANISOU 897 CA THR A 127 10718 11289 6502 -1914 609 -929 C
ATOM 898 C THR A 127 -7.976 -25.083 -24.985 1.00 80.79 C
ANISOU 898 C THR A 127 11468 12176 7054 -2050 527 -965 C
ATOM 899 O THR A 127 -7.560 -26.008 -25.686 1.00 81.50 O
ANISOU 899 O THR A 127 11589 12325 7051 -2100 575 -1143 O
ATOM 900 CB THR A 127 -8.033 -25.735 -22.543 1.00 82.92 C
ANISOU 900 CB THR A 127 11692 12114 7698 -1839 610 -977 C
ATOM 901 OG1 THR A 127 -9.316 -25.187 -22.228 1.00 82.81 O
ANISOU 901 OG1 THR A 127 11643 12059 7761 -1837 499 -827 O
ATOM 902 CG2 THR A 127 -7.203 -25.890 -21.273 1.00 80.14 C
ANISOU 902 CG2 THR A 127 11331 11621 7496 -1716 713 -1001 C
ATOM 903 N ARG A 128 -8.972 -24.254 -25.376 1.00 77.74 N
ANISOU 903 N ARG A 128 11061 11855 6622 -2110 401 -801 N
ATOM 904 CA ARG A 128 -9.662 -24.372 -26.668 1.00113.13 C
ANISOU 904 CA ARG A 128 15561 16491 10932 -2246 305 -811 C
ATOM 905 C ARG A 128 -8.754 -23.914 -27.820 1.00145.64 C
ANISOU 905 C ARG A 128 19710 20805 14821 -2329 337 -811 C
ATOM 906 O ARG A 128 -8.947 -24.328 -28.962 1.00109.28 O
ANISOU 906 O ARG A 128 15140 16345 10036 -2437 314 -907 O
ATOM 907 CB ARG A 128 -10.996 -23.591 -26.676 1.00113.61 C
ANISOU 907 CB ARG A 128 15581 16541 11046 -2283 154 -624 C
ATOM 908 CG ARG A 128 -10.863 -22.070 -26.603 1.00124.35 C
ANISOU 908 CG ARG A 128 16906 17938 12403 -2278 104 -405 C
ATOM 909 CD ARG A 128 -11.996 -21.358 -27.316 1.00136.52 C
ANISOU 909 CD ARG A 128 18419 19567 13886 -2383 -54 -251 C
ATOM 910 NE ARG A 128 -13.152 -21.143 -26.444 1.00145.05 N
ANISOU 910 NE ARG A 128 19442 20501 15168 -2328 -133 -133 N
ATOM 911 CZ ARG A 128 -14.234 -20.449 -26.788 1.00160.17 C
ANISOU 911 CZ ARG A 128 21315 22447 17096 -2396 -274 25 C
ATOM 912 NH1 ARG A 128 -15.235 -20.303 -25.930 1.00146.84 N
ANISOU 912 NH1 ARG A 128 19570 20617 15606 -2336 -328 119 N
ATOM 913 NH2 ARG A 128 -14.323 -19.896 -27.992 1.00148.28 N
ANISOU 913 NH2 ARG A 128 19817 21115 15405 -2528 -360 94 N
ATOM 914 N PRO A 135 -28.308 -17.606 -25.425 1.00 99.21 N
ANISOU 914 N PRO A 135 12821 13926 10946 -2588 -1468 1359 N
ATOM 915 CA PRO A 135 -27.384 -18.736 -25.590 1.00 98.75 C
ANISOU 915 CA PRO A 135 12871 13936 10712 -2589 -1372 1150 C
ATOM 916 C PRO A 135 -27.325 -19.625 -24.349 1.00100.82 C
ANISOU 916 C PRO A 135 13140 14062 11105 -2453 -1233 1020 C
ATOM 917 O PRO A 135 -27.537 -19.143 -23.234 1.00 99.22 O
ANISOU 917 O PRO A 135 12879 13738 11081 -2332 -1164 1077 O
ATOM 918 CB PRO A 135 -26.037 -18.056 -25.850 1.00100.15 C
ANISOU 918 CB PRO A 135 13104 14222 10728 -2584 -1305 1135 C
ATOM 919 N LYS A 136 -27.027 -20.925 -24.553 1.00 97.22 N
ANISOU 919 N LYS A 136 12751 13628 10558 -2475 -1193 845 N
ATOM 920 CA LYS A 136 -26.910 -21.935 -23.495 1.00 95.71 C
ANISOU 920 CA LYS A 136 12569 13320 10476 -2364 -1070 714 C
ATOM 921 C LYS A 136 -25.673 -21.686 -22.623 1.00 97.20 C
ANISOU 921 C LYS A 136 12796 13487 10647 -2243 -908 643 C
ATOM 922 O LYS A 136 -25.707 -21.957 -21.420 1.00 95.72 O
ANISOU 922 O LYS A 136 12583 13179 10606 -2122 -807 614 O
ATOM 923 CB LYS A 136 -26.853 -23.344 -24.102 1.00 99.12 C
ANISOU 923 CB LYS A 136 13061 13791 10808 -2434 -1085 544 C
ATOM 924 N ASN A 137 -24.589 -21.167 -23.235 1.00 92.85 N
ANISOU 924 N ASN A 137 12304 13058 9918 -2279 -885 622 N
ATOM 925 CA ASN A 137 -23.326 -20.848 -22.563 1.00 90.88 C
ANISOU 925 CA ASN A 137 12093 12800 9638 -2178 -745 563 C
ATOM 926 C ASN A 137 -23.498 -19.635 -21.637 1.00 92.35 C
ANISOU 926 C ASN A 137 12211 12903 9975 -2083 -728 709 C
ATOM 927 O ASN A 137 -23.009 -19.657 -20.505 1.00 90.63 O
ANISOU 927 O ASN A 137 11996 12601 9839 -1959 -609 665 O
ATOM 928 CB ASN A 137 -22.192 -20.593 -23.576 1.00 92.30 C
ANISOU 928 CB ASN A 137 12347 13139 9583 -2254 -734 507 C
ATOM 929 CG ASN A 137 -22.572 -20.760 -25.031 1.00116.04 C
ANISOU 929 CG ASN A 137 15378 16289 12424 -2416 -862 518 C
ATOM 930 OD1 ASN A 137 -22.655 -21.876 -25.554 1.00110.56 O
ANISOU 930 OD1 ASN A 137 14723 15627 11656 -2476 -880 389 O
ATOM 931 ND2 ASN A 137 -22.811 -19.650 -25.713 1.00108.45 N
ANISOU 931 ND2 ASN A 137 14389 15418 11398 -2491 -959 673 N
ATOM 932 N LEU A 138 -24.210 -18.590 -22.117 1.00 88.38 N
ANISOU 932 N LEU A 138 11645 12423 9513 -2144 -851 880 N
ATOM 933 CA LEU A 138 -24.468 -17.356 -21.368 1.00 86.86 C
ANISOU 933 CA LEU A 138 11376 12151 9477 -2065 -853 1022 C
ATOM 934 C LEU A 138 -25.498 -17.567 -20.253 1.00 88.25 C
ANISOU 934 C LEU A 138 11480 12172 9879 -1967 -823 1050 C
ATOM 935 O LEU A 138 -25.410 -16.892 -19.227 1.00 86.85 O
ANISOU 935 O LEU A 138 11263 11909 9828 -1853 -755 1090 O
ATOM 936 CB LEU A 138 -24.930 -16.219 -22.300 1.00 88.03 C
ANISOU 936 CB LEU A 138 11469 12367 9612 -2169 -1003 1199 C
ATOM 937 CG LEU A 138 -23.908 -15.676 -23.311 1.00 93.33 C
ANISOU 937 CG LEU A 138 12189 13192 10082 -2256 -1034 1222 C
ATOM 938 CD1 LEU A 138 -24.586 -14.819 -24.356 1.00 94.86 C
ANISOU 938 CD1 LEU A 138 12316 13449 10278 -2373 -1201 1412 C
ATOM 939 CD2 LEU A 138 -22.810 -14.872 -22.631 1.00 94.47 C
ANISOU 939 CD2 LEU A 138 12349 13316 10232 -2153 -927 1207 C
ATOM 940 N LEU A 139 -26.466 -18.494 -20.451 1.00 84.05 N
ANISOU 940 N LEU A 139 10929 11608 9397 -2011 -873 1029 N
ATOM 941 CA LEU A 139 -27.508 -18.824 -19.469 1.00 82.84 C
ANISOU 941 CA LEU A 139 10702 11317 9455 -1929 -847 1060 C
ATOM 942 C LEU A 139 -26.889 -19.445 -18.208 1.00 83.70 C
ANISOU 942 C LEU A 139 10842 11351 9608 -1793 -683 941 C
ATOM 943 O LEU A 139 -27.363 -19.176 -17.102 1.00 82.58 O
ANISOU 943 O LEU A 139 10639 11104 9632 -1687 -623 986 O
ATOM 944 CB LEU A 139 -28.556 -19.776 -20.078 1.00 84.02 C
ANISOU 944 CB LEU A 139 10832 11460 9633 -2019 -944 1057 C
ATOM 945 CG LEU A 139 -29.851 -19.976 -19.278 1.00 88.85 C
ANISOU 945 CG LEU A 139 11345 11939 10476 -1961 -952 1134 C
ATOM 946 CD1 LEU A 139 -30.907 -18.951 -19.667 1.00 89.86 C
ANISOU 946 CD1 LEU A 139 11375 12041 10725 -2005 -1075 1321 C
ATOM 947 CD2 LEU A 139 -30.396 -21.376 -19.470 1.00 92.02 C
ANISOU 947 CD2 LEU A 139 11754 12317 10894 -2011 -986 1060 C
ATOM 948 N GLY A 140 -25.838 -20.248 -18.398 1.00 78.60 N
ANISOU 948 N GLY A 140 10288 10763 8815 -1801 -613 792 N
ATOM 949 CA GLY A 140 -25.095 -20.896 -17.323 1.00 76.53 C
ANISOU 949 CA GLY A 140 10062 10442 8575 -1688 -465 676 C
ATOM 950 C GLY A 140 -24.420 -19.897 -16.405 1.00 77.36 C
ANISOU 950 C GLY A 140 10159 10512 8720 -1578 -382 715 C
ATOM 951 O GLY A 140 -24.487 -20.041 -15.183 1.00 76.04 O
ANISOU 951 O GLY A 140 9969 10256 8668 -1464 -288 701 O
ATOM 952 N ALA A 141 -23.795 -18.857 -16.992 1.00 72.55 N
ANISOU 952 N ALA A 141 9565 9977 8022 -1616 -425 771 N
ATOM 953 CA ALA A 141 -23.120 -17.782 -16.262 1.00 70.77 C
ANISOU 953 CA ALA A 141 9330 9725 7835 -1526 -370 815 C
ATOM 954 C ALA A 141 -24.124 -16.893 -15.528 1.00 72.71 C
ANISOU 954 C ALA A 141 9477 9877 8273 -1462 -398 941 C
ATOM 955 O ALA A 141 -23.818 -16.405 -14.438 1.00 71.44 O
ANISOU 955 O ALA A 141 9301 9652 8192 -1348 -318 941 O
ATOM 956 CB ALA A 141 -22.292 -16.942 -17.218 1.00 71.90 C
ANISOU 956 CB ALA A 141 9504 9975 7840 -1600 -426 854 C
ATOM 957 N LYS A 142 -25.316 -16.689 -16.125 1.00 68.79 N
ANISOU 957 N LYS A 142 8913 9374 7852 -1536 -512 1044 N
ATOM 958 CA LYS A 142 -26.386 -15.868 -15.558 1.00 68.05 C
ANISOU 958 CA LYS A 142 8713 9190 7954 -1487 -547 1169 C
ATOM 959 C LYS A 142 -27.065 -16.562 -14.373 1.00 70.12 C
ANISOU 959 C LYS A 142 8937 9349 8357 -1385 -456 1134 C
ATOM 960 O LYS A 142 -27.386 -15.883 -13.398 1.00 69.25 O
ANISOU 960 O LYS A 142 8766 9161 8385 -1284 -407 1180 O
ATOM 961 CB LYS A 142 -27.428 -15.492 -16.623 1.00 71.63 C
ANISOU 961 CB LYS A 142 9101 9670 8444 -1609 -707 1299 C
ATOM 962 CG LYS A 142 -26.960 -14.389 -17.569 1.00 83.99 C
ANISOU 962 CG LYS A 142 10668 11321 9922 -1693 -804 1387 C
ATOM 963 CD LYS A 142 -28.101 -13.487 -18.024 1.00 94.29 C
ANISOU 963 CD LYS A 142 11862 12594 11369 -1750 -940 1562 C
ATOM 964 CE LYS A 142 -28.174 -12.209 -17.219 1.00104.74 C
ANISOU 964 CE LYS A 142 13113 13841 12843 -1656 -920 1641 C
ATOM 965 NZ LYS A 142 -29.234 -11.297 -17.722 1.00115.01 N
ANISOU 965 NZ LYS A 142 14298 15106 14293 -1717 -1059 1816 N
ATOM 966 N ILE A 143 -27.281 -17.898 -14.444 1.00 65.89 N
ANISOU 966 N ILE A 143 8432 8813 7791 -1410 -433 1054 N
ATOM 967 CA ILE A 143 -27.922 -18.642 -13.349 1.00 64.95 C
ANISOU 967 CA ILE A 143 8272 8602 7804 -1321 -348 1032 C
ATOM 968 C ILE A 143 -26.941 -18.813 -12.172 1.00 66.33 C
ANISOU 968 C ILE A 143 8497 8752 7955 -1198 -199 937 C
ATOM 969 O ILE A 143 -27.389 -18.820 -11.026 1.00 65.56 O
ANISOU 969 O ILE A 143 8350 8582 7980 -1095 -119 954 O
ATOM 970 CB ILE A 143 -28.585 -19.994 -13.763 1.00 68.74 C
ANISOU 970 CB ILE A 143 8751 9074 8293 -1387 -384 994 C
ATOM 971 CG1 ILE A 143 -27.586 -21.039 -14.302 1.00 69.09 C
ANISOU 971 CG1 ILE A 143 8897 9181 8174 -1431 -351 847 C
ATOM 972 CG2 ILE A 143 -29.770 -19.789 -14.707 1.00 70.65 C
ANISOU 972 CG2 ILE A 143 8931 9324 8588 -1499 -537 1103 C
ATOM 973 CD1 ILE A 143 -27.266 -22.135 -13.308 1.00 76.33 C
ANISOU 973 CD1 ILE A 143 9828 10037 9136 -1342 -228 754 C
ATOM 974 N LEU A 144 -25.619 -18.923 -12.448 1.00 61.42 N
ANISOU 974 N LEU A 144 7967 8194 7176 -1210 -162 842 N
ATOM 975 CA LEU A 144 -24.592 -19.050 -11.406 1.00 59.79 C
ANISOU 975 CA LEU A 144 7811 7967 6938 -1103 -32 755 C
ATOM 976 C LEU A 144 -24.441 -17.741 -10.625 1.00 62.49 C
ANISOU 976 C LEU A 144 8120 8274 7347 -1012 -2 813 C
ATOM 977 O LEU A 144 -24.054 -17.774 -9.455 1.00 61.29 O
ANISOU 977 O LEU A 144 7979 8080 7229 -903 104 769 O
ATOM 978 CB LEU A 144 -23.235 -19.486 -11.983 1.00 59.53 C
ANISOU 978 CB LEU A 144 7877 8007 6733 -1146 -7 645 C
ATOM 979 CG LEU A 144 -23.089 -20.962 -12.368 1.00 64.47 C
ANISOU 979 CG LEU A 144 8546 8649 7300 -1198 9 540 C
ATOM 980 CD1 LEU A 144 -21.816 -21.189 -13.158 1.00 64.51 C
ANISOU 980 CD1 LEU A 144 8640 8734 7137 -1249 25 438 C
ATOM 981 CD2 LEU A 144 -23.122 -21.873 -11.150 1.00 66.46 C
ANISOU 981 CD2 LEU A 144 8786 8823 7644 -1105 112 493 C
ATOM 982 N SER A 145 -24.768 -16.598 -11.266 1.00 59.03 N
ANISOU 982 N SER A 145 7638 7854 6935 -1059 -99 912 N
ATOM 983 CA SER A 145 -24.748 -15.270 -10.651 1.00 58.35 C
ANISOU 983 CA SER A 145 7505 7727 6938 -982 -92 973 C
ATOM 984 C SER A 145 -25.839 -15.184 -9.581 1.00 61.47 C
ANISOU 984 C SER A 145 7814 8033 7509 -894 -48 1018 C
ATOM 985 O SER A 145 -25.572 -14.716 -8.476 1.00 60.52 O
ANISOU 985 O SER A 145 7684 7867 7444 -780 37 993 O
ATOM 986 CB SER A 145 -24.943 -14.185 -11.705 1.00 62.84 C
ANISOU 986 CB SER A 145 8038 8335 7505 -1070 -221 1078 C
ATOM 987 OG SER A 145 -23.941 -14.249 -12.706 1.00 72.60 O
ANISOU 987 OG SER A 145 9352 9663 8571 -1145 -249 1040 O
ATOM 988 N VAL A 146 -27.050 -15.691 -9.903 1.00 58.08 N
ANISOU 988 N VAL A 146 7323 7582 7164 -945 -101 1078 N
ATOM 989 CA VAL A 146 -28.219 -15.738 -9.016 1.00 57.83 C
ANISOU 989 CA VAL A 146 7199 7470 7304 -875 -62 1131 C
ATOM 990 C VAL A 146 -27.905 -16.650 -7.814 1.00 60.44 C
ANISOU 990 C VAL A 146 7562 7777 7625 -776 80 1041 C
ATOM 991 O VAL A 146 -28.246 -16.299 -6.685 1.00 59.93 O
ANISOU 991 O VAL A 146 7450 7662 7660 -669 162 1051 O
ATOM 992 CB VAL A 146 -29.502 -16.200 -9.773 1.00 62.68 C
ANISOU 992 CB VAL A 146 7746 8072 7998 -970 -163 1217 C
ATOM 993 CG1 VAL A 146 -30.730 -16.171 -8.866 1.00 62.84 C
ANISOU 993 CG1 VAL A 146 7666 8010 8201 -897 -112 1272 C
ATOM 994 CG2 VAL A 146 -29.750 -15.354 -11.020 1.00 63.28 C
ANISOU 994 CG2 VAL A 146 7782 8173 8089 -1070 -310 1321 C
ATOM 995 N VAL A 147 -27.226 -17.794 -8.067 1.00 56.14 N
ANISOU 995 N VAL A 147 7099 7273 6961 -812 108 954 N
ATOM 996 CA VAL A 147 -26.821 -18.806 -7.080 1.00 55.15 C
ANISOU 996 CA VAL A 147 7007 7129 6817 -738 228 873 C
ATOM 997 C VAL A 147 -25.950 -18.168 -5.969 1.00 57.88 C
ANISOU 997 C VAL A 147 7388 7467 7136 -623 329 824 C
ATOM 998 O VAL A 147 -26.225 -18.404 -4.793 1.00 57.04 O
ANISOU 998 O VAL A 147 7255 7326 7092 -529 425 817 O
ATOM 999 CB VAL A 147 -26.113 -20.008 -7.779 1.00 58.91 C
ANISOU 999 CB VAL A 147 7561 7648 7175 -814 218 786 C
ATOM 1000 CG1 VAL A 147 -25.234 -20.813 -6.819 1.00 57.90 C
ANISOU 1000 CG1 VAL A 147 7487 7511 7001 -739 338 693 C
ATOM 1001 CG2 VAL A 147 -27.129 -20.919 -8.462 1.00 59.56 C
ANISOU 1001 CG2 VAL A 147 7596 7716 7319 -896 148 822 C
ATOM 1002 N ILE A 148 -24.942 -17.346 -6.344 1.00 53.92 N
ANISOU 1002 N ILE A 148 6942 7000 6544 -633 304 795 N
ATOM 1003 CA ILE A 148 -24.020 -16.675 -5.413 1.00 52.76 C
ANISOU 1003 CA ILE A 148 6833 6844 6368 -533 382 745 C
ATOM 1004 C ILE A 148 -24.758 -15.614 -4.570 1.00 56.59 C
ANISOU 1004 C ILE A 148 7238 7277 6987 -443 404 800 C
ATOM 1005 O ILE A 148 -24.648 -15.643 -3.343 1.00 55.67 O
ANISOU 1005 O ILE A 148 7122 7137 6893 -339 506 762 O
ATOM 1006 CB ILE A 148 -22.803 -16.064 -6.173 1.00 55.44 C
ANISOU 1006 CB ILE A 148 7242 7232 6593 -577 335 714 C
ATOM 1007 CG1 ILE A 148 -21.939 -17.171 -6.815 1.00 55.53 C
ANISOU 1007 CG1 ILE A 148 7337 7294 6469 -644 344 633 C
ATOM 1008 CG2 ILE A 148 -21.945 -15.161 -5.263 1.00 55.57 C
ANISOU 1008 CG2 ILE A 148 7281 7226 6608 -475 391 679 C
ATOM 1009 CD1 ILE A 148 -21.127 -16.726 -8.003 1.00 62.55 C
ANISOU 1009 CD1 ILE A 148 8276 8246 7243 -726 276 624 C
ATOM 1010 N TRP A 149 -25.495 -14.692 -5.225 1.00 53.88 N
ANISOU 1010 N TRP A 149 6823 6917 6731 -484 310 888 N
ATOM 1011 CA TRP A 149 -26.219 -13.601 -4.568 1.00 54.06 C
ANISOU 1011 CA TRP A 149 6758 6883 6899 -407 320 939 C
ATOM 1012 C TRP A 149 -27.287 -14.102 -3.580 1.00 58.93 C
ANISOU 1012 C TRP A 149 7306 7458 7625 -337 402 957 C
ATOM 1013 O TRP A 149 -27.415 -13.518 -2.505 1.00 58.61 O
ANISOU 1013 O TRP A 149 7230 7385 7655 -231 477 940 O
ATOM 1014 CB TRP A 149 -26.844 -12.655 -5.602 1.00 53.34 C
ANISOU 1014 CB TRP A 149 6596 6779 6892 -483 188 1042 C
ATOM 1015 CG TRP A 149 -25.849 -11.715 -6.220 1.00 53.94 C
ANISOU 1015 CG TRP A 149 6713 6883 6900 -515 122 1041 C
ATOM 1016 CD1 TRP A 149 -25.184 -11.882 -7.398 1.00 56.76 C
ANISOU 1016 CD1 TRP A 149 7127 7307 7134 -624 42 1050 C
ATOM 1017 CD2 TRP A 149 -25.384 -10.475 -5.669 1.00 53.57 C
ANISOU 1017 CD2 TRP A 149 6649 6799 6907 -436 133 1029 C
ATOM 1018 NE1 TRP A 149 -24.343 -10.818 -7.624 1.00 55.97 N
ANISOU 1018 NE1 TRP A 149 7041 7215 7010 -620 3 1057 N
ATOM 1019 CE2 TRP A 149 -24.446 -9.938 -6.578 1.00 57.24 C
ANISOU 1019 CE2 TRP A 149 7157 7307 7284 -505 52 1044 C
ATOM 1020 CE3 TRP A 149 -25.679 -9.756 -4.499 1.00 54.91 C
ANISOU 1020 CE3 TRP A 149 6767 6904 7192 -313 202 1003 C
ATOM 1021 CZ2 TRP A 149 -23.788 -8.726 -6.346 1.00 56.41 C
ANISOU 1021 CZ2 TRP A 149 7043 7175 7216 -456 33 1041 C
ATOM 1022 CZ3 TRP A 149 -25.028 -8.553 -4.272 1.00 56.24 C
ANISOU 1022 CZ3 TRP A 149 6931 7044 7392 -263 182 986 C
ATOM 1023 CH2 TRP A 149 -24.100 -8.046 -5.191 1.00 56.67 C
ANISOU 1023 CH2 TRP A 149 7027 7135 7372 -334 94 1010 C
ATOM 1024 N ALA A 150 -28.014 -15.187 -3.917 1.00 56.28 N
ANISOU 1024 N ALA A 150 6951 7128 7304 -395 391 988 N
ATOM 1025 CA ALA A 150 -29.052 -15.757 -3.048 1.00 56.78 C
ANISOU 1025 CA ALA A 150 6942 7156 7474 -338 467 1019 C
ATOM 1026 C ALA A 150 -28.456 -16.518 -1.853 1.00 60.72 C
ANISOU 1026 C ALA A 150 7493 7671 7905 -250 602 940 C
ATOM 1027 O ALA A 150 -28.995 -16.418 -0.749 1.00 60.51 O
ANISOU 1027 O ALA A 150 7413 7623 7954 -157 694 950 O
ATOM 1028 CB ALA A 150 -29.964 -16.677 -3.844 1.00 58.11 C
ANISOU 1028 CB ALA A 150 7071 7320 7688 -435 398 1082 C
ATOM 1029 N PHE A 151 -27.354 -17.272 -2.076 1.00 57.07 N
ANISOU 1029 N PHE A 151 7131 7250 7304 -281 613 866 N
ATOM 1030 CA PHE A 151 -26.650 -18.076 -1.068 1.00 56.51 C
ANISOU 1030 CA PHE A 151 7116 7195 7160 -215 725 796 C
ATOM 1031 C PHE A 151 -26.054 -17.200 0.042 1.00 61.30 C
ANISOU 1031 C PHE A 151 7744 7802 7744 -102 804 748 C
ATOM 1032 O PHE A 151 -26.224 -17.521 1.219 1.00 61.10 O
ANISOU 1032 O PHE A 151 7704 7779 7734 -18 908 737 O
ATOM 1033 CB PHE A 151 -25.539 -18.912 -1.737 1.00 57.56 C
ANISOU 1033 CB PHE A 151 7345 7363 7163 -285 699 728 C
ATOM 1034 CG PHE A 151 -24.793 -19.886 -0.856 1.00 58.35 C
ANISOU 1034 CG PHE A 151 7498 7474 7198 -238 796 664 C
ATOM 1035 CD1 PHE A 151 -25.241 -21.190 -0.700 1.00 61.56 C
ANISOU 1035 CD1 PHE A 151 7880 7871 7640 -260 822 679 C
ATOM 1036 CD2 PHE A 151 -23.607 -19.518 -0.232 1.00 59.60 C
ANISOU 1036 CD2 PHE A 151 7729 7648 7268 -178 849 595 C
ATOM 1037 CE1 PHE A 151 -24.538 -22.098 0.096 1.00 61.97 C
ANISOU 1037 CE1 PHE A 151 7974 7929 7643 -223 903 632 C
ATOM 1038 CE2 PHE A 151 -22.908 -20.426 0.569 1.00 61.93 C
ANISOU 1038 CE2 PHE A 151 8070 7952 7510 -141 930 546 C
ATOM 1039 CZ PHE A 151 -23.379 -21.708 0.729 1.00 60.26 C
ANISOU 1039 CZ PHE A 151 7827 7731 7336 -164 956 568 C
ATOM 1040 N MET A 152 -25.350 -16.113 -0.332 1.00 58.42 N
ANISOU 1040 N MET A 152 7416 7441 7342 -104 754 720 N
ATOM 1041 CA MET A 152 -24.698 -15.207 0.618 1.00 58.34 C
ANISOU 1041 CA MET A 152 7432 7425 7311 -3 811 665 C
ATOM 1042 C MET A 152 -25.715 -14.373 1.395 1.00 63.48 C
ANISOU 1042 C MET A 152 7989 8040 8091 80 849 698 C
ATOM 1043 O MET A 152 -25.471 -14.071 2.564 1.00 63.00 O
ANISOU 1043 O MET A 152 7939 7981 8016 181 937 644 O
ATOM 1044 CB MET A 152 -23.683 -14.292 -0.083 1.00 60.35 C
ANISOU 1044 CB MET A 152 7740 7684 7506 -35 735 636 C
ATOM 1045 CG MET A 152 -22.564 -15.040 -0.786 1.00 63.52 C
ANISOU 1045 CG MET A 152 8235 8125 7776 -108 710 592 C
ATOM 1046 SD MET A 152 -21.528 -16.069 0.279 1.00 67.17 S
ANISOU 1046 SD MET A 152 8781 8607 8133 -49 822 504 S
ATOM 1047 CE MET A 152 -20.499 -16.836 -0.956 1.00 63.40 C
ANISOU 1047 CE MET A 152 8385 8164 7540 -158 765 467 C
ATOM 1048 N PHE A 153 -26.850 -14.011 0.757 1.00 61.26 N
ANISOU 1048 N PHE A 153 7615 7726 7934 36 784 782 N
ATOM 1049 CA PHE A 153 -27.920 -13.239 1.396 1.00 62.07 C
ANISOU 1049 CA PHE A 153 7614 7788 8183 110 820 817 C
ATOM 1050 C PHE A 153 -28.625 -14.081 2.458 1.00 66.55 C
ANISOU 1050 C PHE A 153 8143 8367 8776 176 940 823 C
ATOM 1051 O PHE A 153 -28.974 -13.549 3.510 1.00 66.72 O
ANISOU 1051 O PHE A 153 8125 8381 8845 278 1028 795 O
ATOM 1052 CB PHE A 153 -28.929 -12.715 0.358 1.00 64.63 C
ANISOU 1052 CB PHE A 153 7844 8068 8643 36 709 917 C
ATOM 1053 CG PHE A 153 -30.047 -11.870 0.926 1.00 67.11 C
ANISOU 1053 CG PHE A 153 8039 8330 9132 107 743 958 C
ATOM 1054 CD1 PHE A 153 -29.839 -10.532 1.239 1.00 70.39 C
ANISOU 1054 CD1 PHE A 153 8425 8708 9612 181 746 920 C
ATOM 1055 CD2 PHE A 153 -31.314 -12.406 1.125 1.00 70.00 C
ANISOU 1055 CD2 PHE A 153 8314 8675 9608 101 769 1033 C
ATOM 1056 CE1 PHE A 153 -30.873 -9.751 1.761 1.00 72.26 C
ANISOU 1056 CE1 PHE A 153 8545 8892 10021 250 782 947 C
ATOM 1057 CE2 PHE A 153 -32.348 -11.623 1.648 1.00 73.71 C
ANISOU 1057 CE2 PHE A 153 8665 9094 10247 169 808 1069 C
ATOM 1058 CZ PHE A 153 -32.122 -10.300 1.955 1.00 72.03 C
ANISOU 1058 CZ PHE A 153 8425 8846 10096 243 816 1022 C
ATOM 1059 N LEU A 154 -28.806 -15.393 2.195 1.00 62.93 N
ANISOU 1059 N LEU A 154 7696 7929 8286 117 945 857 N
ATOM 1060 CA LEU A 154 -29.444 -16.322 3.128 1.00 63.19 C
ANISOU 1060 CA LEU A 154 7689 7977 8343 166 1052 879 C
ATOM 1061 C LEU A 154 -28.530 -16.639 4.333 1.00 67.00 C
ANISOU 1061 C LEU A 154 8248 8507 8704 247 1163 799 C
ATOM 1062 O LEU A 154 -29.004 -17.196 5.325 1.00 67.15 O
ANISOU 1062 O LEU A 154 8230 8548 8736 310 1268 814 O
ATOM 1063 CB LEU A 154 -29.876 -17.610 2.410 1.00 63.34 C
ANISOU 1063 CB LEU A 154 7694 7994 8377 72 1008 940 C
ATOM 1064 CG LEU A 154 -31.206 -17.543 1.650 1.00 68.93 C
ANISOU 1064 CG LEU A 154 8296 8658 9237 12 932 1042 C
ATOM 1065 CD1 LEU A 154 -31.267 -18.599 0.567 1.00 69.10 C
ANISOU 1065 CD1 LEU A 154 8336 8678 9242 -104 844 1073 C
ATOM 1066 CD2 LEU A 154 -32.402 -17.691 2.590 1.00 72.11 C
ANISOU 1066 CD2 LEU A 154 8589 9043 9767 86 1027 1104 C
ATOM 1067 N LEU A 155 -27.236 -16.259 4.253 1.00 62.93 N
ANISOU 1067 N LEU A 155 7833 8007 8071 245 1137 720 N
ATOM 1068 CA LEU A 155 -26.251 -16.407 5.328 1.00 62.30 C
ANISOU 1068 CA LEU A 155 7831 7966 7874 317 1223 642 C
ATOM 1069 C LEU A 155 -26.163 -15.122 6.149 1.00 66.81 C
ANISOU 1069 C LEU A 155 8393 8534 8460 419 1268 587 C
ATOM 1070 O LEU A 155 -25.973 -15.180 7.363 1.00 66.56 O
ANISOU 1070 O LEU A 155 8378 8538 8374 504 1370 545 O
ATOM 1071 CB LEU A 155 -24.857 -16.740 4.763 1.00 61.37 C
ANISOU 1071 CB LEU A 155 7822 7860 7635 260 1168 585 C
ATOM 1072 CG LEU A 155 -24.570 -18.179 4.350 1.00 65.63 C
ANISOU 1072 CG LEU A 155 8401 8417 8118 192 1168 593 C
ATOM 1073 CD1 LEU A 155 -23.349 -18.236 3.464 1.00 64.99 C
ANISOU 1073 CD1 LEU A 155 8413 8340 7939 132 1104 536 C
ATOM 1074 CD2 LEU A 155 -24.350 -19.076 5.562 1.00 68.01 C
ANISOU 1074 CD2 LEU A 155 8715 8752 8375 256 1279 585 C
ATOM 1075 N SER A 156 -26.288 -13.965 5.468 1.00 63.82 N
ANISOU 1075 N SER A 156 7984 8111 8155 408 1188 587 N
ATOM 1076 CA SER A 156 -26.192 -12.618 6.033 1.00 64.05 C
ANISOU 1076 CA SER A 156 7996 8118 8223 496 1205 529 C
ATOM 1077 C SER A 156 -27.462 -12.178 6.758 1.00 68.76 C
ANISOU 1077 C SER A 156 8482 8699 8944 572 1278 551 C
ATOM 1078 O SER A 156 -27.357 -11.496 7.778 1.00 68.74 O
ANISOU 1078 O SER A 156 8478 8704 8937 672 1350 478 O
ATOM 1079 CB SER A 156 -25.871 -11.608 4.936 1.00 67.77 C
ANISOU 1079 CB SER A 156 8464 8541 8743 445 1080 536 C
ATOM 1080 OG SER A 156 -24.736 -12.003 4.184 1.00 76.51 O
ANISOU 1080 OG SER A 156 9664 9667 9738 370 1014 521 O
ATOM 1081 N LEU A 157 -28.651 -12.535 6.219 1.00 65.62 N
ANISOU 1081 N LEU A 157 7992 8278 8662 524 1258 648 N
ATOM 1082 CA LEU A 157 -29.958 -12.169 6.775 1.00 66.30 C
ANISOU 1082 CA LEU A 157 7959 8343 8891 586 1324 684 C
ATOM 1083 C LEU A 157 -30.109 -12.613 8.253 1.00 69.76 C
ANISOU 1083 C LEU A 157 8396 8841 9270 688 1482 643 C
ATOM 1084 O LEU A 157 -30.481 -11.751 9.050 1.00 70.12 O
ANISOU 1084 O LEU A 157 8389 8879 9374 781 1549 594 O
ATOM 1085 CB LEU A 157 -31.115 -12.714 5.912 1.00 66.87 C
ANISOU 1085 CB LEU A 157 7941 8381 9087 504 1269 805 C
ATOM 1086 CG LEU A 157 -32.498 -12.073 6.102 1.00 72.95 C
ANISOU 1086 CG LEU A 157 8569 9101 10049 546 1293 860 C
ATOM 1087 CD1 LEU A 157 -32.533 -10.635 5.592 1.00 73.43 C
ANISOU 1087 CD1 LEU A 157 8588 9094 10218 554 1209 840 C
ATOM 1088 CD2 LEU A 157 -33.565 -12.881 5.396 1.00 76.11 C
ANISOU 1088 CD2 LEU A 157 8890 9474 10554 462 1244 984 C
ATOM 1089 N PRO A 158 -29.779 -13.866 8.684 1.00 65.25 N
ANISOU 1089 N PRO A 158 7878 8332 8584 676 1543 656 N
ATOM 1090 CA PRO A 158 -29.922 -14.197 10.113 1.00 65.39 C
ANISOU 1090 CA PRO A 158 7888 8417 8540 772 1691 627 C
ATOM 1091 C PRO A 158 -28.890 -13.486 10.992 1.00 68.27 C
ANISOU 1091 C PRO A 158 8335 8816 8788 854 1735 503 C
ATOM 1092 O PRO A 158 -29.176 -13.250 12.162 1.00 68.50 O
ANISOU 1092 O PRO A 158 8339 8892 8796 950 1849 459 O
ATOM 1093 CB PRO A 158 -29.738 -15.719 10.157 1.00 66.80 C
ANISOU 1093 CB PRO A 158 8100 8641 8640 719 1716 687 C
ATOM 1094 CG PRO A 158 -29.840 -16.179 8.737 1.00 70.77 C
ANISOU 1094 CG PRO A 158 8601 9090 9197 600 1590 751 C
ATOM 1095 CD PRO A 158 -29.315 -15.046 7.928 1.00 65.92 C
ANISOU 1095 CD PRO A 158 8022 8428 8597 578 1486 699 C
ATOM 1096 N ASN A 159 -27.716 -13.110 10.429 1.00 63.46 N
ANISOU 1096 N ASN A 159 7822 8185 8106 819 1644 446 N
ATOM 1097 CA ASN A 159 -26.659 -12.380 11.148 1.00 62.79 C
ANISOU 1097 CA ASN A 159 7817 8119 7920 889 1662 330 C
ATOM 1098 C ASN A 159 -27.104 -10.952 11.504 1.00 67.38 C
ANISOU 1098 C ASN A 159 8337 8660 8604 971 1673 263 C
ATOM 1099 O ASN A 159 -26.582 -10.368 12.455 1.00 67.15 O
ANISOU 1099 O ASN A 159 8346 8659 8508 1058 1730 161 O
ATOM 1100 CB ASN A 159 -25.364 -12.331 10.329 1.00 61.14 C
ANISOU 1100 CB ASN A 159 7709 7885 7638 823 1554 301 C
ATOM 1101 CG ASN A 159 -24.461 -13.529 10.494 1.00 77.47 C
ANISOU 1101 CG ASN A 159 9869 10003 9563 786 1572 304 C
ATOM 1102 OD1 ASN A 159 -24.169 -14.246 9.535 1.00 69.05 O
ANISOU 1102 OD1 ASN A 159 8837 8919 8478 694 1499 344 O
ATOM 1103 ND2 ASN A 159 -23.946 -13.743 11.697 1.00 69.11 N
ANISOU 1103 ND2 ASN A 159 8852 9008 8399 855 1668 259 N
ATOM 1104 N MET A 160 -28.072 -10.405 10.744 1.00 64.55 N
ANISOU 1104 N MET A 160 7879 8232 8414 941 1614 321 N
ATOM 1105 CA MET A 160 -28.638 -9.068 10.930 1.00 65.34 C
ANISOU 1105 CA MET A 160 7895 8275 8655 1008 1612 273 C
ATOM 1106 C MET A 160 -29.777 -9.081 11.961 1.00 71.10 C
ANISOU 1106 C MET A 160 8532 9037 9445 1095 1751 269 C
ATOM 1107 O MET A 160 -29.793 -8.241 12.857 1.00 71.06 O
ANISOU 1107 O MET A 160 8508 9036 9456 1195 1816 167 O
ATOM 1108 CB MET A 160 -29.149 -8.509 9.589 1.00 67.60 C
ANISOU 1108 CB MET A 160 8107 8471 9105 928 1482 355 C
ATOM 1109 CG MET A 160 -28.056 -8.262 8.569 1.00 70.15 C
ANISOU 1109 CG MET A 160 8509 8765 9381 849 1346 355 C
ATOM 1110 SD MET A 160 -28.713 -7.795 6.954 1.00 74.46 S
ANISOU 1110 SD MET A 160 8964 9227 10101 742 1193 473 S
ATOM 1111 CE MET A 160 -27.567 -6.519 6.508 1.00 70.79 C
ANISOU 1111 CE MET A 160 8540 8709 9648 746 1084 409 C
ATOM 1112 N ILE A 161 -30.722 -10.037 11.830 1.00 69.09 N
ANISOU 1112 N ILE A 161 8217 8808 9228 1057 1795 377 N
ATOM 1113 CA ILE A 161 -31.908 -10.191 12.684 1.00 70.77 C
ANISOU 1113 CA ILE A 161 8327 9054 9509 1126 1928 402 C
ATOM 1114 C ILE A 161 -31.527 -10.602 14.124 1.00 76.63 C
ANISOU 1114 C ILE A 161 9125 9906 10085 1214 2073 327 C
ATOM 1115 O ILE A 161 -32.054 -10.023 15.079 1.00 77.27 O
ANISOU 1115 O ILE A 161 9148 10015 10196 1312 2183 264 O
ATOM 1116 CB ILE A 161 -32.917 -11.210 12.056 1.00 73.97 C
ANISOU 1116 CB ILE A 161 8658 9449 9998 1046 1916 553 C
ATOM 1117 CG1 ILE A 161 -33.323 -10.801 10.619 1.00 74.29 C
ANISOU 1117 CG1 ILE A 161 8634 9386 10206 959 1771 630 C
ATOM 1118 CG2 ILE A 161 -34.164 -11.405 12.940 1.00 76.13 C
ANISOU 1118 CG2 ILE A 161 8824 9767 10335 1114 2063 595 C
ATOM 1119 CD1 ILE A 161 -33.814 -11.961 9.721 1.00 81.63 C
ANISOU 1119 CD1 ILE A 161 9540 10304 11173 847 1705 765 C
ATOM 1120 N LEU A 162 -30.620 -11.587 14.275 1.00 73.72 N
ANISOU 1120 N LEU A 162 8865 9601 9544 1177 2072 335 N
ATOM 1121 CA LEU A 162 -30.220 -12.142 15.573 1.00 74.48 C
ANISOU 1121 CA LEU A 162 9017 9810 9472 1240 2196 291 C
ATOM 1122 C LEU A 162 -29.254 -11.249 16.398 1.00 80.35 C
ANISOU 1122 C LEU A 162 9846 10581 10101 1321 2216 137 C
ATOM 1123 O LEU A 162 -28.753 -11.707 17.430 1.00 80.06 O
ANISOU 1123 O LEU A 162 9874 10642 9902 1363 2298 99 O
ATOM 1124 CB LEU A 162 -29.615 -13.543 15.392 1.00 73.51 C
ANISOU 1124 CB LEU A 162 8965 9733 9233 1163 2179 370 C
ATOM 1125 CG LEU A 162 -30.572 -14.644 14.919 1.00 78.22 C
ANISOU 1125 CG LEU A 162 9480 10321 9920 1095 2183 517 C
ATOM 1126 CD1 LEU A 162 -29.807 -15.823 14.358 1.00 77.25 C
ANISOU 1126 CD1 LEU A 162 9432 10202 9717 1002 2116 574 C
ATOM 1127 CD2 LEU A 162 -31.513 -15.086 16.030 1.00 81.90 C
ANISOU 1127 CD2 LEU A 162 9860 10867 10390 1159 2335 567 C
ATOM 1128 N THR A 163 -29.040 -9.979 15.990 1.00 78.48 N
ANISOU 1128 N THR A 163 9601 10263 9954 1345 2140 53 N
ATOM 1129 CA THR A 163 -28.205 -9.032 16.742 1.00 79.21 C
ANISOU 1129 CA THR A 163 9762 10369 9965 1426 2150 -99 C
ATOM 1130 C THR A 163 -29.162 -8.285 17.702 1.00 86.75 C
ANISOU 1130 C THR A 163 10627 11351 10983 1538 2275 -176 C
ATOM 1131 O THR A 163 -29.464 -7.103 17.504 1.00 86.83 O
ANISOU 1131 O THR A 163 10577 11282 11132 1583 2242 -250 O
ATOM 1132 CB THR A 163 -27.382 -8.118 15.792 1.00 84.64 C
ANISOU 1132 CB THR A 163 10491 10953 10717 1390 1998 -145 C
ATOM 1133 OG1 THR A 163 -26.864 -8.881 14.701 1.00 82.01 O
ANISOU 1133 OG1 THR A 163 10207 10593 10359 1277 1896 -49 O
ATOM 1134 CG2 THR A 163 -26.233 -7.411 16.506 1.00 82.31 C
ANISOU 1134 CG2 THR A 163 10291 10672 10312 1455 1989 -289 C
ATOM 1135 N ASN A 164 -29.673 -9.014 18.719 1.00 85.80 N
ANISOU 1135 N ASN A 164 10488 11344 10769 1579 2418 -151 N
ATOM 1136 CA ASN A 164 -30.635 -8.489 19.690 1.00 88.12 C
ANISOU 1136 CA ASN A 164 10692 11687 11101 1683 2561 -214 C
ATOM 1137 C ASN A 164 -30.211 -8.769 21.146 1.00 94.60 C
ANISOU 1137 C ASN A 164 11585 12653 11704 1756 2687 -295 C
ATOM 1138 O ASN A 164 -30.454 -9.853 21.686 1.00 94.45 O
ANISOU 1138 O ASN A 164 11567 12740 11579 1742 2777 -205 O
ATOM 1139 CB ASN A 164 -32.058 -9.028 19.418 1.00 89.45 C
ANISOU 1139 CB ASN A 164 10726 11851 11410 1662 2625 -78 C
ATOM 1140 CG ASN A 164 -32.149 -10.460 18.922 1.00110.20 C
ANISOU 1140 CG ASN A 164 13365 14505 14001 1562 2601 87 C
ATOM 1141 OD1 ASN A 164 -31.398 -11.353 19.333 1.00103.34 O
ANISOU 1141 OD1 ASN A 164 12593 13713 12959 1533 2609 109 O
ATOM 1142 ND2 ASN A 164 -33.100 -10.713 18.035 1.00101.85 N
ANISOU 1142 ND2 ASN A 164 12203 13378 13117 1507 2567 208 N
ATOM 1143 N ARG A 165 -29.572 -7.760 21.767 1.00 92.99 N
ANISOU 1143 N ARG A 165 11438 12454 11439 1832 2686 -463 N
ATOM 1144 CA ARG A 165 -29.106 -7.735 23.159 1.00 94.36 C
ANISOU 1144 CA ARG A 165 11685 12759 11407 1911 2791 -576 C
ATOM 1145 C ARG A 165 -28.859 -6.284 23.570 1.00100.68 C
ANISOU 1145 C ARG A 165 12494 13511 12247 2001 2774 -772 C
ATOM 1146 O ARG A 165 -28.175 -5.550 22.848 1.00 99.39 O
ANISOU 1146 O ARG A 165 12376 13238 12150 1977 2634 -822 O
ATOM 1147 CB ARG A 165 -27.845 -8.593 23.365 1.00 93.44 C
ANISOU 1147 CB ARG A 165 11707 12710 11084 1855 2745 -540 C
ATOM 1148 N GLN A 166 -29.446 -5.867 24.710 1.00100.09 N
ANISOU 1148 N GLN A 166 12369 13517 12144 2106 2917 -881 N
ATOM 1149 CA GLN A 166 -29.364 -4.507 25.248 1.00101.55 C
ANISOU 1149 CA GLN A 166 12543 13666 12376 2207 2927 -1085 C
ATOM 1150 C GLN A 166 -27.908 -4.116 25.591 1.00106.09 C
ANISOU 1150 C GLN A 166 13263 14243 12804 2216 2834 -1208 C
ATOM 1151 O GLN A 166 -27.256 -4.822 26.366 1.00105.56 O
ANISOU 1151 O GLN A 166 13299 14300 12508 2209 2873 -1206 O
ATOM 1152 CB GLN A 166 -30.272 -4.366 26.487 1.00104.97 C
ANISOU 1152 CB GLN A 166 12912 14226 12746 2312 3123 -1173 C
ATOM 1153 CG GLN A 166 -30.534 -2.921 26.939 1.00119.45 C
ANISOU 1153 CG GLN A 166 14697 16009 14681 2424 3153 -1389 C
ATOM 1154 CD GLN A 166 -29.536 -2.399 27.952 1.00136.50 C
ANISOU 1154 CD GLN A 166 16977 18252 16636 2491 3165 -1577 C
ATOM 1155 OE1 GLN A 166 -29.070 -3.115 28.849 1.00131.24 O
ANISOU 1155 OE1 GLN A 166 16410 17738 15718 2483 3222 -1561 O
ATOM 1156 NE2 GLN A 166 -29.209 -1.120 27.851 1.00128.58 N
ANISOU 1156 NE2 GLN A 166 15962 17150 15744 2559 3108 -1760 N
ATOM 1157 N PRO A 167 -27.385 -2.995 25.029 1.00103.25 N
ANISOU 1157 N PRO A 167 12907 13742 12582 2228 2704 -1307 N
ATOM 1158 CA PRO A 167 -26.018 -2.577 25.379 1.00102.88 C
ANISOU 1158 CA PRO A 167 12990 13688 12411 2240 2612 -1425 C
ATOM 1159 C PRO A 167 -26.025 -1.855 26.729 1.00109.35 C
ANISOU 1159 C PRO A 167 13832 14597 13118 2358 2714 -1630 C
ATOM 1160 O PRO A 167 -26.458 -0.702 26.820 1.00110.12 O
ANISOU 1160 O PRO A 167 13860 14618 13362 2437 2717 -1775 O
ATOM 1161 CB PRO A 167 -25.600 -1.669 24.208 1.00103.71 C
ANISOU 1161 CB PRO A 167 13066 13607 12731 2208 2443 -1436 C
ATOM 1162 CG PRO A 167 -26.846 -1.449 23.377 1.00108.30 C
ANISOU 1162 CG PRO A 167 13497 14103 13548 2187 2453 -1339 C
ATOM 1163 CD PRO A 167 -28.015 -2.033 24.104 1.00105.09 C
ANISOU 1163 CD PRO A 167 13019 13815 13095 2233 2635 -1314 C
ATOM 1164 N ARG A 168 -25.599 -2.569 27.790 1.00106.81 N
ANISOU 1164 N ARG A 168 13603 14443 12537 2370 2803 -1638 N
ATOM 1165 CA ARG A 168 -25.564 -2.074 29.170 1.00108.66 C
ANISOU 1165 CA ARG A 168 13876 14801 12607 2472 2912 -1821 C
ATOM 1166 C ARG A 168 -24.551 -0.932 29.345 1.00112.77 C
ANISOU 1166 C ARG A 168 14468 15243 13137 2523 2801 -2017 C
ATOM 1167 O ARG A 168 -24.877 0.071 29.984 1.00114.20 O
ANISOU 1167 O ARG A 168 14611 15428 13352 2625 2860 -2206 O
ATOM 1168 CB ARG A 168 -25.249 -3.217 30.148 1.00109.33 C
ANISOU 1168 CB ARG A 168 14056 15080 12407 2448 2998 -1751 C
ATOM 1169 N ASP A 169 -23.338 -1.084 28.775 1.00107.37 N
ANISOU 1169 N ASP A 169 13881 14482 12433 2454 2642 -1974 N
ATOM 1170 CA ASP A 169 -22.269 -0.085 28.846 1.00107.02 C
ANISOU 1170 CA ASP A 169 13906 14350 12406 2490 2516 -2135 C
ATOM 1171 C ASP A 169 -22.148 0.688 27.531 1.00109.02 C
ANISOU 1171 C ASP A 169 14097 14397 12930 2455 2362 -2106 C
ATOM 1172 O ASP A 169 -22.485 0.157 26.471 1.00107.41 O
ANISOU 1172 O ASP A 169 13839 14131 12840 2373 2324 -1932 O
ATOM 1173 CB ASP A 169 -20.932 -0.751 29.197 1.00107.97 C
ANISOU 1173 CB ASP A 169 14182 14539 12303 2442 2447 -2111 C
ATOM 1174 N LYS A 170 -21.669 1.944 27.608 1.00105.35 N
ANISOU 1174 N LYS A 170 13636 13827 12566 2514 2271 -2277 N
ATOM 1175 CA LYS A 170 -21.488 2.828 26.454 1.00103.93 C
ANISOU 1175 CA LYS A 170 13392 13450 12646 2489 2117 -2263 C
ATOM 1176 C LYS A 170 -20.001 2.898 26.028 1.00104.91 C
ANISOU 1176 C LYS A 170 13628 13506 12727 2432 1949 -2244 C
ATOM 1177 O LYS A 170 -19.591 3.863 25.374 1.00104.28 O
ANISOU 1177 O LYS A 170 13515 13273 12832 2434 1814 -2287 O
ATOM 1178 CB LYS A 170 -22.040 4.230 26.770 1.00108.30 C
ANISOU 1178 CB LYS A 170 13848 13914 13387 2596 2126 -2460 C
ATOM 1179 N ASN A 171 -19.210 1.855 26.366 1.00 99.33 N
ANISOU 1179 N ASN A 171 13044 12908 11791 2377 1956 -2166 N
ATOM 1180 CA ASN A 171 -17.781 1.777 26.042 1.00 97.23 C
ANISOU 1180 CA ASN A 171 12887 12590 11468 2321 1812 -2137 C
ATOM 1181 C ASN A 171 -17.388 0.431 25.407 1.00 97.75 C
ANISOU 1181 C ASN A 171 13007 12703 11430 2208 1800 -1931 C
ATOM 1182 O ASN A 171 -16.438 0.395 24.622 1.00 95.97 O
ANISOU 1182 O ASN A 171 12828 12394 11244 2140 1671 -1859 O
ATOM 1183 CB ASN A 171 -16.939 2.019 27.292 1.00 99.08 C
ANISOU 1183 CB ASN A 171 13232 12899 11516 2385 1813 -2302 C
ATOM 1184 N VAL A 172 -18.105 -0.665 25.752 1.00 93.02 N
ANISOU 1184 N VAL A 172 12400 12236 10706 2189 1934 -1839 N
ATOM 1185 CA VAL A 172 -17.861 -2.032 25.259 1.00 90.58 C
ANISOU 1185 CA VAL A 172 12133 11981 10303 2088 1941 -1650 C
ATOM 1186 C VAL A 172 -18.228 -2.097 23.754 1.00 90.65 C
ANISOU 1186 C VAL A 172 12060 11872 10510 2009 1868 -1508 C
ATOM 1187 O VAL A 172 -19.399 -2.251 23.399 1.00 90.57 O
ANISOU 1187 O VAL A 172 11950 11866 10599 2005 1939 -1444 O
ATOM 1188 CB VAL A 172 -18.616 -3.098 26.114 1.00 95.39 C
ANISOU 1188 CB VAL A 172 12738 12761 10746 2098 2106 -1596 C
ATOM 1189 CG1 VAL A 172 -18.291 -4.517 25.657 1.00 93.79 C
ANISOU 1189 CG1 VAL A 172 12577 12606 10453 1995 2103 -1409 C
ATOM 1190 CG2 VAL A 172 -18.305 -2.940 27.602 1.00 96.71 C
ANISOU 1190 CG2 VAL A 172 12978 13054 10713 2178 2178 -1742 C
ATOM 1191 N LYS A 173 -17.210 -1.963 22.882 1.00 83.83 N
ANISOU 1191 N LYS A 173 11240 10908 9702 1945 1726 -1461 N
ATOM 1192 CA LYS A 173 -17.384 -1.937 21.427 1.00 81.51 C
ANISOU 1192 CA LYS A 173 10883 10508 9580 1864 1640 -1336 C
ATOM 1193 C LYS A 173 -17.147 -3.316 20.770 1.00 81.30 C
ANISOU 1193 C LYS A 173 10893 10525 9474 1758 1643 -1164 C
ATOM 1194 O LYS A 173 -16.186 -3.484 20.011 1.00 79.68 O
ANISOU 1194 O LYS A 173 10730 10257 9287 1686 1537 -1099 O
ATOM 1195 CB LYS A 173 -16.463 -0.875 20.789 1.00 83.60 C
ANISOU 1195 CB LYS A 173 11161 10638 9967 1855 1483 -1381 C
ATOM 1196 CG LYS A 173 -16.772 0.572 21.181 1.00 99.41 C
ANISOU 1196 CG LYS A 173 13099 12559 12114 1949 1454 -1535 C
ATOM 1197 CD LYS A 173 -16.486 1.560 20.043 1.00108.57 C
ANISOU 1197 CD LYS A 173 14197 13564 13493 1913 1307 -1499 C
ATOM 1198 CE LYS A 173 -15.038 1.985 19.947 1.00117.56 C
ANISOU 1198 CE LYS A 173 15415 14635 14616 1901 1177 -1537 C
ATOM 1199 NZ LYS A 173 -14.776 2.754 18.702 1.00125.00 N
ANISOU 1199 NZ LYS A 173 16288 15438 15768 1854 1038 -1473 N
ATOM 1200 N LYS A 174 -18.043 -4.289 21.036 1.00 75.95 N
ANISOU 1200 N LYS A 174 10188 9948 8719 1748 1763 -1091 N
ATOM 1201 CA LYS A 174 -17.950 -5.621 20.426 1.00 73.52 C
ANISOU 1201 CA LYS A 174 9902 9675 8357 1650 1767 -934 C
ATOM 1202 C LYS A 174 -19.340 -6.187 20.100 1.00 75.50 C
ANISOU 1202 C LYS A 174 10050 9953 8683 1629 1851 -834 C
ATOM 1203 O LYS A 174 -20.223 -6.232 20.958 1.00 76.28 O
ANISOU 1203 O LYS A 174 10103 10129 8751 1692 1970 -866 O
ATOM 1204 CB LYS A 174 -17.104 -6.617 21.248 1.00 75.55 C
ANISOU 1204 CB LYS A 174 10264 10033 8407 1635 1805 -918 C
ATOM 1205 CG LYS A 174 -17.423 -6.731 22.735 1.00 89.39 C
ANISOU 1205 CG LYS A 174 12039 11912 10012 1717 1924 -998 C
ATOM 1206 CD LYS A 174 -16.151 -6.812 23.590 1.00 98.31 C
ANISOU 1206 CD LYS A 174 13290 13087 10976 1731 1889 -1065 C
ATOM 1207 CE LYS A 174 -15.496 -8.175 23.630 1.00105.60 C
ANISOU 1207 CE LYS A 174 14279 14068 11778 1653 1891 -943 C
ATOM 1208 NZ LYS A 174 -14.385 -8.218 24.618 1.00112.62 N
ANISOU 1208 NZ LYS A 174 15276 15010 12506 1673 1865 -1007 N
ATOM 1209 N CYS A 175 -19.513 -6.592 18.826 1.00 69.32 N
ANISOU 1209 N CYS A 175 9230 9105 8002 1538 1784 -714 N
ATOM 1210 CA CYS A 175 -20.736 -7.129 18.220 1.00 68.40 C
ANISOU 1210 CA CYS A 175 9016 8989 7984 1497 1826 -602 C
ATOM 1211 C CYS A 175 -21.153 -8.461 18.845 1.00 72.89 C
ANISOU 1211 C CYS A 175 9590 9671 8434 1483 1940 -524 C
ATOM 1212 O CYS A 175 -22.353 -8.730 18.919 1.00 73.32 O
ANISOU 1212 O CYS A 175 9553 9754 8550 1497 2023 -474 O
ATOM 1213 CB CYS A 175 -20.572 -7.264 16.708 1.00 66.82 C
ANISOU 1213 CB CYS A 175 8800 8701 7886 1393 1710 -500 C
ATOM 1214 SG CYS A 175 -19.861 -5.804 15.898 1.00 69.86 S
ANISOU 1214 SG CYS A 175 9188 8960 8394 1391 1560 -563 S
ATOM 1215 N SER A 176 -20.178 -9.290 19.284 1.00 68.88 N
ANISOU 1215 N SER A 176 9179 9222 7769 1454 1942 -505 N
ATOM 1216 CA SER A 176 -20.428 -10.592 19.918 1.00 68.80 C
ANISOU 1216 CA SER A 176 9177 9319 7645 1435 2038 -421 C
ATOM 1217 C SER A 176 -21.269 -10.448 21.200 1.00 73.96 C
ANISOU 1217 C SER A 176 9792 10078 8233 1527 2177 -470 C
ATOM 1218 O SER A 176 -22.085 -11.321 21.497 1.00 74.03 O
ANISOU 1218 O SER A 176 9751 10162 8215 1516 2270 -378 O
ATOM 1219 CB SER A 176 -19.112 -11.299 20.231 1.00 71.41 C
ANISOU 1219 CB SER A 176 9619 9682 7833 1396 2002 -408 C
ATOM 1220 OG SER A 176 -18.280 -10.523 21.077 1.00 80.09 O
ANISOU 1220 OG SER A 176 10795 10794 8840 1458 1981 -532 O
ATOM 1221 N PHE A 177 -21.086 -9.328 21.929 1.00 71.16 N
ANISOU 1221 N PHE A 177 9453 9728 7856 1616 2191 -616 N
ATOM 1222 CA PHE A 177 -21.792 -8.993 23.169 1.00 72.49 C
ANISOU 1222 CA PHE A 177 9589 9999 7955 1712 2323 -694 C
ATOM 1223 C PHE A 177 -23.223 -8.487 22.896 1.00 76.28 C
ANISOU 1223 C PHE A 177 9935 10447 8602 1748 2386 -686 C
ATOM 1224 O PHE A 177 -24.046 -8.473 23.813 1.00 77.22 O
ANISOU 1224 O PHE A 177 10002 10659 8680 1815 2518 -715 O
ATOM 1225 CB PHE A 177 -20.989 -7.937 23.957 1.00 75.10 C
ANISOU 1225 CB PHE A 177 9993 10339 8203 1791 2302 -869 C
ATOM 1226 CG PHE A 177 -19.951 -8.462 24.930 1.00 76.80 C
ANISOU 1226 CG PHE A 177 10327 10648 8206 1789 2305 -890 C
ATOM 1227 CD1 PHE A 177 -19.068 -9.472 24.559 1.00 78.73 C
ANISOU 1227 CD1 PHE A 177 10636 10887 8390 1700 2242 -778 C
ATOM 1228 CD2 PHE A 177 -19.820 -7.907 26.198 1.00 80.51 C
ANISOU 1228 CD2 PHE A 177 10843 11206 8540 1876 2363 -1029 C
ATOM 1229 CE1 PHE A 177 -18.108 -9.951 25.457 1.00 79.72 C
ANISOU 1229 CE1 PHE A 177 10864 11093 8335 1694 2238 -789 C
ATOM 1230 CE2 PHE A 177 -18.850 -8.377 27.090 1.00 83.42 C
ANISOU 1230 CE2 PHE A 177 11322 11662 8712 1868 2354 -1041 C
ATOM 1231 CZ PHE A 177 -18.000 -9.394 26.713 1.00 80.17 C
ANISOU 1231 CZ PHE A 177 10966 11239 8254 1776 2290 -915 C
ATOM 1232 N LEU A 178 -23.513 -8.083 21.641 1.00 71.42 N
ANISOU 1232 N LEU A 178 9260 9704 8174 1701 2292 -642 N
ATOM 1233 CA LEU A 178 -24.824 -7.585 21.205 1.00 71.62 C
ANISOU 1233 CA LEU A 178 9151 9674 8386 1721 2326 -618 C
ATOM 1234 C LEU A 178 -25.669 -8.695 20.549 1.00 74.24 C
ANISOU 1234 C LEU A 178 9415 10015 8776 1643 2351 -444 C
ATOM 1235 O LEU A 178 -26.807 -8.439 20.144 1.00 74.16 O
ANISOU 1235 O LEU A 178 9290 9963 8924 1649 2379 -399 O
ATOM 1236 CB LEU A 178 -24.650 -6.414 20.216 1.00 71.25 C
ANISOU 1236 CB LEU A 178 9073 9480 8519 1710 2196 -664 C
ATOM 1237 CG LEU A 178 -24.120 -5.099 20.782 1.00 76.63 C
ANISOU 1237 CG LEU A 178 9790 10122 9204 1792 2159 -838 C
ATOM 1238 CD1 LEU A 178 -23.316 -4.351 19.743 1.00 75.86 C
ANISOU 1238 CD1 LEU A 178 9701 9887 9234 1744 1996 -839 C
ATOM 1239 CD2 LEU A 178 -25.249 -4.226 21.297 1.00 81.15 C
ANISOU 1239 CD2 LEU A 178 10264 10700 9871 1896 2257 -943 C
ATOM 1240 N LYS A 179 -25.119 -9.922 20.458 1.00 69.58 N
ANISOU 1240 N LYS A 179 8892 9475 8071 1571 2339 -347 N
ATOM 1241 CA LYS A 179 -25.794 -11.066 19.840 1.00 68.86 C
ANISOU 1241 CA LYS A 179 8745 9389 8030 1493 2350 -186 C
ATOM 1242 C LYS A 179 -26.366 -12.027 20.881 1.00 73.51 C
ANISOU 1242 C LYS A 179 9307 10108 8515 1520 2493 -124 C
ATOM 1243 O LYS A 179 -25.774 -12.214 21.948 1.00 73.62 O
ANISOU 1243 O LYS A 179 9391 10222 8360 1564 2554 -180 O
ATOM 1244 CB LYS A 179 -24.840 -11.829 18.901 1.00 69.59 C
ANISOU 1244 CB LYS A 179 8915 9437 8090 1388 2235 -115 C
ATOM 1245 CG LYS A 179 -24.448 -11.046 17.650 1.00 81.05 C
ANISOU 1245 CG LYS A 179 10379 10765 9652 1343 2093 -142 C
ATOM 1246 CD LYS A 179 -23.739 -11.915 16.623 1.00 88.23 C
ANISOU 1246 CD LYS A 179 11333 11635 10556 1230 1998 -50 C
ATOM 1247 CE LYS A 179 -24.630 -12.271 15.456 1.00 98.10 C
ANISOU 1247 CE LYS A 179 12494 12820 11960 1160 1948 50 C
ATOM 1248 NZ LYS A 179 -24.819 -11.124 14.527 1.00106.43 N
ANISOU 1248 NZ LYS A 179 13516 13778 13146 1155 1851 12 N
ATOM 1249 N SER A 180 -27.510 -12.654 20.546 1.00 70.05 N
ANISOU 1249 N SER A 180 8766 9670 8179 1488 2539 0 N
ATOM 1250 CA SER A 180 -28.204 -13.637 21.381 1.00 70.59 C
ANISOU 1250 CA SER A 180 8786 9854 8179 1503 2670 90 C
ATOM 1251 C SER A 180 -27.457 -14.987 21.382 1.00 73.34 C
ANISOU 1251 C SER A 180 9202 10244 8418 1425 2640 191 C
ATOM 1252 O SER A 180 -26.488 -15.149 20.637 1.00 71.52 O
ANISOU 1252 O SER A 180 9051 9947 8176 1361 2522 184 O
ATOM 1253 CB SER A 180 -29.637 -13.820 20.890 1.00 74.69 C
ANISOU 1253 CB SER A 180 9164 10340 8873 1494 2715 192 C
ATOM 1254 OG SER A 180 -29.676 -14.231 19.534 1.00 81.72 O
ANISOU 1254 OG SER A 180 10033 11124 9893 1395 2595 285 O
ATOM 1255 N GLU A 181 -27.908 -15.948 22.222 1.00 70.75 N
ANISOU 1255 N GLU A 181 8837 10026 8018 1430 2748 288 N
ATOM 1256 CA GLU A 181 -27.315 -17.286 22.347 1.00 69.97 C
ANISOU 1256 CA GLU A 181 8783 9969 7834 1360 2731 396 C
ATOM 1257 C GLU A 181 -27.312 -18.017 21.002 1.00 72.75 C
ANISOU 1257 C GLU A 181 9116 10209 8318 1255 2616 490 C
ATOM 1258 O GLU A 181 -26.266 -18.528 20.606 1.00 71.22 O
ANISOU 1258 O GLU A 181 9005 9980 8075 1194 2527 491 O
ATOM 1259 CB GLU A 181 -28.043 -18.123 23.411 1.00 72.64 C
ANISOU 1259 CB GLU A 181 9053 10439 8108 1384 2869 502 C
ATOM 1260 CG GLU A 181 -27.700 -17.732 24.837 1.00 84.16 C
ANISOU 1260 CG GLU A 181 10569 12041 9369 1461 2968 426 C
ATOM 1261 N PHE A 182 -28.458 -18.023 20.285 1.00 69.75 N
ANISOU 1261 N PHE A 182 8627 9768 8106 1235 2615 559 N
ATOM 1262 CA PHE A 182 -28.583 -18.653 18.965 1.00 68.62 C
ANISOU 1262 CA PHE A 182 8459 9521 8094 1136 2505 641 C
ATOM 1263 C PHE A 182 -27.856 -17.816 17.902 1.00 70.46 C
ANISOU 1263 C PHE A 182 8756 9649 8365 1105 2374 547 C
ATOM 1264 O PHE A 182 -27.306 -18.380 16.955 1.00 69.01 O
ANISOU 1264 O PHE A 182 8610 9400 8212 1018 2269 579 O
ATOM 1265 CB PHE A 182 -30.064 -18.879 18.586 1.00 71.42 C
ANISOU 1265 CB PHE A 182 8674 9848 8616 1126 2542 745 C
ATOM 1266 CG PHE A 182 -30.323 -19.381 17.179 1.00 72.41 C
ANISOU 1266 CG PHE A 182 8764 9862 8887 1028 2423 817 C
ATOM 1267 CD1 PHE A 182 -29.749 -20.567 16.727 1.00 74.86 C
ANISOU 1267 CD1 PHE A 182 9112 10150 9181 940 2353 883 C
ATOM 1268 CD2 PHE A 182 -31.164 -18.686 16.319 1.00 74.97 C
ANISOU 1268 CD2 PHE A 182 9011 10105 9369 1022 2379 821 C
ATOM 1269 CE1 PHE A 182 -29.982 -21.024 15.425 1.00 75.27 C
ANISOU 1269 CE1 PHE A 182 9136 10106 9358 849 2242 936 C
ATOM 1270 CE2 PHE A 182 -31.402 -19.148 15.021 1.00 77.32 C
ANISOU 1270 CE2 PHE A 182 9280 10309 9788 927 2263 888 C
ATOM 1271 CZ PHE A 182 -30.810 -20.313 14.582 1.00 74.67 C
ANISOU 1271 CZ PHE A 182 8991 9959 9421 841 2197 940 C
ATOM 1272 N GLY A 183 -27.845 -16.495 18.089 1.00 66.59 N
ANISOU 1272 N GLY A 183 8278 9148 7875 1176 2382 431 N
ATOM 1273 CA GLY A 183 -27.171 -15.550 17.204 1.00 65.24 C
ANISOU 1273 CA GLY A 183 8160 8885 7743 1159 2265 343 C
ATOM 1274 C GLY A 183 -25.666 -15.719 17.202 1.00 67.14 C
ANISOU 1274 C GLY A 183 8530 9127 7853 1131 2198 286 C
ATOM 1275 O GLY A 183 -25.020 -15.554 16.162 1.00 65.75 O
ANISOU 1275 O GLY A 183 8398 8872 7711 1071 2083 270 O
ATOM 1276 N LEU A 184 -25.106 -16.073 18.372 1.00 63.14 N
ANISOU 1276 N LEU A 184 8082 8715 7194 1173 2271 261 N
ATOM 1277 CA LEU A 184 -23.680 -16.323 18.569 1.00 61.64 C
ANISOU 1277 CA LEU A 184 8010 8535 6877 1152 2219 216 C
ATOM 1278 C LEU A 184 -23.298 -17.675 17.961 1.00 63.26 C
ANISOU 1278 C LEU A 184 8231 8720 7086 1054 2171 319 C
ATOM 1279 O LEU A 184 -22.168 -17.836 17.500 1.00 61.74 O
ANISOU 1279 O LEU A 184 8121 8487 6849 1008 2089 291 O
ATOM 1280 CB LEU A 184 -23.346 -16.278 20.070 1.00 62.61 C
ANISOU 1280 CB LEU A 184 8178 8770 6839 1228 2314 164 C
ATOM 1281 CG LEU A 184 -21.919 -15.887 20.467 1.00 66.90 C
ANISOU 1281 CG LEU A 184 8844 9316 7260 1242 2258 67 C
ATOM 1282 CD1 LEU A 184 -21.616 -14.426 20.129 1.00 67.06 C
ANISOU 1282 CD1 LEU A 184 8887 9270 7325 1292 2202 -65 C
ATOM 1283 CD2 LEU A 184 -21.709 -16.095 21.947 1.00 70.48 C
ANISOU 1283 CD2 LEU A 184 9336 9895 7547 1297 2351 50 C
ATOM 1284 N VAL A 185 -24.252 -18.635 17.944 1.00 59.42 N
ANISOU 1284 N VAL A 185 7659 8256 6663 1024 2221 436 N
ATOM 1285 CA VAL A 185 -24.080 -19.973 17.361 1.00 58.23 C
ANISOU 1285 CA VAL A 185 7500 8079 6545 933 2179 537 C
ATOM 1286 C VAL A 185 -24.045 -19.825 15.830 1.00 60.05 C
ANISOU 1286 C VAL A 185 7727 8200 6887 857 2061 533 C
ATOM 1287 O VAL A 185 -23.141 -20.371 15.193 1.00 58.63 O
ANISOU 1287 O VAL A 185 7608 7980 6689 789 1985 530 O
ATOM 1288 CB VAL A 185 -25.168 -20.980 17.848 1.00 63.03 C
ANISOU 1288 CB VAL A 185 8006 8742 7200 930 2268 665 C
ATOM 1289 CG1 VAL A 185 -25.123 -22.292 17.064 1.00 62.18 C
ANISOU 1289 CG1 VAL A 185 7869 8580 7179 832 2206 765 C
ATOM 1290 CG2 VAL A 185 -25.027 -21.259 19.340 1.00 63.71 C
ANISOU 1290 CG2 VAL A 185 8109 8949 7151 986 2374 685 C
ATOM 1291 N TRP A 186 -24.996 -19.046 15.256 1.00 56.10 N
ANISOU 1291 N TRP A 186 7158 7656 6500 868 2045 529 N
ATOM 1292 CA TRP A 186 -25.082 -18.779 13.816 1.00 54.96 C
ANISOU 1292 CA TRP A 186 7004 7420 6458 795 1932 532 C
ATOM 1293 C TRP A 186 -23.829 -18.036 13.320 1.00 56.95 C
ANISOU 1293 C TRP A 186 7356 7632 6650 784 1845 434 C
ATOM 1294 O TRP A 186 -23.409 -18.253 12.184 1.00 55.78 O
ANISOU 1294 O TRP A 186 7235 7429 6532 704 1750 440 O
ATOM 1295 CB TRP A 186 -26.353 -17.986 13.469 1.00 54.48 C
ANISOU 1295 CB TRP A 186 6843 7325 6532 817 1936 554 C
ATOM 1296 CG TRP A 186 -26.593 -17.872 11.991 1.00 55.07 C
ANISOU 1296 CG TRP A 186 6895 7316 6714 731 1818 584 C
ATOM 1297 CD1 TRP A 186 -26.304 -16.803 11.195 1.00 57.58 C
ANISOU 1297 CD1 TRP A 186 7233 7577 7069 716 1729 530 C
ATOM 1298 CD2 TRP A 186 -27.086 -18.899 11.120 1.00 54.76 C
ANISOU 1298 CD2 TRP A 186 6813 7245 6749 640 1769 676 C
ATOM 1299 NE1 TRP A 186 -26.624 -17.086 9.887 1.00 56.73 N
ANISOU 1299 NE1 TRP A 186 7098 7414 7044 621 1631 587 N
ATOM 1300 CE2 TRP A 186 -27.100 -18.368 9.811 1.00 58.26 C
ANISOU 1300 CE2 TRP A 186 7256 7620 7260 574 1652 669 C
ATOM 1301 CE3 TRP A 186 -27.534 -20.217 11.321 1.00 56.28 C
ANISOU 1301 CE3 TRP A 186 6962 7459 6963 608 1808 765 C
ATOM 1302 CZ2 TRP A 186 -27.547 -19.106 8.708 1.00 57.42 C
ANISOU 1302 CZ2 TRP A 186 7114 7473 7228 476 1574 739 C
ATOM 1303 CZ3 TRP A 186 -27.976 -20.946 10.228 1.00 57.54 C
ANISOU 1303 CZ3 TRP A 186 7083 7566 7213 514 1728 831 C
ATOM 1304 CH2 TRP A 186 -27.984 -20.390 8.941 1.00 57.78 C
ANISOU 1304 CH2 TRP A 186 7121 7535 7297 450 1613 813 C
ATOM 1305 N HIS A 187 -23.227 -17.190 14.183 1.00 52.74 N
ANISOU 1305 N HIS A 187 6877 7131 6031 862 1879 344 N
ATOM 1306 CA HIS A 187 -21.999 -16.437 13.912 1.00 51.33 C
ANISOU 1306 CA HIS A 187 6789 6918 5794 864 1806 252 C
ATOM 1307 C HIS A 187 -20.821 -17.405 13.731 1.00 54.16 C
ANISOU 1307 C HIS A 187 7230 7279 6070 803 1769 262 C
ATOM 1308 O HIS A 187 -20.026 -17.232 12.807 1.00 52.87 O
ANISOU 1308 O HIS A 187 7117 7062 5911 749 1680 234 O
ATOM 1309 CB HIS A 187 -21.731 -15.447 15.061 1.00 52.43 C
ANISOU 1309 CB HIS A 187 6960 7099 5863 967 1861 156 C
ATOM 1310 CG HIS A 187 -20.447 -14.684 14.944 1.00 54.90 C
ANISOU 1310 CG HIS A 187 7364 7377 6120 977 1787 63 C
ATOM 1311 ND1 HIS A 187 -19.391 -14.915 15.807 1.00 56.39 N
ANISOU 1311 ND1 HIS A 187 7639 7609 6178 1007 1808 15 N
ATOM 1312 CD2 HIS A 187 -20.095 -13.711 14.075 1.00 55.98 C
ANISOU 1312 CD2 HIS A 187 7511 7438 6321 959 1691 20 C
ATOM 1313 CE1 HIS A 187 -18.437 -14.077 15.437 1.00 55.16 C
ANISOU 1313 CE1 HIS A 187 7543 7400 6017 1008 1726 -59 C
ATOM 1314 NE2 HIS A 187 -18.817 -13.330 14.401 1.00 55.27 N
ANISOU 1314 NE2 HIS A 187 7513 7343 6146 981 1655 -56 N
ATOM 1315 N GLU A 188 -20.743 -18.436 14.596 1.00 51.01 N
ANISOU 1315 N GLU A 188 6836 6940 5605 808 1840 309 N
ATOM 1316 CA GLU A 188 -19.713 -19.476 14.581 1.00 50.22 C
ANISOU 1316 CA GLU A 188 6797 6841 5443 755 1817 330 C
ATOM 1317 C GLU A 188 -19.852 -20.369 13.337 1.00 53.02 C
ANISOU 1317 C GLU A 188 7124 7138 5882 655 1753 387 C
ATOM 1318 O GLU A 188 -18.838 -20.763 12.757 1.00 51.98 O
ANISOU 1318 O GLU A 188 7052 6971 5727 600 1694 364 O
ATOM 1319 CB GLU A 188 -19.801 -20.321 15.864 1.00 52.41 C
ANISOU 1319 CB GLU A 188 7064 7201 5649 787 1910 384 C
ATOM 1320 CG GLU A 188 -18.553 -21.137 16.163 1.00 64.52 C
ANISOU 1320 CG GLU A 188 8672 8742 7102 756 1891 386 C
ATOM 1321 CD GLU A 188 -18.657 -22.094 17.338 1.00 90.70 C
ANISOU 1321 CD GLU A 188 11967 12138 10356 773 1971 462 C
ATOM 1322 OE1 GLU A 188 -19.173 -21.687 18.405 1.00 88.11 O
ANISOU 1322 OE1 GLU A 188 11614 11891 9971 844 2055 465 O
ATOM 1323 OE2 GLU A 188 -18.190 -23.248 17.198 1.00 85.81 O
ANISOU 1323 OE2 GLU A 188 11356 11503 9746 714 1951 519 O
ATOM 1324 N ILE A 189 -21.105 -20.676 12.930 1.00 49.35 N
ANISOU 1324 N ILE A 189 6569 6664 5518 633 1765 456 N
ATOM 1325 CA ILE A 189 -21.423 -21.515 11.767 1.00 48.43 C
ANISOU 1325 CA ILE A 189 6417 6497 5488 539 1703 509 C
ATOM 1326 C ILE A 189 -21.007 -20.797 10.470 1.00 50.13 C
ANISOU 1326 C ILE A 189 6669 6653 5724 490 1601 453 C
ATOM 1327 O ILE A 189 -20.301 -21.392 9.656 1.00 48.93 O
ANISOU 1327 O ILE A 189 6560 6469 5561 419 1542 438 O
ATOM 1328 CB ILE A 189 -22.933 -21.920 11.757 1.00 52.43 C
ANISOU 1328 CB ILE A 189 6811 7008 6101 535 1740 601 C
ATOM 1329 CG1 ILE A 189 -23.272 -22.846 12.949 1.00 53.65 C
ANISOU 1329 CG1 ILE A 189 6924 7226 6235 570 1839 675 C
ATOM 1330 CG2 ILE A 189 -23.346 -22.580 10.431 1.00 52.78 C
ANISOU 1330 CG2 ILE A 189 6819 6993 6242 437 1659 643 C
ATOM 1331 CD1 ILE A 189 -24.757 -22.861 13.353 1.00 63.14 C
ANISOU 1331 CD1 ILE A 189 8014 8455 7522 605 1908 755 C
ATOM 1332 N VAL A 190 -21.433 -19.526 10.300 1.00 46.02 N
ANISOU 1332 N VAL A 190 6129 6120 5237 528 1582 422 N
ATOM 1333 CA VAL A 190 -21.177 -18.680 9.128 1.00 44.95 C
ANISOU 1333 CA VAL A 190 6013 5935 5131 486 1485 386 C
ATOM 1334 C VAL A 190 -19.661 -18.499 8.899 1.00 47.29 C
ANISOU 1334 C VAL A 190 6411 6220 5337 471 1441 315 C
ATOM 1335 O VAL A 190 -19.210 -18.673 7.766 1.00 46.16 O
ANISOU 1335 O VAL A 190 6294 6047 5197 393 1365 309 O
ATOM 1336 CB VAL A 190 -21.936 -17.326 9.239 1.00 49.30 C
ANISOU 1336 CB VAL A 190 6512 6472 5746 544 1483 371 C
ATOM 1337 CG1 VAL A 190 -21.360 -16.260 8.314 1.00 48.64 C
ANISOU 1337 CG1 VAL A 190 6459 6343 5677 514 1383 330 C
ATOM 1338 CG2 VAL A 190 -23.420 -17.519 8.954 1.00 49.85 C
ANISOU 1338 CG2 VAL A 190 6475 6534 5933 531 1497 452 C
ATOM 1339 N ASN A 191 -18.883 -18.211 9.965 1.00 43.58 N
ANISOU 1339 N ASN A 191 5995 5777 4785 541 1487 263 N
ATOM 1340 CA ASN A 191 -17.428 -18.030 9.880 1.00 42.54 C
ANISOU 1340 CA ASN A 191 5955 5631 4575 533 1448 201 C
ATOM 1341 C ASN A 191 -16.708 -19.314 9.426 1.00 46.46 C
ANISOU 1341 C ASN A 191 6488 6119 5047 458 1433 218 C
ATOM 1342 O ASN A 191 -15.643 -19.225 8.813 1.00 45.12 O
ANISOU 1342 O ASN A 191 6375 5922 4846 420 1379 178 O
ATOM 1343 CB ASN A 191 -16.857 -17.535 11.206 1.00 41.93 C
ANISOU 1343 CB ASN A 191 5924 5588 4420 623 1501 149 C
ATOM 1344 CG ASN A 191 -17.082 -16.060 11.439 1.00 60.10 C
ANISOU 1344 CG ASN A 191 8217 7877 6742 692 1487 92 C
ATOM 1345 OD1 ASN A 191 -16.640 -15.202 10.667 1.00 54.01 O
ANISOU 1345 OD1 ASN A 191 7466 7059 5995 675 1410 57 O
ATOM 1346 ND2 ASN A 191 -17.755 -15.728 12.524 1.00 52.41 N
ANISOU 1346 ND2 ASN A 191 7208 6944 5761 771 1561 80 N
ATOM 1347 N TYR A 192 -17.303 -20.494 9.700 1.00 44.18 N
ANISOU 1347 N TYR A 192 6156 5849 4782 437 1480 279 N
ATOM 1348 CA TYR A 192 -16.778 -21.796 9.279 1.00 43.91 C
ANISOU 1348 CA TYR A 192 6136 5797 4750 366 1467 296 C
ATOM 1349 C TYR A 192 -17.119 -22.023 7.799 1.00 47.22 C
ANISOU 1349 C TYR A 192 6531 6179 5230 277 1396 303 C
ATOM 1350 O TYR A 192 -16.265 -22.499 7.049 1.00 46.53 O
ANISOU 1350 O TYR A 192 6485 6067 5126 216 1355 270 O
ATOM 1351 CB TYR A 192 -17.323 -22.927 10.182 1.00 45.89 C
ANISOU 1351 CB TYR A 192 6340 6079 5018 378 1538 366 C
ATOM 1352 CG TYR A 192 -17.628 -24.237 9.483 1.00 48.02 C
ANISOU 1352 CG TYR A 192 6568 6319 5361 297 1517 411 C
ATOM 1353 CD1 TYR A 192 -18.933 -24.584 9.146 1.00 50.77 C
ANISOU 1353 CD1 TYR A 192 6830 6662 5796 274 1519 475 C
ATOM 1354 CD2 TYR A 192 -16.614 -25.148 9.192 1.00 48.25 C
ANISOU 1354 CD2 TYR A 192 6635 6316 5381 246 1494 388 C
ATOM 1355 CE1 TYR A 192 -19.221 -25.788 8.508 1.00 51.79 C
ANISOU 1355 CE1 TYR A 192 6919 6758 6000 200 1491 511 C
ATOM 1356 CE2 TYR A 192 -16.891 -26.359 8.557 1.00 49.26 C
ANISOU 1356 CE2 TYR A 192 6720 6410 5587 173 1472 416 C
ATOM 1357 CZ TYR A 192 -18.197 -26.676 8.222 1.00 57.50 C
ANISOU 1357 CZ TYR A 192 7683 7450 6714 150 1468 476 C
ATOM 1358 OH TYR A 192 -18.489 -27.867 7.606 1.00 58.77 O
ANISOU 1358 OH TYR A 192 7799 7571 6959 79 1439 500 O
ATOM 1359 N ILE A 193 -18.370 -21.692 7.394 1.00 43.53 N
ANISOU 1359 N ILE A 193 5993 5711 4834 269 1383 347 N
ATOM 1360 CA ILE A 193 -18.870 -21.814 6.018 1.00 42.94 C
ANISOU 1360 CA ILE A 193 5890 5611 4816 184 1309 363 C
ATOM 1361 C ILE A 193 -18.042 -20.888 5.106 1.00 45.94 C
ANISOU 1361 C ILE A 193 6325 5977 5153 153 1236 307 C
ATOM 1362 O ILE A 193 -17.688 -21.290 3.997 1.00 45.45 O
ANISOU 1362 O ILE A 193 6282 5902 5083 71 1179 290 O
ATOM 1363 CB ILE A 193 -20.402 -21.521 5.948 1.00 46.55 C
ANISOU 1363 CB ILE A 193 6254 6068 5365 192 1312 431 C
ATOM 1364 CG1 ILE A 193 -21.207 -22.628 6.666 1.00 47.30 C
ANISOU 1364 CG1 ILE A 193 6286 6174 5512 202 1376 499 C
ATOM 1365 CG2 ILE A 193 -20.897 -21.346 4.499 1.00 47.34 C
ANISOU 1365 CG2 ILE A 193 6329 6144 5515 107 1218 446 C
ATOM 1366 CD1 ILE A 193 -22.717 -22.357 6.831 1.00 55.60 C
ANISOU 1366 CD1 ILE A 193 7238 7227 6659 224 1397 574 C
ATOM 1367 N CYS A 194 -17.690 -19.683 5.606 1.00 41.98 N
ANISOU 1367 N CYS A 194 5848 5479 4622 219 1240 277 N
ATOM 1368 CA CYS A 194 -16.885 -18.682 4.903 1.00 41.21 C
ANISOU 1368 CA CYS A 194 5796 5368 4494 202 1173 235 C
ATOM 1369 C CYS A 194 -15.434 -19.153 4.718 1.00 44.08 C
ANISOU 1369 C CYS A 194 6239 5727 4783 173 1165 182 C
ATOM 1370 O CYS A 194 -14.791 -18.738 3.753 1.00 43.54 O
ANISOU 1370 O CYS A 194 6200 5650 4691 122 1104 159 O
ATOM 1371 CB CYS A 194 -16.948 -17.339 5.619 1.00 41.73 C
ANISOU 1371 CB CYS A 194 5857 5431 4568 288 1181 216 C
ATOM 1372 SG CYS A 194 -18.515 -16.457 5.394 1.00 46.45 S
ANISOU 1372 SG CYS A 194 6354 6017 5276 305 1160 270 S
ATOM 1373 N GLN A 195 -14.926 -20.024 5.619 1.00 40.23 N
ANISOU 1373 N GLN A 195 5778 5244 4263 202 1226 169 N
ATOM 1374 CA GLN A 195 -13.583 -20.607 5.501 1.00 39.34 C
ANISOU 1374 CA GLN A 195 5731 5119 4099 175 1225 124 C
ATOM 1375 C GLN A 195 -13.583 -21.627 4.365 1.00 43.04 C
ANISOU 1375 C GLN A 195 6189 5576 4587 79 1196 121 C
ATOM 1376 O GLN A 195 -12.625 -21.686 3.593 1.00 42.37 O
ANISOU 1376 O GLN A 195 6149 5481 4467 32 1165 77 O
ATOM 1377 CB GLN A 195 -13.131 -21.261 6.819 1.00 40.62 C
ANISOU 1377 CB GLN A 195 5911 5287 4234 229 1292 125 C
ATOM 1378 CG GLN A 195 -12.611 -20.281 7.870 1.00 54.01 C
ANISOU 1378 CG GLN A 195 7648 6993 5881 315 1310 97 C
ATOM 1379 CD GLN A 195 -11.231 -19.734 7.580 1.00 69.14 C
ANISOU 1379 CD GLN A 195 9633 8883 7755 309 1269 42 C
ATOM 1380 OE1 GLN A 195 -10.299 -20.458 7.207 1.00 63.59 O
ANISOU 1380 OE1 GLN A 195 8963 8160 7040 264 1264 25 O
ATOM 1381 NE2 GLN A 195 -11.059 -18.442 7.803 1.00 60.35 N
ANISOU 1381 NE2 GLN A 195 8537 7764 6628 358 1240 15 N
ATOM 1382 N VAL A 196 -14.686 -22.402 4.249 1.00 39.80 N
ANISOU 1382 N VAL A 196 5718 5169 4235 51 1207 167 N
ATOM 1383 CA VAL A 196 -14.918 -23.414 3.211 1.00 39.55 C
ANISOU 1383 CA VAL A 196 5666 5125 4234 -38 1176 163 C
ATOM 1384 C VAL A 196 -15.046 -22.703 1.843 1.00 43.17 C
ANISOU 1384 C VAL A 196 6130 5595 4676 -102 1099 149 C
ATOM 1385 O VAL A 196 -14.425 -23.145 0.875 1.00 42.42 O
ANISOU 1385 O VAL A 196 6064 5501 4553 -174 1067 103 O
ATOM 1386 CB VAL A 196 -16.159 -24.296 3.546 1.00 43.80 C
ANISOU 1386 CB VAL A 196 6129 5660 4852 -43 1202 226 C
ATOM 1387 CG1 VAL A 196 -16.480 -25.278 2.420 1.00 43.87 C
ANISOU 1387 CG1 VAL A 196 6114 5652 4905 -137 1156 215 C
ATOM 1388 CG2 VAL A 196 -15.964 -25.044 4.862 1.00 43.57 C
ANISOU 1388 CG2 VAL A 196 6093 5629 4834 11 1275 250 C
ATOM 1389 N ILE A 197 -15.813 -21.584 1.791 1.00 39.91 N
ANISOU 1389 N ILE A 197 5688 5195 4282 -76 1071 189 N
ATOM 1390 CA ILE A 197 -16.042 -20.757 0.597 1.00 39.83 C
ANISOU 1390 CA ILE A 197 5671 5198 4264 -133 992 198 C
ATOM 1391 C ILE A 197 -14.701 -20.198 0.084 1.00 43.91 C
ANISOU 1391 C ILE A 197 6255 5724 4705 -150 965 147 C
ATOM 1392 O ILE A 197 -14.438 -20.279 -1.119 1.00 43.57 O
ANISOU 1392 O ILE A 197 6227 5701 4626 -232 913 130 O
ATOM 1393 CB ILE A 197 -17.088 -19.634 0.883 1.00 43.09 C
ANISOU 1393 CB ILE A 197 6027 5610 4737 -87 974 258 C
ATOM 1394 CG1 ILE A 197 -18.518 -20.214 0.899 1.00 43.90 C
ANISOU 1394 CG1 ILE A 197 6052 5706 4923 -103 979 319 C
ATOM 1395 CG2 ILE A 197 -16.988 -18.465 -0.119 1.00 44.03 C
ANISOU 1395 CG2 ILE A 197 6146 5738 4846 -128 890 272 C
ATOM 1396 CD1 ILE A 197 -19.527 -19.391 1.667 1.00 50.90 C
ANISOU 1396 CD1 ILE A 197 6874 6584 5882 -30 1003 371 C
ATOM 1397 N PHE A 198 -13.857 -19.663 0.993 1.00 40.52 N
ANISOU 1397 N PHE A 198 5865 5282 4250 -75 1000 121 N
ATOM 1398 CA PHE A 198 -12.553 -19.108 0.633 1.00 40.17 C
ANISOU 1398 CA PHE A 198 5878 5237 4146 -83 976 80 C
ATOM 1399 C PHE A 198 -11.613 -20.196 0.102 1.00 44.77 C
ANISOU 1399 C PHE A 198 6503 5821 4685 -141 993 26 C
ATOM 1400 O PHE A 198 -11.073 -20.030 -0.990 1.00 44.33 O
ANISOU 1400 O PHE A 198 6468 5787 4587 -207 952 6 O
ATOM 1401 CB PHE A 198 -11.902 -18.360 1.819 1.00 41.55 C
ANISOU 1401 CB PHE A 198 6082 5391 4313 13 1006 64 C
ATOM 1402 CG PHE A 198 -10.404 -18.150 1.703 1.00 42.54 C
ANISOU 1402 CG PHE A 198 6270 5505 4388 12 999 18 C
ATOM 1403 CD1 PHE A 198 -9.880 -17.222 0.809 1.00 45.36 C
ANISOU 1403 CD1 PHE A 198 6640 5870 4726 -23 938 21 C
ATOM 1404 CD2 PHE A 198 -9.519 -18.890 2.480 1.00 44.36 C
ANISOU 1404 CD2 PHE A 198 6542 5716 4596 42 1051 -19 C
ATOM 1405 CE1 PHE A 198 -8.498 -17.042 0.691 1.00 45.79 C
ANISOU 1405 CE1 PHE A 198 6746 5913 4741 -25 935 -15 C
ATOM 1406 CE2 PHE A 198 -8.137 -18.705 2.365 1.00 46.68 C
ANISOU 1406 CE2 PHE A 198 6888 5992 4855 40 1043 -57 C
ATOM 1407 CZ PHE A 198 -7.637 -17.780 1.475 1.00 44.58 C
ANISOU 1407 CZ PHE A 198 6633 5734 4572 9 988 -55 C
ATOM 1408 N TRP A 199 -11.421 -21.289 0.870 1.00 41.94 N
ANISOU 1408 N TRP A 199 6152 5442 4342 -119 1053 6 N
ATOM 1409 CA TRP A 199 -10.508 -22.380 0.525 1.00 41.98 C
ANISOU 1409 CA TRP A 199 6188 5434 4330 -164 1075 -50 C
ATOM 1410 C TRP A 199 -10.896 -23.119 -0.761 1.00 46.07 C
ANISOU 1410 C TRP A 199 6688 5970 4847 -261 1043 -73 C
ATOM 1411 O TRP A 199 -9.990 -23.543 -1.474 1.00 45.59 O
ANISOU 1411 O TRP A 199 6659 5913 4749 -311 1042 -132 O
ATOM 1412 CB TRP A 199 -10.349 -23.365 1.687 1.00 40.92 C
ANISOU 1412 CB TRP A 199 6048 5267 4232 -121 1137 -50 C
ATOM 1413 CG TRP A 199 -9.325 -22.909 2.685 1.00 41.75 C
ANISOU 1413 CG TRP A 199 6197 5355 4312 -51 1165 -60 C
ATOM 1414 CD1 TRP A 199 -9.561 -22.281 3.872 1.00 44.61 C
ANISOU 1414 CD1 TRP A 199 6558 5720 4673 32 1189 -27 C
ATOM 1415 CD2 TRP A 199 -7.899 -22.962 2.535 1.00 41.24 C
ANISOU 1415 CD2 TRP A 199 6183 5267 4218 -57 1169 -109 C
ATOM 1416 NE1 TRP A 199 -8.371 -21.967 4.488 1.00 43.80 N
ANISOU 1416 NE1 TRP A 199 6506 5598 4539 74 1200 -53 N
ATOM 1417 CE2 TRP A 199 -7.334 -22.373 3.688 1.00 44.97 C
ANISOU 1417 CE2 TRP A 199 6684 5726 4676 21 1187 -98 C
ATOM 1418 CE3 TRP A 199 -7.039 -23.472 1.545 1.00 42.50 C
ANISOU 1418 CE3 TRP A 199 6365 5418 4364 -122 1161 -164 C
ATOM 1419 CZ2 TRP A 199 -5.950 -22.283 3.882 1.00 43.89 C
ANISOU 1419 CZ2 TRP A 199 6596 5560 4521 34 1189 -131 C
ATOM 1420 CZ3 TRP A 199 -5.668 -23.385 1.739 1.00 43.59 C
ANISOU 1420 CZ3 TRP A 199 6546 5528 4487 -106 1173 -197 C
ATOM 1421 CH2 TRP A 199 -5.136 -22.795 2.894 1.00 43.93 C
ANISOU 1421 CH2 TRP A 199 6616 5550 4525 -29 1183 -177 C
ATOM 1422 N ILE A 200 -12.205 -23.238 -1.085 1.00 42.94 N
ANISOU 1422 N ILE A 200 6240 5587 4490 -288 1015 -29 N
ATOM 1423 CA ILE A 200 -12.654 -23.893 -2.322 1.00 43.15 C
ANISOU 1423 CA ILE A 200 6249 5634 4512 -383 973 -52 C
ATOM 1424 C ILE A 200 -12.247 -23.011 -3.526 1.00 47.10 C
ANISOU 1424 C ILE A 200 6777 6183 4935 -441 915 -64 C
ATOM 1425 O ILE A 200 -11.715 -23.537 -4.502 1.00 46.81 O
ANISOU 1425 O ILE A 200 6764 6170 4849 -514 902 -124 O
ATOM 1426 CB ILE A 200 -14.178 -24.258 -2.278 1.00 46.75 C
ANISOU 1426 CB ILE A 200 6637 6085 5041 -396 952 8 C
ATOM 1427 CG1 ILE A 200 -14.379 -25.770 -2.059 1.00 47.54 C
ANISOU 1427 CG1 ILE A 200 6712 6151 5201 -422 979 -20 C
ATOM 1428 CG2 ILE A 200 -14.978 -23.790 -3.504 1.00 47.90 C
ANISOU 1428 CG2 ILE A 200 6760 6270 5172 -466 871 40 C
ATOM 1429 CD1 ILE A 200 -14.342 -26.230 -0.614 1.00 55.66 C
ANISOU 1429 CD1 ILE A 200 7710 7143 6296 -347 1042 22 C
ATOM 1430 N ASN A 201 -12.435 -21.677 -3.417 1.00 43.60 N
ANISOU 1430 N ASN A 201 6330 5755 4483 -407 882 -8 N
ATOM 1431 CA ASN A 201 -12.079 -20.709 -4.456 1.00 43.47 C
ANISOU 1431 CA ASN A 201 6330 5785 4404 -457 822 3 C
ATOM 1432 C ASN A 201 -10.564 -20.541 -4.559 1.00 47.15 C
ANISOU 1432 C ASN A 201 6853 6254 4808 -451 848 -50 C
ATOM 1433 O ASN A 201 -10.045 -20.429 -5.668 1.00 46.81 O
ANISOU 1433 O ASN A 201 6830 6259 4695 -521 819 -72 O
ATOM 1434 CB ASN A 201 -12.740 -19.361 -4.192 1.00 43.35 C
ANISOU 1434 CB ASN A 201 6278 5768 4426 -417 777 84 C
ATOM 1435 CG ASN A 201 -14.177 -19.292 -4.629 1.00 63.48 C
ANISOU 1435 CG ASN A 201 8766 8327 7026 -455 726 146 C
ATOM 1436 OD1 ASN A 201 -14.482 -19.144 -5.817 1.00 58.52 O
ANISOU 1436 OD1 ASN A 201 8127 7743 6364 -543 659 166 O
ATOM 1437 ND2 ASN A 201 -15.095 -19.370 -3.677 1.00 54.38 N
ANISOU 1437 ND2 ASN A 201 7569 7136 5955 -390 755 183 N
ATOM 1438 N PHE A 202 -9.860 -20.529 -3.406 1.00 43.54 N
ANISOU 1438 N PHE A 202 6419 5751 4375 -369 903 -68 N
ATOM 1439 CA PHE A 202 -8.405 -20.392 -3.325 1.00 43.08 C
ANISOU 1439 CA PHE A 202 6410 5681 4278 -352 930 -113 C
ATOM 1440 C PHE A 202 -7.714 -21.606 -3.953 1.00 47.05 C
ANISOU 1440 C PHE A 202 6936 6190 4752 -413 965 -191 C
ATOM 1441 O PHE A 202 -6.745 -21.420 -4.688 1.00 46.63 O
ANISOU 1441 O PHE A 202 6912 6162 4643 -450 964 -225 O
ATOM 1442 CB PHE A 202 -7.956 -20.189 -1.866 1.00 44.48 C
ANISOU 1442 CB PHE A 202 6602 5804 4493 -253 974 -110 C
ATOM 1443 CG PHE A 202 -6.475 -20.012 -1.613 1.00 45.80 C
ANISOU 1443 CG PHE A 202 6816 5948 4637 -227 995 -146 C
ATOM 1444 CD1 PHE A 202 -5.721 -19.123 -2.374 1.00 49.03 C
ANISOU 1444 CD1 PHE A 202 7243 6381 5006 -253 956 -139 C
ATOM 1445 CD2 PHE A 202 -5.850 -20.676 -0.564 1.00 47.79 C
ANISOU 1445 CD2 PHE A 202 7090 6152 4915 -177 1048 -174 C
ATOM 1446 CE1 PHE A 202 -4.356 -18.950 -2.126 1.00 49.66 C
ANISOU 1446 CE1 PHE A 202 7360 6433 5076 -228 974 -166 C
ATOM 1447 CE2 PHE A 202 -4.488 -20.495 -0.311 1.00 50.30 C
ANISOU 1447 CE2 PHE A 202 7448 6442 5223 -154 1061 -201 C
ATOM 1448 CZ PHE A 202 -3.750 -19.632 -1.092 1.00 48.43 C
ANISOU 1448 CZ PHE A 202 7227 6225 4950 -178 1025 -198 C
ATOM 1449 N LEU A 203 -8.235 -22.832 -3.706 1.00 43.64 N
ANISOU 1449 N LEU A 203 6483 5735 4363 -426 994 -219 N
ATOM 1450 CA LEU A 203 -7.685 -24.062 -4.287 1.00 43.61 C
ANISOU 1450 CA LEU A 203 6490 5726 4353 -483 1025 -303 C
ATOM 1451 C LEU A 203 -7.971 -24.134 -5.792 1.00 47.66 C
ANISOU 1451 C LEU A 203 7004 6307 4799 -582 981 -334 C
ATOM 1452 O LEU A 203 -7.168 -24.713 -6.523 1.00 47.66 O
ANISOU 1452 O LEU A 203 7026 6324 4756 -632 1003 -414 O
ATOM 1453 CB LEU A 203 -8.209 -25.322 -3.580 1.00 43.86 C
ANISOU 1453 CB LEU A 203 6490 5707 4469 -469 1059 -316 C
ATOM 1454 CG LEU A 203 -7.511 -25.702 -2.265 1.00 48.29 C
ANISOU 1454 CG LEU A 203 7057 6205 5086 -394 1114 -310 C
ATOM 1455 CD1 LEU A 203 -8.415 -26.554 -1.392 1.00 48.62 C
ANISOU 1455 CD1 LEU A 203 7051 6211 5210 -369 1133 -273 C
ATOM 1456 CD2 LEU A 203 -6.191 -26.428 -2.518 1.00 51.04 C
ANISOU 1456 CD2 LEU A 203 7433 6522 5439 -412 1154 -389 C
ATOM 1457 N ILE A 204 -9.093 -23.528 -6.252 1.00 43.98 N
ANISOU 1457 N ILE A 204 6508 5880 4320 -610 918 -270 N
ATOM 1458 CA ILE A 204 -9.479 -23.463 -7.668 1.00 44.20 C
ANISOU 1458 CA ILE A 204 6535 5984 4275 -708 861 -281 C
ATOM 1459 C ILE A 204 -8.460 -22.585 -8.421 1.00 47.22 C
ANISOU 1459 C ILE A 204 6953 6424 4564 -735 850 -283 C
ATOM 1460 O ILE A 204 -7.980 -22.985 -9.482 1.00 47.17 O
ANISOU 1460 O ILE A 204 6968 6476 4479 -811 850 -347 O
ATOM 1461 CB ILE A 204 -10.952 -22.959 -7.824 1.00 47.69 C
ANISOU 1461 CB ILE A 204 6931 6443 4747 -724 791 -192 C
ATOM 1462 CG1 ILE A 204 -11.950 -24.141 -7.757 1.00 48.51 C
ANISOU 1462 CG1 ILE A 204 6998 6517 4915 -750 788 -213 C
ATOM 1463 CG2 ILE A 204 -11.166 -22.124 -9.104 1.00 48.98 C
ANISOU 1463 CG2 ILE A 204 7095 6691 4825 -804 713 -152 C
ATOM 1464 CD1 ILE A 204 -13.426 -23.761 -7.430 1.00 55.06 C
ANISOU 1464 CD1 ILE A 204 7771 7333 5819 -734 740 -116 C
ATOM 1465 N VAL A 205 -8.110 -21.419 -7.840 1.00 42.97 N
ANISOU 1465 N VAL A 205 6419 5870 4038 -673 842 -217 N
ATOM 1466 CA VAL A 205 -7.170 -20.443 -8.398 1.00 42.62 C
ANISOU 1466 CA VAL A 205 6398 5871 3927 -688 825 -197 C
ATOM 1467 C VAL A 205 -5.744 -21.041 -8.439 1.00 46.19 C
ANISOU 1467 C VAL A 205 6890 6310 4352 -685 896 -284 C
ATOM 1468 O VAL A 205 -5.037 -20.804 -9.418 1.00 46.34 O
ANISOU 1468 O VAL A 205 6926 6393 4287 -742 894 -303 O
ATOM 1469 CB VAL A 205 -7.238 -19.087 -7.635 1.00 45.97 C
ANISOU 1469 CB VAL A 205 6805 6263 4397 -616 791 -106 C
ATOM 1470 CG1 VAL A 205 -6.144 -18.127 -8.082 1.00 45.67 C
ANISOU 1470 CG1 VAL A 205 6784 6260 4308 -628 772 -79 C
ATOM 1471 CG2 VAL A 205 -8.605 -18.429 -7.811 1.00 46.15 C
ANISOU 1471 CG2 VAL A 205 6780 6302 4454 -629 720 -22 C
ATOM 1472 N ILE A 206 -5.349 -21.844 -7.422 1.00 42.09 N
ANISOU 1472 N ILE A 206 6379 5712 3902 -623 958 -331 N
ATOM 1473 CA ILE A 206 -4.026 -22.489 -7.364 1.00 41.77 C
ANISOU 1473 CA ILE A 206 6366 5642 3860 -617 1024 -411 C
ATOM 1474 C ILE A 206 -3.900 -23.550 -8.480 1.00 46.15 C
ANISOU 1474 C ILE A 206 6927 6243 4366 -703 1048 -508 C
ATOM 1475 O ILE A 206 -2.932 -23.505 -9.240 1.00 45.97 O
ANISOU 1475 O ILE A 206 6923 6262 4279 -742 1074 -554 O
ATOM 1476 CB ILE A 206 -3.716 -23.090 -5.956 1.00 44.34 C
ANISOU 1476 CB ILE A 206 6694 5872 4283 -535 1074 -424 C
ATOM 1477 CG1 ILE A 206 -3.513 -21.975 -4.905 1.00 44.21 C
ANISOU 1477 CG1 ILE A 206 6685 5818 4294 -449 1058 -350 C
ATOM 1478 CG2 ILE A 206 -2.489 -24.028 -5.993 1.00 45.01 C
ANISOU 1478 CG2 ILE A 206 6794 5919 4388 -543 1140 -514 C
ATOM 1479 CD1 ILE A 206 -3.748 -22.415 -3.445 1.00 50.84 C
ANISOU 1479 CD1 ILE A 206 7518 6585 5213 -371 1087 -336 C
ATOM 1480 N VAL A 207 -4.874 -24.484 -8.572 1.00 43.14 N
ANISOU 1480 N VAL A 207 6522 5852 4015 -733 1040 -541 N
ATOM 1481 CA VAL A 207 -4.899 -25.576 -9.558 1.00 43.85 C
ANISOU 1481 CA VAL A 207 6612 5976 4073 -812 1055 -647 C
ATOM 1482 C VAL A 207 -4.867 -25.001 -10.993 1.00 49.15 C
ANISOU 1482 C VAL A 207 7301 6766 4610 -900 1018 -653 C
ATOM 1483 O VAL A 207 -4.046 -25.455 -11.794 1.00 49.35 O
ANISOU 1483 O VAL A 207 7345 6832 4574 -947 1059 -746 O
ATOM 1484 CB VAL A 207 -6.097 -26.540 -9.324 1.00 47.79 C
ANISOU 1484 CB VAL A 207 7076 6436 4645 -823 1035 -659 C
ATOM 1485 CG1 VAL A 207 -6.327 -27.469 -10.514 1.00 48.56 C
ANISOU 1485 CG1 VAL A 207 7171 6585 4693 -918 1021 -758 C
ATOM 1486 CG2 VAL A 207 -5.895 -27.356 -8.050 1.00 47.08 C
ANISOU 1486 CG2 VAL A 207 6967 6240 4679 -755 1088 -676 C
ATOM 1487 N CYS A 208 -5.708 -23.982 -11.289 1.00 46.13 N
ANISOU 1487 N CYS A 208 6906 6438 4184 -920 941 -552 N
ATOM 1488 CA CYS A 208 -5.772 -23.321 -12.598 1.00 46.89 C
ANISOU 1488 CA CYS A 208 7011 6653 4153 -1007 891 -529 C
ATOM 1489 C CYS A 208 -4.420 -22.701 -12.966 1.00 51.18 C
ANISOU 1489 C CYS A 208 7580 7241 4625 -1010 928 -531 C
ATOM 1490 O CYS A 208 -3.923 -22.954 -14.065 1.00 51.80 O
ANISOU 1490 O CYS A 208 7677 7411 4595 -1086 943 -592 O
ATOM 1491 CB CYS A 208 -6.882 -22.276 -12.630 1.00 47.22 C
ANISOU 1491 CB CYS A 208 7024 6721 4197 -1014 799 -399 C
ATOM 1492 SG CYS A 208 -8.551 -22.968 -12.751 1.00 51.69 S
ANISOU 1492 SG CYS A 208 7555 7279 4805 -1057 738 -394 S
ATOM 1493 N TYR A 209 -3.820 -21.925 -12.036 1.00 46.91 N
ANISOU 1493 N TYR A 209 7039 6637 4145 -927 943 -469 N
ATOM 1494 CA TYR A 209 -2.524 -21.263 -12.204 1.00 46.58 C
ANISOU 1494 CA TYR A 209 7014 6619 4064 -917 973 -455 C
ATOM 1495 C TYR A 209 -1.408 -22.286 -12.486 1.00 50.16 C
ANISOU 1495 C TYR A 209 7490 7065 4503 -930 1065 -582 C
ATOM 1496 O TYR A 209 -0.593 -22.050 -13.377 1.00 50.19 O
ANISOU 1496 O TYR A 209 7506 7148 4418 -979 1090 -604 O
ATOM 1497 CB TYR A 209 -2.190 -20.405 -10.960 1.00 47.02 C
ANISOU 1497 CB TYR A 209 7065 6588 4213 -817 964 -373 C
ATOM 1498 CG TYR A 209 -0.716 -20.120 -10.772 1.00 48.90 C
ANISOU 1498 CG TYR A 209 7320 6802 4457 -783 1014 -385 C
ATOM 1499 CD1 TYR A 209 -0.097 -19.069 -11.443 1.00 51.13 C
ANISOU 1499 CD1 TYR A 209 7598 7149 4679 -811 987 -317 C
ATOM 1500 CD2 TYR A 209 0.066 -20.914 -9.937 1.00 49.31 C
ANISOU 1500 CD2 TYR A 209 7386 6764 4585 -727 1085 -455 C
ATOM 1501 CE1 TYR A 209 1.267 -18.824 -11.300 1.00 51.65 C
ANISOU 1501 CE1 TYR A 209 7675 7191 4760 -781 1032 -323 C
ATOM 1502 CE2 TYR A 209 1.433 -20.691 -9.801 1.00 50.11 C
ANISOU 1502 CE2 TYR A 209 7499 6839 4701 -700 1128 -464 C
ATOM 1503 CZ TYR A 209 2.027 -19.635 -10.473 1.00 58.44 C
ANISOU 1503 CZ TYR A 209 8550 7957 5696 -725 1103 -398 C
ATOM 1504 OH TYR A 209 3.371 -19.403 -10.324 1.00 60.07 O
ANISOU 1504 OH TYR A 209 8763 8132 5928 -697 1143 -400 O
ATOM 1505 N THR A 210 -1.369 -23.401 -11.719 1.00 46.21 N
ANISOU 1505 N THR A 210 6988 6471 4098 -888 1115 -661 N
ATOM 1506 CA THR A 210 -0.367 -24.470 -11.847 1.00 46.20 C
ANISOU 1506 CA THR A 210 6996 6437 4121 -893 1202 -785 C
ATOM 1507 C THR A 210 -0.421 -25.088 -13.251 1.00 51.37 C
ANISOU 1507 C THR A 210 7657 7192 4668 -991 1218 -889 C
ATOM 1508 O THR A 210 0.628 -25.264 -13.868 1.00 51.33 O
ANISOU 1508 O THR A 210 7662 7219 4620 -1016 1284 -967 O
ATOM 1509 CB THR A 210 -0.556 -25.541 -10.748 1.00 52.69 C
ANISOU 1509 CB THR A 210 7803 7137 5079 -835 1232 -829 C
ATOM 1510 OG1 THR A 210 -0.673 -24.904 -9.476 1.00 51.96 O
ANISOU 1510 OG1 THR A 210 7707 6972 5062 -750 1209 -729 O
ATOM 1511 CG2 THR A 210 0.591 -26.547 -10.700 1.00 50.54 C
ANISOU 1511 CG2 THR A 210 7530 6807 4866 -828 1318 -942 C
ATOM 1512 N LEU A 211 -1.639 -25.386 -13.751 1.00 48.73 N
ANISOU 1512 N LEU A 211 7317 6910 4290 -1048 1159 -889 N
ATOM 1513 CA LEU A 211 -1.875 -25.979 -15.069 1.00 50.01 C
ANISOU 1513 CA LEU A 211 7488 7173 4340 -1146 1159 -989 C
ATOM 1514 C LEU A 211 -1.424 -25.042 -16.199 1.00 55.48 C
ANISOU 1514 C LEU A 211 8198 8010 4873 -1212 1143 -947 C
ATOM 1515 O LEU A 211 -0.870 -25.520 -17.191 1.00 56.21 O
ANISOU 1515 O LEU A 211 8305 8188 4863 -1280 1187 -1052 O
ATOM 1516 CB LEU A 211 -3.357 -26.352 -15.243 1.00 50.41 C
ANISOU 1516 CB LEU A 211 7523 7230 4400 -1185 1084 -984 C
ATOM 1517 CG LEU A 211 -3.868 -27.554 -14.436 1.00 54.69 C
ANISOU 1517 CG LEU A 211 8041 7648 5092 -1140 1100 -1039 C
ATOM 1518 CD1 LEU A 211 -5.361 -27.465 -14.224 1.00 54.85 C
ANISOU 1518 CD1 LEU A 211 8036 7658 5144 -1152 1015 -967 C
ATOM 1519 CD2 LEU A 211 -3.516 -28.874 -15.109 1.00 58.02 C
ANISOU 1519 CD2 LEU A 211 8462 8056 5529 -1179 1159 -1213 C
ATOM 1520 N ILE A 212 -1.639 -23.717 -16.033 1.00 52.05 N
ANISOU 1520 N ILE A 212 7757 7599 4420 -1193 1083 -795 N
ATOM 1521 CA ILE A 212 -1.242 -22.681 -16.996 1.00 52.62 C
ANISOU 1521 CA ILE A 212 7834 7800 4358 -1252 1058 -721 C
ATOM 1522 C ILE A 212 0.294 -22.589 -17.032 1.00 57.38 C
ANISOU 1522 C ILE A 212 8446 8403 4951 -1227 1149 -760 C
ATOM 1523 O ILE A 212 0.875 -22.599 -18.120 1.00 58.08 O
ANISOU 1523 O ILE A 212 8545 8609 4912 -1297 1185 -805 O
ATOM 1524 CB ILE A 212 -1.922 -21.315 -16.661 1.00 55.08 C
ANISOU 1524 CB ILE A 212 8123 8114 4691 -1233 960 -544 C
ATOM 1525 CG1 ILE A 212 -3.421 -21.353 -17.020 1.00 55.85 C
ANISOU 1525 CG1 ILE A 212 8207 8249 4765 -1288 868 -505 C
ATOM 1526 CG2 ILE A 212 -1.224 -20.127 -17.358 1.00 56.15 C
ANISOU 1526 CG2 ILE A 212 8253 8350 4732 -1270 941 -445 C
ATOM 1527 CD1 ILE A 212 -4.316 -20.410 -16.221 1.00 62.36 C
ANISOU 1527 CD1 ILE A 212 8998 9013 5682 -1238 785 -362 C
ATOM 1528 N THR A 213 0.939 -22.531 -15.846 1.00 53.54 N
ANISOU 1528 N THR A 213 7955 7788 4600 -1130 1186 -744 N
ATOM 1529 CA THR A 213 2.396 -22.450 -15.697 1.00 53.54 C
ANISOU 1529 CA THR A 213 7957 7759 4624 -1095 1267 -770 C
ATOM 1530 C THR A 213 3.053 -23.728 -16.247 1.00 59.15 C
ANISOU 1530 C THR A 213 8677 8483 5314 -1129 1365 -942 C
ATOM 1531 O THR A 213 4.100 -23.635 -16.889 1.00 59.25 O
ANISOU 1531 O THR A 213 8691 8555 5267 -1153 1431 -978 O
ATOM 1532 CB THR A 213 2.780 -22.176 -14.235 1.00 60.14 C
ANISOU 1532 CB THR A 213 8787 8448 5614 -986 1269 -715 C
ATOM 1533 OG1 THR A 213 1.915 -21.171 -13.702 1.00 58.99 O
ANISOU 1533 OG1 THR A 213 8632 8284 5498 -955 1176 -586 O
ATOM 1534 CG2 THR A 213 4.223 -21.713 -14.087 1.00 58.65 C
ANISOU 1534 CG2 THR A 213 8596 8237 5450 -951 1319 -690 C
ATOM 1535 N LYS A 214 2.415 -24.904 -16.033 1.00 56.71 N
ANISOU 1535 N LYS A 214 8367 8121 5058 -1134 1373 -1048 N
ATOM 1536 CA LYS A 214 2.884 -26.201 -16.535 1.00 57.73 C
ANISOU 1536 CA LYS A 214 8498 8250 5188 -1167 1457 -1224 C
ATOM 1537 C LYS A 214 2.842 -26.219 -18.069 1.00 64.10 C
ANISOU 1537 C LYS A 214 9319 9226 5808 -1272 1465 -1290 C
ATOM 1538 O LYS A 214 3.768 -26.736 -18.699 1.00 64.70 O
ANISOU 1538 O LYS A 214 9397 9345 5841 -1299 1555 -1408 O
ATOM 1539 CB LYS A 214 2.041 -27.349 -15.954 1.00 59.96 C
ANISOU 1539 CB LYS A 214 8767 8431 5583 -1148 1444 -1301 C
ATOM 1540 CG LYS A 214 2.772 -28.687 -15.904 1.00 75.07 C
ANISOU 1540 CG LYS A 214 10665 10265 7591 -1137 1536 -1464 C
ATOM 1541 CD LYS A 214 2.249 -29.599 -14.794 1.00 85.49 C
ANISOU 1541 CD LYS A 214 11959 11437 9087 -1082 1523 -1480 C
ATOM 1542 CE LYS A 214 2.942 -29.364 -13.469 1.00 96.07 C
ANISOU 1542 CE LYS A 214 13288 12652 10564 -989 1549 -1407 C
ATOM 1543 NZ LYS A 214 2.412 -30.253 -12.402 1.00104.80 N
ANISOU 1543 NZ LYS A 214 14366 13628 11825 -940 1529 -1399 N
ATOM 1544 N GLU A 215 1.779 -25.623 -18.660 1.00 61.42 N
ANISOU 1544 N GLU A 215 8989 8989 5360 -1331 1372 -1210 N
ATOM 1545 CA GLU A 215 1.582 -25.505 -20.108 1.00 62.80 C
ANISOU 1545 CA GLU A 215 9181 9342 5340 -1440 1360 -1247 C
ATOM 1546 C GLU A 215 2.626 -24.553 -20.707 1.00 67.17 C
ANISOU 1546 C GLU A 215 9735 10000 5788 -1460 1398 -1176 C
ATOM 1547 O GLU A 215 3.103 -24.804 -21.815 1.00 68.03 O
ANISOU 1547 O GLU A 215 9855 10239 5754 -1531 1454 -1263 O
ATOM 1548 CB GLU A 215 0.147 -25.032 -20.423 1.00 64.40 C
ANISOU 1548 CB GLU A 215 9385 9607 5478 -1494 1236 -1153 C
ATOM 1549 CG GLU A 215 -0.246 -25.051 -21.897 1.00 76.76 C
ANISOU 1549 CG GLU A 215 10969 11357 6838 -1615 1206 -1193 C
ATOM 1550 CD GLU A 215 -0.126 -26.365 -22.650 1.00 99.92 C
ANISOU 1550 CD GLU A 215 13921 14338 9706 -1671 1271 -1406 C
ATOM 1551 OE1 GLU A 215 -0.453 -27.426 -22.071 1.00 94.76 O
ANISOU 1551 OE1 GLU A 215 13260 13568 9177 -1638 1283 -1516 O
ATOM 1552 OE2 GLU A 215 0.267 -26.325 -23.839 1.00 95.50 O
ANISOU 1552 OE2 GLU A 215 13379 13935 8970 -1749 1309 -1463 O
ATOM 1553 N LEU A 216 2.997 -23.486 -19.963 1.00 62.86 N
ANISOU 1553 N LEU A 216 9173 9395 5315 -1395 1371 -1024 N
ATOM 1554 CA LEU A 216 4.011 -22.507 -20.371 1.00 62.95 C
ANISOU 1554 CA LEU A 216 9175 9482 5261 -1402 1399 -933 C
ATOM 1555 C LEU A 216 5.390 -23.174 -20.463 1.00 67.12 C
ANISOU 1555 C LEU A 216 9701 9989 5812 -1382 1532 -1057 C
ATOM 1556 O LEU A 216 6.162 -22.831 -21.357 1.00 67.36 O
ANISOU 1556 O LEU A 216 9728 10145 5722 -1432 1583 -1055 O
ATOM 1557 CB LEU A 216 4.049 -21.317 -19.395 1.00 61.73 C
ANISOU 1557 CB LEU A 216 9001 9237 5218 -1327 1334 -758 C
ATOM 1558 CG LEU A 216 4.639 -20.014 -19.943 1.00 66.76 C
ANISOU 1558 CG LEU A 216 9618 9962 5786 -1348 1318 -620 C
ATOM 1559 CD1 LEU A 216 3.798 -18.826 -19.535 1.00 66.43 C
ANISOU 1559 CD1 LEU A 216 9556 9915 5771 -1340 1193 -440 C
ATOM 1560 CD2 LEU A 216 6.079 -19.820 -19.489 1.00 68.62 C
ANISOU 1560 CD2 LEU A 216 9841 10110 6121 -1275 1397 -621 C
ATOM 1561 N TYR A 217 5.687 -24.126 -19.549 1.00 63.39 N
ANISOU 1561 N TYR A 217 9226 9363 5498 -1311 1587 -1158 N
ATOM 1562 CA TYR A 217 6.944 -24.880 -19.533 1.00 63.80 C
ANISOU 1562 CA TYR A 217 9266 9369 5606 -1286 1711 -1282 C
ATOM 1563 C TYR A 217 6.993 -25.866 -20.699 1.00 68.98 C
ANISOU 1563 C TYR A 217 9932 10133 6144 -1365 1783 -1464 C
ATOM 1564 O TYR A 217 8.043 -26.014 -21.324 1.00 69.33 O
ANISOU 1564 O TYR A 217 9967 10239 6137 -1385 1883 -1537 O
ATOM 1565 CB TYR A 217 7.137 -25.635 -18.202 1.00 64.29 C
ANISOU 1565 CB TYR A 217 9315 9231 5879 -1194 1735 -1327 C
ATOM 1566 CG TYR A 217 7.214 -24.774 -16.957 1.00 65.16 C
ANISOU 1566 CG TYR A 217 9420 9228 6111 -1108 1675 -1173 C
ATOM 1567 CD1 TYR A 217 7.876 -23.549 -16.970 1.00 67.02 C
ANISOU 1567 CD1 TYR A 217 9648 9499 6316 -1094 1654 -1035 C
ATOM 1568 CD2 TYR A 217 6.709 -25.228 -15.742 1.00 65.03 C
ANISOU 1568 CD2 TYR A 217 9401 9064 6245 -1040 1645 -1171 C
ATOM 1569 CE1 TYR A 217 7.966 -22.762 -15.822 1.00 66.85 C
ANISOU 1569 CE1 TYR A 217 9622 9369 6409 -1014 1597 -909 C
ATOM 1570 CE2 TYR A 217 6.803 -24.456 -14.585 1.00 64.81 C
ANISOU 1570 CE2 TYR A 217 9370 8938 6318 -961 1594 -1042 C
ATOM 1571 CZ TYR A 217 7.437 -23.225 -14.629 1.00 72.65 C
ANISOU 1571 CZ TYR A 217 10360 9966 7278 -948 1569 -919 C
ATOM 1572 OH TYR A 217 7.529 -22.459 -13.491 1.00 73.12 O
ANISOU 1572 OH TYR A 217 10418 9928 7438 -870 1515 -806 O
ATOM 1573 N ARG A 218 5.854 -26.537 -20.987 1.00 65.87 N
ANISOU 1573 N ARG A 218 9553 9761 5712 -1410 1731 -1539 N
ATOM 1574 CA ARG A 218 5.704 -27.505 -22.077 1.00 67.12 C
ANISOU 1574 CA ARG A 218 9725 10020 5758 -1489 1779 -1723 C
ATOM 1575 C ARG A 218 5.848 -26.816 -23.440 1.00 71.92 C
ANISOU 1575 C ARG A 218 10349 10848 6128 -1584 1784 -1694 C
ATOM 1576 O ARG A 218 6.445 -27.389 -24.353 1.00 72.73 O
ANISOU 1576 O ARG A 218 10456 11048 6129 -1634 1877 -1842 O
ATOM 1577 CB ARG A 218 4.351 -28.223 -21.976 1.00 67.45 C
ANISOU 1577 CB ARG A 218 9776 10025 5827 -1512 1697 -1777 C
ATOM 1578 N SER A 219 5.321 -25.579 -23.561 1.00 68.06 N
ANISOU 1578 N SER A 219 9866 10438 5557 -1609 1684 -1503 N
ATOM 1579 CA SER A 219 5.393 -24.758 -24.771 1.00 69.08 C
ANISOU 1579 CA SER A 219 10004 10777 5467 -1701 1669 -1430 C
ATOM 1580 C SER A 219 6.794 -24.175 -24.955 1.00 73.34 C
ANISOU 1580 C SER A 219 10522 11360 5985 -1682 1761 -1378 C
ATOM 1581 O SER A 219 7.198 -23.918 -26.089 1.00 74.37 O
ANISOU 1581 O SER A 219 10655 11671 5930 -1760 1804 -1387 O
ATOM 1582 CB SER A 219 4.362 -23.637 -24.721 1.00 71.98 C
ANISOU 1582 CB SER A 219 10370 11188 5792 -1729 1523 -1230 C
ATOM 1583 OG SER A 219 3.053 -24.168 -24.605 1.00 80.62 O
ANISOU 1583 OG SER A 219 11480 12257 6894 -1757 1440 -1276 O
ATOM 1584 N TYR A 220 7.532 -23.970 -23.845 1.00 68.88 N
ANISOU 1584 N TYR A 220 9933 10631 5607 -1581 1789 -1322 N
ATOM 1585 CA TYR A 220 8.899 -23.449 -23.854 1.00 68.96 C
ANISOU 1585 CA TYR A 220 9916 10649 5637 -1551 1872 -1267 C
ATOM 1586 C TYR A 220 9.863 -24.510 -24.391 1.00 75.05 C
ANISOU 1586 C TYR A 220 10681 11444 6389 -1561 2024 -1468 C
ATOM 1587 O TYR A 220 10.668 -24.197 -25.268 1.00 75.73 O
ANISOU 1587 O TYR A 220 10754 11666 6355 -1604 2101 -1464 O
ATOM 1588 CB TYR A 220 9.323 -22.984 -22.443 1.00 68.25 C
ANISOU 1588 CB TYR A 220 9804 10365 5761 -1440 1845 -1156 C
ATOM 1589 CG TYR A 220 10.766 -22.533 -22.333 1.00 69.89 C
ANISOU 1589 CG TYR A 220 9981 10549 6025 -1399 1931 -1114 C
ATOM 1590 CD1 TYR A 220 11.144 -21.243 -22.691 1.00 72.02 C
ANISOU 1590 CD1 TYR A 220 10228 10912 6224 -1421 1900 -942 C
ATOM 1591 CD2 TYR A 220 11.748 -23.387 -21.838 1.00 70.45 C
ANISOU 1591 CD2 TYR A 220 10037 10495 6236 -1340 2037 -1237 C
ATOM 1592 CE1 TYR A 220 12.472 -20.827 -22.606 1.00 72.80 C
ANISOU 1592 CE1 TYR A 220 10292 10986 6381 -1386 1977 -898 C
ATOM 1593 CE2 TYR A 220 13.080 -22.982 -21.746 1.00 71.36 C
ANISOU 1593 CE2 TYR A 220 10118 10583 6413 -1305 2114 -1195 C
ATOM 1594 CZ TYR A 220 13.435 -21.696 -22.118 1.00 78.86 C
ANISOU 1594 CZ TYR A 220 11047 11629 7286 -1326 2084 -1025 C
ATOM 1595 OH TYR A 220 14.742 -21.286 -22.012 1.00 79.94 O
ANISOU 1595 OH TYR A 220 11145 11733 7494 -1291 2156 -975 O
ATOM 1596 N VAL A 221 9.779 -25.753 -23.856 1.00 72.27 N
ANISOU 1596 N VAL A 221 10333 10960 6169 -1521 2068 -1637 N
ATOM 1597 CA VAL A 221 10.619 -26.905 -24.213 1.00 73.54 C
ANISOU 1597 CA VAL A 221 10479 11104 6360 -1520 2208 -1848 C
ATOM 1598 C VAL A 221 10.525 -27.178 -25.730 1.00 80.88 C
ANISOU 1598 C VAL A 221 11427 12253 7050 -1627 2262 -1971 C
ATOM 1599 O VAL A 221 11.564 -27.330 -26.376 1.00 81.48 O
ANISOU 1599 O VAL A 221 11485 12411 7064 -1644 2385 -2046 O
ATOM 1600 CB VAL A 221 10.264 -28.159 -23.355 1.00 76.65 C
ANISOU 1600 CB VAL A 221 10867 11309 6949 -1465 2212 -1987 C
ATOM 1601 CG1 VAL A 221 10.887 -29.438 -23.914 1.00 77.88 C
ANISOU 1601 CG1 VAL A 221 11006 11467 7117 -1485 2339 -2232 C
ATOM 1602 CG2 VAL A 221 10.683 -27.962 -21.900 1.00 74.64 C
ANISOU 1602 CG2 VAL A 221 10588 10850 6923 -1359 2196 -1887 C
ATOM 1603 N ARG A 222 9.296 -27.184 -26.292 1.00 79.21 N
ANISOU 1603 N ARG A 222 11251 12143 6703 -1700 2169 -1982 N
ATOM 1604 CA ARG A 222 9.042 -27.417 -27.720 1.00 81.66 C
ANISOU 1604 CA ARG A 222 11587 12671 6768 -1810 2196 -2093 C
ATOM 1605 C ARG A 222 9.649 -26.312 -28.599 1.00 87.85 C
ANISOU 1605 C ARG A 222 12366 13656 7358 -1868 2223 -1960 C
ATOM 1606 O ARG A 222 10.138 -26.610 -29.690 1.00 89.37 O
ANISOU 1606 O ARG A 222 12563 14017 7378 -1934 2320 -2078 O
ATOM 1607 CB ARG A 222 7.538 -27.549 -28.000 1.00 82.16 C
ANISOU 1607 CB ARG A 222 11687 12786 6745 -1873 2064 -2093 C
ATOM 1608 CG ARG A 222 6.948 -28.875 -27.528 1.00 92.68 C
ANISOU 1608 CG ARG A 222 13022 13969 8221 -1844 2056 -2273 C
ATOM 1609 CD ARG A 222 5.649 -29.217 -28.233 1.00104.14 C
ANISOU 1609 CD ARG A 222 14510 15521 9538 -1932 1958 -2335 C
ATOM 1610 NE ARG A 222 4.524 -28.411 -27.754 1.00111.23 N
ANISOU 1610 NE ARG A 222 15417 16399 10447 -1936 1804 -2132 N
ATOM 1611 CZ ARG A 222 3.288 -28.481 -28.240 1.00125.64 C
ANISOU 1611 CZ ARG A 222 17268 18307 12164 -2013 1692 -2125 C
ATOM 1612 NH1 ARG A 222 3.002 -29.322 -29.227 1.00114.48 N
ANISOU 1612 NH1 ARG A 222 15880 17005 10613 -2094 1711 -2314 N
ATOM 1613 NH2 ARG A 222 2.330 -27.711 -27.744 1.00111.06 N
ANISOU 1613 NH2 ARG A 222 15419 16428 10350 -2009 1560 -1933 N
ATOM 1614 N THR A 223 9.632 -25.052 -28.118 1.00 84.15 N
ANISOU 1614 N THR A 223 11882 13169 6924 -1842 2140 -1717 N
ATOM 1615 CA THR A 223 10.194 -23.901 -28.830 1.00 85.15 C
ANISOU 1615 CA THR A 223 11990 13464 6900 -1890 2148 -1553 C
ATOM 1616 C THR A 223 11.728 -23.914 -28.691 1.00 90.60 C
ANISOU 1616 C THR A 223 12640 14116 7668 -1836 2292 -1578 C
ATOM 1617 O THR A 223 12.424 -23.543 -29.639 1.00 91.64 O
ANISOU 1617 O THR A 223 12757 14425 7637 -1894 2371 -1562 O
ATOM 1618 CB THR A 223 9.557 -22.594 -28.329 1.00 91.61 C
ANISOU 1618 CB THR A 223 12798 14252 7757 -1879 1996 -1293 C
ATOM 1619 OG1 THR A 223 8.137 -22.741 -28.343 1.00 91.16 O
ANISOU 1619 OG1 THR A 223 12772 14204 7659 -1920 1871 -1289 O
ATOM 1620 CG2 THR A 223 9.931 -21.391 -29.184 1.00 91.30 C
ANISOU 1620 CG2 THR A 223 12734 14398 7557 -1944 1980 -1108 C
ATOM 1621 N ALA A1001 12.246 -24.357 -27.524 1.00 73.84 N
ANISOU 1621 N ALA A1001 9729 12489 5839 -1182 2949 -1043 N
ATOM 1622 CA ALA A1001 13.684 -24.458 -27.248 1.00 73.35 C
ANISOU 1622 CA ALA A1001 9734 12240 5897 -934 3138 -1056 C
ATOM 1623 C ALA A1001 14.340 -25.527 -28.132 1.00 80.26 C
ANISOU 1623 C ALA A1001 10997 12946 6552 -880 3225 -1166 C
ATOM 1624 O ALA A1001 15.457 -25.316 -28.606 1.00 79.79 O
ANISOU 1624 O ALA A1001 10956 12859 6502 -652 3386 -1177 O
ATOM 1625 CB ALA A1001 13.921 -24.773 -25.778 1.00 72.67 C
ANISOU 1625 CB ALA A1001 9566 12046 5998 -906 3155 -1078 C
ATOM 1626 N ASP A1002 13.634 -26.655 -28.371 1.00 79.82 N
ANISOU 1626 N ASP A1002 11254 12802 6273 -1099 3114 -1256 N
ATOM 1627 CA ASP A1002 14.098 -27.755 -29.222 1.00 82.58 C
ANISOU 1627 CA ASP A1002 12047 12964 6367 -1055 3154 -1378 C
ATOM 1628 C ASP A1002 14.089 -27.337 -30.693 1.00 89.10 C
ANISOU 1628 C ASP A1002 12910 13917 7028 -1030 3188 -1355 C
ATOM 1629 O ASP A1002 14.910 -27.826 -31.471 1.00 90.23 O
ANISOU 1629 O ASP A1002 13301 13966 7016 -854 3303 -1443 O
ATOM 1630 CB ASP A1002 13.232 -29.013 -29.023 1.00 86.33 C
ANISOU 1630 CB ASP A1002 12887 13287 6626 -1362 2991 -1464 C
ATOM 1631 CG ASP A1002 13.305 -29.643 -27.641 1.00 96.59 C
ANISOU 1631 CG ASP A1002 14279 14406 8016 -1419 2950 -1500 C
ATOM 1632 OD1 ASP A1002 14.409 -29.660 -27.049 1.00 96.05 O
ANISOU 1632 OD1 ASP A1002 14111 14242 8141 -1126 3068 -1507 O
ATOM 1633 OD2 ASP A1002 12.268 -30.156 -27.170 1.00103.43 O
ANISOU 1633 OD2 ASP A1002 15330 15235 8734 -1777 2796 -1524 O
ATOM 1634 N LEU A1003 13.160 -26.432 -31.066 1.00 86.41 N
ANISOU 1634 N LEU A1003 12331 13802 6700 -1187 3081 -1248 N
ATOM 1635 CA LEU A1003 13.020 -25.887 -32.417 1.00 87.97 C
ANISOU 1635 CA LEU A1003 12557 14127 6739 -1189 3078 -1203 C
ATOM 1636 C LEU A1003 14.179 -24.935 -32.726 1.00 92.39 C
ANISOU 1636 C LEU A1003 12968 14734 7402 -935 3266 -1135 C
ATOM 1637 O LEU A1003 14.712 -24.960 -33.836 1.00 93.48 O
ANISOU 1637 O LEU A1003 13276 14885 7357 -866 3366 -1163 O
ATOM 1638 CB LEU A1003 11.674 -25.156 -32.557 1.00 87.98 C
ANISOU 1638 CB LEU A1003 12329 14362 6737 -1379 2878 -1112 C
ATOM 1639 CG LEU A1003 10.910 -25.375 -33.861 1.00 95.14 C
ANISOU 1639 CG LEU A1003 13437 15358 7354 -1571 2746 -1137 C
ATOM 1640 CD1 LEU A1003 9.416 -25.300 -33.627 1.00 95.83 C
ANISOU 1640 CD1 LEU A1003 13329 15678 7405 -1820 2514 -1125 C
ATOM 1641 CD2 LEU A1003 11.329 -24.374 -34.933 1.00 98.28 C
ANISOU 1641 CD2 LEU A1003 13832 15833 7675 -1443 2792 -1055 C
ATOM 1642 N GLU A1004 14.572 -24.108 -31.733 1.00 87.95 N
ANISOU 1642 N GLU A1004 12097 14210 7109 -822 3316 -1052 N
ATOM 1643 CA GLU A1004 15.669 -23.145 -31.839 1.00 87.69 C
ANISOU 1643 CA GLU A1004 11899 14241 7176 -645 3483 -974 C
ATOM 1644 C GLU A1004 17.031 -23.850 -31.820 1.00 93.58 C
ANISOU 1644 C GLU A1004 12753 14917 7886 -442 3694 -1092 C
ATOM 1645 O GLU A1004 17.978 -23.337 -32.416 1.00 93.80 O
ANISOU 1645 O GLU A1004 12726 15061 7852 -341 3857 -1070 O
ATOM 1646 CB GLU A1004 15.587 -22.103 -30.713 1.00 86.83 C
ANISOU 1646 CB GLU A1004 11465 14178 7348 -611 3441 -857 C
ATOM 1647 CG GLU A1004 15.441 -20.672 -31.208 1.00 97.76 C
ANISOU 1647 CG GLU A1004 12729 15681 8735 -641 3365 -703 C
ATOM 1648 CD GLU A1004 14.135 -20.328 -31.902 1.00120.78 C
ANISOU 1648 CD GLU A1004 15712 18681 11497 -771 3150 -675 C
ATOM 1649 OE1 GLU A1004 14.186 -19.909 -33.081 1.00115.82 O
ANISOU 1649 OE1 GLU A1004 15222 18102 10683 -803 3142 -622 O
ATOM 1650 OE2 GLU A1004 13.064 -20.472 -31.270 1.00115.47 O
ANISOU 1650 OE2 GLU A1004 14948 18057 10871 -851 2987 -712 O
ATOM 1651 N ASP A1005 17.125 -25.021 -31.147 1.00 91.57 N
ANISOU 1651 N ASP A1005 12663 14491 7638 -381 3682 -1224 N
ATOM 1652 CA ASP A1005 18.345 -25.834 -31.068 1.00 93.24 C
ANISOU 1652 CA ASP A1005 13016 14624 7786 -120 3840 -1372 C
ATOM 1653 C ASP A1005 18.677 -26.458 -32.426 1.00101.77 C
ANISOU 1653 C ASP A1005 14391 15724 8552 -52 3914 -1484 C
ATOM 1654 O ASP A1005 19.855 -26.643 -32.741 1.00102.73 O
ANISOU 1654 O ASP A1005 14505 15939 8587 197 4097 -1579 O
ATOM 1655 CB ASP A1005 18.214 -26.931 -29.999 1.00 94.84 C
ANISOU 1655 CB ASP A1005 13413 14585 8038 -81 3752 -1480 C
ATOM 1656 CG ASP A1005 18.490 -26.476 -28.577 1.00102.95 C
ANISOU 1656 CG ASP A1005 14162 15596 9358 2 3769 -1427 C
ATOM 1657 OD1 ASP A1005 19.370 -25.603 -28.390 1.00102.32 O
ANISOU 1657 OD1 ASP A1005 13759 15686 9431 117 3896 -1348 O
ATOM 1658 OD2 ASP A1005 17.869 -27.031 -27.647 1.00108.95 O
ANISOU 1658 OD2 ASP A1005 15055 16171 10171 -67 3655 -1467 O
ATOM 1659 N ASN A1006 17.637 -26.773 -33.228 1.00100.71 N
ANISOU 1659 N ASN A1006 14494 15540 8230 -274 3772 -1480 N
ATOM 1660 CA ASN A1006 17.772 -27.324 -34.577 1.00103.81 C
ANISOU 1660 CA ASN A1006 15195 15943 8306 -254 3814 -1574 C
ATOM 1661 C ASN A1006 18.279 -26.241 -35.533 1.00109.83 C
ANISOU 1661 C ASN A1006 15756 16961 9014 -253 3947 -1472 C
ATOM 1662 O ASN A1006 18.988 -26.554 -36.492 1.00111.75 O
ANISOU 1662 O ASN A1006 16154 17287 9019 -136 4083 -1564 O
ATOM 1663 CB ASN A1006 16.442 -27.903 -35.066 1.00105.14 C
ANISOU 1663 CB ASN A1006 15656 15996 8297 -541 3598 -1584 C
ATOM 1664 CG ASN A1006 15.947 -29.101 -34.286 1.00126.80 C
ANISOU 1664 CG ASN A1006 18703 18475 11000 -619 3460 -1691 C
ATOM 1665 OD1 ASN A1006 16.719 -29.934 -33.791 1.00120.85 O
ANISOU 1665 OD1 ASN A1006 18124 17548 10248 -385 3523 -1817 O
ATOM 1666 ND2 ASN A1006 14.634 -29.236 -34.194 1.00119.34 N
ANISOU 1666 ND2 ASN A1006 17853 17507 9984 -962 3255 -1650 N
ATOM 1667 N TRP A1007 17.927 -24.967 -35.253 1.00105.84 N
ANISOU 1667 N TRP A1007 14934 16575 8706 -383 3902 -1285 N
ATOM 1668 CA TRP A1007 18.370 -23.806 -36.022 1.00106.82 C
ANISOU 1668 CA TRP A1007 14905 16903 8779 -431 3996 -1156 C
ATOM 1669 C TRP A1007 19.840 -23.496 -35.728 1.00113.39 C
ANISOU 1669 C TRP A1007 15517 17891 9676 -250 4238 -1173 C
ATOM 1670 O TRP A1007 20.535 -22.978 -36.603 1.00114.33 O
ANISOU 1670 O TRP A1007 15571 18208 9663 -299 4370 -1107 O
ATOM 1671 CB TRP A1007 17.496 -22.578 -35.733 1.00103.72 C
ANISOU 1671 CB TRP A1007 14328 16537 8542 -608 3817 -962 C
ATOM 1672 CG TRP A1007 16.227 -22.520 -36.532 1.00105.45 C
ANISOU 1672 CG TRP A1007 14720 16750 8596 -789 3610 -926 C
ATOM 1673 CD1 TRP A1007 14.954 -22.622 -36.056 1.00107.58 C
ANISOU 1673 CD1 TRP A1007 14967 16978 8932 -911 3381 -916 C
ATOM 1674 CD2 TRP A1007 16.111 -22.323 -37.949 1.00107.47 C
ANISOU 1674 CD2 TRP A1007 15176 17082 8575 -876 3612 -901 C
ATOM 1675 NE1 TRP A1007 14.051 -22.508 -37.087 1.00108.57 N
ANISOU 1675 NE1 TRP A1007 15248 17162 8841 -1055 3230 -891 N
ATOM 1676 CE2 TRP A1007 14.734 -22.324 -38.261 1.00111.71 C
ANISOU 1676 CE2 TRP A1007 15807 17607 9031 -1032 3362 -876 C
ATOM 1677 CE3 TRP A1007 17.041 -22.151 -38.992 1.00110.59 C
ANISOU 1677 CE3 TRP A1007 15671 17589 8759 -850 3802 -902 C
ATOM 1678 CZ2 TRP A1007 14.262 -22.161 -39.570 1.00113.08 C
ANISOU 1678 CZ2 TRP A1007 16191 17838 8936 -1144 3283 -847 C
ATOM 1679 CZ3 TRP A1007 16.572 -21.990 -40.287 1.00114.04 C
ANISOU 1679 CZ3 TRP A1007 16332 18073 8924 -978 3735 -869 C
ATOM 1680 CH2 TRP A1007 15.199 -21.999 -40.566 1.00114.84 C
ANISOU 1680 CH2 TRP A1007 16547 18123 8965 -1113 3471 -841 C
ATOM 1681 N GLU A1008 20.312 -23.815 -34.501 1.00110.95 N
ANISOU 1681 N GLU A1008 15096 17514 9545 -63 4291 -1261 N
ATOM 1682 CA GLU A1008 21.706 -23.616 -34.090 1.00112.20 C
ANISOU 1682 CA GLU A1008 15014 17860 9759 130 4509 -1305 C
ATOM 1683 C GLU A1008 22.602 -24.648 -34.778 1.00121.49 C
ANISOU 1683 C GLU A1008 16358 19131 10672 386 4672 -1527 C
ATOM 1684 O GLU A1008 23.680 -24.292 -35.253 1.00122.88 O
ANISOU 1684 O GLU A1008 16360 19608 10720 468 4883 -1560 O
ATOM 1685 CB GLU A1008 21.869 -23.679 -32.558 1.00111.38 C
ANISOU 1685 CB GLU A1008 14709 17654 9957 239 4473 -1301 C
ATOM 1686 CG GLU A1008 21.170 -22.566 -31.787 1.00119.92 C
ANISOU 1686 CG GLU A1008 15589 18680 11296 41 4333 -1101 C
ATOM 1687 CD GLU A1008 21.388 -21.143 -32.270 1.00142.29 C
ANISOU 1687 CD GLU A1008 18289 21671 14105 -151 4351 -913 C
ATOM 1688 OE1 GLU A1008 22.561 -20.718 -32.382 1.00139.24 O
ANISOU 1688 OE1 GLU A1008 17737 21499 13669 -137 4534 -888 O
ATOM 1689 OE2 GLU A1008 20.379 -20.448 -32.526 1.00135.59 O
ANISOU 1689 OE2 GLU A1008 17511 20742 13265 -321 4169 -795 O
ATOM 1690 N THR A1009 22.125 -25.909 -34.890 1.00120.84 N
ANISOU 1690 N THR A1009 16633 18810 10472 497 4566 -1685 N
ATOM 1691 CA THR A1009 22.832 -27.002 -35.573 1.00124.74 C
ANISOU 1691 CA THR A1009 17386 19330 10678 785 4673 -1922 C
ATOM 1692 C THR A1009 22.569 -26.908 -37.097 1.00132.81 C
ANISOU 1692 C THR A1009 18596 20470 11397 648 4716 -1920 C
ATOM 1693 O THR A1009 22.531 -27.922 -37.800 1.00134.86 O
ANISOU 1693 O THR A1009 19216 20636 11388 789 4708 -2095 O
ATOM 1694 CB THR A1009 22.439 -28.371 -34.980 1.00133.78 C
ANISOU 1694 CB THR A1009 18922 20110 11797 935 4507 -2080 C
ATOM 1695 OG1 THR A1009 21.016 -28.473 -34.903 1.00132.26 O
ANISOU 1695 OG1 THR A1009 18913 19674 11667 598 4277 -1964 O
ATOM 1696 CG2 THR A1009 23.060 -28.621 -33.610 1.00131.55 C
ANISOU 1696 CG2 THR A1009 18503 19759 11721 1192 4518 -2150 C
ATOM 1697 N LEU A1010 22.406 -25.666 -37.589 1.00130.32 N
ANISOU 1697 N LEU A1010 18067 20339 11109 376 4749 -1718 N
ATOM 1698 CA LEU A1010 22.160 -25.289 -38.980 1.00132.77 C
ANISOU 1698 CA LEU A1010 18511 20780 11155 190 4781 -1662 C
ATOM 1699 C LEU A1010 22.905 -23.983 -39.289 1.00138.85 C
ANISOU 1699 C LEU A1010 18961 21881 11916 50 4954 -1514 C
ATOM 1700 O LEU A1010 23.409 -23.816 -40.401 1.00141.04 O
ANISOU 1700 O LEU A1010 19279 22402 11906 13 5112 -1547 O
ATOM 1701 CB LEU A1010 20.648 -25.136 -39.225 1.00131.52 C
ANISOU 1701 CB LEU A1010 18551 20393 11028 -97 4518 -1528 C
ATOM 1702 CG LEU A1010 20.191 -25.114 -40.682 1.00138.43 C
ANISOU 1702 CG LEU A1010 19690 21313 11593 -257 4486 -1514 C
ATOM 1703 CD1 LEU A1010 19.058 -26.087 -40.907 1.00138.80 C
ANISOU 1703 CD1 LEU A1010 20084 21097 11557 -353 4255 -1574 C
ATOM 1704 CD2 LEU A1010 19.778 -23.717 -41.105 1.00140.31 C
ANISOU 1704 CD2 LEU A1010 19785 21678 11850 -521 4440 -1279 C
ATOM 1705 N ASN A1011 22.974 -23.068 -38.297 1.00134.50 N
ANISOU 1705 N ASN A1011 18117 21334 11652 -51 4919 -1352 N
ATOM 1706 CA ASN A1011 23.650 -21.773 -38.399 1.00135.34 C
ANISOU 1706 CA ASN A1011 17958 21703 11761 -238 5045 -1188 C
ATOM 1707 C ASN A1011 25.128 -21.886 -38.006 1.00142.38 C
ANISOU 1707 C ASN A1011 18545 22924 12629 -47 5305 -1310 C
ATOM 1708 O ASN A1011 25.983 -21.383 -38.738 1.00144.57 O
ANISOU 1708 O ASN A1011 18702 23555 12670 -153 5508 -1302 O
ATOM 1709 CB ASN A1011 22.944 -20.719 -37.535 1.00133.36 C
ANISOU 1709 CB ASN A1011 17586 21278 11805 -426 4857 -966 C
ATOM 1710 CG ASN A1011 21.704 -20.118 -38.161 1.00156.10 C
ANISOU 1710 CG ASN A1011 20682 23993 14635 -658 4631 -803 C
ATOM 1711 OD1 ASN A1011 20.841 -20.812 -38.713 1.00151.07 O
ANISOU 1711 OD1 ASN A1011 20297 23225 13879 -657 4507 -867 O
ATOM 1712 ND2 ASN A1011 21.571 -18.804 -38.053 1.00147.10 N
ANISOU 1712 ND2 ASN A1011 19464 22852 13575 -853 4549 -594 N
ATOM 1713 N ASP A1012 25.428 -22.543 -36.861 1.00138.87 N
ANISOU 1713 N ASP A1012 17970 22392 12404 221 5295 -1427 N
ATOM 1714 CA ASP A1012 26.796 -22.737 -36.364 1.00140.77 C
ANISOU 1714 CA ASP A1012 17894 22955 12637 460 5508 -1567 C
ATOM 1715 C ASP A1012 27.583 -23.713 -37.247 1.00149.59 C
ANISOU 1715 C ASP A1012 19089 24332 13416 755 5692 -1831 C
ATOM 1716 O ASP A1012 28.787 -23.523 -37.432 1.00151.70 O
ANISOU 1716 O ASP A1012 19053 25060 13525 834 5927 -1917 O
ATOM 1717 CB ASP A1012 26.795 -23.226 -34.909 1.00140.41 C
ANISOU 1717 CB ASP A1012 17754 22697 12900 693 5407 -1626 C
ATOM 1718 CG ASP A1012 26.442 -22.144 -33.913 1.00148.24 C
ANISOU 1718 CG ASP A1012 18529 23593 14203 457 5308 -1398 C
ATOM 1719 OD1 ASP A1012 25.250 -22.032 -33.557 1.00146.36 O
ANISOU 1719 OD1 ASP A1012 18453 23020 14136 309 5090 -1272 O
ATOM 1720 OD2 ASP A1012 27.357 -21.407 -33.488 1.00154.80 O
ANISOU 1720 OD2 ASP A1012 19023 24708 15086 421 5445 -1356 O
ATOM 1721 N ASN A1013 26.903 -24.746 -37.792 1.00147.74 N
ANISOU 1721 N ASN A1013 19259 23829 13046 908 5582 -1965 N
ATOM 1722 CA ASN A1013 27.502 -25.750 -38.677 1.00151.75 C
ANISOU 1722 CA ASN A1013 19934 24517 13207 1224 5719 -2233 C
ATOM 1723 C ASN A1013 27.856 -25.145 -40.042 1.00159.07 C
ANISOU 1723 C ASN A1013 20822 25811 13808 1001 5902 -2192 C
ATOM 1724 O ASN A1013 28.825 -25.586 -40.662 1.00162.29 O
ANISOU 1724 O ASN A1013 21144 26600 13918 1245 6115 -2404 O
ATOM 1725 CB ASN A1013 26.570 -26.952 -38.851 1.00152.99 C
ANISOU 1725 CB ASN A1013 20606 24224 13301 1383 5514 -2362 C
ATOM 1726 CG ASN A1013 26.996 -28.181 -38.080 1.00178.68 C
ANISOU 1726 CG ASN A1013 23996 27331 16564 1863 5474 -2617 C
ATOM 1727 OD1 ASN A1013 27.210 -28.149 -36.861 1.00171.93 O
ANISOU 1727 OD1 ASN A1013 22913 26459 15955 2001 5455 -2615 O
ATOM 1728 ND2 ASN A1013 27.099 -29.305 -38.773 1.00173.59 N
ANISOU 1728 ND2 ASN A1013 23778 26543 15636 2132 5435 -2842 N
ATOM 1729 N LEU A1014 27.086 -24.127 -40.491 1.00154.79 N
ANISOU 1729 N LEU A1014 20343 25170 13300 554 5811 -1928 N
ATOM 1730 CA LEU A1014 27.302 -23.411 -41.753 1.00157.36 C
ANISOU 1730 CA LEU A1014 20680 25790 13318 262 5949 -1838 C
ATOM 1731 C LEU A1014 28.588 -22.572 -41.684 1.00164.14 C
ANISOU 1731 C LEU A1014 21095 27178 14091 137 6208 -1798 C
ATOM 1732 O LEU A1014 29.257 -22.398 -42.705 1.00167.28 O
ANISOU 1732 O LEU A1014 21433 27987 14137 33 6421 -1850 O
ATOM 1733 CB LEU A1014 26.092 -22.516 -42.075 1.00155.21 C
ANISOU 1733 CB LEU A1014 20627 25217 13127 -145 5728 -1561 C
ATOM 1734 CG LEU A1014 25.880 -22.161 -43.550 1.00162.29 C
ANISOU 1734 CG LEU A1014 21752 26241 13669 -403 5774 -1494 C
ATOM 1735 CD1 LEU A1014 24.420 -22.273 -43.931 1.00160.83 C
ANISOU 1735 CD1 LEU A1014 21948 25642 13517 -534 5487 -1395 C
ATOM 1736 CD2 LEU A1014 26.393 -20.766 -43.863 1.00165.58 C
ANISOU 1736 CD2 LEU A1014 21984 26935 13992 -792 5882 -1273 C
ATOM 1737 N LYS A1015 28.927 -22.063 -40.478 1.00159.27 N
ANISOU 1737 N LYS A1015 20171 26570 13775 116 6188 -1707 N
ATOM 1738 CA LYS A1015 30.127 -21.265 -40.207 1.00160.99 C
ANISOU 1738 CA LYS A1015 19948 27279 13942 -40 6405 -1659 C
ATOM 1739 C LYS A1015 31.398 -22.117 -40.333 1.00169.04 C
ANISOU 1739 C LYS A1015 20679 28813 14736 356 6664 -1973 C
ATOM 1740 O LYS A1015 32.441 -21.599 -40.740 1.00171.38 O
ANISOU 1740 O LYS A1015 20644 29686 14786 192 6912 -1991 O
ATOM 1741 CB LYS A1015 30.048 -20.636 -38.808 1.00160.13 C
ANISOU 1741 CB LYS A1015 19636 26980 14227 -127 6277 -1497 C
ATOM 1742 N VAL A1016 31.302 -23.420 -39.986 1.00165.82 N
ANISOU 1742 N VAL A1016 20414 28206 14383 874 6595 -2226 N
ATOM 1743 CA VAL A1016 32.394 -24.400 -40.062 1.00169.18 C
ANISOU 1743 CA VAL A1016 20644 29047 14589 1385 6783 -2570 C
ATOM 1744 C VAL A1016 32.696 -24.691 -41.547 1.00177.06 C
ANISOU 1744 C VAL A1016 21760 30392 15123 1408 6969 -2720 C
ATOM 1745 O VAL A1016 33.866 -24.816 -41.914 1.00180.49 O
ANISOU 1745 O VAL A1016 21851 31460 15268 1599 7229 -2927 O
ATOM 1746 CB VAL A1016 32.074 -25.698 -39.260 1.00171.75 C
ANISOU 1746 CB VAL A1016 21219 28948 15092 1923 6595 -2779 C
ATOM 1747 CG1 VAL A1016 33.260 -26.662 -39.252 1.00175.95 C
ANISOU 1747 CG1 VAL A1016 21556 29909 15389 2522 6758 -3149 C
ATOM 1748 CG2 VAL A1016 31.648 -25.377 -37.828 1.00167.08 C
ANISOU 1748 CG2 VAL A1016 20545 27992 14947 1845 6404 -2610 C
ATOM 1749 N ILE A1017 31.639 -24.757 -42.392 1.00173.38 N
ANISOU 1749 N ILE A1017 21755 29548 14574 1199 6836 -2616 N
ATOM 1750 CA ILE A1017 31.712 -24.992 -43.844 1.00176.94 C
ANISOU 1750 CA ILE A1017 22404 30231 14594 1163 6975 -2721 C
ATOM 1751 C ILE A1017 32.454 -23.812 -44.520 1.00183.42 C
ANISOU 1751 C ILE A1017 22884 31644 15163 699 7228 -2578 C
ATOM 1752 O ILE A1017 33.231 -24.032 -45.453 1.00187.58 O
ANISOU 1752 O ILE A1017 23293 32700 15280 779 7476 -2762 O
ATOM 1753 CB ILE A1017 30.285 -25.229 -44.440 1.00177.97 C
ANISOU 1753 CB ILE A1017 23109 29764 14746 994 6723 -2602 C
ATOM 1754 CG1 ILE A1017 29.631 -26.489 -43.823 1.00176.93 C
ANISOU 1754 CG1 ILE A1017 23342 29122 14760 1429 6500 -2783 C
ATOM 1755 CG2 ILE A1017 30.304 -25.334 -45.977 1.00182.25 C
ANISOU 1755 CG2 ILE A1017 23868 30530 14850 849 6852 -2649 C
ATOM 1756 CD1 ILE A1017 28.094 -26.540 -43.870 1.00179.36 C
ANISOU 1756 CD1 ILE A1017 24106 28805 15238 1185 6191 -2607 C
ATOM 1757 N GLU A1018 32.242 -22.577 -44.012 1.00177.02 N
ANISOU 1757 N GLU A1018 21930 30753 14575 216 7160 -2261 N
ATOM 1758 CA GLU A1018 32.886 -21.353 -44.500 1.00178.98 C
ANISOU 1758 CA GLU A1018 21920 31485 14598 -311 7355 -2079 C
ATOM 1759 C GLU A1018 34.395 -21.345 -44.191 1.00186.30 C
ANISOU 1759 C GLU A1018 22257 33163 15364 -181 7652 -2265 C
ATOM 1760 O GLU A1018 35.158 -20.695 -44.909 1.00189.25 O
ANISOU 1760 O GLU A1018 22477 33961 15468 -500 7888 -2184 O
ATOM 1761 CB GLU A1018 32.216 -20.116 -43.885 1.00176.66 C
ANISOU 1761 CB GLU A1018 21708 30814 14599 -797 7148 -1707 C
ATOM 1762 N LYS A1019 34.814 -22.068 -43.131 1.00181.70 N
ANISOU 1762 N LYS A1019 21442 32582 15014 321 7625 -2466 N
ATOM 1763 CA LYS A1019 36.208 -22.181 -42.693 1.00184.61 C
ANISOU 1763 CA LYS A1019 21224 33656 15263 550 7866 -2679 C
ATOM 1764 C LYS A1019 36.810 -23.568 -43.024 1.00188.59 C
ANISOU 1764 C LYS A1019 22005 33825 15825 1271 7983 -2960 C
ATOM 1765 O LYS A1019 37.984 -23.807 -42.726 1.00189.27 O
ANISOU 1765 O LYS A1019 21838 34075 16002 1543 8178 -3088 O
ATOM 1766 CB LYS A1019 36.310 -21.901 -41.185 1.00183.79 C
ANISOU 1766 CB LYS A1019 20885 33354 15593 602 7727 -2582 C
ATOM 1767 N ALA A1020 36.015 -24.464 -43.653 1.00186.53 N
ANISOU 1767 N ALA A1020 21990 33658 15226 1537 7859 -3202 N
ATOM 1768 CA ALA A1020 36.425 -25.821 -44.038 1.00186.86 C
ANISOU 1768 CA ALA A1020 22496 33150 15351 2138 7932 -3451 C
ATOM 1769 C ALA A1020 37.466 -25.806 -45.163 1.00192.14 C
ANISOU 1769 C ALA A1020 23368 33649 15987 2073 8298 -3425 C
ATOM 1770 O ALA A1020 37.504 -24.863 -45.957 1.00192.17 O
ANISOU 1770 O ALA A1020 23340 33828 15848 1608 8440 -3169 O
ATOM 1771 CB ALA A1020 35.212 -26.632 -44.466 1.00187.80 C
ANISOU 1771 CB ALA A1020 23053 33044 15259 2332 7681 -3579 C
ATOM 1772 N ASP A1021 38.307 -26.858 -45.226 1.00191.24 N
ANISOU 1772 N ASP A1021 23289 33564 15810 2591 8432 -3781 N
ATOM 1773 CA ASP A1021 39.374 -26.993 -46.221 1.00192.72 C
ANISOU 1773 CA ASP A1021 23707 33486 16033 2556 8802 -3782 C
ATOM 1774 C ASP A1021 39.249 -28.283 -47.050 1.00196.94 C
ANISOU 1774 C ASP A1021 24995 33203 16632 2773 8843 -3995 C
ATOM 1775 O ASP A1021 39.518 -28.253 -48.252 1.00197.97 O
ANISOU 1775 O ASP A1021 25447 33149 16625 2613 9075 -3932 O
ATOM 1776 CB ASP A1021 40.758 -26.933 -45.544 1.00193.69 C
ANISOU 1776 CB ASP A1021 23603 33401 16587 2647 9034 -3763 C
ATOM 1777 CG ASP A1021 40.950 -27.912 -44.399 1.00199.32 C
ANISOU 1777 CG ASP A1021 24770 32885 18079 2849 8917 -3827 C
ATOM 1778 OD1 ASP A1021 40.285 -27.742 -43.353 1.00198.15 O
ANISOU 1778 OD1 ASP A1021 24386 32956 17948 2940 8614 -3835 O
ATOM 1779 OD2 ASP A1021 41.780 -28.835 -44.542 1.00203.71 O
ANISOU 1779 OD2 ASP A1021 25749 32559 19091 2897 9125 -3931 O
ATOM 1780 N ASN A1022 38.854 -29.405 -46.412 1.00194.78 N
ANISOU 1780 N ASN A1022 24742 32995 16269 3265 8590 -4368 N
ATOM 1781 CA ASN A1022 38.712 -30.712 -47.064 1.00195.84 C
ANISOU 1781 CA ASN A1022 25452 32617 16339 3481 8570 -4674 C
ATOM 1782 C ASN A1022 37.240 -31.050 -47.361 1.00197.68 C
ANISOU 1782 C ASN A1022 26170 32486 16454 3376 8241 -4647 C
ATOM 1783 O ASN A1022 36.337 -30.497 -46.727 1.00195.86 O
ANISOU 1783 O ASN A1022 25744 32497 16177 3346 7976 -4472 O
ATOM 1784 CB ASN A1022 39.361 -31.817 -46.217 1.00196.79 C
ANISOU 1784 CB ASN A1022 25573 32486 16714 3915 8526 -5011 C
ATOM 1785 CG ASN A1022 38.800 -31.960 -44.822 1.00211.32 C
ANISOU 1785 CG ASN A1022 27740 33155 19397 3537 8253 -4799 C
ATOM 1786 OD1 ASN A1022 37.901 -32.767 -44.569 1.00207.35 O
ANISOU 1786 OD1 ASN A1022 27401 32780 18602 3914 7903 -5031 O
ATOM 1787 ND2 ASN A1022 39.341 -31.204 -43.878 1.00204.76 N
ANISOU 1787 ND2 ASN A1022 26240 33022 18536 3796 8272 -4727 N
ATOM 1788 N ALA A1023 37.013 -31.962 -48.331 1.00195.83 N
ANISOU 1788 N ALA A1023 26376 32093 15939 3495 8236 -4904 N
ATOM 1789 CA ALA A1023 35.689 -32.414 -48.771 1.00195.21 C
ANISOU 1789 CA ALA A1023 26730 31836 15605 3488 7926 -4946 C
ATOM 1790 C ALA A1023 34.966 -33.256 -47.707 1.00196.02 C
ANISOU 1790 C ALA A1023 27043 31497 15937 3709 7536 -5061 C
ATOM 1791 O ALA A1023 33.733 -33.251 -47.671 1.00194.22 O
ANISOU 1791 O ALA A1023 27046 31165 15586 3663 7238 -4934 O
ATOM 1792 CB ALA A1023 35.815 -33.213 -50.059 1.00198.31 C
ANISOU 1792 CB ALA A1023 27609 31933 15807 3400 8056 -5183 C
ATOM 1793 N ALA A1024 35.726 -33.978 -46.856 1.00193.07 N
ANISOU 1793 N ALA A1024 26527 31137 15693 4182 7511 -5327 N
ATOM 1794 CA ALA A1024 35.190 -34.831 -45.788 1.00191.04 C
ANISOU 1794 CA ALA A1024 26487 30516 15584 4519 7138 -5447 C
ATOM 1795 C ALA A1024 34.554 -34.010 -44.656 1.00189.74 C
ANISOU 1795 C ALA A1024 26072 30340 15681 4375 6965 -5117 C
ATOM 1796 O ALA A1024 33.589 -34.472 -44.043 1.00188.19 O
ANISOU 1796 O ALA A1024 26178 29857 15470 4576 6618 -5087 O
ATOM 1797 CB ALA A1024 36.289 -35.721 -45.229 1.00192.73 C
ANISOU 1797 CB ALA A1024 26658 30530 16042 4824 7203 -5760 C
ATOM 1798 N GLN A1025 35.092 -32.802 -44.384 1.00185.30 N
ANISOU 1798 N GLN A1025 24890 30419 15098 4322 7180 -4908 N
ATOM 1799 CA GLN A1025 34.596 -31.891 -43.346 1.00184.88 C
ANISOU 1799 CA GLN A1025 24249 31189 14807 4664 7004 -4706 C
ATOM 1800 C GLN A1025 33.255 -31.267 -43.748 1.00185.29 C
ANISOU 1800 C GLN A1025 24530 31010 14862 4162 6845 -4380 C
ATOM 1801 O GLN A1025 32.399 -31.061 -42.886 1.00180.87 O
ANISOU 1801 O GLN A1025 24120 29916 14687 3904 6616 -4148 O
ATOM 1802 CB GLN A1025 35.624 -30.789 -43.056 1.00184.31 C
ANISOU 1802 CB GLN A1025 23600 31360 15072 4193 7317 -4527 C
ATOM 1803 N VAL A1026 33.078 -30.969 -45.052 1.00182.40 N
ANISOU 1803 N VAL A1026 24262 30843 14197 3876 6978 -4339 N
ATOM 1804 CA VAL A1026 31.859 -30.375 -45.616 1.00178.51 C
ANISOU 1804 CA VAL A1026 24075 29950 13801 3256 6847 -4020 C
ATOM 1805 C VAL A1026 30.743 -31.441 -45.657 1.00180.69 C
ANISOU 1805 C VAL A1026 25076 29481 14097 3387 6534 -4074 C
ATOM 1806 O VAL A1026 29.596 -31.132 -45.328 1.00176.33 O
ANISOU 1806 O VAL A1026 24738 28434 13824 2978 6307 -3809 O
ATOM 1807 CB VAL A1026 32.107 -29.737 -47.016 1.00185.05 C
ANISOU 1807 CB VAL A1026 24795 31252 14262 2924 7086 -3971 C
ATOM 1808 CG1 VAL A1026 30.880 -28.970 -47.509 1.00181.20 C
ANISOU 1808 CG1 VAL A1026 24570 30377 13900 2277 6931 -3614 C
ATOM 1809 CG2 VAL A1026 33.329 -28.820 -47.003 1.00187.25 C
ANISOU 1809 CG2 VAL A1026 24380 32335 14431 2804 7412 -3966 C
ATOM 1810 N LYS A1027 31.093 -32.690 -46.042 1.00180.73 N
ANISOU 1810 N LYS A1027 25458 29429 13783 3957 6514 -4428 N
ATOM 1811 CA LYS A1027 30.177 -33.833 -46.142 1.00180.36 C
ANISOU 1811 CA LYS A1027 26166 28698 13664 4108 6219 -4526 C
ATOM 1812 C LYS A1027 29.580 -34.223 -44.781 1.00180.10 C
ANISOU 1812 C LYS A1027 26336 28086 14007 4130 5932 -4438 C
ATOM 1813 O LYS A1027 28.421 -34.639 -44.729 1.00177.53 O
ANISOU 1813 O LYS A1027 26531 27170 13752 3884 5664 -4332 O
ATOM 1814 CB LYS A1027 30.893 -35.041 -46.760 1.00187.86 C
ANISOU 1814 CB LYS A1027 27445 29677 14256 4649 6269 -4953 C
ATOM 1815 N ASP A1028 30.368 -34.090 -43.694 1.00175.96 N
ANISOU 1815 N ASP A1028 25399 27759 13699 4402 5988 -4486 N
ATOM 1816 CA ASP A1028 29.950 -34.406 -42.324 1.00172.52 C
ANISOU 1816 CA ASP A1028 25101 26837 13612 4439 5742 -4410 C
ATOM 1817 C ASP A1028 28.952 -33.363 -41.796 1.00170.91 C
ANISOU 1817 C ASP A1028 24706 26420 13814 3759 5643 -4007 C
ATOM 1818 O ASP A1028 27.975 -33.734 -41.143 1.00168.21 O
ANISOU 1818 O ASP A1028 24735 25519 13659 3572 5376 -3896 O
ATOM 1819 CB ASP A1028 31.177 -34.497 -41.395 1.00175.39 C
ANISOU 1819 CB ASP A1028 25039 27544 14057 4947 5846 -4590 C
ATOM 1820 CG ASP A1028 30.854 -34.903 -39.970 1.00177.85 C
ANISOU 1820 CG ASP A1028 25492 27377 14708 5011 5601 -4522 C
ATOM 1821 OD1 ASP A1028 30.821 -34.014 -39.094 1.00173.62 O
ANISOU 1821 OD1 ASP A1028 24475 26962 14529 4714 5641 -4292 O
ATOM 1822 OD2 ASP A1028 30.643 -36.112 -39.731 1.00183.77 O
ANISOU 1822 OD2 ASP A1028 26865 27617 15341 5345 5362 -4700 O
ATOM 1823 N ALA A1029 29.204 -32.069 -42.079 1.00165.49 N
ANISOU 1823 N ALA A1029 23459 26189 13231 3392 5851 -3797 N
ATOM 1824 CA ALA A1029 28.360 -30.952 -41.651 1.00160.45 C
ANISOU 1824 CA ALA A1029 22611 25410 12942 2800 5768 -3430 C
ATOM 1825 C ALA A1029 27.039 -30.892 -42.429 1.00163.18 C
ANISOU 1825 C ALA A1029 23364 25413 13224 2373 5601 -3266 C
ATOM 1826 O ALA A1029 26.029 -30.466 -41.867 1.00159.23 O
ANISOU 1826 O ALA A1029 22898 24597 13007 2004 5409 -3029 O
ATOM 1827 CB ALA A1029 29.114 -29.642 -41.808 1.00160.93 C
ANISOU 1827 CB ALA A1029 22050 26045 13050 2560 6025 -3281 C
ATOM 1828 N LEU A1030 27.049 -31.313 -43.714 1.00162.82 N
ANISOU 1828 N LEU A1030 23609 25461 12795 2436 5670 -3403 N
ATOM 1829 CA LEU A1030 25.875 -31.324 -44.594 1.00161.92 C
ANISOU 1829 CA LEU A1030 23892 25071 12558 2064 5517 -3280 C
ATOM 1830 C LEU A1030 24.838 -32.362 -44.147 1.00163.20 C
ANISOU 1830 C LEU A1030 24610 24624 12774 2056 5200 -3317 C
ATOM 1831 O LEU A1030 23.638 -32.102 -44.251 1.00160.23 O
ANISOU 1831 O LEU A1030 24387 23988 12504 1624 5006 -3113 O
ATOM 1832 CB LEU A1030 26.293 -31.596 -46.044 1.00166.36 C
ANISOU 1832 CB LEU A1030 24633 25909 12665 2186 5684 -3452 C
ATOM 1833 N THR A1031 25.301 -33.528 -43.651 1.00160.89 N
ANISOU 1833 N THR A1031 24628 24122 12380 2525 5135 -3580 N
ATOM 1834 CA THR A1031 24.449 -34.620 -43.165 1.00160.05 C
ANISOU 1834 CA THR A1031 25119 23424 12270 2516 4830 -3636 C
ATOM 1835 C THR A1031 23.809 -34.219 -41.822 1.00159.00 C
ANISOU 1835 C THR A1031 24784 23066 12563 2242 4673 -3418 C
ATOM 1836 O THR A1031 22.657 -34.576 -41.565 1.00157.14 O
ANISOU 1836 O THR A1031 24888 22432 12385 1917 4422 -3318 O
ATOM 1837 CB THR A1031 25.255 -35.929 -43.055 1.00170.22 C
ANISOU 1837 CB THR A1031 26842 24551 13283 3139 4801 -3990 C
ATOM 1838 OG1 THR A1031 26.124 -36.055 -44.184 1.00173.04 O
ANISOU 1838 OG1 THR A1031 27153 25309 13284 3485 5032 -4207 O
ATOM 1839 CG2 THR A1031 24.364 -37.165 -42.960 1.00169.72 C
ANISOU 1839 CG2 THR A1031 27580 23862 13043 3077 4484 -4073 C
ATOM 1840 N LYS A1032 24.557 -33.470 -40.984 1.00153.21 N
ANISOU 1840 N LYS A1032 23487 22621 12104 2354 4824 -3351 N
ATOM 1841 CA LYS A1032 24.106 -32.978 -39.680 1.00148.76 C
ANISOU 1841 CA LYS A1032 22663 21912 11947 2136 4713 -3153 C
ATOM 1842 C LYS A1032 23.057 -31.869 -39.842 1.00148.50 C
ANISOU 1842 C LYS A1032 22395 21917 12113 1569 4651 -2844 C
ATOM 1843 O LYS A1032 22.101 -31.821 -39.067 1.00145.36 O
ANISOU 1843 O LYS A1032 22040 21252 11939 1292 4452 -2700 O
ATOM 1844 CB LYS A1032 25.297 -32.468 -38.855 1.00150.86 C
ANISOU 1844 CB LYS A1032 22401 22516 12404 2435 4903 -3187 C
ATOM 1845 N MET A1033 23.242 -30.988 -40.850 1.00145.05 N
ANISOU 1845 N MET A1033 21723 21823 11566 1410 4812 -2752 N
ATOM 1846 CA MET A1033 22.333 -29.883 -41.172 1.00142.12 C
ANISOU 1846 CA MET A1033 21167 21508 11323 935 4746 -2476 C
ATOM 1847 C MET A1033 21.013 -30.395 -41.752 1.00144.79 C
ANISOU 1847 C MET A1033 21946 21541 11526 650 4504 -2440 C
ATOM 1848 O MET A1033 19.967 -29.791 -41.507 1.00141.75 O
ANISOU 1848 O MET A1033 21462 21073 11325 300 4337 -2239 O
ATOM 1849 CB MET A1033 22.993 -28.916 -42.164 1.00145.93 C
ANISOU 1849 CB MET A1033 21378 22418 11650 861 4977 -2412 C
ATOM 1850 CG MET A1033 23.706 -27.761 -41.498 1.00147.95 C
ANISOU 1850 CG MET A1033 21095 22971 12147 802 5128 -2262 C
ATOM 1851 SD MET A1033 24.493 -26.635 -42.680 1.00154.58 S
ANISOU 1851 SD MET A1033 21676 24322 12733 641 5399 -2185 S
ATOM 1852 CE MET A1033 23.057 -25.800 -43.351 1.00149.89 C
ANISOU 1852 CE MET A1033 21291 23536 12123 162 5183 -1923 C
ATOM 1853 N ARG A1034 21.069 -31.498 -42.527 1.00143.65 N
ANISOU 1853 N ARG A1034 22282 21258 11040 810 4480 -2647 N
ATOM 1854 CA ARG A1034 19.909 -32.135 -43.156 1.00143.90 C
ANISOU 1854 CA ARG A1034 22788 21010 10878 541 4251 -2646 C
ATOM 1855 C ARG A1034 19.016 -32.809 -42.109 1.00144.95 C
ANISOU 1855 C ARG A1034 23148 20766 11160 382 3994 -2627 C
ATOM 1856 O ARG A1034 17.792 -32.765 -42.238 1.00143.68 O
ANISOU 1856 O ARG A1034 23110 20485 10996 -13 3786 -2508 O
ATOM 1857 CB ARG A1034 20.361 -33.159 -44.207 1.00148.47 C
ANISOU 1857 CB ARG A1034 23851 21529 11031 797 4303 -2894 C
ATOM 1858 N ALA A1035 19.630 -33.423 -41.076 1.00140.37 N
ANISOU 1858 N ALA A1035 22616 20031 10688 678 4003 -2748 N
ATOM 1859 CA ALA A1035 18.931 -34.102 -39.982 1.00138.61 C
ANISOU 1859 CA ALA A1035 22632 19449 10582 533 3775 -2739 C
ATOM 1860 C ALA A1035 18.256 -33.098 -39.042 1.00137.06 C
ANISOU 1860 C ALA A1035 21957 19356 10764 208 3712 -2495 C
ATOM 1861 O ALA A1035 17.152 -33.367 -38.563 1.00135.76 O
ANISOU 1861 O ALA A1035 21937 19009 10638 -145 3494 -2417 O
ATOM 1862 CB ALA A1035 19.902 -34.977 -39.204 1.00140.73 C
ANISOU 1862 CB ALA A1035 23100 19535 10835 993 3807 -2942 C
ATOM 1863 N ALA A1036 18.918 -31.948 -38.783 1.00130.37 N
ANISOU 1863 N ALA A1036 20550 18820 10167 315 3898 -2382 N
ATOM 1864 CA ALA A1036 18.421 -30.873 -37.919 1.00126.02 C
ANISOU 1864 CA ALA A1036 19533 18383 9966 78 3854 -2162 C
ATOM 1865 C ALA A1036 17.210 -30.171 -38.542 1.00127.68 C
ANISOU 1865 C ALA A1036 19657 18697 10159 -319 3722 -1989 C
ATOM 1866 O ALA A1036 16.254 -29.864 -37.828 1.00125.24 O
ANISOU 1866 O ALA A1036 19186 18365 10034 -579 3561 -1863 O
ATOM 1867 CB ALA A1036 19.527 -29.865 -37.649 1.00125.43 C
ANISOU 1867 CB ALA A1036 18969 18598 10092 295 4082 -2104 C
ATOM 1868 N ALA A1037 17.248 -29.933 -39.870 1.00125.00 N
ANISOU 1868 N ALA A1037 19421 18495 9579 -348 3784 -1995 N
ATOM 1869 CA ALA A1037 16.169 -29.293 -40.627 1.00124.11 C
ANISOU 1869 CA ALA A1037 19271 18488 9397 -675 3648 -1849 C
ATOM 1870 C ALA A1037 14.958 -30.223 -40.759 1.00127.65 C
ANISOU 1870 C ALA A1037 20091 18735 9675 -956 3396 -1896 C
ATOM 1871 O ALA A1037 13.823 -29.742 -40.782 1.00126.31 O
ANISOU 1871 O ALA A1037 19787 18656 9549 -1256 3216 -1768 O
ATOM 1872 CB ALA A1037 16.667 -28.882 -42.002 1.00126.87 C
ANISOU 1872 CB ALA A1037 19675 19024 9504 -614 3794 -1856 C
ATOM 1873 N LEU A1038 15.203 -31.549 -40.840 1.00125.40 N
ANISOU 1873 N LEU A1038 20283 18190 9172 -856 3371 -2086 N
ATOM 1874 CA LEU A1038 14.162 -32.575 -40.944 1.00126.38 C
ANISOU 1874 CA LEU A1038 20848 18087 9083 -1160 3130 -2146 C
ATOM 1875 C LEU A1038 13.435 -32.749 -39.609 1.00126.93 C
ANISOU 1875 C LEU A1038 20808 18060 9360 -1388 2972 -2085 C
ATOM 1876 O LEU A1038 12.216 -32.925 -39.604 1.00126.84 O
ANISOU 1876 O LEU A1038 20858 18065 9269 -1790 2761 -2030 O
ATOM 1877 CB LEU A1038 14.760 -33.913 -41.400 1.00129.84 C
ANISOU 1877 CB LEU A1038 21903 18236 9195 -952 3144 -2374 C
ATOM 1878 N ASP A1039 14.183 -32.688 -38.484 1.00120.66 N
ANISOU 1878 N ASP A1039 19836 17201 8810 -1144 3076 -2100 N
ATOM 1879 CA ASP A1039 13.665 -32.811 -37.117 1.00118.21 C
ANISOU 1879 CA ASP A1039 19403 16804 8706 -1322 2959 -2046 C
ATOM 1880 C ASP A1039 12.774 -31.612 -36.756 1.00117.99 C
ANISOU 1880 C ASP A1039 18822 17084 8924 -1566 2896 -1853 C
ATOM 1881 O ASP A1039 11.752 -31.795 -36.092 1.00117.13 O
ANISOU 1881 O ASP A1039 18660 16995 8850 -1895 2724 -1807 O
ATOM 1882 CB ASP A1039 14.827 -32.942 -36.115 1.00119.03 C
ANISOU 1882 CB ASP A1039 19442 16783 9002 -942 3101 -2114 C
ATOM 1883 CG ASP A1039 14.403 -33.133 -34.671 1.00127.94 C
ANISOU 1883 CG ASP A1039 20461 17812 10340 -1102 2997 -2060 C
ATOM 1884 OD1 ASP A1039 13.860 -34.213 -34.349 1.00130.15 O
ANISOU 1884 OD1 ASP A1039 21171 17837 10442 -1355 2818 -2121 O
ATOM 1885 OD2 ASP A1039 14.642 -32.216 -33.858 1.00131.37 O
ANISOU 1885 OD2 ASP A1039 20409 18413 11092 -991 3092 -1957 O
ATOM 1886 N ALA A1040 13.159 -30.398 -37.201 1.00112.06 N
ANISOU 1886 N ALA A1040 17684 16582 8312 -1406 3024 -1749 N
ATOM 1887 CA ALA A1040 12.416 -29.157 -36.966 1.00109.26 C
ANISOU 1887 CA ALA A1040 16852 16500 8163 -1549 2952 -1577 C
ATOM 1888 C ALA A1040 11.122 -29.114 -37.794 1.00113.38 C
ANISOU 1888 C ALA A1040 17433 17168 8479 -1874 2746 -1537 C
ATOM 1889 O ALA A1040 10.156 -28.469 -37.380 1.00111.94 O
ANISOU 1889 O ALA A1040 16921 17199 8411 -2046 2603 -1439 O
ATOM 1890 CB ALA A1040 13.288 -27.956 -37.288 1.00108.69 C
ANISOU 1890 CB ALA A1040 16471 16588 8238 -1293 3133 -1483 C
ATOM 1891 N GLN A1041 11.107 -29.805 -38.956 1.00111.63 N
ANISOU 1891 N GLN A1041 17626 16850 7939 -1937 2725 -1627 N
ATOM 1892 CA GLN A1041 9.954 -29.914 -39.856 1.00112.92 C
ANISOU 1892 CA GLN A1041 17911 17138 7856 -2250 2525 -1611 C
ATOM 1893 C GLN A1041 8.862 -30.790 -39.218 1.00117.15 C
ANISOU 1893 C GLN A1041 18573 17644 8296 -2639 2313 -1655 C
ATOM 1894 O GLN A1041 7.673 -30.504 -39.378 1.00117.38 O
ANISOU 1894 O GLN A1041 18409 17930 8260 -2931 2120 -1599 O
ATOM 1895 CB GLN A1041 10.393 -30.498 -41.213 1.00116.80 C
ANISOU 1895 CB GLN A1041 18852 17502 8023 -2185 2585 -1709 C
ATOM 1896 CG GLN A1041 9.341 -30.391 -42.318 1.00130.08 C
ANISOU 1896 CG GLN A1041 20649 19333 9444 -2475 2392 -1682 C
ATOM 1897 CD GLN A1041 9.631 -31.309 -43.479 1.00148.68 C
ANISOU 1897 CD GLN A1041 23564 21492 11436 -2484 2409 -1815 C
ATOM 1898 OE1 GLN A1041 9.652 -32.539 -43.347 1.00144.97 O
ANISOU 1898 OE1 GLN A1041 23535 20746 10802 -2536 2382 -1952 O
ATOM 1899 NE2 GLN A1041 9.823 -30.732 -44.654 1.00141.17 N
ANISOU 1899 NE2 GLN A1041 22649 20666 10324 -2445 2431 -1779 N
ATOM 1900 N LYS A1042 9.277 -31.851 -38.495 1.00113.64 N
ANISOU 1900 N LYS A1042 18458 16904 7817 -2646 2339 -1760 N
ATOM 1901 CA LYS A1042 8.398 -32.798 -37.802 1.00114.52 C
ANISOU 1901 CA LYS A1042 18780 16933 7798 -3056 2153 -1804 C
ATOM 1902 C LYS A1042 7.747 -32.165 -36.569 1.00115.63 C
ANISOU 1902 C LYS A1042 18403 17328 8203 -3206 2093 -1707 C
ATOM 1903 O LYS A1042 6.645 -32.563 -36.192 1.00116.47 O
ANISOU 1903 O LYS A1042 18502 17568 8182 -3641 1913 -1709 O
ATOM 1904 CB LYS A1042 9.185 -34.051 -37.375 1.00118.31 C
ANISOU 1904 CB LYS A1042 19823 16968 8161 -2953 2196 -1940 C
ATOM 1905 CG LYS A1042 9.700 -34.898 -38.533 1.00135.75 C
ANISOU 1905 CG LYS A1042 22633 18903 10042 -2819 2217 -2076 C
ATOM 1906 CD LYS A1042 10.925 -35.703 -38.126 1.00146.51 C
ANISOU 1906 CD LYS A1042 24389 19885 11393 -2430 2333 -2214 C
ATOM 1907 CE LYS A1042 11.640 -36.281 -39.322 1.00160.19 C
ANISOU 1907 CE LYS A1042 26585 21432 12849 -2125 2414 -2362 C
ATOM 1908 NZ LYS A1042 12.947 -36.881 -38.945 1.00169.80 N
ANISOU 1908 NZ LYS A1042 28004 22405 14106 -1601 2566 -2503 N
ATOM 1909 N ALA A1043 8.444 -31.194 -35.940 1.00108.86 N
ANISOU 1909 N ALA A1043 17123 16553 7687 -2862 2245 -1631 N
ATOM 1910 CA ALA A1043 8.027 -30.484 -34.727 1.00106.28 C
ANISOU 1910 CA ALA A1043 16299 16444 7638 -2900 2220 -1547 C
ATOM 1911 C ALA A1043 6.720 -29.700 -34.904 1.00110.12 C
ANISOU 1911 C ALA A1043 16375 17368 8100 -3144 2038 -1477 C
ATOM 1912 O ALA A1043 6.449 -29.174 -35.986 1.00110.55 O
ANISOU 1912 O ALA A1043 16393 17579 8031 -3126 1977 -1449 O
ATOM 1913 CB ALA A1043 9.130 -29.539 -34.278 1.00104.13 C
ANISOU 1913 CB ALA A1043 15719 16153 7691 -2462 2415 -1479 C
ATOM 1914 N THR A1044 5.921 -29.629 -33.818 1.00105.93 N
ANISOU 1914 N THR A1044 15526 17052 7669 -3352 1949 -1460 N
ATOM 1915 CA THR A1044 4.643 -28.918 -33.758 1.00106.23 C
ANISOU 1915 CA THR A1044 15100 17577 7684 -3545 1772 -1424 C
ATOM 1916 C THR A1044 4.819 -27.679 -32.845 1.00106.79 C
ANISOU 1916 C THR A1044 14652 17820 8102 -3233 1831 -1347 C
ATOM 1917 O THR A1044 4.962 -27.837 -31.628 1.00105.03 O
ANISOU 1917 O THR A1044 14305 17577 8026 -3283 1875 -1355 O
ATOM 1918 CB THR A1044 3.516 -29.870 -33.296 1.00116.79 C
ANISOU 1918 CB THR A1044 16510 19091 8772 -4099 1610 -1492 C
ATOM 1919 OG1 THR A1044 3.547 -31.059 -34.089 1.00118.86 O
ANISOU 1919 OG1 THR A1044 17366 19078 8716 -4363 1566 -1561 O
ATOM 1920 CG2 THR A1044 2.130 -29.233 -33.381 1.00116.93 C
ANISOU 1920 CG2 THR A1044 16032 19704 8693 -4312 1413 -1488 C
ATOM 1921 N PRO A1045 4.847 -26.448 -33.416 1.00102.16 N
ANISOU 1921 N PRO A1045 13814 17372 7630 -2912 1823 -1270 N
ATOM 1922 CA PRO A1045 5.041 -25.252 -32.572 1.00 99.36 C
ANISOU 1922 CA PRO A1045 13041 17131 7579 -2607 1859 -1198 C
ATOM 1923 C PRO A1045 3.786 -24.870 -31.767 1.00103.07 C
ANISOU 1923 C PRO A1045 13048 18057 8056 -2743 1686 -1225 C
ATOM 1924 O PRO A1045 2.691 -25.294 -32.145 1.00105.04 O
ANISOU 1924 O PRO A1045 13235 18620 8057 -3048 1516 -1286 O
ATOM 1925 CB PRO A1045 5.415 -24.165 -33.583 1.00100.88 C
ANISOU 1925 CB PRO A1045 13218 17309 7802 -2290 1860 -1112 C
ATOM 1926 CG PRO A1045 4.799 -24.593 -34.854 1.00108.06 C
ANISOU 1926 CG PRO A1045 14344 18309 8406 -2479 1737 -1146 C
ATOM 1927 CD PRO A1045 4.718 -26.090 -34.845 1.00105.02 C
ANISOU 1927 CD PRO A1045 14315 17758 7829 -2822 1770 -1243 C
ATOM 1928 N PRO A1046 3.904 -24.060 -30.676 1.00 97.35 N
ANISOU 1928 N PRO A1046 11980 17416 7592 -2524 1720 -1191 N
ATOM 1929 CA PRO A1046 2.708 -23.701 -29.885 1.00 98.01 C
ANISOU 1929 CA PRO A1046 11596 17984 7658 -2621 1563 -1242 C
ATOM 1930 C PRO A1046 1.694 -22.821 -30.625 1.00103.37 C
ANISOU 1930 C PRO A1046 11986 19086 8206 -2485 1339 -1254 C
ATOM 1931 O PRO A1046 0.530 -22.787 -30.221 1.00104.87 O
ANISOU 1931 O PRO A1046 11797 19771 8277 -2629 1184 -1336 O
ATOM 1932 CB PRO A1046 3.284 -22.951 -28.677 1.00 97.04 C
ANISOU 1932 CB PRO A1046 11249 17771 7851 -2334 1667 -1198 C
ATOM 1933 CG PRO A1046 4.729 -23.309 -28.639 1.00 99.37 C
ANISOU 1933 CG PRO A1046 11913 17543 8300 -2225 1887 -1142 C
ATOM 1934 CD PRO A1046 5.121 -23.484 -30.069 1.00 95.94 C
ANISOU 1934 CD PRO A1046 11817 16924 7711 -2197 1902 -1118 C
ATOM 1935 N LYS A1047 2.123 -22.110 -31.688 1.00 99.40 N
ANISOU 1935 N LYS A1047 11654 18415 7698 -2209 1315 -1180 N
ATOM 1936 CA LYS A1047 1.245 -21.250 -32.487 1.00101.09 C
ANISOU 1936 CA LYS A1047 11677 18966 7768 -2033 1078 -1185 C
ATOM 1937 C LYS A1047 0.297 -22.087 -33.349 1.00108.03 C
ANISOU 1937 C LYS A1047 12614 20120 8314 -2397 932 -1264 C
ATOM 1938 O LYS A1047 -0.857 -21.697 -33.538 1.00110.14 O
ANISOU 1938 O LYS A1047 12548 20879 8420 -2385 700 -1331 O
ATOM 1939 CB LYS A1047 2.056 -20.288 -33.367 1.00102.39 C
ANISOU 1939 CB LYS A1047 12083 18819 8004 -1673 1097 -1066 C
ATOM 1940 CG LYS A1047 2.645 -19.113 -32.600 1.00110.73 C
ANISOU 1940 CG LYS A1047 13011 19729 9333 -1295 1145 -989 C
ATOM 1941 CD LYS A1047 3.078 -18.000 -33.535 1.00118.88 C
ANISOU 1941 CD LYS A1047 14239 20581 10347 -980 1066 -878 C
ATOM 1942 CE LYS A1047 3.841 -16.930 -32.802 1.00125.55 C
ANISOU 1942 CE LYS A1047 15093 21163 11448 -697 1164 -781 C
ATOM 1943 NZ LYS A1047 4.271 -15.838 -33.712 1.00135.02 N
ANISOU 1943 NZ LYS A1047 16551 22160 12592 -454 1079 -657 N
ATOM 1944 N LEU A1048 0.779 -23.240 -33.855 1.00104.61 N
ANISOU 1944 N LEU A1048 12606 19384 7759 -2708 1053 -1269 N
ATOM 1945 CA LEU A1048 -0.005 -24.154 -34.691 1.00107.36 C
ANISOU 1945 CA LEU A1048 13105 19915 7772 -3107 926 -1339 C
ATOM 1946 C LEU A1048 -0.528 -25.344 -33.851 1.00111.48 C
ANISOU 1946 C LEU A1048 13602 20588 8169 -3614 937 -1428 C
ATOM 1947 O LEU A1048 -0.552 -26.483 -34.326 1.00112.68 O
ANISOU 1947 O LEU A1048 14129 20599 8087 -4006 938 -1466 O
ATOM 1948 CB LEU A1048 0.829 -24.648 -35.902 1.00107.55 C
ANISOU 1948 CB LEU A1048 13680 19498 7688 -3119 1028 -1296 C
ATOM 1949 CG LEU A1048 1.564 -23.598 -36.760 1.00111.30 C
ANISOU 1949 CG LEU A1048 14281 19747 8262 -2692 1069 -1192 C
ATOM 1950 CD1 LEU A1048 2.449 -24.267 -37.792 1.00111.80 C
ANISOU 1950 CD1 LEU A1048 14868 19418 8193 -2756 1209 -1176 C
ATOM 1951 CD2 LEU A1048 0.595 -22.651 -37.455 1.00115.95 C
ANISOU 1951 CD2 LEU A1048 14617 20708 8729 -2515 806 -1179 C
ATOM 1952 N GLU A1049 -0.964 -25.061 -32.606 1.00106.81 N
ANISOU 1952 N GLU A1049 12592 20286 7706 -3619 932 -1462 N
ATOM 1953 CA GLU A1049 -1.491 -26.062 -31.676 1.00107.64 C
ANISOU 1953 CA GLU A1049 12632 20578 7688 -4115 942 -1536 C
ATOM 1954 C GLU A1049 -2.907 -26.495 -32.068 1.00115.45 C
ANISOU 1954 C GLU A1049 13385 22168 8313 -4563 722 -1632 C
ATOM 1955 O GLU A1049 -3.151 -27.693 -32.224 1.00116.94 O
ANISOU 1955 O GLU A1049 13905 22288 8239 -5093 704 -1667 O
ATOM 1956 CB GLU A1049 -1.474 -25.530 -30.234 1.00107.16 C
ANISOU 1956 CB GLU A1049 12168 20678 7871 -3950 1011 -1542 C
ATOM 1957 CG GLU A1049 -0.286 -26.015 -29.419 1.00113.99 C
ANISOU 1957 CG GLU A1049 13357 21000 8953 -3936 1235 -1492 C
ATOM 1958 CD GLU A1049 -0.229 -25.544 -27.978 1.00131.62 C
ANISOU 1958 CD GLU A1049 15222 23364 11424 -3780 1306 -1493 C
ATOM 1959 OE1 GLU A1049 0.897 -25.314 -27.479 1.00120.86 O
ANISOU 1959 OE1 GLU A1049 14047 21548 10326 -3530 1477 -1428 O
ATOM 1960 OE2 GLU A1049 -1.299 -25.424 -27.337 1.00127.90 O
ANISOU 1960 OE2 GLU A1049 14265 23474 10859 -3906 1190 -1569 O
ATOM 1961 N ASP A1050 -3.831 -25.525 -32.239 1.00113.75 N
ANISOU 1961 N ASP A1050 12617 22547 8057 -4344 539 -1683 N
ATOM 1962 CA ASP A1050 -5.228 -25.774 -32.609 1.00118.00 C
ANISOU 1962 CA ASP A1050 12809 23782 8245 -4708 312 -1792 C
ATOM 1963 C ASP A1050 -5.409 -25.729 -34.144 1.00123.95 C
ANISOU 1963 C ASP A1050 13783 24512 8799 -4660 159 -1779 C
ATOM 1964 O ASP A1050 -6.416 -25.219 -34.644 1.00126.30 O
ANISOU 1964 O ASP A1050 13684 25387 8918 -4578 -69 -1851 O
ATOM 1965 CB ASP A1050 -6.151 -24.764 -31.905 1.00121.02 C
ANISOU 1965 CB ASP A1050 12452 24866 8662 -4436 180 -1884 C
ATOM 1966 N LYS A1051 -4.431 -26.292 -34.880 1.00119.33 N
ANISOU 1966 N LYS A1051 13837 23278 8227 -4701 282 -1699 N
ATOM 1967 CA LYS A1051 -4.422 -26.353 -36.343 1.00120.76 C
ANISOU 1967 CA LYS A1051 14335 23330 8221 -4677 178 -1676 C
ATOM 1968 C LYS A1051 -4.297 -27.802 -36.812 1.00126.94 C
ANISOU 1968 C LYS A1051 15676 23817 8738 -5241 218 -1695 C
ATOM 1969 O LYS A1051 -3.423 -28.532 -36.336 1.00124.55 O
ANISOU 1969 O LYS A1051 15789 23001 8533 -5346 411 -1667 O
ATOM 1970 CB LYS A1051 -3.276 -25.498 -36.927 1.00120.12 C
ANISOU 1970 CB LYS A1051 14518 22732 8390 -4100 292 -1564 C
ATOM 1971 CG LYS A1051 -3.352 -24.003 -36.608 1.00131.30 C
ANISOU 1971 CG LYS A1051 15508 24346 10034 -3527 221 -1531 C
ATOM 1972 CD LYS A1051 -4.126 -23.210 -37.655 1.00143.54 C
ANISOU 1972 CD LYS A1051 16893 26238 11407 -3287 -47 -1545 C
ATOM 1973 CE LYS A1051 -4.156 -21.739 -37.320 1.00154.02 C
ANISOU 1973 CE LYS A1051 17919 27663 12938 -2685 -137 -1511 C
ATOM 1974 NZ LYS A1051 -4.938 -20.961 -38.316 1.00166.30 N
ANISOU 1974 NZ LYS A1051 19340 29553 14294 -2417 -439 -1536 N
ATOM 1975 N SER A1052 -5.178 -28.215 -37.739 1.00127.75 N
ANISOU 1975 N SER A1052 15810 24241 8489 -5586 15 -1750 N
ATOM 1976 CA SER A1052 -5.205 -29.561 -38.320 1.00129.98 C
ANISOU 1976 CA SER A1052 16657 24273 8454 -6146 -1 -1777 C
ATOM 1977 C SER A1052 -3.992 -29.783 -39.251 1.00131.97 C
ANISOU 1977 C SER A1052 17569 23804 8769 -5881 145 -1712 C
ATOM 1978 O SER A1052 -3.498 -28.802 -39.808 1.00129.65 O
ANISOU 1978 O SER A1052 17208 23392 8661 -5352 181 -1649 O
ATOM 1979 CB SER A1052 -6.506 -29.771 -39.093 1.00138.11 C
ANISOU 1979 CB SER A1052 17482 25899 9094 -6544 -274 -1852 C
ATOM 1980 OG SER A1052 -7.637 -29.663 -38.245 1.00149.82 O
ANISOU 1980 OG SER A1052 18339 28121 10465 -6841 -400 -1936 O
ATOM 1981 N PRO A1053 -3.501 -31.034 -39.469 1.00129.21 N
ANISOU 1981 N PRO A1053 17876 22979 8238 -6228 219 -1732 N
ATOM 1982 CA PRO A1053 -2.345 -31.221 -40.374 1.00127.71 C
ANISOU 1982 CA PRO A1053 18268 22172 8083 -5924 362 -1698 C
ATOM 1983 C PRO A1053 -2.663 -30.903 -41.842 1.00133.29 C
ANISOU 1983 C PRO A1053 19063 22993 8590 -5840 225 -1691 C
ATOM 1984 O PRO A1053 -1.741 -30.707 -42.635 1.00131.01 O
ANISOU 1984 O PRO A1053 19107 22308 8362 -5489 350 -1652 O
ATOM 1985 CB PRO A1053 -1.988 -32.704 -40.201 1.00130.91 C
ANISOU 1985 CB PRO A1053 19342 22128 8268 -6346 410 -1755 C
ATOM 1986 CG PRO A1053 -2.687 -33.141 -38.951 1.00136.13 C
ANISOU 1986 CG PRO A1053 19772 23074 8879 -6806 348 -1786 C
ATOM 1987 CD PRO A1053 -3.934 -32.325 -38.899 1.00133.05 C
ANISOU 1987 CD PRO A1053 18643 23455 8454 -6896 169 -1794 C
ATOM 1988 N ASP A1054 -3.963 -30.837 -42.191 1.00133.22 N
ANISOU 1988 N ASP A1054 18735 23557 8327 -6162 -32 -1733 N
ATOM 1989 CA ASP A1054 -4.469 -30.533 -43.532 1.00135.16 C
ANISOU 1989 CA ASP A1054 19011 23996 8347 -6128 -214 -1733 C
ATOM 1990 C ASP A1054 -4.702 -29.015 -43.733 1.00137.53 C
ANISOU 1990 C ASP A1054 18767 24645 8843 -5596 -303 -1680 C
ATOM 1991 O ASP A1054 -5.046 -28.599 -44.843 1.00139.01 O
ANISOU 1991 O ASP A1054 18972 24978 8865 -5485 -466 -1669 O
ATOM 1992 CB ASP A1054 -5.768 -31.317 -43.804 1.00141.63 C
ANISOU 1992 CB ASP A1054 19790 25274 8748 -6786 -469 -1818 C
ATOM 1993 CG ASP A1054 -6.854 -31.100 -42.768 1.00154.30 C
ANISOU 1993 CG ASP A1054 20719 27573 10333 -7051 -601 -1871 C
ATOM 1994 OD1 ASP A1054 -7.636 -30.138 -42.921 1.00155.73 O
ANISOU 1994 OD1 ASP A1054 20312 28337 10522 -6827 -777 -1889 O
ATOM 1995 OD2 ASP A1054 -6.916 -31.887 -41.801 1.00160.95 O
ANISOU 1995 OD2 ASP A1054 21632 28387 11135 -7470 -535 -1902 O
ATOM 1996 N SER A1055 -4.511 -28.200 -42.669 1.00131.47 N
ANISOU 1996 N SER A1055 17565 23984 8404 -5264 -216 -1649 N
ATOM 1997 CA SER A1055 -4.690 -26.742 -42.708 1.00130.29 C
ANISOU 1997 CA SER A1055 16962 24104 8438 -4727 -314 -1603 C
ATOM 1998 C SER A1055 -3.555 -26.057 -43.502 1.00131.35 C
ANISOU 1998 C SER A1055 17459 23726 8723 -4257 -178 -1493 C
ATOM 1999 O SER A1055 -2.449 -26.604 -43.541 1.00128.95 O
ANISOU 1999 O SER A1055 17605 22887 8501 -4263 67 -1460 O
ATOM 2000 CB SER A1055 -4.765 -26.171 -41.293 1.00131.70 C
ANISOU 2000 CB SER A1055 16639 24502 8899 -4539 -254 -1611 C
ATOM 2001 OG SER A1055 -3.523 -26.262 -40.614 1.00137.07 O
ANISOU 2001 OG SER A1055 17566 24641 9873 -4371 33 -1547 O
ATOM 2002 N PRO A1056 -3.789 -24.869 -44.126 1.00127.85 N
ANISOU 2002 N PRO A1056 16846 23443 8289 -3854 -339 -1440 N
ATOM 2003 CA PRO A1056 -2.708 -24.219 -44.894 1.00125.71 C
ANISOU 2003 CA PRO A1056 16952 22698 8113 -3487 -207 -1325 C
ATOM 2004 C PRO A1056 -1.530 -23.752 -44.030 1.00124.71 C
ANISOU 2004 C PRO A1056 16858 22184 8344 -3195 72 -1248 C
ATOM 2005 O PRO A1056 -0.388 -23.844 -44.480 1.00122.73 O
ANISOU 2005 O PRO A1056 17020 21476 8136 -3126 299 -1192 O
ATOM 2006 CB PRO A1056 -3.407 -23.029 -45.560 1.00129.42 C
ANISOU 2006 CB PRO A1056 17202 23475 8498 -3147 -492 -1290 C
ATOM 2007 CG PRO A1056 -4.595 -22.754 -44.713 1.00135.48 C
ANISOU 2007 CG PRO A1056 17360 24848 9267 -3147 -712 -1386 C
ATOM 2008 CD PRO A1056 -5.043 -24.088 -44.203 1.00132.06 C
ANISOU 2008 CD PRO A1056 16872 24600 8706 -3715 -662 -1491 C
ATOM 2009 N GLU A1057 -1.808 -23.283 -42.791 1.00119.21 N
ANISOU 2009 N GLU A1057 15714 21700 7880 -3037 58 -1258 N
ATOM 2010 CA GLU A1057 -0.825 -22.791 -41.813 1.00115.03 C
ANISOU 2010 CA GLU A1057 15139 20873 7696 -2768 288 -1191 C
ATOM 2011 C GLU A1057 0.210 -23.870 -41.460 1.00116.17 C
ANISOU 2011 C GLU A1057 15622 20595 7920 -2980 586 -1204 C
ATOM 2012 O GLU A1057 1.398 -23.561 -41.344 1.00113.11 O
ANISOU 2012 O GLU A1057 15415 19833 7729 -2749 811 -1131 O
ATOM 2013 CB GLU A1057 -1.531 -22.296 -40.538 1.00115.85 C
ANISOU 2013 CB GLU A1057 14693 21355 7970 -2650 189 -1236 C
ATOM 2014 CG GLU A1057 -2.231 -20.952 -40.679 1.00127.09 C
ANISOU 2014 CG GLU A1057 15798 23111 9380 -2252 -82 -1222 C
ATOM 2015 CD GLU A1057 -3.576 -20.966 -41.382 1.00151.06 C
ANISOU 2015 CD GLU A1057 18593 26695 12106 -2368 -405 -1320 C
ATOM 2016 OE1 GLU A1057 -4.467 -21.740 -40.959 1.00146.08 O
ANISOU 2016 OE1 GLU A1057 17684 26472 11349 -2739 -463 -1436 O
ATOM 2017 OE2 GLU A1057 -3.747 -20.184 -42.344 1.00147.85 O
ANISOU 2017 OE2 GLU A1057 18276 26333 11567 -2097 -611 -1280 O
ATOM 2018 N MET A1058 -0.246 -25.130 -41.308 1.00113.85 N
ANISOU 2018 N MET A1058 15435 20373 7448 -3421 571 -1302 N
ATOM 2019 CA MET A1058 0.590 -26.297 -41.017 1.00112.51 C
ANISOU 2019 CA MET A1058 15662 19799 7285 -3632 793 -1339 C
ATOM 2020 C MET A1058 1.420 -26.694 -42.245 1.00117.05 C
ANISOU 2020 C MET A1058 16779 19994 7701 -3590 908 -1328 C
ATOM 2021 O MET A1058 2.577 -27.095 -42.096 1.00114.85 O
ANISOU 2021 O MET A1058 16799 19317 7522 -3476 1147 -1330 O
ATOM 2022 CB MET A1058 -0.285 -27.477 -40.567 1.00116.92 C
ANISOU 2022 CB MET A1058 16230 20557 7636 -4157 686 -1443 C
ATOM 2023 CG MET A1058 -0.434 -27.583 -39.071 1.00119.02 C
ANISOU 2023 CG MET A1058 16174 20954 8095 -4244 736 -1465 C
ATOM 2024 SD MET A1058 0.774 -28.718 -38.354 1.00121.14 S
ANISOU 2024 SD MET A1058 16920 20632 8476 -4319 1001 -1485 S
ATOM 2025 CE MET A1058 0.127 -28.866 -36.711 1.00117.79 C
ANISOU 2025 CE MET A1058 16112 20523 8121 -4633 951 -1527 C
ATOM 2026 N LYS A1059 0.823 -26.583 -43.453 1.00116.43 N
ANISOU 2026 N LYS A1059 16812 20070 7357 -3670 733 -1328 N
ATOM 2027 CA LYS A1059 1.454 -26.915 -44.734 1.00117.50 C
ANISOU 2027 CA LYS A1059 17445 19913 7286 -3652 813 -1327 C
ATOM 2028 C LYS A1059 2.572 -25.931 -45.088 1.00120.00 C
ANISOU 2028 C LYS A1059 17817 20012 7765 -3230 988 -1222 C
ATOM 2029 O LYS A1059 3.594 -26.359 -45.626 1.00119.27 O
ANISOU 2029 O LYS A1059 18108 19595 7612 -3159 1198 -1235 O
ATOM 2030 CB LYS A1059 0.415 -26.961 -45.863 1.00123.35 C
ANISOU 2030 CB LYS A1059 18252 20924 7690 -3874 548 -1352 C
ATOM 2031 CG LYS A1059 -0.478 -28.200 -45.826 1.00139.86 C
ANISOU 2031 CG LYS A1059 20441 23176 9524 -4393 400 -1463 C
ATOM 2032 CD LYS A1059 -1.388 -28.310 -47.049 1.00152.79 C
ANISOU 2032 CD LYS A1059 22181 25069 10803 -4630 144 -1492 C
ATOM 2033 CE LYS A1059 -2.659 -27.501 -46.927 1.00163.75 C
ANISOU 2033 CE LYS A1059 23004 27042 12172 -4594 -140 -1480 C
ATOM 2034 NZ LYS A1059 -3.595 -27.774 -48.048 1.00175.05 N
ANISOU 2034 NZ LYS A1059 24519 28766 13227 -4890 -407 -1529 N
ATOM 2035 N ASP A1060 2.384 -24.625 -44.781 1.00116.12 N
ANISOU 2035 N ASP A1060 16959 19709 7451 -2958 896 -1125 N
ATOM 2036 CA ASP A1060 3.368 -23.563 -45.034 1.00114.73 C
ANISOU 2036 CA ASP A1060 16834 19346 7410 -2613 1030 -1006 C
ATOM 2037 C ASP A1060 4.648 -23.783 -44.217 1.00116.24 C
ANISOU 2037 C ASP A1060 17076 19242 7850 -2482 1347 -999 C
ATOM 2038 O ASP A1060 5.742 -23.493 -44.705 1.00115.26 O
ANISOU 2038 O ASP A1060 17163 18904 7727 -2327 1546 -945 O
ATOM 2039 CB ASP A1060 2.777 -22.176 -44.718 1.00116.42 C
ANISOU 2039 CB ASP A1060 16684 19801 7749 -2361 819 -917 C
ATOM 2040 CG ASP A1060 1.639 -21.731 -45.620 1.00129.96 C
ANISOU 2040 CG ASP A1060 18309 21849 9222 -2394 476 -928 C
ATOM 2041 OD1 ASP A1060 1.749 -21.912 -46.855 1.00132.91 O
ANISOU 2041 OD1 ASP A1060 19004 22176 9322 -2520 425 -933 O
ATOM 2042 OD2 ASP A1060 0.660 -21.153 -45.098 1.00136.00 O
ANISOU 2042 OD2 ASP A1060 18676 22938 10057 -2269 254 -942 O
ATOM 2043 N PHE A1061 4.503 -24.303 -42.982 1.00111.70 N
ANISOU 2043 N PHE A1061 16296 18686 7457 -2562 1388 -1059 N
ATOM 2044 CA PHE A1061 5.602 -24.606 -42.064 1.00109.18 C
ANISOU 2044 CA PHE A1061 15993 18116 7373 -2445 1651 -1070 C
ATOM 2045 C PHE A1061 6.394 -25.825 -42.555 1.00114.39 C
ANISOU 2045 C PHE A1061 17104 18491 7869 -2535 1837 -1170 C
ATOM 2046 O PHE A1061 7.623 -25.811 -42.497 1.00112.75 O
ANISOU 2046 O PHE A1061 17014 18074 7753 -2328 2080 -1166 O
ATOM 2047 CB PHE A1061 5.056 -24.844 -40.642 1.00109.61 C
ANISOU 2047 CB PHE A1061 15724 18301 7623 -2539 1594 -1110 C
ATOM 2048 CG PHE A1061 6.091 -25.029 -39.556 1.00108.57 C
ANISOU 2048 CG PHE A1061 15569 17934 7749 -2410 1826 -1119 C
ATOM 2049 CD1 PHE A1061 6.699 -23.931 -38.956 1.00109.25 C
ANISOU 2049 CD1 PHE A1061 15410 17992 8109 -2123 1925 -1023 C
ATOM 2050 CD2 PHE A1061 6.419 -26.298 -39.094 1.00110.89 C
ANISOU 2050 CD2 PHE A1061 16106 18032 7994 -2583 1915 -1224 C
ATOM 2051 CE1 PHE A1061 7.643 -24.103 -37.939 1.00107.94 C
ANISOU 2051 CE1 PHE A1061 15204 17635 8174 -2008 2126 -1035 C
ATOM 2052 CE2 PHE A1061 7.362 -26.469 -38.077 1.00111.55 C
ANISOU 2052 CE2 PHE A1061 16173 17906 8305 -2436 2104 -1239 C
ATOM 2053 CZ PHE A1061 7.966 -25.371 -37.504 1.00107.21 C
ANISOU 2053 CZ PHE A1061 15334 17364 8037 -2150 2213 -1145 C
ATOM 2054 N ARG A1062 5.688 -26.867 -43.046 1.00113.78 N
ANISOU 2054 N ARG A1062 17283 18425 7524 -2835 1711 -1269 N
ATOM 2055 CA ARG A1062 6.284 -28.109 -43.550 1.00115.32 C
ANISOU 2055 CA ARG A1062 17978 18332 7507 -2919 1832 -1386 C
ATOM 2056 C ARG A1062 7.047 -27.884 -44.861 1.00121.04 C
ANISOU 2056 C ARG A1062 18988 18952 8048 -2754 1955 -1378 C
ATOM 2057 O ARG A1062 8.184 -28.355 -44.980 1.00120.54 O
ANISOU 2057 O ARG A1062 19178 18659 7962 -2575 2184 -1447 O
ATOM 2058 CB ARG A1062 5.213 -29.195 -43.748 1.00118.28 C
ANISOU 2058 CB ARG A1062 18582 18751 7607 -3336 1623 -1481 C
ATOM 2059 CG ARG A1062 4.701 -29.809 -42.453 1.00128.30 C
ANISOU 2059 CG ARG A1062 19720 20047 8982 -3565 1559 -1523 C
ATOM 2060 CD ARG A1062 3.827 -31.017 -42.719 1.00141.93 C
ANISOU 2060 CD ARG A1062 21803 21748 10376 -4031 1383 -1622 C
ATOM 2061 NE ARG A1062 3.230 -31.537 -41.488 1.00150.85 N
ANISOU 2061 NE ARG A1062 22783 22966 11565 -4330 1300 -1647 N
ATOM 2062 CZ ARG A1062 2.003 -31.248 -41.066 1.00166.17 C
ANISOU 2062 CZ ARG A1062 24321 25342 13475 -4633 1099 -1625 C
ATOM 2063 NH1 ARG A1062 1.220 -30.446 -41.778 1.00154.31 N
ANISOU 2063 NH1 ARG A1062 22530 24214 11886 -4641 939 -1584 N
ATOM 2064 NH2 ARG A1062 1.546 -31.763 -39.933 1.00153.32 N
ANISOU 2064 NH2 ARG A1062 22576 23802 11877 -4928 1052 -1651 N
ATOM 2065 N HIS A1063 6.418 -27.169 -45.832 1.00119.48 N
ANISOU 2065 N HIS A1063 18747 18950 7702 -2804 1797 -1302 N
ATOM 2066 CA AHIS A1063 7.015 -26.882 -47.137 0.50120.94 C
ANISOU 2066 CA AHIS A1063 19204 19073 7676 -2698 1890 -1280 C
ATOM 2067 CA BHIS A1063 7.002 -26.868 -47.143 0.50120.82 C
ANISOU 2067 CA BHIS A1063 19184 19063 7660 -2699 1886 -1278 C
ATOM 2068 C HIS A1063 8.150 -25.861 -47.019 1.00123.24 C
ANISOU 2068 C HIS A1063 19345 19328 8153 -2399 2117 -1181 C
ATOM 2069 O HIS A1063 9.106 -25.928 -47.792 1.00123.76 O
ANISOU 2069 O HIS A1063 19655 19296 8071 -2291 2318 -1207 O
ATOM 2070 CB AHIS A1063 5.953 -26.394 -48.139 0.50123.85 C
ANISOU 2070 CB AHIS A1063 19578 19657 7824 -2846 1624 -1220 C
ATOM 2071 CB BHIS A1063 5.923 -26.345 -48.110 0.50123.52 C
ANISOU 2071 CB BHIS A1063 19504 19631 7798 -2842 1613 -1212 C
ATOM 2072 CG AHIS A1063 4.835 -27.368 -48.377 0.50129.55 C
ANISOU 2072 CG AHIS A1063 20448 20464 8310 -3190 1397 -1317 C
ATOM 2073 CG BHIS A1063 6.437 -25.983 -49.471 0.50128.51 C
ANISOU 2073 CG BHIS A1063 20420 20217 8193 -2766 1678 -1171 C
ATOM 2074 ND1AHIS A1063 3.533 -26.936 -48.564 0.50132.65 N
ANISOU 2074 ND1AHIS A1063 20611 21174 8614 -3351 1092 -1277 N
ATOM 2075 ND1BHIS A1063 6.874 -26.949 -50.359 0.50132.35 N
ANISOU 2075 ND1BHIS A1063 21355 20544 8389 -2845 1781 -1283 N
ATOM 2076 CD2AHIS A1063 4.856 -28.722 -48.431 0.50132.68 C
ANISOU 2076 CD2AHIS A1063 21211 20677 8525 -3401 1422 -1453 C
ATOM 2077 CD2BHIS A1063 6.565 -24.767 -50.050 0.50130.27 C
ANISOU 2077 CD2BHIS A1063 20565 20525 8407 -2631 1645 -1032 C
ATOM 2078 CE1AHIS A1063 2.812 -28.031 -48.739 0.50134.22 C
ANISOU 2078 CE1AHIS A1063 21012 21405 8581 -3700 956 -1383 C
ATOM 2079 CE1BHIS A1063 7.260 -26.292 -51.441 0.50132.94 C
ANISOU 2079 CE1BHIS A1063 21569 20646 8295 -2765 1827 -1210 C
ATOM 2080 NE2AHIS A1063 3.564 -29.129 -48.668 0.50134.68 N
ANISOU 2080 NE2AHIS A1063 21467 21137 8571 -3755 1140 -1486 N
ATOM 2081 NE2BHIS A1063 7.089 -24.977 -51.302 0.50132.14 N
ANISOU 2081 NE2BHIS A1063 21180 20680 8348 -2653 1742 -1051 N
ATOM 2082 N GLY A1064 8.039 -24.948 -46.051 1.00118.19 N
ANISOU 2082 N GLY A1064 18312 18784 7810 -2287 2083 -1078 N
ATOM 2083 CA GLY A1064 9.035 -23.914 -45.777 1.00116.67 C
ANISOU 2083 CA GLY A1064 17960 18564 7806 -2057 2267 -970 C
ATOM 2084 C GLY A1064 10.415 -24.474 -45.488 1.00120.71 C
ANISOU 2084 C GLY A1064 18568 18917 8380 -1914 2587 -1053 C
ATOM 2085 O GLY A1064 11.416 -23.937 -45.970 1.00120.29 O
ANISOU 2085 O GLY A1064 18550 18866 8290 -1792 2787 -1004 O
ATOM 2086 N PHE A1065 10.468 -25.580 -44.722 1.00117.88 N
ANISOU 2086 N PHE A1065 18267 18436 8084 -1937 2625 -1186 N
ATOM 2087 CA PHE A1065 11.709 -26.274 -44.381 1.00117.97 C
ANISOU 2087 CA PHE A1065 18396 18294 8132 -1753 2889 -1301 C
ATOM 2088 C PHE A1065 12.225 -27.089 -45.561 1.00126.27 C
ANISOU 2088 C PHE A1065 19867 19268 8843 -1723 3004 -1429 C
ATOM 2089 O PHE A1065 13.439 -27.186 -45.732 1.00126.17 O
ANISOU 2089 O PHE A1065 19898 19249 8793 -1505 3257 -1492 O
ATOM 2090 CB PHE A1065 11.518 -27.183 -43.157 1.00118.63 C
ANISOU 2090 CB PHE A1065 18469 18237 8366 -1782 2848 -1398 C
ATOM 2091 CG PHE A1065 11.670 -26.478 -41.830 1.00117.15 C
ANISOU 2091 CG PHE A1065 17873 18098 8542 -1688 2872 -1309 C
ATOM 2092 CD1 PHE A1065 12.929 -26.190 -41.316 1.00118.84 C
ANISOU 2092 CD1 PHE A1065 17942 18281 8930 -1436 3109 -1305 C
ATOM 2093 CD2 PHE A1065 10.555 -26.120 -41.084 1.00118.07 C
ANISOU 2093 CD2 PHE A1065 17734 18321 8804 -1851 2657 -1243 C
ATOM 2094 CE1 PHE A1065 13.069 -25.536 -40.090 1.00117.12 C
ANISOU 2094 CE1 PHE A1065 17368 18096 9037 -1361 3121 -1222 C
ATOM 2095 CE2 PHE A1065 10.695 -25.472 -39.854 1.00118.32 C
ANISOU 2095 CE2 PHE A1065 17405 18396 9156 -1750 2679 -1171 C
ATOM 2096 CZ PHE A1065 11.950 -25.182 -39.366 1.00114.95 C
ANISOU 2096 CZ PHE A1065 16875 17892 8907 -1511 2907 -1156 C
ATOM 2097 N ASP A1066 11.306 -27.660 -46.380 1.00126.57 N
ANISOU 2097 N ASP A1066 20195 19280 8615 -1939 2815 -1476 N
ATOM 2098 CA ASP A1066 11.620 -28.475 -47.561 1.00130.15 C
ANISOU 2098 CA ASP A1066 21097 19647 8708 -1933 2883 -1606 C
ATOM 2099 C ASP A1066 12.405 -27.684 -48.618 1.00137.28 C
ANISOU 2099 C ASP A1066 22001 20694 9465 -1822 3056 -1543 C
ATOM 2100 O ASP A1066 13.219 -28.278 -49.327 1.00138.94 O
ANISOU 2100 O ASP A1066 22491 20869 9432 -1690 3237 -1675 O
ATOM 2101 CB ASP A1066 10.345 -29.062 -48.184 1.00133.90 C
ANISOU 2101 CB ASP A1066 21846 20093 8937 -2243 2608 -1639 C
ATOM 2102 CG ASP A1066 10.342 -30.577 -48.250 1.00144.77 C
ANISOU 2102 CG ASP A1066 23700 21214 10093 -2295 2588 -1834 C
ATOM 2103 OD1 ASP A1066 11.084 -31.137 -49.087 1.00147.07 O
ANISOU 2103 OD1 ASP A1066 24334 21394 10151 -2110 2753 -1965 O
ATOM 2104 OD2 ASP A1066 9.583 -31.202 -47.480 1.00150.20 O
ANISOU 2104 OD2 ASP A1066 24440 21820 10811 -2529 2400 -1861 O
ATOM 2105 N ILE A1067 12.172 -26.354 -48.710 1.00134.57 N
ANISOU 2105 N ILE A1067 21372 20515 9243 -1872 2996 -1351 N
ATOM 2106 CA ILE A1067 12.882 -25.450 -49.625 1.00136.44 C
ANISOU 2106 CA ILE A1067 21615 20887 9339 -1831 3144 -1255 C
ATOM 2107 C ILE A1067 14.348 -25.357 -49.158 1.00142.13 C
ANISOU 2107 C ILE A1067 22178 21659 10164 -1605 3476 -1303 C
ATOM 2108 O ILE A1067 15.260 -25.406 -49.987 1.00143.87 O
ANISOU 2108 O ILE A1067 22533 21984 10147 -1533 3699 -1363 O
ATOM 2109 CB ILE A1067 12.191 -24.052 -49.724 1.00138.74 C
ANISOU 2109 CB ILE A1067 21706 21285 9725 -1939 2942 -1034 C
ATOM 2110 CG1 ILE A1067 10.718 -24.181 -50.178 1.00140.34 C
ANISOU 2110 CG1 ILE A1067 22025 21504 9793 -2128 2600 -1012 C
ATOM 2111 CG2 ILE A1067 12.962 -23.100 -50.659 1.00140.85 C
ANISOU 2111 CG2 ILE A1067 22034 21659 9823 -1943 3092 -915 C
ATOM 2112 CD1 ILE A1067 9.776 -23.098 -49.636 1.00146.82 C
ANISOU 2112 CD1 ILE A1067 22552 22421 10813 -2148 2329 -859 C
ATOM 2113 N LEU A1068 14.560 -25.272 -47.828 1.00137.96 N
ANISOU 2113 N LEU A1068 21356 21091 9972 -1497 3506 -1290 N
ATOM 2114 CA LEU A1068 15.887 -25.208 -47.208 1.00137.97 C
ANISOU 2114 CA LEU A1068 21155 21163 10105 -1279 3789 -1341 C
ATOM 2115 C LEU A1068 16.588 -26.572 -47.275 1.00145.45 C
ANISOU 2115 C LEU A1068 22335 22032 10899 -1063 3948 -1591 C
ATOM 2116 O LEU A1068 17.798 -26.612 -47.502 1.00146.44 O
ANISOU 2116 O LEU A1068 22409 22313 10917 -870 4216 -1683 O
ATOM 2117 CB LEU A1068 15.803 -24.722 -45.747 1.00134.86 C
ANISOU 2117 CB LEU A1068 20401 20732 10110 -1234 3739 -1252 C
ATOM 2118 CG LEU A1068 15.126 -23.367 -45.486 1.00138.04 C
ANISOU 2118 CG LEU A1068 20583 21181 10683 -1379 3550 -1027 C
ATOM 2119 CD1 LEU A1068 14.715 -23.246 -44.041 1.00135.40 C
ANISOU 2119 CD1 LEU A1068 19973 20772 10701 -1337 3438 -996 C
ATOM 2120 CD2 LEU A1068 16.027 -22.196 -45.868 1.00140.97 C
ANISOU 2120 CD2 LEU A1068 20841 21704 11018 -1397 3706 -885 C
ATOM 2121 N VAL A1069 15.826 -27.680 -47.093 1.00143.76 N
ANISOU 2121 N VAL A1069 22392 21590 10640 -1100 3769 -1709 N
ATOM 2122 CA VAL A1069 16.308 -29.071 -47.155 1.00146.26 C
ANISOU 2122 CA VAL A1069 23057 21742 10773 -895 3842 -1954 C
ATOM 2123 C VAL A1069 16.845 -29.354 -48.575 1.00154.73 C
ANISOU 2123 C VAL A1069 24420 22920 11448 -814 3987 -2069 C
ATOM 2124 O VAL A1069 17.917 -29.950 -48.716 1.00156.14 O
ANISOU 2124 O VAL A1069 24694 23148 11482 -504 4200 -2259 O
ATOM 2125 CB VAL A1069 15.200 -30.082 -46.719 1.00150.35 C
ANISOU 2125 CB VAL A1069 23871 21977 11279 -1068 3569 -2015 C
ATOM 2126 CG1 VAL A1069 15.497 -31.510 -47.182 1.00153.30 C
ANISOU 2126 CG1 VAL A1069 24783 22127 11338 -918 3579 -2259 C
ATOM 2127 CG2 VAL A1069 14.991 -30.051 -45.209 1.00147.34 C
ANISOU 2127 CG2 VAL A1069 23229 21503 11251 -1075 3493 -1963 C
ATOM 2128 N GLY A1070 16.109 -28.885 -49.588 1.00153.16 N
ANISOU 2128 N GLY A1070 24341 22782 11071 -1071 3867 -1958 N
ATOM 2129 CA GLY A1070 16.449 -29.020 -51.002 1.00156.64 C
ANISOU 2129 CA GLY A1070 25062 23333 11123 -1061 3976 -2035 C
ATOM 2130 C GLY A1070 17.803 -28.441 -51.362 1.00162.66 C
ANISOU 2130 C GLY A1070 25609 24398 11795 -871 4311 -2060 C
ATOM 2131 O GLY A1070 18.568 -29.080 -52.087 1.00165.26 O
ANISOU 2131 O GLY A1070 26151 24816 11826 -660 4496 -2260 O
ATOM 2132 N GLN A1071 18.120 -27.241 -50.825 1.00157.85 N
ANISOU 2132 N GLN A1071 24581 23968 11427 -948 4387 -1868 N
ATOM 2133 CA GLN A1071 19.394 -26.546 -51.040 1.00159.08 C
ANISOU 2133 CA GLN A1071 24473 24462 11509 -859 4698 -1857 C
ATOM 2134 C GLN A1071 20.564 -27.313 -50.407 1.00164.20 C
ANISOU 2134 C GLN A1071 24990 25212 12188 -476 4933 -2088 C
ATOM 2135 O GLN A1071 21.673 -27.271 -50.943 1.00166.52 O
ANISOU 2135 O GLN A1071 25188 25831 12250 -330 5214 -2201 O
ATOM 2136 CB GLN A1071 19.336 -25.112 -50.495 1.00158.07 C
ANISOU 2136 CB GLN A1071 23987 24431 11640 -1066 4668 -1589 C
ATOM 2137 CG GLN A1071 19.012 -24.063 -51.555 1.00174.58 C
ANISOU 2137 CG GLN A1071 26185 26626 13521 -1368 4610 -1392 C
ATOM 2138 CD GLN A1071 17.532 -23.914 -51.801 1.00193.30 C
ANISOU 2138 CD GLN A1071 28756 28758 15932 -1560 4250 -1267 C
ATOM 2139 OE1 GLN A1071 16.848 -23.115 -51.153 1.00187.10 O
ANISOU 2139 OE1 GLN A1071 27803 27885 15403 -1665 4050 -1087 O
ATOM 2140 NE2 GLN A1071 17.008 -24.659 -52.762 1.00188.25 N
ANISOU 2140 NE2 GLN A1071 28474 28033 15018 -1599 4153 -1370 N
ATOM 2141 N ILE A1072 20.313 -28.019 -49.282 1.00159.09 N
ANISOU 2141 N ILE A1072 24339 24311 11798 -312 4812 -2165 N
ATOM 2142 CA ILE A1072 21.307 -28.848 -48.588 1.00159.79 C
ANISOU 2142 CA ILE A1072 24363 24431 11919 96 4971 -2396 C
ATOM 2143 C ILE A1072 21.535 -30.119 -49.429 1.00167.48 C
ANISOU 2143 C ILE A1072 25797 25331 12506 356 5009 -2676 C
ATOM 2144 O ILE A1072 22.682 -30.533 -49.608 1.00169.68 O
ANISOU 2144 O ILE A1072 26016 25856 12599 714 5247 -2891 O
ATOM 2145 CB ILE A1072 20.883 -29.165 -47.117 1.00159.81 C
ANISOU 2145 CB ILE A1072 24283 24144 12295 156 4798 -2374 C
ATOM 2146 CG1 ILE A1072 20.687 -27.866 -46.293 1.00156.66 C
ANISOU 2146 CG1 ILE A1072 23446 23817 12262 -82 4751 -2105 C
ATOM 2147 CG2 ILE A1072 21.891 -30.101 -46.424 1.00161.72 C
ANISOU 2147 CG2 ILE A1072 24505 24396 12544 615 4936 -2620 C
ATOM 2148 CD1 ILE A1072 19.741 -27.989 -45.077 1.00160.79 C
ANISOU 2148 CD1 ILE A1072 23949 24030 13114 -182 4497 -2022 C
ATOM 2149 N ASP A1073 20.439 -30.702 -49.970 1.00164.71 N
ANISOU 2149 N ASP A1073 25900 24672 12012 174 4768 -2680 N
ATOM 2150 CA ASP A1073 20.442 -31.901 -50.815 1.00168.32 C
ANISOU 2150 CA ASP A1073 26893 24979 12081 359 4743 -2926 C
ATOM 2151 C ASP A1073 21.184 -31.666 -52.139 1.00175.68 C
ANISOU 2151 C ASP A1073 27846 26268 12635 426 4985 -3008 C
ATOM 2152 O ASP A1073 21.825 -32.590 -52.642 1.00178.74 O
ANISOU 2152 O ASP A1073 28516 26693 12705 777 5099 -3283 O
ATOM 2153 CB ASP A1073 19.006 -32.365 -51.094 1.00169.89 C
ANISOU 2153 CB ASP A1073 27524 24806 12223 33 4412 -2860 C
ATOM 2154 N ASP A1074 21.095 -30.436 -52.695 1.00171.74 N
ANISOU 2154 N ASP A1074 27078 26029 12147 97 5053 -2776 N
ATOM 2155 CA ASP A1074 21.774 -30.039 -53.934 1.00175.02 C
ANISOU 2155 CA ASP A1074 27481 26819 12201 66 5288 -2809 C
ATOM 2156 C ASP A1074 23.287 -29.959 -53.709 1.00182.27 C
ANISOU 2156 C ASP A1074 28030 28181 13043 400 5641 -2972 C
ATOM 2157 O ASP A1074 24.058 -30.356 -54.585 1.00185.76 O
ANISOU 2157 O ASP A1074 28570 28913 13099 606 5857 -3179 O
ATOM 2158 CB ASP A1074 21.235 -28.692 -54.453 1.00175.20 C
ANISOU 2158 CB ASP A1074 27345 26955 12269 -400 5229 -2493 C
ATOM 2159 CG ASP A1074 19.791 -28.699 -54.931 1.00181.30 C
ANISOU 2159 CG ASP A1074 28448 27402 13034 -718 4891 -2347 C
ATOM 2160 OD1 ASP A1074 19.215 -29.801 -55.082 1.00181.72 O
ANISOU 2160 OD1 ASP A1074 28901 27168 12978 -641 4722 -2497 O
ATOM 2161 OD2 ASP A1074 19.234 -27.602 -55.148 1.00183.34 O
ANISOU 2161 OD2 ASP A1074 28581 27699 13381 -1043 4780 -2088 O
ATOM 2162 N ALA A1075 23.702 -29.460 -52.526 1.00177.39 N
ANISOU 2162 N ALA A1075 26974 27647 12777 459 5696 -2891 N
ATOM 2163 CA ALA A1075 25.103 -29.344 -52.117 1.00179.25 C
ANISOU 2163 CA ALA A1075 26785 28332 12989 760 6004 -3035 C
ATOM 2164 C ALA A1075 25.660 -30.704 -51.674 1.00185.84 C
ANISOU 2164 C ALA A1075 27791 29073 13748 1339 6024 -3381 C
ATOM 2165 O ALA A1075 26.872 -30.916 -51.745 1.00188.54 O
ANISOU 2165 O ALA A1075 27890 29849 13898 1701 6290 -3605 O
ATOM 2166 CB ALA A1075 25.235 -28.329 -50.991 1.00176.48 C
ANISOU 2166 CB ALA A1075 25950 28060 13045 576 6011 -2806 C
ATOM 2167 N LEU A1076 24.770 -31.619 -51.222 1.00181.29 N
ANISOU 2167 N LEU A1076 27644 27946 13291 1418 5732 -3429 N
ATOM 2168 CA LEU A1076 25.108 -32.975 -50.773 1.00183.17 C
ANISOU 2168 CA LEU A1076 28200 27954 13442 1940 5670 -3738 C
ATOM 2169 C LEU A1076 25.594 -33.846 -51.937 1.00191.56 C
ANISOU 2169 C LEU A1076 29650 29137 13998 2280 5779 -4044 C
ATOM 2170 O LEU A1076 26.480 -34.679 -51.740 1.00193.09 O
ANISOU 2170 O LEU A1076 29693 29451 14222 2563 5799 -4401 O
ATOM 2171 CB LEU A1076 23.901 -33.635 -50.097 1.00180.89 C
ANISOU 2171 CB LEU A1076 28338 27033 13360 1798 5309 -3669 C
ATOM 2172 N LYS A1077 25.014 -33.650 -53.141 1.00189.30 N
ANISOU 2172 N LYS A1077 29618 28852 13455 1965 5759 -3966 N
ATOM 2173 CA LYS A1077 25.377 -34.372 -54.364 1.00190.65 C
ANISOU 2173 CA LYS A1077 29564 29387 13489 1801 5642 -4323 C
ATOM 2174 C LYS A1077 26.778 -33.966 -54.832 1.00187.06 C
ANISOU 2174 C LYS A1077 28181 29001 13890 1439 5556 -4195 C
ATOM 2175 O LYS A1077 27.520 -34.807 -55.342 1.00188.01 O
ANISOU 2175 O LYS A1077 28369 29081 13984 1537 5618 -4464 O
ATOM 2176 CB LYS A1077 24.346 -34.114 -55.471 1.00191.52 C
ANISOU 2176 CB LYS A1077 29616 29604 13549 1395 5326 -4150 C
ATOM 2177 N LEU A1078 27.135 -32.679 -54.641 1.00188.22 N
ANISOU 2177 N LEU A1078 28367 29582 13568 1473 6117 -4093 N
ATOM 2178 CA LEU A1078 28.440 -32.114 -54.997 1.00184.10 C
ANISOU 2178 CA LEU A1078 27480 28939 13531 1466 6215 -3848 C
ATOM 2179 C LEU A1078 29.516 -32.568 -54.003 1.00185.48 C
ANISOU 2179 C LEU A1078 27395 28891 14187 1594 6280 -3990 C
ATOM 2180 O LEU A1078 30.641 -32.854 -54.414 1.00188.60 O
ANISOU 2180 O LEU A1078 27832 29464 14362 1746 6670 -4244 O
ATOM 2181 CB LEU A1078 28.374 -30.575 -55.044 1.00186.77 C
ANISOU 2181 CB LEU A1078 27806 29641 13515 1374 6583 -3519 C
ATOM 2182 CG LEU A1078 27.505 -29.954 -56.142 1.00186.56 C
ANISOU 2182 CG LEU A1078 27719 29421 13746 1154 6094 -3078 C
ATOM 2183 CD1 LEU A1078 26.862 -28.671 -55.666 1.00191.33 C
ANISOU 2183 CD1 LEU A1078 28476 30431 13788 1072 6447 -2846 C
ATOM 2184 CD2 LEU A1078 28.305 -29.705 -57.412 1.00188.65 C
ANISOU 2184 CD2 LEU A1078 27907 29686 14086 1123 6123 -2960 C
ATOM 2185 N ALA A1079 29.163 -32.636 -52.702 1.00182.69 N
ANISOU 2185 N ALA A1079 27058 28542 13814 1654 6353 -4113 N
ATOM 2186 CA ALA A1079 30.053 -33.050 -51.612 1.00181.30 C
ANISOU 2186 CA ALA A1079 26696 28214 13976 1802 6473 -4297 C
ATOM 2187 C ALA A1079 30.377 -34.550 -51.670 1.00184.41 C
ANISOU 2187 C ALA A1079 27156 28289 14625 1898 6198 -4619 C
ATOM 2188 O ALA A1079 31.468 -34.948 -51.256 1.00186.58 O
ANISOU 2188 O ALA A1079 27356 28554 14982 2079 6467 -4867 O
ATOM 2189 CB ALA A1079 29.426 -32.708 -50.270 1.00184.76 C
ANISOU 2189 CB ALA A1079 27131 28946 14125 2076 6587 -4332 C
ATOM 2190 N ASN A1080 29.432 -35.373 -52.176 1.00182.34 N
ANISOU 2190 N ASN A1080 27178 27967 14137 1848 5917 -4787 N
ATOM 2191 CA ASN A1080 29.576 -36.827 -52.313 1.00183.89 C
ANISOU 2191 CA ASN A1080 27560 27973 14336 1942 5763 -5182 C
ATOM 2192 C ASN A1080 30.628 -37.197 -53.366 1.00192.37 C
ANISOU 2192 C ASN A1080 28742 29215 15134 2085 6101 -5448 C
ATOM 2193 O ASN A1080 31.319 -38.204 -53.206 1.00193.09 O
ANISOU 2193 O ASN A1080 28873 29148 15344 2227 6136 -5769 O
ATOM 2194 CB ASN A1080 28.235 -37.468 -52.672 1.00185.20 C
ANISOU 2194 CB ASN A1080 27970 28063 14335 1808 5361 -5225 C
ATOM 2195 CG ASN A1080 27.612 -38.244 -51.541 1.00202.84 C
ANISOU 2195 CG ASN A1080 30084 29872 17115 1725 4865 -5173 C
ATOM 2196 OD1 ASN A1080 27.014 -37.680 -50.619 1.00195.02 O
ANISOU 2196 OD1 ASN A1080 28809 28656 16634 1583 4543 -4768 O
ATOM 2197 ND2 ASN A1080 27.725 -39.563 -51.596 1.00199.07 N
ANISOU 2197 ND2 ASN A1080 29949 29388 16301 1853 4928 -5730 N
ATOM 2198 N GLU A1081 30.741 -36.384 -54.435 1.00189.99 N
ANISOU 2198 N GLU A1081 28435 29165 14585 2018 6269 -5237 N
ATOM 2199 CA GLU A1081 31.693 -36.580 -55.533 1.00194.42 C
ANISOU 2199 CA GLU A1081 29118 29962 14789 2145 6646 -5466 C
ATOM 2200 C GLU A1081 33.129 -36.263 -55.088 1.00197.28 C
ANISOU 2200 C GLU A1081 29187 30338 15433 2279 6986 -5441 C
ATOM 2201 O GLU A1081 34.056 -36.982 -55.464 1.00198.60 O
ANISOU 2201 O GLU A1081 29372 30479 15610 2425 7148 -5700 O
ATOM 2202 CB GLU A1081 31.308 -35.719 -56.749 1.00196.90 C
ANISOU 2202 CB GLU A1081 29514 30543 14755 2008 6700 -5200 C
ATOM 2203 CG GLU A1081 30.024 -36.157 -57.434 1.00204.09 C
ANISOU 2203 CG GLU A1081 30514 31215 15814 1816 6097 -5033 C
ATOM 2204 CD GLU A1081 29.537 -35.228 -58.527 1.00223.73 C
ANISOU 2204 CD GLU A1081 32747 33551 18708 1561 5686 -4407 C
ATOM 2205 OE1 GLU A1081 29.572 -35.635 -59.710 1.00227.57 O
ANISOU 2205 OE1 GLU A1081 33464 34182 18819 1571 5722 -4563 O
ATOM 2206 OE2 GLU A1081 29.111 -34.096 -58.203 1.00219.45 O
ANISOU 2206 OE2 GLU A1081 32181 33207 17993 1498 5842 -4175 O
ATOM 2207 N GLY A1082 33.287 -35.198 -54.300 1.00192.81 N
ANISOU 2207 N GLY A1082 28419 29911 14928 2263 7210 -5216 N
ATOM 2208 CA GLY A1082 34.575 -34.750 -53.777 1.00192.12 C
ANISOU 2208 CA GLY A1082 28030 29881 15087 2375 7552 -5162 C
ATOM 2209 C GLY A1082 34.877 -33.280 -54.003 1.00194.05 C
ANISOU 2209 C GLY A1082 28014 30307 15411 2219 7696 -4685 C
ATOM 2210 O GLY A1082 36.026 -32.858 -53.846 1.00193.48 O
ANISOU 2210 O GLY A1082 27674 30298 15541 2275 7955 -4595 O
ATOM 2211 N LYS A1083 33.848 -32.489 -54.366 1.00192.12 N
ANISOU 2211 N LYS A1083 27909 30244 14843 2053 7652 -4452 N
ATOM 2212 CA LYS A1083 33.961 -31.051 -54.630 1.00191.73 C
ANISOU 2212 CA LYS A1083 27693 30402 14755 1888 7818 -4014 C
ATOM 2213 C LYS A1083 33.884 -30.248 -53.330 1.00192.92 C
ANISOU 2213 C LYS A1083 27540 30412 15347 1807 7724 -3727 C
ATOM 2214 O LYS A1083 33.086 -30.578 -52.449 1.00188.57 O
ANISOU 2214 O LYS A1083 26957 29561 15129 1780 7334 -3721 O
ATOM 2215 CB LYS A1083 32.868 -30.591 -55.609 1.00193.56 C
ANISOU 2215 CB LYS A1083 28115 30679 14748 1694 7558 -3759 C
ATOM 2216 CG LYS A1083 33.064 -31.104 -57.030 1.00210.63 C
ANISOU 2216 CG LYS A1083 30386 32786 16858 1671 7394 -3793 C
ATOM 2217 CD LYS A1083 31.736 -31.386 -57.713 1.00222.84 C
ANISOU 2217 CD LYS A1083 32169 34224 18274 1566 6980 -3768 C
ATOM 2218 CE LYS A1083 31.929 -31.962 -59.093 1.00233.76 C
ANISOU 2218 CE LYS A1083 33517 35365 19937 1504 6614 -3700 C
ATOM 2219 NZ LYS A1083 30.630 -32.286 -59.739 1.00240.75 N
ANISOU 2219 NZ LYS A1083 34435 35914 21125 1358 5971 -3548 N
ATOM 2220 N VAL A1084 34.715 -29.193 -53.217 1.00189.95 N
ANISOU 2220 N VAL A1084 26926 30220 15027 1742 8030 -3459 N
ATOM 2221 CA VAL A1084 34.779 -28.328 -52.033 1.00186.35 C
ANISOU 2221 CA VAL A1084 26173 29668 14965 1652 7987 -3177 C
ATOM 2222 C VAL A1084 34.183 -26.946 -52.367 1.00189.06 C
ANISOU 2222 C VAL A1084 26482 30067 15284 1389 7872 -2693 C
ATOM 2223 O VAL A1084 33.257 -26.512 -51.682 1.00186.99 O
ANISOU 2223 O VAL A1084 26205 29677 15166 1283 7626 -2512 O
ATOM 2224 CB VAL A1084 36.222 -28.217 -51.455 1.00190.80 C
ANISOU 2224 CB VAL A1084 26434 30303 15758 1767 8329 -3231 C
ATOM 2225 CG1 VAL A1084 36.251 -27.362 -50.188 1.00188.05 C
ANISOU 2225 CG1 VAL A1084 25809 29914 15727 1688 8348 -2991 C
ATOM 2226 CG2 VAL A1084 36.819 -29.595 -51.177 1.00191.86 C
ANISOU 2226 CG2 VAL A1084 26600 30308 15992 2026 8364 -3685 C
ATOM 2227 N LYS A1085 34.715 -26.265 -53.407 1.00191.37 N
ANISOU 2227 N LYS A1085 26878 30797 15036 1342 8374 -2593 N
ATOM 2228 CA LYS A1085 34.270 -24.934 -53.838 1.00191.04 C
ANISOU 2228 CA LYS A1085 26852 30846 14887 1097 8333 -2137 C
ATOM 2229 C LYS A1085 32.870 -24.963 -54.464 1.00192.40 C
ANISOU 2229 C LYS A1085 27252 30817 15034 982 7824 -2012 C
ATOM 2230 O LYS A1085 32.101 -24.019 -54.267 1.00190.29 O
ANISOU 2230 O LYS A1085 26988 30507 14807 810 7661 -1679 O
ATOM 2231 CB LYS A1085 35.271 -24.313 -54.823 1.00195.68 C
ANISOU 2231 CB LYS A1085 27382 31599 15368 1020 8561 -1961 C
ATOM 2232 CG LYS A1085 36.493 -23.707 -54.145 1.00207.35 C
ANISOU 2232 CG LYS A1085 28464 32946 17374 971 8595 -1782 C
ATOM 2233 CD LYS A1085 37.369 -22.952 -55.131 1.00219.34 C
ANISOU 2233 CD LYS A1085 29880 34409 19048 828 8514 -1508 C
ATOM 2234 CE LYS A1085 38.518 -22.259 -54.442 1.00222.83 C
ANISOU 2234 CE LYS A1085 29935 34622 20106 744 8382 -1298 C
ATOM 2235 NZ LYS A1085 39.352 -21.491 -55.402 1.00227.16 N
ANISOU 2235 NZ LYS A1085 30342 34818 21152 571 7904 -993 N
ATOM 2236 N GLU A1086 32.545 -26.036 -55.214 1.00190.99 N
ANISOU 2236 N GLU A1086 27311 30630 14628 1094 7717 -2315 N
ATOM 2237 CA GLU A1086 31.247 -26.219 -55.874 1.00188.56 C
ANISOU 2237 CA GLU A1086 27195 30127 14323 999 7226 -2229 C
ATOM 2238 C GLU A1086 30.133 -26.491 -54.856 1.00188.16 C
ANISOU 2238 C GLU A1086 27115 29808 14568 977 6844 -2221 C
ATOM 2239 O GLU A1086 29.005 -26.035 -55.054 1.00187.39 O
ANISOU 2239 O GLU A1086 27155 29713 14332 860 6642 -2026 O
ATOM 2240 CB GLU A1086 31.314 -27.358 -56.903 1.00195.04 C
ANISOU 2240 CB GLU A1086 28327 31136 14641 1147 7374 -2628 C
ATOM 2241 CG GLU A1086 32.033 -26.983 -58.187 1.00209.11 C
ANISOU 2241 CG GLU A1086 30184 33136 16130 1113 7601 -2545 C
ATOM 2242 CD GLU A1086 32.155 -28.103 -59.201 1.00232.93 C
ANISOU 2242 CD GLU A1086 33356 36078 19068 1216 7462 -2848 C
ATOM 2243 OE1 GLU A1086 33.295 -28.559 -59.446 1.00236.20 O
ANISOU 2243 OE1 GLU A1086 33849 36818 19080 1389 8020 -3166 O
ATOM 2244 OE2 GLU A1086 31.113 -28.526 -59.752 1.00227.32 O
ANISOU 2244 OE2 GLU A1086 32939 35422 18010 1206 7294 -2960 O
ATOM 2245 N ALA A1087 30.452 -27.228 -53.772 1.00186.46 N
ANISOU 2245 N ALA A1087 26875 29641 14329 1142 7067 -2540 N
ATOM 2246 CA ALA A1087 29.511 -27.571 -52.705 1.00187.97 C
ANISOU 2246 CA ALA A1087 27198 29879 14341 1192 7079 -2692 C
ATOM 2247 C ALA A1087 29.263 -26.386 -51.762 1.00188.49 C
ANISOU 2247 C ALA A1087 26656 30429 14534 849 6989 -2506 C
ATOM 2248 O ALA A1087 28.134 -26.216 -51.297 1.00188.33 O
ANISOU 2248 O ALA A1087 26292 30988 14277 323 6767 -2704 O
ATOM 2249 CB ALA A1087 30.026 -28.765 -51.916 1.00187.26 C
ANISOU 2249 CB ALA A1087 27018 29551 14582 1373 6986 -3060 C
ATOM 2250 N GLN A1088 30.311 -25.576 -51.481 1.00185.79 N
ANISOU 2250 N GLN A1088 25800 30611 14181 703 7248 -2482 N
ATOM 2251 CA GLN A1088 30.243 -24.400 -50.605 1.00185.26 C
ANISOU 2251 CA GLN A1088 25034 31273 14082 146 7223 -2438 C
ATOM 2252 C GLN A1088 29.398 -23.278 -51.218 1.00186.09 C
ANISOU 2252 C GLN A1088 25368 31150 14190 -373 7059 -2058 C
ATOM 2253 O GLN A1088 28.722 -22.560 -50.479 1.00183.61 O
ANISOU 2253 O GLN A1088 24872 30888 14005 -834 6896 -1969 O
ATOM 2254 CB GLN A1088 31.649 -23.876 -50.276 1.00184.30 C
ANISOU 2254 CB GLN A1088 24884 30747 14396 423 7478 -2151 C
ATOM 2255 CG GLN A1088 32.297 -24.584 -49.088 1.00194.79 C
ANISOU 2255 CG GLN A1088 26473 31095 16444 942 7515 -2118 C
ATOM 2256 CD GLN A1088 33.671 -24.059 -48.733 1.00214.37 C
ANISOU 2256 CD GLN A1088 28812 33370 19270 1009 7799 -1960 C
ATOM 2257 OE1 GLN A1088 33.958 -22.857 -48.804 1.00210.56 O
ANISOU 2257 OE1 GLN A1088 28112 33105 18785 765 7862 -1664 O
ATOM 2258 NE2 GLN A1088 34.540 -24.952 -48.283 1.00208.23 N
ANISOU 2258 NE2 GLN A1088 27810 32809 18499 1246 7965 -2346 N
ATOM 2259 N ALA A1089 29.439 -23.129 -52.560 1.00183.91 N
ANISOU 2259 N ALA A1089 25393 30869 13617 -434 7131 -1955 N
ATOM 2260 CA ALA A1089 28.675 -22.123 -53.304 1.00183.45 C
ANISOU 2260 CA ALA A1089 25521 30787 13394 -990 6984 -1694 C
ATOM 2261 C ALA A1089 27.175 -22.439 -53.278 1.00185.25 C
ANISOU 2261 C ALA A1089 26033 30794 13561 -1329 6704 -1814 C
ATOM 2262 O ALA A1089 26.359 -21.517 -53.231 1.00182.62 O
ANISOU 2262 O ALA A1089 25855 30151 13383 -1673 6469 -1524 O
ATOM 2263 CB ALA A1089 29.171 -22.045 -54.740 1.00182.92 C
ANISOU 2263 CB ALA A1089 25949 30113 13439 -332 6992 -1271 C
ATOM 2264 N ALA A1090 26.822 -23.741 -53.299 1.00180.65 N
ANISOU 2264 N ALA A1090 25671 29995 12973 -910 6633 -2065 N
ATOM 2265 CA ALA A1090 25.442 -24.229 -53.248 1.00177.32 C
ANISOU 2265 CA ALA A1090 25660 28987 12725 -871 6285 -2019 C
ATOM 2266 C ALA A1090 24.893 -24.173 -51.820 1.00175.37 C
ANISOU 2266 C ALA A1090 25277 28369 12985 -781 6058 -1925 C
ATOM 2267 O ALA A1090 23.688 -23.998 -51.637 1.00171.99 O
ANISOU 2267 O ALA A1090 25069 27528 12751 -932 5752 -1767 O
ATOM 2268 CB ALA A1090 25.371 -25.650 -53.781 1.00180.32 C
ANISOU 2268 CB ALA A1090 26355 29287 12872 -492 6301 -2329 C
ATOM 2269 N ALA A1091 25.779 -24.326 -50.814 1.00170.86 N
ANISOU 2269 N ALA A1091 24330 27980 12608 -532 6207 -2033 N
ATOM 2270 CA ALA A1091 25.431 -24.279 -49.392 1.00166.40 C
ANISOU 2270 CA ALA A1091 23601 27117 12507 -432 6032 -1961 C
ATOM 2271 C ALA A1091 25.220 -22.836 -48.919 1.00166.70 C
ANISOU 2271 C ALA A1091 23426 27136 12775 -815 5950 -1642 C
ATOM 2272 O ALA A1091 24.427 -22.606 -48.006 1.00162.35 O
ANISOU 2272 O ALA A1091 22861 26242 12585 -840 5714 -1515 O
ATOM 2273 CB ALA A1091 26.520 -24.944 -48.565 1.00167.88 C
ANISOU 2273 CB ALA A1091 23490 27523 12775 -9 6217 -2203 C
ATOM 2274 N GLU A1092 25.920 -21.869 -49.549 1.00164.87 N
ANISOU 2274 N GLU A1092 23059 27277 12309 -1124 6137 -1517 N
ATOM 2275 CA GLU A1092 25.828 -20.443 -49.223 1.00162.92 C
ANISOU 2275 CA GLU A1092 22695 27009 12200 -1516 6059 -1213 C
ATOM 2276 C GLU A1092 24.532 -19.813 -49.773 1.00165.12 C
ANISOU 2276 C GLU A1092 23359 26914 12466 -1796 5751 -981 C
ATOM 2277 O GLU A1092 24.207 -18.680 -49.410 1.00163.10 O
ANISOU 2277 O GLU A1092 23099 26514 12358 -2054 5594 -731 O
ATOM 2278 CB GLU A1092 27.058 -19.689 -49.754 1.00167.79 C
ANISOU 2278 CB GLU A1092 23076 28170 12507 -1792 6366 -1170 C
ATOM 2279 CG GLU A1092 27.610 -18.655 -48.784 1.00177.38 C
ANISOU 2279 CG GLU A1092 23968 29486 13944 -2000 6393 -993 C
ATOM 2280 CD GLU A1092 28.350 -19.214 -47.583 1.00199.19 C
ANISOU 2280 CD GLU A1092 26304 32417 16962 -1651 6523 -1174 C
ATOM 2281 OE1 GLU A1092 29.415 -19.843 -47.778 1.00205.06 O
ANISOU 2281 OE1 GLU A1092 26801 33622 17492 -1419 6804 -1425 O
ATOM 2282 OE2 GLU A1092 27.874 -19.005 -46.444 1.00193.76 O
ANISOU 2282 OE2 GLU A1092 25525 31423 16673 -1597 6340 -1071 O
ATOM 2283 N GLN A1093 23.785 -20.559 -50.621 1.00162.27 N
ANISOU 2283 N GLN A1093 23344 26392 11920 -1720 5644 -1075 N
ATOM 2284 CA GLN A1093 22.511 -20.138 -51.221 1.00161.21 C
ANISOU 2284 CA GLN A1093 23576 25938 11739 -1928 5337 -901 C
ATOM 2285 C GLN A1093 21.389 -20.051 -50.168 1.00159.81 C
ANISOU 2285 C GLN A1093 23382 25362 11977 -1844 5006 -807 C
ATOM 2286 O GLN A1093 20.341 -19.462 -50.441 1.00158.62 O
ANISOU 2286 O GLN A1093 23447 24984 11839 -2003 4722 -640 O
ATOM 2287 CB GLN A1093 22.103 -21.093 -52.358 1.00164.97 C
ANISOU 2287 CB GLN A1093 24394 26387 11901 -1846 5328 -1064 C
ATOM 2288 CG GLN A1093 22.904 -20.915 -53.646 1.00186.88 C
ANISOU 2288 CG GLN A1093 27274 29532 14200 -2020 5588 -1098 C
ATOM 2289 CD GLN A1093 22.388 -19.774 -54.485 1.00212.81 C
ANISOU 2289 CD GLN A1093 30841 32739 17278 -2420 5427 -836 C
ATOM 2290 OE1 GLN A1093 21.426 -19.915 -55.246 1.00211.59 O
ANISOU 2290 OE1 GLN A1093 31042 32369 16985 -2473 5212 -809 O
ATOM 2291 NE2 GLN A1093 23.020 -18.616 -54.367 1.00207.16 N
ANISOU 2291 NE2 GLN A1093 30006 32190 16514 -2720 5509 -636 N
ATOM 2292 N LEU A1094 21.622 -20.623 -48.969 1.00153.14 N
ANISOU 2292 N LEU A1094 22275 24461 11449 -1587 5041 -923 N
ATOM 2293 CA LEU A1094 20.694 -20.610 -47.834 1.00148.95 C
ANISOU 2293 CA LEU A1094 21667 23618 11310 -1504 4775 -860 C
ATOM 2294 C LEU A1094 20.701 -19.243 -47.122 1.00151.29 C
ANISOU 2294 C LEU A1094 21780 23881 11821 -1676 4684 -621 C
ATOM 2295 O LEU A1094 19.790 -18.957 -46.341 1.00148.26 O
ANISOU 2295 O LEU A1094 21363 23257 11711 -1653 4426 -528 O
ATOM 2296 CB LEU A1094 21.058 -21.728 -46.834 1.00147.36 C
ANISOU 2296 CB LEU A1094 21293 23375 11324 -1183 4862 -1074 C
ATOM 2297 CG LEU A1094 20.798 -23.171 -47.279 1.00152.87 C
ANISOU 2297 CG LEU A1094 22261 23960 11865 -984 4844 -1309 C
ATOM 2298 CD1 LEU A1094 21.757 -24.128 -46.606 1.00153.27 C
ANISOU 2298 CD1 LEU A1094 22177 24093 11964 -642 5043 -1546 C
ATOM 2299 CD2 LEU A1094 19.371 -23.591 -46.989 1.00152.87 C
ANISOU 2299 CD2 LEU A1094 22438 23626 12018 -1034 4518 -1278 C
ATOM 2300 N LYS A1095 21.726 -18.407 -47.396 1.00149.79 N
ANISOU 2300 N LYS A1095 21482 23951 11478 -1861 4894 -528 N
ATOM 2301 CA LYS A1095 21.906 -17.074 -46.812 1.00148.78 C
ANISOU 2301 CA LYS A1095 21248 23797 11484 -2067 4826 -299 C
ATOM 2302 C LYS A1095 21.364 -15.947 -47.723 1.00154.26 C
ANISOU 2302 C LYS A1095 22287 24386 11938 -2376 4635 -70 C
ATOM 2303 O LYS A1095 21.460 -14.774 -47.352 1.00153.67 O
ANISOU 2303 O LYS A1095 22234 24241 11915 -2568 4539 134 O
ATOM 2304 CB LYS A1095 23.392 -16.826 -46.497 1.00152.79 C
ANISOU 2304 CB LYS A1095 21448 24667 11938 -2141 5153 -328 C
ATOM 2305 CG LYS A1095 23.877 -17.512 -45.222 1.00165.92 C
ANISOU 2305 CG LYS A1095 22747 26363 13931 -1843 5251 -480 C
ATOM 2306 CD LYS A1095 25.357 -17.250 -44.950 1.00178.50 C
ANISOU 2306 CD LYS A1095 24000 28383 15441 -1907 5570 -526 C
ATOM 2307 CE LYS A1095 25.604 -16.016 -44.113 1.00188.70 C
ANISOU 2307 CE LYS A1095 25155 29653 16888 -2163 5515 -302 C
ATOM 2308 NZ LYS A1095 27.055 -15.793 -43.880 1.00199.68 N
ANISOU 2308 NZ LYS A1095 26187 31518 18164 -2267 5828 -356 N
ATOM 2309 N THR A1096 20.784 -16.302 -48.895 1.00152.51 N
ANISOU 2309 N THR A1096 22377 24127 11444 -2417 4555 -103 N
ATOM 2310 CA THR A1096 20.214 -15.348 -49.863 1.00154.21 C
ANISOU 2310 CA THR A1096 22973 24224 11394 -2676 4346 98 C
ATOM 2311 C THR A1096 18.989 -14.634 -49.274 1.00154.97 C
ANISOU 2311 C THR A1096 23163 23982 11735 -2607 3942 247 C
ATOM 2312 O THR A1096 18.319 -15.194 -48.406 1.00151.89 O
ANISOU 2312 O THR A1096 22595 23463 11654 -2357 3810 150 O
ATOM 2313 CB THR A1096 19.853 -16.044 -51.187 1.00166.47 C
ANISOU 2313 CB THR A1096 24816 25821 12615 -2696 4347 1 C
ATOM 2314 OG1 THR A1096 19.003 -17.162 -50.928 1.00164.76 O
ANISOU 2314 OG1 THR A1096 24566 25462 12573 -2422 4222 -172 O
ATOM 2315 CG2 THR A1096 21.080 -16.477 -51.981 1.00168.94 C
ANISOU 2315 CG2 THR A1096 25101 26508 12581 -2807 4732 -117 C
ATOM 2316 N THR A1097 18.704 -13.403 -49.760 1.00152.22 N
ANISOU 2316 N THR A1097 23118 23502 11216 -2826 3739 475 N
ATOM 2317 CA THR A1097 17.610 -12.512 -49.332 1.00150.41 C
ANISOU 2317 CA THR A1097 23036 22972 11140 -2742 3332 627 C
ATOM 2318 C THR A1097 16.252 -13.243 -49.216 1.00150.70 C
ANISOU 2318 C THR A1097 23029 22889 11340 -2463 3063 510 C
ATOM 2319 O THR A1097 15.523 -13.006 -48.250 1.00147.97 O
ANISOU 2319 O THR A1097 22528 22408 11287 -2269 2839 524 O
ATOM 2320 CB THR A1097 17.492 -11.305 -50.288 1.00163.37 C
ANISOU 2320 CB THR A1097 25159 24485 12428 -3005 3138 851 C
ATOM 2321 OG1 THR A1097 18.795 -10.869 -50.683 1.00166.23 O
ANISOU 2321 OG1 THR A1097 25605 25058 12497 -3359 3447 920 O
ATOM 2322 CG2 THR A1097 16.728 -10.136 -49.670 1.00161.81 C
ANISOU 2322 CG2 THR A1097 25110 23998 12371 -2937 2787 1029 C
ATOM 2323 N ARG A1098 15.927 -14.125 -50.184 1.00147.07 N
ANISOU 2323 N ARG A1098 22701 22506 10673 -2465 3089 391 N
ATOM 2324 CA ARG A1098 14.678 -14.890 -50.200 1.00145.08 C
ANISOU 2324 CA ARG A1098 22424 22190 10511 -2280 2849 275 C
ATOM 2325 C ARG A1098 14.695 -16.009 -49.144 1.00144.17 C
ANISOU 2325 C ARG A1098 21943 22120 10713 -2094 2984 84 C
ATOM 2326 O ARG A1098 13.705 -16.174 -48.431 1.00141.87 O
ANISOU 2326 O ARG A1098 21492 21757 10653 -1945 2755 49 O
ATOM 2327 CB ARG A1098 14.416 -15.470 -51.602 1.00147.77 C
ANISOU 2327 CB ARG A1098 23068 22588 10490 -2385 2839 216 C
ATOM 2328 CG ARG A1098 12.993 -15.982 -51.806 1.00156.61 C
ANISOU 2328 CG ARG A1098 24225 23652 11628 -2266 2521 138 C
ATOM 2329 CD ARG A1098 12.992 -17.423 -52.273 1.00164.23 C
ANISOU 2329 CD ARG A1098 25240 24704 12456 -2281 2673 -62 C
ATOM 2330 NE ARG A1098 11.641 -17.986 -52.308 1.00169.10 N
ANISOU 2330 NE ARG A1098 25835 25297 13117 -2212 2384 -149 N
ATOM 2331 CZ ARG A1098 11.359 -19.244 -52.631 1.00180.47 C
ANISOU 2331 CZ ARG A1098 27338 26768 14465 -2232 2436 -326 C
ATOM 2332 NH1 ARG A1098 12.332 -20.089 -52.952 1.00168.21 N
ANISOU 2332 NH1 ARG A1098 25885 25253 12774 -2255 2759 -449 N
ATOM 2333 NH2 ARG A1098 10.103 -19.668 -52.634 1.00166.68 N
ANISOU 2333 NH2 ARG A1098 25562 25032 12737 -2231 2156 -389 N
ATOM 2334 N ASN A1099 15.810 -16.769 -49.050 1.00139.25 N
ANISOU 2334 N ASN A1099 21200 21635 10075 -2098 3343 -45 N
ATOM 2335 CA ASN A1099 15.972 -17.879 -48.104 1.00136.18 C
ANISOU 2335 CA ASN A1099 20542 21263 9938 -1915 3479 -232 C
ATOM 2336 C ASN A1099 16.114 -17.396 -46.651 1.00135.36 C
ANISOU 2336 C ASN A1099 20117 21106 10207 -1811 3474 -180 C
ATOM 2337 O ASN A1099 15.719 -18.122 -45.735 1.00132.79 O
ANISOU 2337 O ASN A1099 19596 20726 10131 -1661 3442 -294 O
ATOM 2338 CB ASN A1099 17.159 -18.753 -48.490 1.00138.59 C
ANISOU 2338 CB ASN A1099 20848 21738 10072 -1891 3838 -397 C
ATOM 2339 CG ASN A1099 16.852 -19.693 -49.628 1.00164.56 C
ANISOU 2339 CG ASN A1099 24419 25036 13069 -1901 3830 -533 C
ATOM 2340 OD1 ASN A1099 16.978 -19.346 -50.806 1.00161.91 O
ANISOU 2340 OD1 ASN A1099 24340 24771 12406 -2058 3842 -475 O
ATOM 2341 ND2 ASN A1099 16.429 -20.905 -49.299 1.00155.74 N
ANISOU 2341 ND2 ASN A1099 23297 23832 12044 -1755 3798 -714 N
ATOM 2342 N ALA A1100 16.664 -16.178 -46.441 1.00130.50 N
ANISOU 2342 N ALA A1100 19481 20494 9607 -1915 3493 -4 N
ATOM 2343 CA ALA A1100 16.823 -15.568 -45.115 1.00127.04 C
ANISOU 2343 CA ALA A1100 18784 19993 9494 -1838 3469 66 C
ATOM 2344 C ALA A1100 15.461 -15.152 -44.550 1.00127.08 C
ANISOU 2344 C ALA A1100 18763 19830 9691 -1713 3102 122 C
ATOM 2345 O ALA A1100 15.271 -15.170 -43.333 1.00124.22 O
ANISOU 2345 O ALA A1100 18138 19421 9639 -1573 3062 92 O
ATOM 2346 CB ALA A1100 17.751 -14.366 -45.192 1.00129.12 C
ANISOU 2346 CB ALA A1100 19111 20299 9648 -2039 3570 243 C
ATOM 2347 N TYR A1101 14.518 -14.788 -45.445 1.00123.56 N
ANISOU 2347 N TYR A1101 18580 19326 9040 -1750 2833 191 N
ATOM 2348 CA TYR A1101 13.142 -14.409 -45.120 1.00121.91 C
ANISOU 2348 CA TYR A1101 18348 19036 8936 -1604 2459 218 C
ATOM 2349 C TYR A1101 12.363 -15.651 -44.659 1.00121.86 C
ANISOU 2349 C TYR A1101 18127 19104 9070 -1505 2418 33 C
ATOM 2350 O TYR A1101 11.538 -15.548 -43.748 1.00119.80 O
ANISOU 2350 O TYR A1101 17644 18848 9028 -1368 2227 7 O
ATOM 2351 CB TYR A1101 12.472 -13.731 -46.337 1.00126.08 C
ANISOU 2351 CB TYR A1101 19242 19513 9148 -1665 2193 330 C
ATOM 2352 CG TYR A1101 10.957 -13.772 -46.350 1.00128.27 C
ANISOU 2352 CG TYR A1101 19489 19820 9428 -1508 1828 277 C
ATOM 2353 CD1 TYR A1101 10.209 -12.970 -45.492 1.00129.52 C
ANISOU 2353 CD1 TYR A1101 19507 19942 9763 -1295 1540 318 C
ATOM 2354 CD2 TYR A1101 10.270 -14.591 -47.242 1.00130.49 C
ANISOU 2354 CD2 TYR A1101 19878 20197 9506 -1571 1763 179 C
ATOM 2355 CE1 TYR A1101 8.815 -13.007 -45.498 1.00131.02 C
ANISOU 2355 CE1 TYR A1101 19607 20247 9928 -1136 1207 248 C
ATOM 2356 CE2 TYR A1101 8.877 -14.632 -47.262 1.00132.09 C
ANISOU 2356 CE2 TYR A1101 20009 20493 9685 -1455 1425 123 C
ATOM 2357 CZ TYR A1101 8.153 -13.836 -46.388 1.00138.97 C
ANISOU 2357 CZ TYR A1101 20688 21382 10731 -1233 1151 153 C
ATOM 2358 OH TYR A1101 6.779 -13.871 -46.407 1.00141.13 O
ANISOU 2358 OH TYR A1101 20836 21831 10956 -1105 819 77 O
ATOM 2359 N ILE A1102 12.638 -16.816 -45.289 1.00117.41 N
ANISOU 2359 N ILE A1102 17653 18603 8353 -1588 2594 -100 N
ATOM 2360 CA ILE A1102 12.027 -18.113 -44.970 1.00115.58 C
ANISOU 2360 CA ILE A1102 17321 18408 8187 -1562 2574 -277 C
ATOM 2361 C ILE A1102 12.477 -18.532 -43.557 1.00114.55 C
ANISOU 2361 C ILE A1102 16887 18251 8385 -1458 2710 -349 C
ATOM 2362 O ILE A1102 11.642 -18.961 -42.758 1.00112.82 O
ANISOU 2362 O ILE A1102 16490 18049 8327 -1420 2557 -414 O
ATOM 2363 CB ILE A1102 12.367 -19.177 -46.060 1.00120.65 C
ANISOU 2363 CB ILE A1102 18216 19074 8550 -1661 2743 -400 C
ATOM 2364 CG1 ILE A1102 11.738 -18.789 -47.425 1.00123.81 C
ANISOU 2364 CG1 ILE A1102 18916 19503 8624 -1774 2554 -337 C
ATOM 2365 CG2 ILE A1102 11.926 -20.592 -45.640 1.00120.70 C
ANISOU 2365 CG2 ILE A1102 18182 19060 8617 -1653 2758 -588 C
ATOM 2366 CD1 ILE A1102 12.440 -19.359 -48.674 1.00133.44 C
ANISOU 2366 CD1 ILE A1102 20437 20751 9513 -1878 2761 -409 C
ATOM 2367 N GLN A1103 13.781 -18.354 -43.245 1.00108.77 N
ANISOU 2367 N GLN A1103 16087 17507 7735 -1428 2987 -331 N
ATOM 2368 CA GLN A1103 14.368 -18.654 -41.935 1.00105.33 C
ANISOU 2368 CA GLN A1103 15380 17044 7598 -1317 3128 -387 C
ATOM 2369 C GLN A1103 13.776 -17.744 -40.855 1.00105.03 C
ANISOU 2369 C GLN A1103 15123 16967 7818 -1244 2929 -281 C
ATOM 2370 O GLN A1103 13.548 -18.203 -39.738 1.00102.59 O
ANISOU 2370 O GLN A1103 14593 16638 7749 -1164 2918 -350 O
ATOM 2371 CB GLN A1103 15.896 -18.514 -41.973 1.00107.03 C
ANISOU 2371 CB GLN A1103 15555 17318 7793 -1306 3449 -386 C
ATOM 2372 N LYS A1104 13.508 -16.466 -41.203 1.00100.80 N
ANISOU 2372 N LYS A1104 14684 16409 7206 -1262 2759 -120 N
ATOM 2373 CA LYS A1104 12.903 -15.474 -40.311 1.00 98.65 C
ANISOU 2373 CA LYS A1104 14270 16089 7125 -1147 2533 -25 C
ATOM 2374 C LYS A1104 11.416 -15.764 -40.089 1.00100.52 C
ANISOU 2374 C LYS A1104 14390 16407 7395 -1063 2244 -100 C
ATOM 2375 O LYS A1104 10.890 -15.443 -39.021 1.00 98.64 O
ANISOU 2375 O LYS A1104 13920 16191 7369 -932 2109 -102 O
ATOM 2376 CB LYS A1104 13.088 -14.054 -40.862 1.00102.79 C
ANISOU 2376 CB LYS A1104 15033 16528 7495 -1182 2411 162 C
ATOM 2377 CG LYS A1104 14.383 -13.398 -40.412 1.00116.45 C
ANISOU 2377 CG LYS A1104 16747 18198 9298 -1259 2627 263 C
ATOM 2378 CD LYS A1104 14.387 -11.905 -40.714 1.00127.95 C
ANISOU 2378 CD LYS A1104 18454 19513 10646 -1289 2422 458 C
ATOM 2379 CE LYS A1104 15.466 -11.162 -39.962 1.00138.18 C
ANISOU 2379 CE LYS A1104 19679 20742 12079 -1359 2565 556 C
ATOM 2380 NZ LYS A1104 15.140 -11.009 -38.517 1.00144.42 N
ANISOU 2380 NZ LYS A1104 20170 21490 13212 -1151 2488 506 N
ATOM 2381 N TYR A1105 10.742 -16.367 -41.093 1.00 97.31 N
ANISOU 2381 N TYR A1105 14133 16079 6760 -1151 2152 -168 N
ATOM 2382 CA TYR A1105 9.325 -16.727 -41.015 1.00 96.90 C
ANISOU 2382 CA TYR A1105 13956 16179 6682 -1129 1885 -253 C
ATOM 2383 C TYR A1105 9.134 -17.965 -40.129 1.00 97.34 C
ANISOU 2383 C TYR A1105 13799 16293 6895 -1196 1986 -402 C
ATOM 2384 O TYR A1105 8.325 -17.919 -39.201 1.00 96.10 O
ANISOU 2384 O TYR A1105 13369 16259 6883 -1140 1835 -445 O
ATOM 2385 CB TYR A1105 8.726 -16.953 -42.423 1.00100.75 C
ANISOU 2385 CB TYR A1105 14704 16734 6844 -1236 1746 -266 C
ATOM 2386 CG TYR A1105 7.373 -17.637 -42.425 1.00103.37 C
ANISOU 2386 CG TYR A1105 14897 17275 7106 -1294 1522 -386 C
ATOM 2387 CD1 TYR A1105 6.221 -16.953 -42.046 1.00106.08 C
ANISOU 2387 CD1 TYR A1105 15026 17808 7471 -1150 1204 -382 C
ATOM 2388 CD2 TYR A1105 7.243 -18.968 -42.814 1.00104.67 C
ANISOU 2388 CD2 TYR A1105 15153 17467 7150 -1496 1616 -512 C
ATOM 2389 CE1 TYR A1105 4.976 -17.580 -42.037 1.00108.11 C
ANISOU 2389 CE1 TYR A1105 15101 18341 7635 -1238 1003 -501 C
ATOM 2390 CE2 TYR A1105 6.003 -19.606 -42.809 1.00106.74 C
ANISOU 2390 CE2 TYR A1105 15296 17945 7316 -1621 1406 -616 C
ATOM 2391 CZ TYR A1105 4.871 -18.907 -42.422 1.00114.75 C
ANISOU 2391 CZ TYR A1105 16037 19209 8354 -1509 1107 -610 C
ATOM 2392 OH TYR A1105 3.646 -19.529 -42.421 1.00117.19 O
ANISOU 2392 OH TYR A1105 16177 19810 8538 -1666 905 -721 O
ATOM 2393 N LEU A1106 9.875 -19.061 -40.416 1.00 92.27 N
ANISOU 2393 N LEU A1106 13303 15563 6191 -1309 2231 -488 N
ATOM 2394 CA LEU A1106 9.802 -20.337 -39.691 1.00 90.29 C
ANISOU 2394 CA LEU A1106 12977 15298 6032 -1389 2322 -631 C
ATOM 2395 C LEU A1106 10.194 -20.200 -38.211 1.00 89.88 C
ANISOU 2395 C LEU A1106 12654 15200 6296 -1282 2412 -628 C
ATOM 2396 O LEU A1106 9.639 -20.918 -37.375 1.00 88.56 O
ANISOU 2396 O LEU A1106 12347 15076 6223 -1352 2359 -715 O
ATOM 2397 CB LEU A1106 10.672 -21.411 -40.367 1.00 91.17 C
ANISOU 2397 CB LEU A1106 13375 15285 5979 -1455 2551 -727 C
ATOM 2398 CG LEU A1106 10.233 -21.890 -41.756 1.00 98.30 C
ANISOU 2398 CG LEU A1106 14583 16218 6550 -1591 2474 -770 C
ATOM 2399 CD1 LEU A1106 11.335 -22.663 -42.427 1.00 99.49 C
ANISOU 2399 CD1 LEU A1106 15012 16246 6542 -1578 2728 -867 C
ATOM 2400 CD2 LEU A1106 8.972 -22.742 -41.692 1.00101.54 C
ANISOU 2400 CD2 LEU A1106 14990 16727 6864 -1777 2248 -859 C
ATOM 2401 N ARG A 224 11.133 -19.283 -37.891 1.00100.28 N
ANISOU 2401 N ARG A 224 13863 17325 6913 -2703 2205 -884 N
ATOM 2402 CA ARG A 224 11.563 -19.013 -36.516 1.00 97.09 C
ANISOU 2402 CA ARG A 224 13421 16638 6829 -2565 2196 -812 C
ATOM 2403 C ARG A 224 10.461 -18.274 -35.753 1.00 97.76 C
ANISOU 2403 C ARG A 224 13503 16586 7057 -2544 1995 -621 C
ATOM 2404 O ARG A 224 10.190 -18.612 -34.602 1.00 95.35 O
ANISOU 2404 O ARG A 224 13207 16035 6986 -2443 1960 -674 O
ATOM 2405 CB ARG A 224 12.872 -18.210 -36.487 1.00 97.35 C
ANISOU 2405 CB ARG A 224 13384 16693 6912 -2530 2287 -661 C
ATOM 2406 CG ARG A 224 14.121 -19.077 -36.423 1.00108.09 C
ANISOU 2406 CG ARG A 224 14734 18017 8318 -2470 2496 -868 C
ATOM 2407 CD ARG A 224 15.356 -18.239 -36.159 1.00117.97 C
ANISOU 2407 CD ARG A 224 15909 19247 9668 -2423 2565 -696 C
ATOM 2408 NE ARG A 224 16.499 -19.057 -35.751 1.00126.59 N
ANISOU 2408 NE ARG A 224 16981 20200 10916 -2329 2735 -873 N
ATOM 2409 CZ ARG A 224 17.694 -18.569 -35.428 1.00141.07 C
ANISOU 2409 CZ ARG A 224 18749 21975 12877 -2270 2816 -769 C
ATOM 2410 NH1 ARG A 224 17.918 -17.261 -35.465 1.00129.03 N
ANISOU 2410 NH1 ARG A 224 17167 20515 11341 -2294 2743 -489 N
ATOM 2411 NH2 ARG A 224 18.675 -19.386 -35.068 1.00127.59 N
ANISOU 2411 NH2 ARG A 224 17024 20135 11319 -2188 2965 -939 N
ATOM 2412 N GLY A 225 9.826 -17.303 -36.418 1.00 94.12 N
ANISOU 2412 N GLY A 225 13024 16288 6448 -2643 1868 -406 N
ATOM 2413 CA GLY A 225 8.734 -16.498 -35.878 1.00 92.19 C
ANISOU 2413 CA GLY A 225 12766 15946 6315 -2642 1672 -209 C
ATOM 2414 C GLY A 225 7.480 -17.290 -35.563 1.00 94.39 C
ANISOU 2414 C GLY A 225 13102 16134 6627 -2644 1583 -341 C
ATOM 2415 O GLY A 225 6.776 -16.971 -34.602 1.00 92.36 O
ANISOU 2415 O GLY A 225 12834 15699 6559 -2588 1459 -242 O
ATOM 2416 N VAL A 226 7.195 -18.333 -36.372 1.00 91.50 N
ANISOU 2416 N VAL A 226 12795 15891 6081 -2709 1645 -567 N
ATOM 2417 CA VAL A 226 6.047 -19.235 -36.204 1.00 90.57 C
ANISOU 2417 CA VAL A 226 12732 15699 5982 -2718 1571 -720 C
ATOM 2418 C VAL A 226 6.297 -20.126 -34.964 1.00 91.47 C
ANISOU 2418 C VAL A 226 12856 15539 6358 -2579 1641 -893 C
ATOM 2419 O VAL A 226 5.369 -20.379 -34.193 1.00 89.83 O
ANISOU 2419 O VAL A 226 12661 15163 6307 -2532 1543 -897 O
ATOM 2420 CB VAL A 226 5.773 -20.061 -37.500 1.00 96.88 C
ANISOU 2420 CB VAL A 226 13586 16733 6491 -2841 1608 -902 C
ATOM 2421 CG1 VAL A 226 4.760 -21.182 -37.267 1.00 96.42 C
ANISOU 2421 CG1 VAL A 226 13582 16567 6485 -2830 1570 -1119 C
ATOM 2422 CG2 VAL A 226 5.303 -19.157 -38.637 1.00 98.35 C
ANISOU 2422 CG2 VAL A 226 13765 17170 6433 -2985 1492 -704 C
ATOM 2423 N GLY A 227 7.550 -20.543 -34.776 1.00 87.02 N
ANISOU 2423 N GLY A 227 12281 14938 5845 -2516 1808 -1019 N
ATOM 2424 CA GLY A 227 7.980 -21.375 -33.656 1.00 84.85 C
ANISOU 2424 CA GLY A 227 12008 14418 5814 -2390 1889 -1177 C
ATOM 2425 C GLY A 227 7.825 -20.736 -32.288 1.00 85.19 C
ANISOU 2425 C GLY A 227 12020 14221 6127 -2280 1807 -1023 C
ATOM 2426 O GLY A 227 7.507 -21.434 -31.323 1.00 83.44 O
ANISOU 2426 O GLY A 227 11813 13798 6094 -2198 1802 -1131 O
ATOM 2427 N LYS A 228 8.022 -19.398 -32.211 1.00 80.39 N
ANISOU 2427 N LYS A 228 11368 13637 5539 -2281 1737 -769 N
ATOM 2428 CA LYS A 228 7.951 -18.545 -31.013 1.00 77.74 C
ANISOU 2428 CA LYS A 228 10996 13101 5440 -2184 1651 -595 C
ATOM 2429 C LYS A 228 6.691 -18.773 -30.154 1.00 79.86 C
ANISOU 2429 C LYS A 228 11286 13206 5849 -2142 1530 -602 C
ATOM 2430 O LYS A 228 5.614 -19.037 -30.693 1.00 80.30 O
ANISOU 2430 O LYS A 228 11373 13344 5793 -2217 1455 -642 O
ATOM 2431 CB LYS A 228 8.013 -17.061 -31.423 1.00 80.19 C
ANISOU 2431 CB LYS A 228 11255 13517 5694 -2232 1562 -321 C
ATOM 2432 CG LYS A 228 9.312 -16.340 -31.054 1.00 90.58 C
ANISOU 2432 CG LYS A 228 12518 14784 7114 -2168 1635 -214 C
ATOM 2433 CD LYS A 228 10.470 -16.654 -31.998 1.00100.48 C
ANISOU 2433 CD LYS A 228 13763 16224 8192 -2224 1787 -285 C
ATOM 2434 CE LYS A 228 11.757 -15.993 -31.575 1.00109.10 C
ANISOU 2434 CE LYS A 228 14801 17234 9418 -2148 1873 -210 C
ATOM 2435 NZ LYS A 228 12.905 -16.452 -32.400 1.00118.87 N
ANISOU 2435 NZ LYS A 228 16029 18632 10504 -2189 2044 -316 N
ATOM 2436 N VAL A 229 6.842 -18.651 -28.816 1.00 73.94 N
ANISOU 2436 N VAL A 229 10519 12230 5344 -2024 1511 -559 N
ATOM 2437 CA VAL A 229 5.769 -18.818 -27.825 1.00 72.09 C
ANISOU 2437 CA VAL A 229 10297 11825 5268 -1966 1411 -553 C
ATOM 2438 C VAL A 229 4.811 -17.605 -27.907 1.00 75.67 C
ANISOU 2438 C VAL A 229 10723 12319 5707 -2009 1248 -328 C
ATOM 2439 O VAL A 229 5.269 -16.469 -27.762 1.00 74.82 O
ANISOU 2439 O VAL A 229 10571 12213 5645 -1993 1211 -146 O
ATOM 2440 CB VAL A 229 6.321 -19.023 -26.380 1.00 74.04 C
ANISOU 2440 CB VAL A 229 10533 11832 5766 -1828 1452 -580 C
ATOM 2441 CG1 VAL A 229 5.193 -19.154 -25.356 1.00 72.39 C
ANISOU 2441 CG1 VAL A 229 10334 11462 5709 -1770 1355 -570 C
ATOM 2442 CG2 VAL A 229 7.243 -20.235 -26.303 1.00 74.09 C
ANISOU 2442 CG2 VAL A 229 10555 11791 5805 -1790 1607 -791 C
ATOM 2443 N PRO A 230 3.485 -17.822 -28.116 1.00 72.43 N
ANISOU 2443 N PRO A 230 10334 11934 5254 -2061 1145 -334 N
ATOM 2444 CA PRO A 230 2.558 -16.676 -28.203 1.00 72.15 C
ANISOU 2444 CA PRO A 230 10263 11926 5223 -2102 988 -117 C
ATOM 2445 C PRO A 230 2.228 -16.044 -26.842 1.00 73.87 C
ANISOU 2445 C PRO A 230 10451 11932 5686 -1990 919 -13 C
ATOM 2446 O PRO A 230 2.632 -16.568 -25.800 1.00 72.10 O
ANISOU 2446 O PRO A 230 10240 11539 5614 -1886 983 -117 O
ATOM 2447 CB PRO A 230 1.308 -17.285 -28.846 1.00 74.84 C
ANISOU 2447 CB PRO A 230 10636 12354 5444 -2193 914 -183 C
ATOM 2448 CG PRO A 230 1.336 -18.713 -28.445 1.00 78.92 C
ANISOU 2448 CG PRO A 230 11199 12782 6004 -2148 1007 -425 C
ATOM 2449 CD PRO A 230 2.780 -19.108 -28.316 1.00 74.30 C
ANISOU 2449 CD PRO A 230 10617 12166 5446 -2088 1162 -532 C
ATOM 2450 N ARG A 231 1.490 -14.911 -26.858 1.00 70.23 N
ANISOU 2450 N ARG A 231 9943 11479 5260 -2014 784 194 N
ATOM 2451 CA ARG A 231 1.062 -14.198 -25.648 1.00 68.33 C
ANISOU 2451 CA ARG A 231 9668 11053 5241 -1916 707 300 C
ATOM 2452 C ARG A 231 -0.105 -14.920 -24.964 1.00 70.64 C
ANISOU 2452 C ARG A 231 9985 11227 5627 -1878 667 211 C
ATOM 2453 O ARG A 231 -0.283 -14.766 -23.756 1.00 68.78 O
ANISOU 2453 O ARG A 231 9740 10816 5579 -1771 658 217 O
ATOM 2454 CB ARG A 231 0.667 -12.742 -25.964 1.00 69.19 C
ANISOU 2454 CB ARG A 231 9712 11211 5366 -1961 573 541 C
ATOM 2455 CG ARG A 231 1.359 -11.696 -25.085 1.00 79.15 C
ANISOU 2455 CG ARG A 231 10923 12341 6810 -1865 554 666 C
ATOM 2456 CD ARG A 231 0.857 -11.659 -23.647 1.00 88.96 C
ANISOU 2456 CD ARG A 231 12164 13366 8270 -1743 527 638 C
ATOM 2457 NE ARG A 231 -0.314 -10.797 -23.486 1.00 99.73 N
ANISOU 2457 NE ARG A 231 13475 14686 9733 -1748 384 793 N
ATOM 2458 CZ ARG A 231 -1.113 -10.803 -22.422 1.00113.57 C
ANISOU 2458 CZ ARG A 231 15223 16282 11645 -1665 342 776 C
ATOM 2459 NH1 ARG A 231 -2.150 -9.980 -22.358 1.00102.52 N
ANISOU 2459 NH1 ARG A 231 13767 14848 10339 -1674 216 918 N
ATOM 2460 NH2 ARG A 231 -0.887 -11.643 -21.419 1.00 97.96 N
ANISOU 2460 NH2 ARG A 231 13293 14186 9741 -1576 427 620 N
ATOM 2461 N LYS A 232 -0.883 -15.717 -25.735 1.00 67.55 N
ANISOU 2461 N LYS A 232 9625 10937 5103 -1966 646 126 N
ATOM 2462 CA LYS A 232 -2.033 -16.501 -25.264 1.00 66.55 C
ANISOU 2462 CA LYS A 232 9519 10721 5045 -1950 606 40 C
ATOM 2463 C LYS A 232 -1.645 -17.463 -24.137 1.00 68.25 C
ANISOU 2463 C LYS A 232 9762 10768 5402 -1836 707 -119 C
ATOM 2464 O LYS A 232 -2.485 -17.777 -23.291 1.00 67.20 O
ANISOU 2464 O LYS A 232 9626 10506 5402 -1780 670 -137 O
ATOM 2465 CB LYS A 232 -2.657 -17.287 -26.425 1.00 70.65 C
ANISOU 2465 CB LYS A 232 10073 11395 5377 -2071 586 -52 C
ATOM 2466 N LYS A 233 -0.375 -17.915 -24.124 1.00 63.78 N
ANISOU 2466 N LYS A 233 9217 10205 4813 -1805 832 -226 N
ATOM 2467 CA LYS A 233 0.174 -18.815 -23.109 1.00 62.08 C
ANISOU 2467 CA LYS A 233 9021 9836 4731 -1704 932 -368 C
ATOM 2468 C LYS A 233 0.395 -18.068 -21.787 1.00 64.15 C
ANISOU 2468 C LYS A 233 9256 9933 5186 -1587 913 -268 C
ATOM 2469 O LYS A 233 0.059 -18.598 -20.726 1.00 62.62 O
ANISOU 2469 O LYS A 233 9069 9591 5131 -1506 928 -329 O
ATOM 2470 CB LYS A 233 1.485 -19.462 -23.601 1.00 64.66 C
ANISOU 2470 CB LYS A 233 9369 10223 4975 -1715 1068 -502 C
ATOM 2471 CG LYS A 233 1.314 -20.424 -24.783 1.00 74.92 C
ANISOU 2471 CG LYS A 233 10701 11669 6094 -1817 1105 -652 C
ATOM 2472 CD LYS A 233 0.690 -21.760 -24.375 1.00 82.05 C
ANISOU 2472 CD LYS A 233 11629 12477 7069 -1796 1124 -824 C
ATOM 2473 CE LYS A 233 0.226 -22.565 -25.561 1.00 90.84 C
ANISOU 2473 CE LYS A 233 12772 13736 8008 -1906 1120 -951 C
ATOM 2474 NZ LYS A 233 -0.413 -23.838 -25.140 1.00 97.05 N
ANISOU 2474 NZ LYS A 233 13574 14416 8886 -1883 1129 -1112 N
ATOM 2475 N VAL A 234 0.935 -16.835 -21.858 1.00 60.54 N
ANISOU 2475 N VAL A 234 8764 9502 4735 -1582 876 -112 N
ATOM 2476 CA VAL A 234 1.204 -15.975 -20.700 1.00 58.95 C
ANISOU 2476 CA VAL A 234 8535 9156 4709 -1477 848 -12 C
ATOM 2477 C VAL A 234 -0.129 -15.333 -20.257 1.00 62.59 C
ANISOU 2477 C VAL A 234 8968 9559 5254 -1463 726 96 C
ATOM 2478 O VAL A 234 -0.568 -14.342 -20.849 1.00 62.64 O
ANISOU 2478 O VAL A 234 8937 9641 5222 -1521 630 241 O
ATOM 2479 CB VAL A 234 2.312 -14.919 -21.006 1.00 62.87 C
ANISOU 2479 CB VAL A 234 8998 9698 5191 -1479 853 109 C
ATOM 2480 CG1 VAL A 234 2.643 -14.082 -19.773 1.00 61.39 C
ANISOU 2480 CG1 VAL A 234 8783 9352 5190 -1368 819 197 C
ATOM 2481 CG2 VAL A 234 3.575 -15.576 -21.556 1.00 63.20 C
ANISOU 2481 CG2 VAL A 234 9061 9805 5146 -1497 980 3 C
ATOM 2482 N ASN A 235 -0.783 -15.926 -19.238 1.00 58.47 N
ANISOU 2482 N ASN A 235 8459 8905 4852 -1390 732 26 N
ATOM 2483 CA ASN A 235 -2.066 -15.439 -18.726 1.00 57.94 C
ANISOU 2483 CA ASN A 235 8363 8773 4878 -1367 632 111 C
ATOM 2484 C ASN A 235 -1.848 -14.490 -17.544 1.00 61.14 C
ANISOU 2484 C ASN A 235 8740 9047 5444 -1260 607 198 C
ATOM 2485 O ASN A 235 -1.623 -14.935 -16.414 1.00 59.91 O
ANISOU 2485 O ASN A 235 8603 8768 5393 -1165 662 126 O
ATOM 2486 CB ASN A 235 -2.990 -16.603 -18.339 1.00 57.76 C
ANISOU 2486 CB ASN A 235 8363 8693 4889 -1355 648 -2 C
ATOM 2487 CG ASN A 235 -4.457 -16.238 -18.281 1.00 77.28 C
ANISOU 2487 CG ASN A 235 10802 11152 7408 -1374 542 86 C
ATOM 2488 OD1 ASN A 235 -4.873 -15.279 -17.618 1.00 69.43 O
ANISOU 2488 OD1 ASN A 235 9771 10076 6533 -1313 485 189 O
ATOM 2489 ND2 ASN A 235 -5.282 -17.017 -18.959 1.00 69.84 N
ANISOU 2489 ND2 ASN A 235 9871 10287 6379 -1460 511 41 N
ATOM 2490 N VAL A 236 -1.922 -13.178 -17.819 1.00 58.11 N
ANISOU 2490 N VAL A 236 8308 8692 5079 -1278 519 353 N
ATOM 2491 CA VAL A 236 -1.737 -12.110 -16.835 1.00 57.19 C
ANISOU 2491 CA VAL A 236 8155 8460 5114 -1187 477 444 C
ATOM 2492 C VAL A 236 -2.979 -12.005 -15.909 1.00 60.57 C
ANISOU 2492 C VAL A 236 8564 8783 5667 -1126 423 457 C
ATOM 2493 O VAL A 236 -2.815 -11.740 -14.718 1.00 59.23 O
ANISOU 2493 O VAL A 236 8392 8489 5624 -1021 436 446 O
ATOM 2494 CB VAL A 236 -1.370 -10.754 -17.517 1.00 61.86 C
ANISOU 2494 CB VAL A 236 8693 9119 5694 -1234 397 607 C
ATOM 2495 CG1 VAL A 236 -2.469 -10.248 -18.455 1.00 62.80 C
ANISOU 2495 CG1 VAL A 236 8769 9337 5756 -1334 290 720 C
ATOM 2496 CG2 VAL A 236 -0.982 -9.688 -16.499 1.00 60.89 C
ANISOU 2496 CG2 VAL A 236 8532 8867 5736 -1134 358 683 C
ATOM 2497 N LYS A 237 -4.196 -12.251 -16.450 1.00 57.76 N
ANISOU 2497 N LYS A 237 8195 8479 5271 -1192 369 474 N
ATOM 2498 CA LYS A 237 -5.471 -12.168 -15.725 1.00 57.21 C
ANISOU 2498 CA LYS A 237 8098 8326 5312 -1149 318 495 C
ATOM 2499 C LYS A 237 -5.545 -13.140 -14.541 1.00 59.29 C
ANISOU 2499 C LYS A 237 8398 8480 5648 -1056 401 372 C
ATOM 2500 O LYS A 237 -5.956 -12.725 -13.457 1.00 58.26 O
ANISOU 2500 O LYS A 237 8247 8244 5647 -965 389 393 O
ATOM 2501 CB LYS A 237 -6.659 -12.411 -16.667 1.00 61.16 C
ANISOU 2501 CB LYS A 237 8581 8915 5742 -1253 249 531 C
ATOM 2502 CG LYS A 237 -6.961 -11.241 -17.594 1.00 81.04 C
ANISOU 2502 CG LYS A 237 11042 11519 8231 -1337 136 691 C
ATOM 2503 CD LYS A 237 -8.290 -11.435 -18.305 1.00 93.93 C
ANISOU 2503 CD LYS A 237 12648 13205 9834 -1423 52 738 C
ATOM 2504 CE LYS A 237 -8.574 -10.364 -19.329 1.00107.51 C
ANISOU 2504 CE LYS A 237 14309 15017 11524 -1518 -68 907 C
ATOM 2505 NZ LYS A 237 -7.772 -10.546 -20.570 1.00118.36 N
ANISOU 2505 NZ LYS A 237 15711 16556 12702 -1628 -58 912 N
ATOM 2506 N VAL A 238 -5.142 -14.414 -14.743 1.00 55.07 N
ANISOU 2506 N VAL A 238 7915 7974 5035 -1079 484 244 N
ATOM 2507 CA VAL A 238 -5.151 -15.456 -13.705 1.00 53.72 C
ANISOU 2507 CA VAL A 238 7774 7707 4929 -1003 562 131 C
ATOM 2508 C VAL A 238 -4.095 -15.112 -12.627 1.00 55.44 C
ANISOU 2508 C VAL A 238 8006 7832 5226 -901 615 116 C
ATOM 2509 O VAL A 238 -4.367 -15.303 -11.436 1.00 54.18 O
ANISOU 2509 O VAL A 238 7850 7572 5164 -813 640 87 O
ATOM 2510 CB VAL A 238 -4.966 -16.880 -14.311 1.00 58.15 C
ANISOU 2510 CB VAL A 238 8376 8320 5398 -1062 628 1 C
ATOM 2511 CG1 VAL A 238 -4.733 -17.940 -13.233 1.00 57.24 C
ANISOU 2511 CG1 VAL A 238 8286 8101 5362 -983 712 -108 C
ATOM 2512 CG2 VAL A 238 -6.167 -17.264 -15.174 1.00 58.79 C
ANISOU 2512 CG2 VAL A 238 8443 8472 5424 -1151 565 10 C
ATOM 2513 N PHE A 239 -2.931 -14.554 -13.039 1.00 51.11 N
ANISOU 2513 N PHE A 239 7463 7320 4638 -913 623 146 N
ATOM 2514 CA PHE A 239 -1.875 -14.150 -12.107 1.00 49.57 C
ANISOU 2514 CA PHE A 239 7277 7036 4520 -824 659 142 C
ATOM 2515 C PHE A 239 -2.323 -12.963 -11.232 1.00 52.40 C
ANISOU 2515 C PHE A 239 7599 7314 4998 -748 588 232 C
ATOM 2516 O PHE A 239 -1.939 -12.905 -10.062 1.00 51.25 O
ANISOU 2516 O PHE A 239 7467 7068 4937 -654 617 200 O
ATOM 2517 CB PHE A 239 -0.554 -13.825 -12.825 1.00 51.51 C
ANISOU 2517 CB PHE A 239 7529 7341 4701 -860 684 158 C
ATOM 2518 CG PHE A 239 0.588 -13.623 -11.856 1.00 52.16 C
ANISOU 2518 CG PHE A 239 7626 7324 4868 -770 726 139 C
ATOM 2519 CD1 PHE A 239 1.235 -14.711 -11.280 1.00 54.64 C
ANISOU 2519 CD1 PHE A 239 7980 7583 5199 -731 817 25 C
ATOM 2520 CD2 PHE A 239 0.977 -12.344 -11.471 1.00 54.00 C
ANISOU 2520 CD2 PHE A 239 7828 7510 5179 -723 666 236 C
ATOM 2521 CE1 PHE A 239 2.261 -14.523 -10.351 1.00 54.82 C
ANISOU 2521 CE1 PHE A 239 8014 7510 5303 -651 846 14 C
ATOM 2522 CE2 PHE A 239 1.996 -12.159 -10.534 1.00 56.06 C
ANISOU 2522 CE2 PHE A 239 8104 7675 5522 -640 694 216 C
ATOM 2523 CZ PHE A 239 2.634 -13.249 -9.987 1.00 53.64 C
ANISOU 2523 CZ PHE A 239 7840 7319 5221 -606 784 108 C
ATOM 2524 N ILE A 240 -3.133 -12.032 -11.785 1.00 48.86 N
ANISOU 2524 N ILE A 240 7100 6906 4558 -791 495 342 N
ATOM 2525 CA ILE A 240 -3.655 -10.888 -11.027 1.00 48.06 C
ANISOU 2525 CA ILE A 240 6953 6726 4583 -723 423 423 C
ATOM 2526 C ILE A 240 -4.586 -11.424 -9.912 1.00 51.00 C
ANISOU 2526 C ILE A 240 7331 7018 5028 -650 449 365 C
ATOM 2527 O ILE A 240 -4.490 -10.959 -8.775 1.00 50.09 O
ANISOU 2527 O ILE A 240 7211 6810 5010 -553 452 358 O
ATOM 2528 CB ILE A 240 -4.342 -9.836 -11.954 1.00 51.87 C
ANISOU 2528 CB ILE A 240 7370 7268 5070 -794 314 558 C
ATOM 2529 CG1 ILE A 240 -3.290 -9.109 -12.825 1.00 52.80 C
ANISOU 2529 CG1 ILE A 240 7473 7455 5135 -849 287 634 C
ATOM 2530 CG2 ILE A 240 -5.168 -8.808 -11.152 1.00 52.25 C
ANISOU 2530 CG2 ILE A 240 7360 7224 5268 -723 241 625 C
ATOM 2531 CD1 ILE A 240 -3.810 -8.523 -14.155 1.00 61.80 C
ANISOU 2531 CD1 ILE A 240 8563 8708 6211 -964 198 756 C
ATOM 2532 N ILE A 241 -5.417 -12.447 -10.227 1.00 47.30 N
ANISOU 2532 N ILE A 241 6874 6589 4509 -697 472 319 N
ATOM 2533 CA ILE A 241 -6.345 -13.075 -9.279 1.00 46.57 C
ANISOU 2533 CA ILE A 241 6781 6434 4478 -641 502 272 C
ATOM 2534 C ILE A 241 -5.563 -13.755 -8.130 1.00 49.53 C
ANISOU 2534 C ILE A 241 7203 6735 4880 -556 590 179 C
ATOM 2535 O ILE A 241 -5.876 -13.487 -6.967 1.00 48.64 O
ANISOU 2535 O ILE A 241 7083 6547 4852 -467 599 176 O
ATOM 2536 CB ILE A 241 -7.326 -14.064 -9.987 1.00 50.12 C
ANISOU 2536 CB ILE A 241 7228 6942 4871 -720 500 248 C
ATOM 2537 CG1 ILE A 241 -8.179 -13.337 -11.048 1.00 51.34 C
ANISOU 2537 CG1 ILE A 241 7332 7163 5012 -802 399 354 C
ATOM 2538 CG2 ILE A 241 -8.237 -14.781 -8.971 1.00 50.37 C
ANISOU 2538 CG2 ILE A 241 7257 6907 4974 -659 540 202 C
ATOM 2539 CD1 ILE A 241 -8.692 -14.220 -12.172 1.00 59.49 C
ANISOU 2539 CD1 ILE A 241 8372 8287 5944 -912 383 334 C
ATOM 2540 N ILE A 242 -4.543 -14.595 -8.447 1.00 45.90 N
ANISOU 2540 N ILE A 242 6789 6300 4351 -583 655 106 N
ATOM 2541 CA ILE A 242 -3.754 -15.314 -7.436 1.00 45.02 C
ANISOU 2541 CA ILE A 242 6717 6119 4270 -513 733 25 C
ATOM 2542 C ILE A 242 -3.005 -14.320 -6.513 1.00 48.78 C
ANISOU 2542 C ILE A 242 7196 6523 4816 -425 720 54 C
ATOM 2543 O ILE A 242 -2.973 -14.549 -5.302 1.00 47.94 O
ANISOU 2543 O ILE A 242 7105 6345 4765 -345 753 20 O
ATOM 2544 CB ILE A 242 -2.827 -16.419 -8.036 1.00 48.20 C
ANISOU 2544 CB ILE A 242 7157 6554 4602 -564 803 -61 C
ATOM 2545 CG1 ILE A 242 -2.475 -17.483 -6.980 1.00 48.11 C
ANISOU 2545 CG1 ILE A 242 7172 6467 4639 -504 878 -142 C
ATOM 2546 CG2 ILE A 242 -1.584 -15.878 -8.757 1.00 49.15 C
ANISOU 2546 CG2 ILE A 242 7287 6709 4677 -590 806 -45 C
ATOM 2547 CD1 ILE A 242 -2.308 -18.905 -7.496 1.00 56.37 C
ANISOU 2547 CD1 ILE A 242 8238 7536 5646 -559 942 -238 C
ATOM 2548 N ALA A 243 -2.478 -13.203 -7.068 1.00 45.62 N
ANISOU 2548 N ALA A 243 6777 6143 4415 -442 665 122 N
ATOM 2549 CA ALA A 243 -1.787 -12.162 -6.301 1.00 44.94 C
ANISOU 2549 CA ALA A 243 6686 5985 4403 -364 636 154 C
ATOM 2550 C ALA A 243 -2.764 -11.447 -5.355 1.00 48.24 C
ANISOU 2550 C ALA A 243 7074 6346 4910 -292 593 182 C
ATOM 2551 O ALA A 243 -2.398 -11.161 -4.216 1.00 47.31 O
ANISOU 2551 O ALA A 243 6972 6153 4851 -203 603 155 O
ATOM 2552 CB ALA A 243 -1.130 -11.162 -7.239 1.00 46.09 C
ANISOU 2552 CB ALA A 243 6805 6171 4535 -411 580 232 C
ATOM 2553 N VAL A 244 -4.013 -11.208 -5.814 1.00 45.11 N
ANISOU 2553 N VAL A 244 6633 5985 4523 -329 546 232 N
ATOM 2554 CA VAL A 244 -5.075 -10.575 -5.024 1.00 45.14 C
ANISOU 2554 CA VAL A 244 6597 5939 4616 -266 511 257 C
ATOM 2555 C VAL A 244 -5.430 -11.497 -3.837 1.00 48.38 C
ANISOU 2555 C VAL A 244 7038 6306 5037 -197 586 180 C
ATOM 2556 O VAL A 244 -5.554 -11.011 -2.714 1.00 47.87 O
ANISOU 2556 O VAL A 244 6971 6180 5038 -107 589 164 O
ATOM 2557 CB VAL A 244 -6.307 -10.210 -5.907 1.00 49.98 C
ANISOU 2557 CB VAL A 244 7150 6600 5239 -334 445 334 C
ATOM 2558 CG1 VAL A 244 -7.601 -10.122 -5.097 1.00 49.85 C
ANISOU 2558 CG1 VAL A 244 7098 6542 5300 -280 446 332 C
ATOM 2559 CG2 VAL A 244 -6.065 -8.906 -6.662 1.00 50.35 C
ANISOU 2559 CG2 VAL A 244 7147 6658 5326 -366 352 432 C
ATOM 2560 N PHE A 245 -5.528 -12.820 -4.079 1.00 44.36 N
ANISOU 2560 N PHE A 245 6557 5832 4465 -240 647 131 N
ATOM 2561 CA PHE A 245 -5.833 -13.812 -3.046 1.00 43.53 C
ANISOU 2561 CA PHE A 245 6475 5693 4371 -187 718 70 C
ATOM 2562 C PHE A 245 -4.756 -13.844 -1.946 1.00 47.17 C
ANISOU 2562 C PHE A 245 6979 6095 4846 -108 757 24 C
ATOM 2563 O PHE A 245 -5.110 -13.807 -0.770 1.00 46.73 O
ANISOU 2563 O PHE A 245 6924 5999 4830 -30 777 8 O
ATOM 2564 CB PHE A 245 -6.006 -15.209 -3.663 1.00 45.15 C
ANISOU 2564 CB PHE A 245 6696 5940 4518 -257 764 28 C
ATOM 2565 CG PHE A 245 -7.436 -15.580 -3.975 1.00 46.78 C
ANISOU 2565 CG PHE A 245 6862 6175 4736 -295 748 54 C
ATOM 2566 CD1 PHE A 245 -8.010 -15.241 -5.194 1.00 50.10 C
ANISOU 2566 CD1 PHE A 245 7252 6654 5131 -378 685 105 C
ATOM 2567 CD2 PHE A 245 -8.204 -16.284 -3.056 1.00 48.60 C
ANISOU 2567 CD2 PHE A 245 7083 6377 5005 -252 794 34 C
ATOM 2568 CE1 PHE A 245 -9.333 -15.586 -5.482 1.00 51.36 C
ANISOU 2568 CE1 PHE A 245 7371 6833 5309 -415 662 133 C
ATOM 2569 CE2 PHE A 245 -9.526 -16.633 -3.347 1.00 51.74 C
ANISOU 2569 CE2 PHE A 245 7437 6795 5425 -287 777 64 C
ATOM 2570 CZ PHE A 245 -10.081 -16.282 -4.558 1.00 50.27 C
ANISOU 2570 CZ PHE A 245 7222 6659 5220 -368 709 111 C
ATOM 2571 N PHE A 246 -3.459 -13.857 -2.329 1.00 43.55 N
ANISOU 2571 N PHE A 246 6554 5637 4357 -130 764 6 N
ATOM 2572 CA PHE A 246 -2.322 -13.909 -1.401 1.00 42.72 C
ANISOU 2572 CA PHE A 246 6490 5474 4269 -67 793 -32 C
ATOM 2573 C PHE A 246 -2.118 -12.623 -0.580 1.00 45.99 C
ANISOU 2573 C PHE A 246 6897 5835 4744 13 742 -10 C
ATOM 2574 O PHE A 246 -1.605 -12.707 0.539 1.00 45.40 O
ANISOU 2574 O PHE A 246 6852 5709 4687 84 765 -46 O
ATOM 2575 CB PHE A 246 -1.018 -14.238 -2.149 1.00 44.35 C
ANISOU 2575 CB PHE A 246 6722 5692 4439 -117 810 -48 C
ATOM 2576 CG PHE A 246 -0.828 -15.693 -2.512 1.00 45.82 C
ANISOU 2576 CG PHE A 246 6927 5901 4581 -170 879 -105 C
ATOM 2577 CD1 PHE A 246 -0.868 -16.683 -1.536 1.00 48.55 C
ANISOU 2577 CD1 PHE A 246 7293 6207 4947 -131 935 -152 C
ATOM 2578 CD2 PHE A 246 -0.549 -16.069 -3.819 1.00 48.36 C
ANISOU 2578 CD2 PHE A 246 7244 6285 4844 -258 887 -113 C
ATOM 2579 CE1 PHE A 246 -0.671 -18.025 -1.867 1.00 49.51 C
ANISOU 2579 CE1 PHE A 246 7423 6338 5051 -180 992 -205 C
ATOM 2580 CE2 PHE A 246 -0.346 -17.412 -4.149 1.00 51.37 C
ANISOU 2580 CE2 PHE A 246 7640 6682 5197 -304 951 -180 C
ATOM 2581 CZ PHE A 246 -0.417 -18.382 -3.171 1.00 49.18 C
ANISOU 2581 CZ PHE A 246 7376 6351 4959 -263 1000 -226 C
ATOM 2582 N ILE A 247 -2.497 -11.450 -1.123 1.00 42.20 N
ANISOU 2582 N ILE A 247 6374 5363 4298 2 669 49 N
ATOM 2583 CA ILE A 247 -2.313 -10.166 -0.438 1.00 41.93 C
ANISOU 2583 CA ILE A 247 6322 5270 4338 75 611 65 C
ATOM 2584 C ILE A 247 -3.589 -9.737 0.332 1.00 45.79 C
ANISOU 2584 C ILE A 247 6778 5741 4879 135 602 62 C
ATOM 2585 O ILE A 247 -3.476 -9.275 1.471 1.00 45.31 O
ANISOU 2585 O ILE A 247 6729 5629 4858 221 600 24 O
ATOM 2586 CB ILE A 247 -1.844 -9.057 -1.443 1.00 45.33 C
ANISOU 2586 CB ILE A 247 6716 5709 4799 30 531 138 C
ATOM 2587 CG1 ILE A 247 -0.481 -9.421 -2.090 1.00 45.39 C
ANISOU 2587 CG1 ILE A 247 6755 5733 4759 -18 550 138 C
ATOM 2588 CG2 ILE A 247 -1.777 -7.661 -0.782 1.00 46.29 C
ANISOU 2588 CG2 ILE A 247 6805 5760 5022 104 458 157 C
ATOM 2589 CD1 ILE A 247 -0.175 -8.730 -3.443 1.00 51.46 C
ANISOU 2589 CD1 ILE A 247 7483 6552 5518 -97 493 222 C
ATOM 2590 N CYS A 248 -4.781 -9.882 -0.279 1.00 42.47 N
ANISOU 2590 N CYS A 248 6314 5363 4459 89 596 97 N
ATOM 2591 CA CYS A 248 -6.039 -9.409 0.303 1.00 42.57 C
ANISOU 2591 CA CYS A 248 6281 5360 4534 139 586 103 C
ATOM 2592 C CYS A 248 -6.775 -10.434 1.176 1.00 45.69 C
ANISOU 2592 C CYS A 248 6693 5766 4903 175 668 58 C
ATOM 2593 O CYS A 248 -7.220 -10.066 2.264 1.00 45.57 O
ANISOU 2593 O CYS A 248 6670 5720 4926 259 686 27 O
ATOM 2594 CB CYS A 248 -6.967 -8.883 -0.789 1.00 43.60 C
ANISOU 2594 CB CYS A 248 6344 5522 4700 72 525 181 C
ATOM 2595 SG CYS A 248 -6.237 -7.592 -1.830 1.00 47.93 S
ANISOU 2595 SG CYS A 248 6854 6064 5293 26 419 260 S
ATOM 2596 N PHE A 249 -6.968 -11.675 0.693 1.00 41.43 N
ANISOU 2596 N PHE A 249 6170 5271 4303 113 715 54 N
ATOM 2597 CA PHE A 249 -7.796 -12.653 1.400 1.00 40.94 C
ANISOU 2597 CA PHE A 249 6107 5220 4229 136 784 31 C
ATOM 2598 C PHE A 249 -7.051 -13.663 2.280 1.00 44.64 C
ANISOU 2598 C PHE A 249 6632 5678 4651 167 854 -22 C
ATOM 2599 O PHE A 249 -7.591 -14.025 3.326 1.00 44.39 O
ANISOU 2599 O PHE A 249 6598 5644 4624 222 904 -39 O
ATOM 2600 CB PHE A 249 -8.685 -13.417 0.406 1.00 42.78 C
ANISOU 2600 CB PHE A 249 6308 5499 4447 51 784 64 C
ATOM 2601 CG PHE A 249 -9.434 -12.548 -0.581 1.00 44.58 C
ANISOU 2601 CG PHE A 249 6478 5744 4716 2 708 129 C
ATOM 2602 CD1 PHE A 249 -10.341 -11.588 -0.143 1.00 47.85 C
ANISOU 2602 CD1 PHE A 249 6836 6131 5214 54 679 160 C
ATOM 2603 CD2 PHE A 249 -9.245 -12.702 -1.949 1.00 46.51 C
ANISOU 2603 CD2 PHE A 249 6721 6034 4917 -97 666 161 C
ATOM 2604 CE1 PHE A 249 -11.028 -10.783 -1.056 1.00 49.08 C
ANISOU 2604 CE1 PHE A 249 6930 6295 5422 5 600 230 C
ATOM 2605 CE2 PHE A 249 -9.942 -11.905 -2.860 1.00 49.73 C
ANISOU 2605 CE2 PHE A 249 7072 6462 5359 -150 587 234 C
ATOM 2606 CZ PHE A 249 -10.828 -10.952 -2.409 1.00 48.13 C
ANISOU 2606 CZ PHE A 249 6810 6224 5254 -99 552 273 C
ATOM 2607 N VAL A 250 -5.859 -14.142 1.868 1.00 41.15 N
ANISOU 2607 N VAL A 250 6234 5234 4169 129 859 -43 N
ATOM 2608 CA VAL A 250 -5.098 -15.157 2.618 1.00 40.78 C
ANISOU 2608 CA VAL A 250 6234 5170 4092 148 919 -86 C
ATOM 2609 C VAL A 250 -4.764 -14.674 4.068 1.00 44.92 C
ANISOU 2609 C VAL A 250 6784 5658 4627 245 931 -110 C
ATOM 2610 O VAL A 250 -5.180 -15.378 4.991 1.00 44.37 O
ANISOU 2610 O VAL A 250 6719 5595 4544 278 984 -121 O
ATOM 2611 CB VAL A 250 -3.838 -15.676 1.860 1.00 44.29 C
ANISOU 2611 CB VAL A 250 6711 5612 4506 89 923 -105 C
ATOM 2612 CG1 VAL A 250 -2.935 -16.504 2.768 1.00 43.75 C
ANISOU 2612 CG1 VAL A 250 6684 5508 4431 119 972 -142 C
ATOM 2613 CG2 VAL A 250 -4.236 -16.496 0.641 1.00 44.27 C
ANISOU 2613 CG2 VAL A 250 6689 5654 4477 -4 932 -102 C
ATOM 2614 N PRO A 251 -4.093 -13.514 4.325 1.00 41.95 N
ANISOU 2614 N PRO A 251 6420 5246 4272 292 880 -118 N
ATOM 2615 CA PRO A 251 -3.802 -13.134 5.723 1.00 42.04 C
ANISOU 2615 CA PRO A 251 6461 5229 4283 382 890 -153 C
ATOM 2616 C PRO A 251 -5.030 -13.039 6.639 1.00 47.09 C
ANISOU 2616 C PRO A 251 7074 5891 4927 441 924 -160 C
ATOM 2617 O PRO A 251 -4.919 -13.386 7.814 1.00 46.97 O
ANISOU 2617 O PRO A 251 7088 5880 4880 496 965 -187 O
ATOM 2618 CB PRO A 251 -3.130 -11.766 5.583 1.00 43.79 C
ANISOU 2618 CB PRO A 251 6686 5407 4546 411 815 -157 C
ATOM 2619 CG PRO A 251 -2.517 -11.793 4.237 1.00 47.93 C
ANISOU 2619 CG PRO A 251 7201 5936 5074 331 783 -122 C
ATOM 2620 CD PRO A 251 -3.507 -12.530 3.388 1.00 43.55 C
ANISOU 2620 CD PRO A 251 6611 5434 4501 264 810 -94 C
ATOM 2621 N PHE A 252 -6.193 -12.606 6.108 1.00 44.25 N
ANISOU 2621 N PHE A 252 6657 5550 4607 427 910 -131 N
ATOM 2622 CA PHE A 252 -7.429 -12.461 6.881 1.00 44.49 C
ANISOU 2622 CA PHE A 252 6650 5601 4655 483 946 -135 C
ATOM 2623 C PHE A 252 -7.992 -13.806 7.354 1.00 48.74 C
ANISOU 2623 C PHE A 252 7186 6179 5154 471 1025 -122 C
ATOM 2624 O PHE A 252 -8.368 -13.921 8.521 1.00 48.88 O
ANISOU 2624 O PHE A 252 7207 6215 5150 536 1075 -140 O
ATOM 2625 CB PHE A 252 -8.500 -11.691 6.085 1.00 46.57 C
ANISOU 2625 CB PHE A 252 6843 5864 4989 464 903 -98 C
ATOM 2626 CG PHE A 252 -9.822 -11.551 6.805 1.00 48.63 C
ANISOU 2626 CG PHE A 252 7054 6143 5281 517 947 -97 C
ATOM 2627 CD1 PHE A 252 -9.927 -10.789 7.964 1.00 52.08 C
ANISOU 2627 CD1 PHE A 252 7493 6568 5726 613 967 -149 C
ATOM 2628 CD2 PHE A 252 -10.961 -12.190 6.330 1.00 50.98 C
ANISOU 2628 CD2 PHE A 252 7299 6469 5601 470 970 -48 C
ATOM 2629 CE1 PHE A 252 -11.143 -10.683 8.643 1.00 53.58 C
ANISOU 2629 CE1 PHE A 252 7633 6781 5943 664 1020 -153 C
ATOM 2630 CE2 PHE A 252 -12.180 -12.073 7.004 1.00 54.37 C
ANISOU 2630 CE2 PHE A 252 7676 6914 6068 520 1016 -42 C
ATOM 2631 CZ PHE A 252 -12.265 -11.313 8.151 1.00 52.80 C
ANISOU 2631 CZ PHE A 252 7478 6709 5875 617 1046 -95 C
ATOM 2632 N HIS A 253 -8.053 -14.811 6.460 1.00 45.07 N
ANISOU 2632 N HIS A 253 6712 5730 4682 389 1035 -91 N
ATOM 2633 CA HIS A 253 -8.608 -16.133 6.770 1.00 44.89 C
ANISOU 2633 CA HIS A 253 6676 5736 4643 368 1099 -71 C
ATOM 2634 C HIS A 253 -7.658 -16.998 7.608 1.00 49.11 C
ANISOU 2634 C HIS A 253 7260 6265 5133 386 1141 -91 C
ATOM 2635 O HIS A 253 -8.076 -18.041 8.116 1.00 49.02 O
ANISOU 2635 O HIS A 253 7234 6276 5114 386 1196 -69 O
ATOM 2636 CB HIS A 253 -9.003 -16.864 5.483 1.00 45.29 C
ANISOU 2636 CB HIS A 253 6700 5799 4710 274 1085 -43 C
ATOM 2637 CG HIS A 253 -10.113 -16.183 4.750 1.00 48.69 C
ANISOU 2637 CG HIS A 253 7073 6241 5186 251 1046 -7 C
ATOM 2638 ND1 HIS A 253 -9.866 -15.404 3.640 1.00 50.19 N
ANISOU 2638 ND1 HIS A 253 7257 6426 5389 206 976 4 N
ATOM 2639 CD2 HIS A 253 -11.436 -16.145 5.027 1.00 50.62 C
ANISOU 2639 CD2 HIS A 253 7260 6502 5473 269 1067 26 C
ATOM 2640 CE1 HIS A 253 -11.044 -14.943 3.258 1.00 49.94 C
ANISOU 2640 CE1 HIS A 253 7165 6404 5407 193 951 45 C
ATOM 2641 NE2 HIS A 253 -12.016 -15.355 4.069 1.00 50.56 N
ANISOU 2641 NE2 HIS A 253 7211 6493 5509 232 1005 58 N
ATOM 2642 N PHE A 254 -6.401 -16.556 7.772 1.00 45.71 N
ANISOU 2642 N PHE A 254 6881 5803 4683 400 1111 -123 N
ATOM 2643 CA PHE A 254 -5.395 -17.248 8.576 1.00 45.42 C
ANISOU 2643 CA PHE A 254 6892 5753 4614 415 1137 -137 C
ATOM 2644 C PHE A 254 -5.411 -16.712 10.026 1.00 50.58 C
ANISOU 2644 C PHE A 254 7568 6419 5231 505 1153 -156 C
ATOM 2645 O PHE A 254 -4.668 -17.208 10.876 1.00 50.38 O
ANISOU 2645 O PHE A 254 7578 6393 5172 523 1175 -158 O
ATOM 2646 CB PHE A 254 -4.002 -17.102 7.927 1.00 46.47 C
ANISOU 2646 CB PHE A 254 7064 5841 4750 381 1094 -158 C
ATOM 2647 CG PHE A 254 -3.642 -18.160 6.903 1.00 47.50 C
ANISOU 2647 CG PHE A 254 7189 5964 4895 297 1107 -152 C
ATOM 2648 CD1 PHE A 254 -4.451 -18.386 5.793 1.00 50.48 C
ANISOU 2648 CD1 PHE A 254 7527 6366 5287 235 1103 -139 C
ATOM 2649 CD2 PHE A 254 -2.465 -18.886 7.016 1.00 49.32 C
ANISOU 2649 CD2 PHE A 254 7452 6161 5128 278 1119 -166 C
ATOM 2650 CE1 PHE A 254 -4.108 -19.349 4.839 1.00 51.20 C
ANISOU 2650 CE1 PHE A 254 7614 6453 5385 158 1115 -150 C
ATOM 2651 CE2 PHE A 254 -2.121 -19.850 6.061 1.00 51.97 C
ANISOU 2651 CE2 PHE A 254 7777 6486 5484 204 1135 -175 C
ATOM 2652 CZ PHE A 254 -2.944 -20.073 4.977 1.00 50.09 C
ANISOU 2652 CZ PHE A 254 7504 6278 5251 145 1135 -173 C
ATOM 2653 N ALA A 255 -6.297 -15.732 10.310 1.00 47.88 N
ANISOU 2653 N ALA A 255 7202 6090 4900 558 1142 -171 N
ATOM 2654 CA ALA A 255 -6.442 -15.108 11.626 1.00 48.42 C
ANISOU 2654 CA ALA A 255 7288 6177 4931 646 1159 -206 C
ATOM 2655 C ALA A 255 -7.906 -15.046 12.108 1.00 53.17 C
ANISOU 2655 C ALA A 255 7836 6830 5536 686 1214 -194 C
ATOM 2656 O ALA A 255 -8.148 -14.623 13.243 1.00 53.42 O
ANISOU 2656 O ALA A 255 7877 6890 5531 761 1240 -230 O
ATOM 2657 CB ALA A 255 -5.859 -13.704 11.587 1.00 49.19 C
ANISOU 2657 CB ALA A 255 7407 6231 5051 688 1089 -256 C
ATOM 2658 N ARG A 256 -8.871 -15.478 11.268 1.00 49.68 N
ANISOU 2658 N ARG A 256 7338 6402 5137 635 1234 -146 N
ATOM 2659 CA ARG A 256 -10.296 -15.425 11.596 1.00 50.07 C
ANISOU 2659 CA ARG A 256 7325 6492 5208 666 1284 -124 C
ATOM 2660 C ARG A 256 -10.722 -16.466 12.638 1.00 54.56 C
ANISOU 2660 C ARG A 256 7887 7118 5727 687 1367 -92 C
ATOM 2661 O ARG A 256 -11.403 -16.093 13.593 1.00 54.70 O
ANISOU 2661 O ARG A 256 7887 7178 5718 756 1416 -107 O
ATOM 2662 CB ARG A 256 -11.168 -15.563 10.338 1.00 49.90 C
ANISOU 2662 CB ARG A 256 7242 6459 5258 600 1264 -77 C
ATOM 2663 CG ARG A 256 -12.139 -14.399 10.147 1.00 59.36 C
ANISOU 2663 CG ARG A 256 8384 7648 6522 636 1243 -84 C
ATOM 2664 CD ARG A 256 -13.307 -14.427 11.122 1.00 66.27 C
ANISOU 2664 CD ARG A 256 9211 8567 7401 701 1319 -78 C
ATOM 2665 NE ARG A 256 -13.717 -13.079 11.518 1.00 71.01 N
ANISOU 2665 NE ARG A 256 9784 9151 8044 773 1305 -127 N
ATOM 2666 CZ ARG A 256 -14.455 -12.801 12.588 1.00 84.30 C
ANISOU 2666 CZ ARG A 256 11439 10871 9719 852 1373 -154 C
ATOM 2667 NH1 ARG A 256 -14.869 -13.775 13.389 1.00 73.19 N
ANISOU 2667 NH1 ARG A 256 10028 9527 8253 868 1459 -126 N
ATOM 2668 NH2 ARG A 256 -14.779 -11.547 12.869 1.00 70.18 N
ANISOU 2668 NH2 ARG A 256 9622 9059 7986 916 1356 -210 N
ATOM 2669 N ILE A 257 -10.345 -17.751 12.456 1.00 51.24 N
ANISOU 2669 N ILE A 257 7474 6699 5298 627 1384 -47 N
ATOM 2670 CA ILE A 257 -10.705 -18.852 13.368 1.00 51.62 C
ANISOU 2670 CA ILE A 257 7505 6797 5311 634 1455 4 C
ATOM 2671 C ILE A 257 -10.196 -18.568 14.817 1.00 55.69 C
ANISOU 2671 C ILE A 257 8069 7354 5736 707 1483 -24 C
ATOM 2672 O ILE A 257 -11.032 -18.659 15.716 1.00 56.03 O
ANISOU 2672 O ILE A 257 8082 7462 5745 754 1549 -4 O
ATOM 2673 CB ILE A 257 -10.262 -20.258 12.853 1.00 54.45 C
ANISOU 2673 CB ILE A 257 7860 7133 5698 555 1454 52 C
ATOM 2674 CG1 ILE A 257 -10.735 -20.497 11.397 1.00 54.73 C
ANISOU 2674 CG1 ILE A 257 7854 7133 5810 482 1420 66 C
ATOM 2675 CG2 ILE A 257 -10.774 -21.375 13.782 1.00 55.69 C
ANISOU 2675 CG2 ILE A 257 7981 7339 5838 561 1522 121 C
ATOM 2676 CD1 ILE A 257 -9.871 -21.465 10.573 1.00 62.93 C
ANISOU 2676 CD1 ILE A 257 8900 8131 6879 400 1400 75 C
ATOM 2677 N PRO A 258 -8.915 -18.171 15.096 1.00 51.69 N
ANISOU 2677 N PRO A 258 7634 6819 5189 719 1437 -71 N
ATOM 2678 CA PRO A 258 -8.526 -17.897 16.498 1.00 51.85 C
ANISOU 2678 CA PRO A 258 7700 6886 5116 785 1458 -99 C
ATOM 2679 C PRO A 258 -9.261 -16.698 17.111 1.00 55.86 C
ANISOU 2679 C PRO A 258 8198 7431 5596 869 1479 -161 C
ATOM 2680 O PRO A 258 -9.409 -16.636 18.333 1.00 55.91 O
ANISOU 2680 O PRO A 258 8223 7505 5515 926 1524 -178 O
ATOM 2681 CB PRO A 258 -7.019 -17.623 16.408 1.00 53.02 C
ANISOU 2681 CB PRO A 258 7918 6974 5252 773 1386 -139 C
ATOM 2682 CG PRO A 258 -6.592 -18.185 15.099 1.00 56.80 C
ANISOU 2682 CG PRO A 258 8383 7390 5807 691 1353 -110 C
ATOM 2683 CD PRO A 258 -7.759 -17.985 14.193 1.00 52.43 C
ANISOU 2683 CD PRO A 258 7767 6840 5315 672 1364 -98 C
ATOM 2684 N TYR A 259 -9.730 -15.762 16.263 1.00 52.12 N
ANISOU 2684 N TYR A 259 7691 6917 5197 875 1448 -194 N
ATOM 2685 CA TYR A 259 -10.468 -14.578 16.695 1.00 52.49 C
ANISOU 2685 CA TYR A 259 7713 6981 5251 952 1462 -257 C
ATOM 2686 C TYR A 259 -11.944 -14.905 16.965 1.00 56.85 C
ANISOU 2686 C TYR A 259 8188 7593 5819 970 1548 -215 C
ATOM 2687 O TYR A 259 -12.515 -14.362 17.912 1.00 57.22 O
ANISOU 2687 O TYR A 259 8220 7691 5827 1045 1601 -259 O
ATOM 2688 CB TYR A 259 -10.346 -13.444 15.665 1.00 53.16 C
ANISOU 2688 CB TYR A 259 7785 6986 5427 947 1382 -299 C
ATOM 2689 CG TYR A 259 -11.074 -12.184 16.082 1.00 55.63 C
ANISOU 2689 CG TYR A 259 8063 7301 5773 1026 1389 -369 C
ATOM 2690 CD1 TYR A 259 -10.643 -11.435 17.174 1.00 58.19 C
ANISOU 2690 CD1 TYR A 259 8431 7641 6037 1106 1389 -458 C
ATOM 2691 CD2 TYR A 259 -12.220 -11.765 15.414 1.00 56.50 C
ANISOU 2691 CD2 TYR A 259 8092 7394 5981 1022 1396 -348 C
ATOM 2692 CE1 TYR A 259 -11.330 -10.296 17.584 1.00 59.57 C
ANISOU 2692 CE1 TYR A 259 8568 7813 6251 1183 1400 -536 C
ATOM 2693 CE2 TYR A 259 -12.904 -10.616 15.803 1.00 58.03 C
ANISOU 2693 CE2 TYR A 259 8244 7581 6225 1097 1404 -414 C
ATOM 2694 CZ TYR A 259 -12.452 -9.884 16.888 1.00 65.54 C
ANISOU 2694 CZ TYR A 259 9238 8545 7118 1178 1408 -513 C
ATOM 2695 OH TYR A 259 -13.107 -8.748 17.273 1.00 67.14 O
ANISOU 2695 OH TYR A 259 9395 8735 7381 1255 1417 -592 O
ATOM 2696 N THR A 260 -12.558 -15.775 16.134 1.00 53.05 N
ANISOU 2696 N THR A 260 7654 7103 5398 903 1562 -132 N
ATOM 2697 CA THR A 260 -13.957 -16.203 16.269 1.00 53.60 C
ANISOU 2697 CA THR A 260 7643 7221 5502 909 1637 -75 C
ATOM 2698 C THR A 260 -14.147 -16.968 17.592 1.00 58.53 C
ANISOU 2698 C THR A 260 8272 7938 6030 943 1725 -40 C
ATOM 2699 O THR A 260 -15.195 -16.834 18.229 1.00 59.20 O
ANISOU 2699 O THR A 260 8303 8084 6105 993 1802 -31 O
ATOM 2700 CB THR A 260 -14.379 -17.052 15.054 1.00 61.47 C
ANISOU 2700 CB THR A 260 8591 8179 6584 820 1614 3 C
ATOM 2701 OG1 THR A 260 -14.002 -16.381 13.851 1.00 61.30 O
ANISOU 2701 OG1 THR A 260 8583 8085 6625 779 1526 -26 O
ATOM 2702 CG2 THR A 260 -15.879 -17.340 15.020 1.00 60.51 C
ANISOU 2702 CG2 THR A 260 8376 8087 6527 825 1672 61 C
ATOM 2703 N LEU A 261 -13.122 -17.744 18.006 1.00 54.79 N
ANISOU 2703 N LEU A 261 7857 7475 5487 916 1712 -19 N
ATOM 2704 CA LEU A 261 -13.126 -18.533 19.239 1.00 55.37 C
ANISOU 2704 CA LEU A 261 7939 7637 5462 936 1781 27 C
ATOM 2705 C LEU A 261 -13.162 -17.634 20.485 1.00 60.79 C
ANISOU 2705 C LEU A 261 8660 8394 6042 1028 1820 -52 C
ATOM 2706 O LEU A 261 -13.835 -17.978 21.458 1.00 61.32 O
ANISOU 2706 O LEU A 261 8704 8561 6035 1064 1904 -18 O
ATOM 2707 CB LEU A 261 -11.909 -19.477 19.293 1.00 54.73 C
ANISOU 2707 CB LEU A 261 7911 7533 5352 879 1740 68 C
ATOM 2708 CG LEU A 261 -11.807 -20.573 18.218 1.00 58.41 C
ANISOU 2708 CG LEU A 261 8345 7934 5916 788 1708 136 C
ATOM 2709 CD1 LEU A 261 -10.464 -21.260 18.278 1.00 58.01 C
ANISOU 2709 CD1 LEU A 261 8349 7848 5846 743 1663 152 C
ATOM 2710 CD2 LEU A 261 -12.927 -21.601 18.333 1.00 61.11 C
ANISOU 2710 CD2 LEU A 261 8600 8316 6302 763 1773 236 C
ATOM 2711 N SER A 262 -12.475 -16.473 20.438 1.00 57.68 N
ANISOU 2711 N SER A 262 8317 7952 5646 1067 1758 -159 N
ATOM 2712 CA SER A 262 -12.447 -15.501 21.536 1.00 58.73 C
ANISOU 2712 CA SER A 262 8486 8138 5692 1156 1780 -259 C
ATOM 2713 C SER A 262 -13.780 -14.733 21.642 1.00 64.56 C
ANISOU 2713 C SER A 262 9152 8904 6474 1219 1845 -301 C
ATOM 2714 O SER A 262 -14.066 -14.158 22.693 1.00 65.43 O
ANISOU 2714 O SER A 262 9275 9077 6508 1298 1890 -383 O
ATOM 2715 CB SER A 262 -11.283 -14.526 21.366 1.00 61.59 C
ANISOU 2715 CB SER A 262 8921 8423 6059 1171 1680 -354 C
ATOM 2716 OG SER A 262 -11.472 -13.630 20.283 1.00 69.38 O
ANISOU 2716 OG SER A 262 9876 9317 7170 1164 1621 -391 O
ATOM 2717 N GLN A 263 -14.585 -14.732 20.559 1.00 61.40 N
ANISOU 2717 N GLN A 263 8674 8457 6198 1183 1847 -248 N
ATOM 2718 CA GLN A 263 -15.886 -14.061 20.479 1.00 62.30 C
ANISOU 2718 CA GLN A 263 8704 8580 6386 1232 1902 -271 C
ATOM 2719 C GLN A 263 -17.014 -14.942 21.015 1.00 68.40 C
ANISOU 2719 C GLN A 263 9407 9445 7137 1235 2015 -181 C
ATOM 2720 O GLN A 263 -17.906 -14.436 21.698 1.00 69.18 O
ANISOU 2720 O GLN A 263 9459 9604 7220 1306 2098 -218 O
ATOM 2721 CB GLN A 263 -16.203 -13.659 19.029 1.00 62.74 C
ANISOU 2721 CB GLN A 263 8711 8530 6597 1185 1830 -254 C
ATOM 2722 CG GLN A 263 -15.341 -12.531 18.481 1.00 72.87 C
ANISOU 2722 CG GLN A 263 10041 9725 7923 1191 1724 -339 C
ATOM 2723 CD GLN A 263 -15.716 -12.194 17.064 1.00 88.22 C
ANISOU 2723 CD GLN A 263 11931 11581 10009 1137 1654 -304 C
ATOM 2724 OE1 GLN A 263 -15.501 -12.974 16.130 1.00 81.95 O
ANISOU 2724 OE1 GLN A 263 11140 10754 9243 1052 1611 -230 O
ATOM 2725 NE2 GLN A 263 -16.255 -11.004 16.867 1.00 81.28 N
ANISOU 2725 NE2 GLN A 263 10999 10661 9223 1183 1637 -359 N
ATOM 2726 N THR A 264 -16.988 -16.249 20.680 1.00 65.59 N
ANISOU 2726 N THR A 264 9036 9093 6790 1159 2017 -63 N
ATOM 2727 CA THR A 264 -17.998 -17.240 21.073 1.00 66.64 C
ANISOU 2727 CA THR A 264 9096 9302 6921 1147 2111 47 C
ATOM 2728 C THR A 264 -17.987 -17.516 22.581 1.00 72.97 C
ANISOU 2728 C THR A 264 9918 10234 7572 1202 2203 49 C
ATOM 2729 O THR A 264 -19.046 -17.770 23.154 1.00 73.62 O
ANISOU 2729 O THR A 264 9930 10398 7645 1236 2305 95 O
ATOM 2730 CB THR A 264 -17.804 -18.554 20.297 1.00 74.05 C
ANISOU 2730 CB THR A 264 10024 10201 7913 1049 2071 161 C
ATOM 2731 OG1 THR A 264 -16.449 -18.995 20.430 1.00 72.28 O
ANISOU 2731 OG1 THR A 264 9887 9964 7614 1018 2015 149 O
ATOM 2732 CG2 THR A 264 -18.182 -18.431 18.824 1.00 71.82 C
ANISOU 2732 CG2 THR A 264 9700 9815 7776 990 2001 178 C
ATOM 2733 N ARG A 265 -16.797 -17.502 23.212 1.00 70.42 N
ANISOU 2733 N ARG A 265 9689 9936 7131 1207 2168 8 N
ATOM 2734 CA ARG A 265 -16.636 -17.766 24.647 1.00 71.82 C
ANISOU 2734 CA ARG A 265 9898 10245 7145 1250 2241 11 C
ATOM 2735 C ARG A 265 -15.623 -16.814 25.280 1.00 76.82 C
ANISOU 2735 C ARG A 265 10631 10884 7672 1300 2193 -121 C
ATOM 2736 O ARG A 265 -14.603 -16.503 24.659 1.00 75.32 O
ANISOU 2736 O ARG A 265 10503 10598 7517 1268 2088 -161 O
ATOM 2737 CB ARG A 265 -16.175 -19.225 24.895 1.00 72.30 C
ANISOU 2737 CB ARG A 265 9962 10346 7161 1180 2245 149 C
ATOM 2738 CG ARG A 265 -17.095 -20.336 24.364 1.00 84.23 C
ANISOU 2738 CG ARG A 265 11379 11833 8793 1116 2269 288 C
ATOM 2739 CD ARG A 265 -18.228 -20.707 25.312 1.00 98.12 C
ANISOU 2739 CD ARG A 265 13050 13708 10523 1147 2392 373 C
ATOM 2740 NE ARG A 265 -17.767 -21.486 26.464 1.00109.03 N
ANISOU 2740 NE ARG A 265 14452 15213 11761 1146 2443 448 N
ATOM 2741 CZ ARG A 265 -17.693 -22.814 26.499 1.00122.93 C
ANISOU 2741 CZ ARG A 265 16186 16984 13540 1077 2433 589 C
ATOM 2742 NH1 ARG A 265 -18.040 -23.534 25.438 1.00109.39 N
ANISOU 2742 NH1 ARG A 265 14425 15159 11977 1004 2377 657 N
ATOM 2743 NH2 ARG A 265 -17.266 -23.432 27.592 1.00110.25 N
ANISOU 2743 NH2 ARG A 265 14594 15496 11799 1077 2476 661 N
ATOM 2744 N ASP A 266 -15.881 -16.384 26.531 1.00 75.66 N
ANISOU 2744 N ASP A 266 10500 10853 7395 1377 2270 -188 N
ATOM 2745 CA ASP A 266 -14.955 -15.540 27.290 1.00 76.32 C
ANISOU 2745 CA ASP A 266 10680 10959 7361 1427 2228 -317 C
ATOM 2746 C ASP A 266 -13.983 -16.490 28.001 1.00 80.83 C
ANISOU 2746 C ASP A 266 11316 11593 7803 1381 2206 -237 C
ATOM 2747 O ASP A 266 -14.088 -16.740 29.205 1.00 81.55 O
ANISOU 2747 O ASP A 266 11419 11825 7741 1408 2279 -218 O
ATOM 2748 CB ASP A 266 -15.703 -14.604 28.262 1.00 79.93 C
ANISOU 2748 CB ASP A 266 11122 11514 7734 1529 2321 -434 C
ATOM 2749 CG ASP A 266 -14.939 -13.339 28.611 1.00 91.06 C
ANISOU 2749 CG ASP A 266 12612 12895 9093 1591 2257 -608 C
ATOM 2750 OD1 ASP A 266 -15.468 -12.236 28.353 1.00 92.08 O
ANISOU 2750 OD1 ASP A 266 12707 12978 9300 1655 2266 -726 O
ATOM 2751 OD2 ASP A 266 -13.811 -13.452 29.143 1.00 97.22 O
ANISOU 2751 OD2 ASP A 266 13484 13693 9762 1576 2194 -625 O
ATOM 2752 N VAL A 267 -13.075 -17.072 27.202 1.00 76.68 N
ANISOU 2752 N VAL A 267 10821 10965 7348 1305 2108 -180 N
ATOM 2753 CA VAL A 267 -12.095 -18.085 27.583 1.00 76.44 C
ANISOU 2753 CA VAL A 267 10837 10958 7249 1243 2070 -85 C
ATOM 2754 C VAL A 267 -10.659 -17.506 27.546 1.00 79.77 C
ANISOU 2754 C VAL A 267 11358 11301 7649 1237 1952 -167 C
ATOM 2755 O VAL A 267 -9.782 -18.007 28.251 1.00 79.28 O
ANISOU 2755 O VAL A 267 11349 11272 7500 1206 1917 -119 O
ATOM 2756 CB VAL A 267 -12.303 -19.309 26.639 1.00 79.58 C
ANISOU 2756 CB VAL A 267 11166 11297 7775 1157 2066 60 C
ATOM 2757 CG1 VAL A 267 -11.013 -19.818 25.998 1.00 78.14 C
ANISOU 2757 CG1 VAL A 267 11029 11002 7656 1084 1958 92 C
ATOM 2758 CG2 VAL A 267 -13.061 -20.429 27.343 1.00 80.40 C
ANISOU 2758 CG2 VAL A 267 11207 11521 7821 1139 2160 199 C
ATOM 2759 N PHE A 268 -10.438 -16.451 26.747 1.00 76.17 N
ANISOU 2759 N PHE A 268 10922 10742 7278 1267 1890 -283 N
ATOM 2760 CA PHE A 268 -9.140 -15.792 26.601 1.00 75.59 C
ANISOU 2760 CA PHE A 268 10931 10581 7207 1266 1776 -364 C
ATOM 2761 C PHE A 268 -8.972 -14.647 27.602 1.00 81.36 C
ANISOU 2761 C PHE A 268 11721 11367 7825 1351 1771 -506 C
ATOM 2762 O PHE A 268 -9.965 -14.113 28.105 1.00 82.01 O
ANISOU 2762 O PHE A 268 11769 11524 7866 1418 1852 -571 O
ATOM 2763 CB PHE A 268 -8.987 -15.250 25.169 1.00 76.10 C
ANISOU 2763 CB PHE A 268 10975 10500 7438 1244 1705 -398 C
ATOM 2764 CG PHE A 268 -8.705 -16.285 24.107 1.00 76.39 C
ANISOU 2764 CG PHE A 268 10980 10462 7582 1153 1677 -286 C
ATOM 2765 CD1 PHE A 268 -9.730 -17.062 23.579 1.00 79.41 C
ANISOU 2765 CD1 PHE A 268 11279 10860 8032 1120 1742 -200 C
ATOM 2766 CD2 PHE A 268 -7.423 -16.450 23.600 1.00 77.54 C
ANISOU 2766 CD2 PHE A 268 11175 10517 7769 1102 1584 -275 C
ATOM 2767 CE1 PHE A 268 -9.470 -18.011 22.587 1.00 79.34 C
ANISOU 2767 CE1 PHE A 268 11242 10781 8124 1037 1712 -112 C
ATOM 2768 CE2 PHE A 268 -7.164 -17.397 22.605 1.00 79.43 C
ANISOU 2768 CE2 PHE A 268 11383 10689 8108 1020 1563 -188 C
ATOM 2769 CZ PHE A 268 -8.189 -18.170 22.105 1.00 77.52 C
ANISOU 2769 CZ PHE A 268 11062 10465 7925 988 1626 -112 C
ATOM 2770 N ASP A 269 -7.711 -14.256 27.871 1.00 78.52 N
ANISOU 2770 N ASP A 269 11446 10963 7423 1349 1673 -560 N
ATOM 2771 CA ASP A 269 -7.380 -13.137 28.756 1.00 79.84 C
ANISOU 2771 CA ASP A 269 11678 11163 7494 1426 1644 -707 C
ATOM 2772 C ASP A 269 -7.648 -11.808 28.041 1.00 84.54 C
ANISOU 2772 C ASP A 269 12251 11656 8216 1478 1605 -833 C
ATOM 2773 O ASP A 269 -7.825 -11.799 26.819 1.00 83.09 O
ANISOU 2773 O ASP A 269 12017 11367 8185 1442 1577 -793 O
ATOM 2774 CB ASP A 269 -5.913 -13.216 29.217 1.00 81.59 C
ANISOU 2774 CB ASP A 269 11993 11358 7649 1398 1540 -709 C
ATOM 2775 CG ASP A 269 -5.658 -14.178 30.363 1.00 93.14 C
ANISOU 2775 CG ASP A 269 13490 12951 8950 1369 1574 -619 C
ATOM 2776 OD1 ASP A 269 -6.358 -14.074 31.395 1.00 95.30 O
ANISOU 2776 OD1 ASP A 269 13759 13369 9082 1415 1663 -644 O
ATOM 2777 OD2 ASP A 269 -4.714 -14.984 30.257 1.00 98.38 O
ANISOU 2777 OD2 ASP A 269 14182 13571 9626 1301 1508 -525 O
ATOM 2778 N CYS A 270 -7.677 -10.690 28.797 1.00 83.03 N
ANISOU 2778 N CYS A 270 12091 11493 7962 1562 1599 -985 N
ATOM 2779 CA CYS A 270 -7.928 -9.351 28.258 1.00 83.24 C
ANISOU 2779 CA CYS A 270 12090 11423 8115 1620 1559 -1114 C
ATOM 2780 C CYS A 270 -6.880 -8.972 27.201 1.00 83.06 C
ANISOU 2780 C CYS A 270 12086 11238 8235 1578 1425 -1107 C
ATOM 2781 O CYS A 270 -7.258 -8.467 26.145 1.00 81.85 O
ANISOU 2781 O CYS A 270 11873 10990 8238 1576 1402 -1113 O
ATOM 2782 CB CYS A 270 -7.991 -8.313 29.376 1.00 86.09 C
ANISOU 2782 CB CYS A 270 12491 11843 8376 1714 1566 -1285 C
ATOM 2783 SG CYS A 270 -8.364 -6.629 28.812 1.00 90.87 S
ANISOU 2783 SG CYS A 270 13046 12325 9156 1792 1518 -1450 S
ATOM 2784 N THR A 271 -5.586 -9.247 27.469 1.00 77.30 N
ANISOU 2784 N THR A 271 11435 10480 7456 1542 1338 -1086 N
ATOM 2785 CA THR A 271 -4.480 -8.959 26.545 1.00 74.90 C
ANISOU 2785 CA THR A 271 11150 10030 7277 1500 1215 -1071 C
ATOM 2786 C THR A 271 -4.513 -9.897 25.330 1.00 75.12 C
ANISOU 2786 C THR A 271 11130 10005 7405 1413 1225 -929 C
ATOM 2787 O THR A 271 -4.117 -9.481 24.240 1.00 73.74 O
ANISOU 2787 O THR A 271 10932 9717 7369 1387 1158 -921 O
ATOM 2788 CB THR A 271 -3.121 -9.035 27.256 1.00 82.34 C
ANISOU 2788 CB THR A 271 12187 10961 8140 1489 1124 -1086 C
ATOM 2789 OG1 THR A 271 -3.042 -10.237 28.024 1.00 82.35 O
ANISOU 2789 OG1 THR A 271 12218 11072 7998 1452 1178 -995 O
ATOM 2790 CG2 THR A 271 -2.852 -7.825 28.139 1.00 81.90 C
ANISOU 2790 CG2 THR A 271 12179 10902 8037 1572 1068 -1250 C
ATOM 2791 N ALA A 272 -4.989 -11.150 25.517 1.00 69.87 N
ANISOU 2791 N ALA A 272 10447 9427 6672 1368 1308 -817 N
ATOM 2792 CA ALA A 272 -5.104 -12.159 24.458 1.00 67.65 C
ANISOU 2792 CA ALA A 272 10120 9108 6477 1286 1326 -689 C
ATOM 2793 C ALA A 272 -6.203 -11.787 23.456 1.00 69.38 C
ANISOU 2793 C ALA A 272 10253 9297 6811 1289 1367 -686 C
ATOM 2794 O ALA A 272 -5.972 -11.861 22.248 1.00 67.74 O
ANISOU 2794 O ALA A 272 10016 9003 6717 1233 1327 -636 O
ATOM 2795 CB ALA A 272 -5.383 -13.527 25.063 1.00 68.62 C
ANISOU 2795 CB ALA A 272 10238 9331 6502 1246 1400 -579 C
ATOM 2796 N GLU A 273 -7.384 -11.367 23.963 1.00 65.65 N
ANISOU 2796 N GLU A 273 9740 8896 6308 1353 1446 -740 N
ATOM 2797 CA GLU A 273 -8.545 -10.953 23.168 1.00 64.73 C
ANISOU 2797 CA GLU A 273 9537 8756 6303 1364 1487 -739 C
ATOM 2798 C GLU A 273 -8.273 -9.660 22.400 1.00 66.59 C
ANISOU 2798 C GLU A 273 9759 8875 6668 1386 1397 -820 C
ATOM 2799 O GLU A 273 -8.796 -9.489 21.299 1.00 65.49 O
ANISOU 2799 O GLU A 273 9553 8677 6651 1357 1388 -782 O
ATOM 2800 CB GLU A 273 -9.776 -10.775 24.067 1.00 67.48 C
ANISOU 2800 CB GLU A 273 9843 9214 6582 1432 1600 -779 C
ATOM 2801 CG GLU A 273 -10.611 -12.039 24.199 1.00 77.90 C
ANISOU 2801 CG GLU A 273 11103 10609 7889 1391 1699 -656 C
ATOM 2802 CD GLU A 273 -11.757 -12.019 25.195 1.00 96.13 C
ANISOU 2802 CD GLU A 273 13379 13051 10097 1450 1822 -669 C
ATOM 2803 OE1 GLU A 273 -12.252 -10.918 25.533 1.00 87.72 O
ANISOU 2803 OE1 GLU A 273 12296 12004 9028 1531 1852 -786 O
ATOM 2804 OE2 GLU A 273 -12.186 -13.119 25.611 1.00 88.80 O
ANISOU 2804 OE2 GLU A 273 12432 12208 9102 1414 1892 -560 O
ATOM 2805 N ASN A 274 -7.461 -8.755 22.984 1.00 62.47 N
ANISOU 2805 N ASN A 274 9296 8319 6123 1435 1325 -925 N
ATOM 2806 CA ASN A 274 -7.096 -7.470 22.385 1.00 61.59 C
ANISOU 2806 CA ASN A 274 9170 8093 6138 1460 1229 -1002 C
ATOM 2807 C ASN A 274 -6.130 -7.657 21.212 1.00 62.71 C
ANISOU 2807 C ASN A 274 9324 8133 6370 1383 1135 -927 C
ATOM 2808 O ASN A 274 -6.364 -7.076 20.152 1.00 61.86 O
ANISOU 2808 O ASN A 274 9162 7946 6396 1366 1088 -916 O
ATOM 2809 CB ASN A 274 -6.493 -6.529 23.435 1.00 63.42 C
ANISOU 2809 CB ASN A 274 9460 8322 6316 1538 1179 -1140 C
ATOM 2810 CG ASN A 274 -7.487 -5.906 24.395 1.00 86.53 C
ANISOU 2810 CG ASN A 274 12361 11321 9196 1629 1256 -1255 C
ATOM 2811 OD1 ASN A 274 -8.641 -6.337 24.533 1.00 80.35 O
ANISOU 2811 OD1 ASN A 274 11524 10619 8385 1639 1367 -1223 O
ATOM 2812 ND2 ASN A 274 -7.039 -4.894 25.120 1.00 79.08 N
ANISOU 2812 ND2 ASN A 274 11455 10353 8240 1699 1200 -1395 N
ATOM 2813 N THR A 275 -5.068 -8.481 21.393 1.00 57.57 N
ANISOU 2813 N THR A 275 8738 7488 5648 1335 1109 -873 N
ATOM 2814 CA THR A 275 -4.040 -8.781 20.383 1.00 55.57 C
ANISOU 2814 CA THR A 275 8501 7148 5465 1262 1032 -805 C
ATOM 2815 C THR A 275 -4.677 -9.415 19.130 1.00 56.89 C
ANISOU 2815 C THR A 275 8603 7301 5710 1191 1065 -708 C
ATOM 2816 O THR A 275 -4.311 -9.042 18.013 1.00 55.52 O
ANISOU 2816 O THR A 275 8406 7048 5641 1154 1001 -685 O
ATOM 2817 CB THR A 275 -2.942 -9.677 20.990 1.00 63.36 C
ANISOU 2817 CB THR A 275 9562 8155 6359 1229 1016 -765 C
ATOM 2818 OG1 THR A 275 -2.407 -9.031 22.145 1.00 64.39 O
ANISOU 2818 OG1 THR A 275 9752 8304 6409 1294 980 -859 O
ATOM 2819 CG2 THR A 275 -1.805 -9.976 20.013 1.00 60.67 C
ANISOU 2819 CG2 THR A 275 9236 7720 6095 1161 940 -706 C
ATOM 2820 N LEU A 276 -5.642 -10.342 19.323 1.00 52.46 N
ANISOU 2820 N LEU A 276 8011 6822 5100 1174 1162 -650 N
ATOM 2821 CA LEU A 276 -6.359 -11.017 18.236 1.00 51.00 C
ANISOU 2821 CA LEU A 276 7763 6633 4981 1109 1196 -563 C
ATOM 2822 C LEU A 276 -7.204 -10.025 17.427 1.00 53.84 C
ANISOU 2822 C LEU A 276 8053 6950 5453 1125 1177 -587 C
ATOM 2823 O LEU A 276 -7.283 -10.163 16.207 1.00 52.47 O
ANISOU 2823 O LEU A 276 7843 6735 5360 1062 1149 -528 O
ATOM 2824 CB LEU A 276 -7.248 -12.154 18.775 1.00 51.30 C
ANISOU 2824 CB LEU A 276 7776 6765 4948 1097 1300 -501 C
ATOM 2825 CG LEU A 276 -6.546 -13.439 19.236 1.00 55.44 C
ANISOU 2825 CG LEU A 276 8346 7323 5394 1052 1318 -436 C
ATOM 2826 CD1 LEU A 276 -7.463 -14.268 20.107 1.00 56.19 C
ANISOU 2826 CD1 LEU A 276 8416 7525 5410 1065 1418 -389 C
ATOM 2827 CD2 LEU A 276 -6.078 -14.277 18.054 1.00 56.85 C
ANISOU 2827 CD2 LEU A 276 8514 7443 5643 962 1287 -362 C
ATOM 2828 N PHE A 277 -7.804 -9.020 18.104 1.00 50.84 N
ANISOU 2828 N PHE A 277 7655 6581 5080 1208 1187 -675 N
ATOM 2829 CA PHE A 277 -8.627 -7.974 17.491 1.00 50.73 C
ANISOU 2829 CA PHE A 277 7567 6520 5188 1234 1164 -705 C
ATOM 2830 C PHE A 277 -7.793 -7.058 16.590 1.00 54.37 C
ANISOU 2830 C PHE A 277 8030 6876 5752 1213 1047 -717 C
ATOM 2831 O PHE A 277 -8.247 -6.733 15.491 1.00 53.72 O
ANISOU 2831 O PHE A 277 7886 6749 5776 1172 1012 -668 O
ATOM 2832 CB PHE A 277 -9.358 -7.150 18.569 1.00 53.62 C
ANISOU 2832 CB PHE A 277 7915 6924 5536 1334 1212 -810 C
ATOM 2833 CG PHE A 277 -10.087 -5.919 18.073 1.00 55.43 C
ANISOU 2833 CG PHE A 277 8065 7088 5908 1373 1178 -859 C
ATOM 2834 CD1 PHE A 277 -11.349 -6.021 17.502 1.00 58.46 C
ANISOU 2834 CD1 PHE A 277 8360 7483 6369 1361 1229 -809 C
ATOM 2835 CD2 PHE A 277 -9.518 -4.657 18.197 1.00 57.76 C
ANISOU 2835 CD2 PHE A 277 8369 7305 6273 1423 1090 -952 C
ATOM 2836 CE1 PHE A 277 -12.023 -4.884 17.052 1.00 59.85 C
ANISOU 2836 CE1 PHE A 277 8456 7593 6693 1395 1193 -848 C
ATOM 2837 CE2 PHE A 277 -10.192 -3.521 17.741 1.00 61.01 C
ANISOU 2837 CE2 PHE A 277 8697 7648 6836 1457 1053 -992 C
ATOM 2838 CZ PHE A 277 -11.439 -3.642 17.172 1.00 59.28 C
ANISOU 2838 CZ PHE A 277 8389 7441 6694 1443 1106 -938 C
ATOM 2839 N TYR A 278 -6.595 -6.631 17.055 1.00 51.01 N
ANISOU 2839 N TYR A 278 7671 6414 5299 1240 981 -775 N
ATOM 2840 CA TYR A 278 -5.700 -5.746 16.299 1.00 50.48 C
ANISOU 2840 CA TYR A 278 7604 6245 5330 1224 867 -781 C
ATOM 2841 C TYR A 278 -5.163 -6.438 15.039 1.00 52.45 C
ANISOU 2841 C TYR A 278 7853 6469 5607 1124 838 -674 C
ATOM 2842 O TYR A 278 -4.993 -5.775 14.016 1.00 51.70 O
ANISOU 2842 O TYR A 278 7718 6310 5617 1092 766 -644 O
ATOM 2843 CB TYR A 278 -4.535 -5.234 17.169 1.00 52.27 C
ANISOU 2843 CB TYR A 278 7905 6441 5516 1272 805 -861 C
ATOM 2844 CG TYR A 278 -4.951 -4.491 18.424 1.00 55.72 C
ANISOU 2844 CG TYR A 278 8351 6906 5915 1372 827 -986 C
ATOM 2845 CD1 TYR A 278 -5.899 -3.470 18.375 1.00 58.51 C
ANISOU 2845 CD1 TYR A 278 8632 7236 6365 1426 831 -1047 C
ATOM 2846 CD2 TYR A 278 -4.343 -4.755 19.648 1.00 57.05 C
ANISOU 2846 CD2 TYR A 278 8599 7119 5957 1410 836 -1046 C
ATOM 2847 CE1 TYR A 278 -6.280 -2.780 19.524 1.00 60.46 C
ANISOU 2847 CE1 TYR A 278 8884 7510 6578 1521 857 -1177 C
ATOM 2848 CE2 TYR A 278 -4.719 -4.075 20.805 1.00 59.22 C
ANISOU 2848 CE2 TYR A 278 8887 7431 6182 1500 859 -1171 C
ATOM 2849 CZ TYR A 278 -5.683 -3.082 20.737 1.00 67.45 C
ANISOU 2849 CZ TYR A 278 9856 8453 7320 1558 872 -1243 C
ATOM 2850 OH TYR A 278 -6.047 -2.397 21.870 1.00 70.26 O
ANISOU 2850 OH TYR A 278 10221 8844 7629 1650 900 -1381 O
ATOM 2851 N VAL A 279 -4.925 -7.766 15.115 1.00 47.82 N
ANISOU 2851 N VAL A 279 7303 5935 4930 1074 895 -617 N
ATOM 2852 CA VAL A 279 -4.458 -8.611 14.007 1.00 46.30 C
ANISOU 2852 CA VAL A 279 7111 5730 4750 981 886 -529 C
ATOM 2853 C VAL A 279 -5.609 -8.771 12.994 1.00 49.73 C
ANISOU 2853 C VAL A 279 7470 6181 5243 935 912 -471 C
ATOM 2854 O VAL A 279 -5.385 -8.636 11.787 1.00 48.77 O
ANISOU 2854 O VAL A 279 7324 6023 5184 873 862 -422 O
ATOM 2855 CB VAL A 279 -3.924 -9.973 14.538 1.00 49.57 C
ANISOU 2855 CB VAL A 279 7579 6190 5065 950 940 -496 C
ATOM 2856 CG1 VAL A 279 -3.860 -11.037 13.446 1.00 48.46 C
ANISOU 2856 CG1 VAL A 279 7423 6051 4940 856 958 -415 C
ATOM 2857 CG2 VAL A 279 -2.562 -9.802 15.195 1.00 49.32 C
ANISOU 2857 CG2 VAL A 279 7619 6123 4997 972 888 -532 C
ATOM 2858 N LYS A 280 -6.836 -9.026 13.499 1.00 46.53 N
ANISOU 2858 N LYS A 280 7028 5833 4818 965 988 -475 N
ATOM 2859 CA LYS A 280 -8.054 -9.182 12.705 1.00 46.32 C
ANISOU 2859 CA LYS A 280 6926 5823 4850 928 1015 -421 C
ATOM 2860 C LYS A 280 -8.361 -7.890 11.937 1.00 51.15 C
ANISOU 2860 C LYS A 280 7479 6373 5581 935 939 -427 C
ATOM 2861 O LYS A 280 -8.635 -7.959 10.740 1.00 50.54 O
ANISOU 2861 O LYS A 280 7361 6282 5561 865 906 -360 O
ATOM 2862 CB LYS A 280 -9.240 -9.582 13.611 1.00 49.03 C
ANISOU 2862 CB LYS A 280 7240 6236 5154 975 1112 -430 C
ATOM 2863 CG LYS A 280 -10.562 -9.813 12.883 1.00 56.88 C
ANISOU 2863 CG LYS A 280 8152 7245 6215 939 1142 -369 C
ATOM 2864 CD LYS A 280 -11.523 -8.646 13.078 1.00 63.31 C
ANISOU 2864 CD LYS A 280 8898 8040 7116 1003 1140 -412 C
ATOM 2865 CE LYS A 280 -12.745 -8.801 12.219 1.00 69.86 C
ANISOU 2865 CE LYS A 280 9643 8866 8035 957 1144 -340 C
ATOM 2866 NZ LYS A 280 -13.365 -7.491 11.901 1.00 77.43 N
ANISOU 2866 NZ LYS A 280 10530 9769 9120 993 1094 -366 N
ATOM 2867 N GLU A 281 -8.309 -6.727 12.626 1.00 48.79 N
ANISOU 2867 N GLU A 281 7174 6040 5324 1016 908 -508 N
ATOM 2868 CA GLU A 281 -8.593 -5.405 12.061 1.00 49.30 C
ANISOU 2868 CA GLU A 281 7173 6035 5522 1034 831 -519 C
ATOM 2869 C GLU A 281 -7.575 -4.993 10.987 1.00 53.60 C
ANISOU 2869 C GLU A 281 7725 6518 6121 974 729 -472 C
ATOM 2870 O GLU A 281 -7.970 -4.391 9.984 1.00 53.30 O
ANISOU 2870 O GLU A 281 7621 6444 6188 937 671 -421 O
ATOM 2871 CB GLU A 281 -8.646 -4.346 13.171 1.00 51.54 C
ANISOU 2871 CB GLU A 281 7455 6293 5836 1140 823 -633 C
ATOM 2872 CG GLU A 281 -9.798 -3.362 13.027 1.00 62.95 C
ANISOU 2872 CG GLU A 281 8802 7706 7408 1180 818 -654 C
ATOM 2873 CD GLU A 281 -11.206 -3.931 13.074 1.00 83.70 C
ANISOU 2873 CD GLU A 281 11377 10398 10028 1178 915 -620 C
ATOM 2874 OE1 GLU A 281 -11.443 -4.900 13.832 1.00 78.95 O
ANISOU 2874 OE1 GLU A 281 10815 9874 9307 1198 1011 -635 O
ATOM 2875 OE2 GLU A 281 -12.080 -3.391 12.359 1.00 77.74 O
ANISOU 2875 OE2 GLU A 281 10534 9611 9392 1154 892 -570 O
ATOM 2876 N SER A 282 -6.280 -5.324 11.190 1.00 50.22 N
ANISOU 2876 N SER A 282 7374 6082 5626 961 709 -482 N
ATOM 2877 CA SER A 282 -5.198 -5.019 10.247 1.00 49.69 C
ANISOU 2877 CA SER A 282 7317 5963 5600 905 625 -435 C
ATOM 2878 C SER A 282 -5.346 -5.839 8.957 1.00 53.68 C
ANISOU 2878 C SER A 282 7803 6503 6091 801 637 -338 C
ATOM 2879 O SER A 282 -5.182 -5.294 7.863 1.00 53.25 O
ANISOU 2879 O SER A 282 7709 6418 6105 749 569 -281 O
ATOM 2880 CB SER A 282 -3.837 -5.281 10.884 1.00 52.54 C
ANISOU 2880 CB SER A 282 7761 6307 5894 921 611 -470 C
ATOM 2881 OG SER A 282 -3.664 -4.521 12.070 1.00 61.12 O
ANISOU 2881 OG SER A 282 8870 7364 6988 1013 589 -565 O
ATOM 2882 N THR A 283 -5.679 -7.139 9.096 1.00 50.18 N
ANISOU 2882 N THR A 283 7384 6124 5560 771 722 -320 N
ATOM 2883 CA THR A 283 -5.886 -8.071 7.982 1.00 49.63 C
ANISOU 2883 CA THR A 283 7300 6090 5466 675 743 -247 C
ATOM 2884 C THR A 283 -7.195 -7.763 7.242 1.00 54.19 C
ANISOU 2884 C THR A 283 7798 6684 6110 647 735 -200 C
ATOM 2885 O THR A 283 -7.282 -8.016 6.039 1.00 53.40 O
ANISOU 2885 O THR A 283 7674 6598 6017 563 710 -135 O
ATOM 2886 CB THR A 283 -5.863 -9.521 8.473 1.00 57.28 C
ANISOU 2886 CB THR A 283 8315 7111 6340 657 828 -248 C
ATOM 2887 OG1 THR A 283 -6.696 -9.650 9.625 1.00 57.66 O
ANISOU 2887 OG1 THR A 283 8355 7192 6361 724 893 -284 O
ATOM 2888 CG2 THR A 283 -4.459 -10.017 8.778 1.00 55.28 C
ANISOU 2888 CG2 THR A 283 8132 6840 6033 651 825 -266 C
ATOM 2889 N LEU A 284 -8.203 -7.216 7.961 1.00 51.93 N
ANISOU 2889 N LEU A 284 7468 6394 5869 715 757 -233 N
ATOM 2890 CA LEU A 284 -9.509 -6.822 7.415 1.00 52.42 C
ANISOU 2890 CA LEU A 284 7444 6459 6014 699 748 -189 C
ATOM 2891 C LEU A 284 -9.350 -5.628 6.463 1.00 57.12 C
ANISOU 2891 C LEU A 284 7986 6999 6717 671 641 -148 C
ATOM 2892 O LEU A 284 -10.117 -5.503 5.506 1.00 56.63 O
ANISOU 2892 O LEU A 284 7861 6944 6712 612 609 -77 O
ATOM 2893 CB LEU A 284 -10.487 -6.478 8.560 1.00 53.15 C
ANISOU 2893 CB LEU A 284 7504 6557 6135 790 805 -247 C
ATOM 2894 CG LEU A 284 -11.953 -6.218 8.197 1.00 58.43 C
ANISOU 2894 CG LEU A 284 8078 7229 6892 781 815 -203 C
ATOM 2895 CD1 LEU A 284 -12.733 -7.514 8.055 1.00 58.38 C
ANISOU 2895 CD1 LEU A 284 8069 7288 6825 744 898 -161 C
ATOM 2896 CD2 LEU A 284 -12.615 -5.340 9.236 1.00 62.05 C
ANISOU 2896 CD2 LEU A 284 8489 7658 7431 882 831 -274 C
ATOM 2897 N TRP A 285 -8.348 -4.761 6.728 1.00 54.51 N
ANISOU 2897 N TRP A 285 7679 6614 6417 709 581 -186 N
ATOM 2898 CA TRP A 285 -8.037 -3.593 5.904 1.00 54.88 C
ANISOU 2898 CA TRP A 285 7674 6603 6574 686 473 -141 C
ATOM 2899 C TRP A 285 -7.500 -4.032 4.532 1.00 58.76 C
ANISOU 2899 C TRP A 285 8173 7125 7029 575 436 -49 C
ATOM 2900 O TRP A 285 -7.852 -3.421 3.522 1.00 58.47 O
ANISOU 2900 O TRP A 285 8069 7078 7069 521 366 29 O
ATOM 2901 CB TRP A 285 -7.034 -2.667 6.614 1.00 53.78 C
ANISOU 2901 CB TRP A 285 7562 6396 6474 757 421 -209 C
ATOM 2902 CG TRP A 285 -6.704 -1.439 5.821 1.00 55.07 C
ANISOU 2902 CG TRP A 285 7662 6491 6769 738 305 -158 C
ATOM 2903 CD1 TRP A 285 -7.406 -0.271 5.789 1.00 58.80 C
ANISOU 2903 CD1 TRP A 285 8047 6903 7391 777 245 -160 C
ATOM 2904 CD2 TRP A 285 -5.630 -1.287 4.882 1.00 54.48 C
ANISOU 2904 CD2 TRP A 285 7595 6405 6698 669 236 -84 C
ATOM 2905 NE1 TRP A 285 -6.827 0.607 4.904 1.00 58.40 N
ANISOU 2905 NE1 TRP A 285 7947 6800 7440 735 135 -86 N
ATOM 2906 CE2 TRP A 285 -5.737 0.007 4.328 1.00 59.03 C
ANISOU 2906 CE2 TRP A 285 8086 6915 7427 668 131 -36 C
ATOM 2907 CE3 TRP A 285 -4.580 -2.121 4.458 1.00 54.95 C
ANISOU 2907 CE3 TRP A 285 7721 6504 6653 608 256 -53 C
ATOM 2908 CZ2 TRP A 285 -4.830 0.492 3.378 1.00 58.19 C
ANISOU 2908 CZ2 TRP A 285 7958 6788 7363 607 45 51 C
ATOM 2909 CZ3 TRP A 285 -3.683 -1.639 3.519 1.00 56.34 C
ANISOU 2909 CZ3 TRP A 285 7879 6661 6868 551 179 22 C
ATOM 2910 CH2 TRP A 285 -3.809 -0.346 2.992 1.00 57.61 C
ANISOU 2910 CH2 TRP A 285 7955 6763 7173 550 75 78 C
ATOM 2911 N LEU A 286 -6.652 -5.084 4.500 1.00 55.30 N
ANISOU 2911 N LEU A 286 7811 6725 6475 540 483 -57 N
ATOM 2912 CA LEU A 286 -6.080 -5.630 3.266 1.00 55.06 C
ANISOU 2912 CA LEU A 286 7794 6731 6394 438 465 11 C
ATOM 2913 C LEU A 286 -7.166 -6.285 2.410 1.00 60.66 C
ANISOU 2913 C LEU A 286 8465 7500 7081 363 487 68 C
ATOM 2914 O LEU A 286 -7.051 -6.289 1.189 1.00 60.29 O
ANISOU 2914 O LEU A 286 8399 7484 7026 276 444 138 O
ATOM 2915 CB LEU A 286 -4.953 -6.630 3.567 1.00 54.39 C
ANISOU 2915 CB LEU A 286 7794 6663 6209 429 516 -25 C
ATOM 2916 CG LEU A 286 -3.600 -6.019 3.933 1.00 58.85 C
ANISOU 2916 CG LEU A 286 8393 7171 6795 465 469 -49 C
ATOM 2917 CD1 LEU A 286 -2.871 -6.879 4.938 1.00 58.65 C
ANISOU 2917 CD1 LEU A 286 8445 7143 6694 505 531 -114 C
ATOM 2918 CD2 LEU A 286 -2.737 -5.793 2.699 1.00 60.98 C
ANISOU 2918 CD2 LEU A 286 8651 7446 7071 385 415 22 C
ATOM 2919 N THR A 287 -8.226 -6.811 3.054 1.00 58.79 N
ANISOU 2919 N THR A 287 8217 7283 6837 396 552 40 N
ATOM 2920 CA THR A 287 -9.386 -7.422 2.403 1.00 59.48 C
ANISOU 2920 CA THR A 287 8263 7417 6920 336 571 90 C
ATOM 2921 C THR A 287 -10.177 -6.310 1.686 1.00 65.64 C
ANISOU 2921 C THR A 287 8953 8172 7813 314 487 159 C
ATOM 2922 O THR A 287 -10.607 -6.504 0.552 1.00 65.24 O
ANISOU 2922 O THR A 287 8869 8159 7759 224 451 232 O
ATOM 2923 CB THR A 287 -10.196 -8.216 3.450 1.00 68.57 C
ANISOU 2923 CB THR A 287 9423 8586 8044 391 664 44 C
ATOM 2924 OG1 THR A 287 -9.789 -9.583 3.403 1.00 68.90 O
ANISOU 2924 OG1 THR A 287 9522 8671 7986 349 725 33 O
ATOM 2925 CG2 THR A 287 -11.706 -8.117 3.260 1.00 67.61 C
ANISOU 2925 CG2 THR A 287 9222 8473 7993 384 668 86 C
ATOM 2926 N SER A 288 -10.315 -5.136 2.338 1.00 64.20 N
ANISOU 2926 N SER A 288 8730 7927 7736 393 451 133 N
ATOM 2927 CA SER A 288 -11.003 -3.952 1.815 1.00 65.45 C
ANISOU 2927 CA SER A 288 8793 8043 8034 386 365 192 C
ATOM 2928 C SER A 288 -10.269 -3.366 0.598 1.00 70.79 C
ANISOU 2928 C SER A 288 9450 8719 8730 304 266 278 C
ATOM 2929 O SER A 288 -10.902 -2.753 -0.262 1.00 70.78 O
ANISOU 2929 O SER A 288 9369 8713 8811 250 193 367 O
ATOM 2930 CB SER A 288 -11.119 -2.887 2.900 1.00 69.85 C
ANISOU 2930 CB SER A 288 9320 8525 8697 498 355 121 C
ATOM 2931 OG SER A 288 -11.571 -3.404 4.141 1.00 79.24 O
ANISOU 2931 OG SER A 288 10539 9726 9844 580 453 32 O
ATOM 2932 N LEU A 289 -8.935 -3.568 0.536 1.00 68.29 N
ANISOU 2932 N LEU A 289 9200 8408 8337 294 265 259 N
ATOM 2933 CA LEU A 289 -8.028 -3.120 -0.527 1.00 68.78 C
ANISOU 2933 CA LEU A 289 9256 8481 8398 221 188 335 C
ATOM 2934 C LEU A 289 -8.351 -3.802 -1.877 1.00 74.39 C
ANISOU 2934 C LEU A 289 9956 9276 9031 98 178 420 C
ATOM 2935 O LEU A 289 -8.018 -3.246 -2.927 1.00 74.04 O
ANISOU 2935 O LEU A 289 9877 9252 9003 26 101 509 O
ATOM 2936 CB LEU A 289 -6.575 -3.416 -0.100 1.00 68.22 C
ANISOU 2936 CB LEU A 289 9267 8400 8253 246 217 280 C
ATOM 2937 CG LEU A 289 -5.431 -2.796 -0.899 1.00 72.95 C
ANISOU 2937 CG LEU A 289 9860 8992 8864 198 144 344 C
ATOM 2938 CD1 LEU A 289 -5.057 -1.428 -0.357 1.00 73.51 C
ANISOU 2938 CD1 LEU A 289 9887 8969 9076 269 63 341 C
ATOM 2939 CD2 LEU A 289 -4.213 -3.695 -0.864 1.00 74.70 C
ANISOU 2939 CD2 LEU A 289 10169 9244 8970 183 204 303 C
ATOM 2940 N ASN A 290 -9.015 -4.982 -1.849 1.00 72.41 N
ANISOU 2940 N ASN A 290 9733 9078 8699 73 251 394 N
ATOM 2941 CA ASN A 290 -9.397 -5.724 -3.055 1.00 73.16 C
ANISOU 2941 CA ASN A 290 9826 9255 8717 -40 244 455 C
ATOM 2942 C ASN A 290 -10.466 -4.955 -3.853 1.00 80.06 C
ANISOU 2942 C ASN A 290 10604 10130 9683 -95 154 560 C
ATOM 2943 O ASN A 290 -10.438 -5.006 -5.078 1.00 79.83 O
ANISOU 2943 O ASN A 290 10561 10164 9609 -197 100 640 O
ATOM 2944 CB ASN A 290 -9.855 -7.164 -2.719 1.00 73.17 C
ANISOU 2944 CB ASN A 290 9875 9296 8630 -45 340 396 C
ATOM 2945 CG ASN A 290 -11.349 -7.424 -2.664 1.00 94.32 C
ANISOU 2945 CG ASN A 290 12499 11977 11361 -47 348 418 C
ATOM 2946 OD1 ASN A 290 -12.015 -7.612 -3.688 1.00 89.52 O
ANISOU 2946 OD1 ASN A 290 11849 11410 10753 -133 299 490 O
ATOM 2947 ND2 ASN A 290 -11.895 -7.525 -1.466 1.00 84.61 N
ANISOU 2947 ND2 ASN A 290 11271 10711 10166 43 414 357 N
ATOM 2948 N ALA A 291 -11.376 -4.228 -3.160 1.00 78.93 N
ANISOU 2948 N ALA A 291 10395 9923 9673 -27 137 559 N
ATOM 2949 CA ALA A 291 -12.462 -3.440 -3.761 1.00 80.52 C
ANISOU 2949 CA ALA A 291 10492 10107 9994 -67 50 658 C
ATOM 2950 C ALA A 291 -11.940 -2.326 -4.682 1.00 87.31 C
ANISOU 2950 C ALA A 291 11299 10957 10919 -119 -65 758 C
ATOM 2951 O ALA A 291 -12.625 -1.957 -5.639 1.00 87.53 O
ANISOU 2951 O ALA A 291 11254 11006 10995 -201 -148 869 O
ATOM 2952 CB ALA A 291 -13.330 -2.837 -2.670 1.00 81.61 C
ANISOU 2952 CB ALA A 291 10571 10165 10272 35 68 615 C
ATOM 2953 N CYS A 292 -10.733 -1.805 -4.392 1.00 85.59 N
ANISOU 2953 N CYS A 292 11112 10705 10705 -75 -74 727 N
ATOM 2954 CA CYS A 292 -10.067 -0.743 -5.151 1.00 86.72 C
ANISOU 2954 CA CYS A 292 11204 10830 10914 -114 -179 820 C
ATOM 2955 C CYS A 292 -9.034 -1.341 -6.132 1.00 92.51 C
ANISOU 2955 C CYS A 292 11997 11658 11493 -208 -174 861 C
ATOM 2956 O CYS A 292 -8.449 -0.600 -6.926 1.00 92.41 O
ANISOU 2956 O CYS A 292 11945 11656 11511 -260 -256 956 O
ATOM 2957 CB CYS A 292 -9.412 0.264 -4.205 1.00 86.96 C
ANISOU 2957 CB CYS A 292 11225 10757 11060 -6 -198 761 C
ATOM 2958 SG CYS A 292 -10.299 0.516 -2.641 1.00 90.97 S
ANISOU 2958 SG CYS A 292 11711 11172 11681 132 -143 642 S
ATOM 2959 N LEU A 293 -8.817 -2.675 -6.075 1.00 90.30 N
ANISOU 2959 N LEU A 293 11807 11447 11056 -231 -78 790 N
ATOM 2960 CA LEU A 293 -7.847 -3.387 -6.915 1.00 90.70 C
ANISOU 2960 CA LEU A 293 11920 11588 10956 -311 -52 801 C
ATOM 2961 C LEU A 293 -8.498 -4.396 -7.886 1.00 96.47 C
ANISOU 2961 C LEU A 293 12672 12423 11561 -414 -28 818 C
ATOM 2962 O LEU A 293 -7.859 -4.766 -8.872 1.00 96.21 O
ANISOU 2962 O LEU A 293 12671 12476 11407 -499 -23 843 O
ATOM 2963 CB LEU A 293 -6.823 -4.111 -6.030 1.00 89.95 C
ANISOU 2963 CB LEU A 293 11915 11469 10794 -242 41 684 C
ATOM 2964 N ASN A 294 -9.748 -4.838 -7.613 1.00 94.35 N
ANISOU 2964 N ASN A 294 12383 12147 11320 -408 -11 802 N
ATOM 2965 CA ASN A 294 -10.487 -5.790 -8.455 1.00 95.06 C
ANISOU 2965 CA ASN A 294 12486 12323 11308 -501 2 814 C
ATOM 2966 C ASN A 294 -10.807 -5.230 -9.861 1.00101.55 C
ANISOU 2966 C ASN A 294 13252 13220 12112 -623 -103 948 C
ATOM 2967 O ASN A 294 -10.631 -5.991 -10.815 1.00101.36 O
ANISOU 2967 O ASN A 294 13269 13297 11945 -717 -90 949 O
ATOM 2968 CB ASN A 294 -11.775 -6.270 -7.777 1.00 95.80 C
ANISOU 2968 CB ASN A 294 12560 12379 11459 -459 38 777 C
ATOM 2969 CG ASN A 294 -11.615 -7.505 -6.917 1.00118.10 C
ANISOU 2969 CG ASN A 294 15460 15194 14217 -400 155 654 C
ATOM 2970 OD1 ASN A 294 -10.562 -7.764 -6.318 1.00111.97 O
ANISOU 2970 OD1 ASN A 294 14746 14401 13396 -349 214 581 O
ATOM 2971 ND2 ASN A 294 -12.677 -8.289 -6.819 1.00109.86 N
ANISOU 2971 ND2 ASN A 294 14407 14157 13179 -406 186 637 N
ATOM 2972 N PRO A 295 -11.214 -3.940 -10.063 1.00100.07 N
ANISOU 2972 N PRO A 295 12970 12993 12060 -631 -209 1061 N
ATOM 2973 CA PRO A 295 -11.498 -3.473 -11.435 1.00101.30 C
ANISOU 2973 CA PRO A 295 13070 13231 12187 -758 -313 1201 C
ATOM 2974 C PRO A 295 -10.260 -3.362 -12.342 1.00106.58 C
ANISOU 2974 C PRO A 295 13771 13989 12738 -829 -328 1245 C
ATOM 2975 O PRO A 295 -10.421 -3.064 -13.527 1.00106.98 O
ANISOU 2975 O PRO A 295 13783 14128 12735 -943 -408 1361 O
ATOM 2976 CB PRO A 295 -12.129 -2.092 -11.212 1.00103.59 C
ANISOU 2976 CB PRO A 295 13246 13432 12682 -728 -417 1303 C
ATOM 2977 CG PRO A 295 -12.578 -2.090 -9.788 1.00107.37 C
ANISOU 2977 CG PRO A 295 13721 13797 13277 -597 -354 1201 C
ATOM 2978 CD PRO A 295 -11.515 -2.870 -9.091 1.00101.84 C
ANISOU 2978 CD PRO A 295 13124 13096 12473 -530 -242 1068 C
ATOM 2979 N PHE A 296 -9.043 -3.629 -11.809 1.00103.41 N
ANISOU 2979 N PHE A 296 13435 13567 12289 -767 -251 1157 N
ATOM 2980 CA PHE A 296 -7.793 -3.581 -12.576 1.00103.86 C
ANISOU 2980 CA PHE A 296 13522 13702 12238 -824 -247 1189 C
ATOM 2981 C PHE A 296 -7.683 -4.753 -13.564 1.00109.21 C
ANISOU 2981 C PHE A 296 14265 14515 12714 -925 -194 1151 C
ATOM 2982 O PHE A 296 -6.902 -4.666 -14.512 1.00109.17 O
ANISOU 2982 O PHE A 296 14270 14607 12604 -1003 -204 1203 O
ATOM 2983 CB PHE A 296 -6.567 -3.520 -11.654 1.00104.85 C
ANISOU 2983 CB PHE A 296 13692 13754 12393 -724 -183 1106 C
ATOM 2984 CG PHE A 296 -6.225 -2.117 -11.208 1.00106.63 C
ANISOU 2984 CG PHE A 296 13844 13886 12784 -668 -266 1184 C
ATOM 2985 CD1 PHE A 296 -5.361 -1.324 -11.955 1.00110.27 C
ANISOU 2985 CD1 PHE A 296 14264 14389 13246 -726 -332 1299 C
ATOM 2986 CD2 PHE A 296 -6.776 -1.584 -10.049 1.00108.55 C
ANISOU 2986 CD2 PHE A 296 14054 14001 13188 -559 -279 1140 C
ATOM 2987 CE1 PHE A 296 -5.052 -0.022 -11.548 1.00111.42 C
ANISOU 2987 CE1 PHE A 296 14334 14439 13564 -675 -417 1373 C
ATOM 2988 CE2 PHE A 296 -6.465 -0.282 -9.642 1.00111.66 C
ANISOU 2988 CE2 PHE A 296 14376 14301 13746 -506 -361 1200 C
ATOM 2989 CZ PHE A 296 -5.605 0.489 -10.394 1.00110.24 C
ANISOU 2989 CZ PHE A 296 14154 14154 13579 -564 -434 1317 C
ATOM 2990 N ILE A 297 -8.494 -5.820 -13.372 1.00106.72 N
ANISOU 2990 N ILE A 297 13988 14208 12351 -927 -141 1065 N
ATOM 2991 CA ILE A 297 -8.568 -6.976 -14.281 1.00107.46 C
ANISOU 2991 CA ILE A 297 14138 14419 12272 -1021 -100 1016 C
ATOM 2992 C ILE A 297 -9.199 -6.481 -15.599 1.00114.25 C
ANISOU 2992 C ILE A 297 14943 15384 13084 -1151 -210 1154 C
ATOM 2993 O ILE A 297 -8.798 -6.913 -16.683 1.00114.50 O
ANISOU 2993 O ILE A 297 15006 15543 12954 -1252 -205 1160 O
ATOM 2994 CB ILE A 297 -9.349 -8.176 -13.650 1.00110.00 C
ANISOU 2994 CB ILE A 297 14502 14702 12592 -981 -29 899 C
ATOM 2995 CG1 ILE A 297 -8.813 -8.530 -12.242 1.00109.29 C
ANISOU 2995 CG1 ILE A 297 14459 14511 12556 -854 70 782 C
ATOM 2996 CG2 ILE A 297 -9.322 -9.411 -14.570 1.00111.10 C
ANISOU 2996 CG2 ILE A 297 14695 14953 12566 -1079 7 838 C
ATOM 2997 CD1 ILE A 297 -9.804 -9.244 -11.320 1.00115.91 C
ANISOU 2997 CD1 ILE A 297 15303 15276 13461 -786 117 709 C
ATOM 2998 N TYR A 298 -10.154 -5.533 -15.485 1.00112.50 N
ANISOU 2998 N TYR A 298 14633 15105 13007 -1147 -310 1266 N
ATOM 2999 CA TYR A 298 -10.852 -4.896 -16.600 1.00114.10 C
ANISOU 2999 CA TYR A 298 14764 15384 13204 -1262 -435 1421 C
ATOM 3000 C TYR A 298 -9.981 -3.828 -17.266 1.00119.95 C
ANISOU 3000 C TYR A 298 15457 16166 13955 -1303 -503 1551 C
ATOM 3001 O TYR A 298 -10.026 -3.697 -18.489 1.00120.60 O
ANISOU 3001 O TYR A 298 15512 16369 13941 -1426 -577 1665 O
ATOM 3002 CB TYR A 298 -12.168 -4.270 -16.120 1.00115.49 C
ANISOU 3002 CB TYR A 298 14855 15463 13562 -1232 -511 1487 C
ATOM 3003 N PHE A 299 -9.203 -3.061 -16.467 1.00117.02 N
ANISOU 3003 N PHE A 299 15070 15693 13698 -1202 -484 1539 N
ATOM 3004 CA PHE A 299 -8.328 -1.991 -16.959 1.00117.87 C
ANISOU 3004 CA PHE A 299 15125 15819 13844 -1226 -549 1663 C
ATOM 3005 C PHE A 299 -7.127 -2.547 -17.744 1.00123.39 C
ANISOU 3005 C PHE A 299 15887 16649 14345 -1292 -487 1643 C
ATOM 3006 O PHE A 299 -6.649 -1.879 -18.663 1.00123.69 O
ANISOU 3006 O PHE A 299 15877 16766 14352 -1369 -552 1779 O
ATOM 3007 CB PHE A 299 -7.850 -1.083 -15.808 1.00118.96 C
ANISOU 3007 CB PHE A 299 15228 15799 14171 -1094 -550 1642 C
ATOM 3008 CG PHE A 299 -8.936 -0.401 -14.998 1.00120.50 C
ANISOU 3008 CG PHE A 299 15346 15864 14575 -1025 -613 1665 C
ATOM 3009 CD1 PHE A 299 -10.061 0.136 -15.618 1.00124.51 C
ANISOU 3009 CD1 PHE A 299 15767 16390 15150 -1102 -722 1792 C
ATOM 3010 CD2 PHE A 299 -8.803 -0.240 -13.624 1.00121.77 C
ANISOU 3010 CD2 PHE A 299 15515 15883 14868 -885 -567 1561 C
ATOM 3011 CE1 PHE A 299 -11.058 0.769 -14.869 1.00125.47 C
ANISOU 3011 CE1 PHE A 299 15810 16386 15477 -1035 -773 1809 C
ATOM 3012 CE2 PHE A 299 -9.801 0.395 -12.877 1.00124.66 C
ANISOU 3012 CE2 PHE A 299 15807 16135 15425 -819 -615 1571 C
ATOM 3013 CZ PHE A 299 -10.919 0.899 -13.505 1.00123.67 C
ANISOU 3013 CZ PHE A 299 15593 16023 15375 -892 -715 1694 C
ATOM 3014 N PHE A 300 -6.655 -3.764 -17.393 1.00120.61 N
ANISOU 3014 N PHE A 300 15637 16322 13866 -1266 -361 1481 N
ATOM 3015 CA PHE A 300 -5.550 -4.434 -18.083 1.00121.29 C
ANISOU 3015 CA PHE A 300 15786 16530 13767 -1324 -284 1437 C
ATOM 3016 C PHE A 300 -6.124 -5.425 -19.115 1.00127.02 C
ANISOU 3016 C PHE A 300 16556 17401 14307 -1439 -271 1403 C
ATOM 3017 O PHE A 300 -6.003 -6.646 -18.965 1.00126.13 O
ANISOU 3017 O PHE A 300 16522 17303 14099 -1425 -170 1250 O
ATOM 3018 CB PHE A 300 -4.591 -5.121 -17.085 1.00122.05 C
ANISOU 3018 CB PHE A 300 15958 16551 13864 -1219 -157 1280 C
ATOM 3019 CG PHE A 300 -3.660 -4.192 -16.338 1.00123.21 C
ANISOU 3019 CG PHE A 300 16074 16588 14151 -1126 -168 1313 C
ATOM 3020 CD1 PHE A 300 -2.613 -3.553 -16.994 1.00126.96 C
ANISOU 3020 CD1 PHE A 300 16512 17118 14611 -1168 -202 1423 C
ATOM 3021 CD2 PHE A 300 -3.799 -3.994 -14.970 1.00124.42 C
ANISOU 3021 CD2 PHE A 300 16239 16589 14445 -997 -140 1229 C
ATOM 3022 CE1 PHE A 300 -1.748 -2.700 -16.302 1.00127.46 C
ANISOU 3022 CE1 PHE A 300 16544 17071 14813 -1082 -218 1451 C
ATOM 3023 CE2 PHE A 300 -2.931 -3.144 -14.277 1.00126.86 C
ANISOU 3023 CE2 PHE A 300 16523 16796 14880 -913 -156 1249 C
ATOM 3024 CZ PHE A 300 -1.911 -2.503 -14.947 1.00125.52 C
ANISOU 3024 CZ PHE A 300 16314 16670 14708 -955 -198 1359 C
ATOM 3025 N LEU A 301 -6.772 -4.870 -20.159 1.00125.62 N
ANISOU 3025 N LEU A 301 16320 17324 14086 -1555 -380 1550 N
ATOM 3026 CA LEU A 301 -7.412 -5.611 -21.251 1.00126.74 C
ANISOU 3026 CA LEU A 301 16492 17611 14054 -1678 -397 1541 C
ATOM 3027 C LEU A 301 -7.107 -4.976 -22.622 1.00132.68 C
ANISOU 3027 C LEU A 301 17206 18534 14673 -1814 -471 1696 C
ATOM 3028 O LEU A 301 -6.410 -3.959 -22.692 1.00132.36 O
ANISOU 3028 O LEU A 301 17120 18497 14673 -1808 -492 1799 O
ATOM 3029 CB LEU A 301 -8.935 -5.661 -21.018 1.00126.96 C
ANISOU 3029 CB LEU A 301 16482 17579 14178 -1685 -475 1568 C
ATOM 3030 CG LEU A 301 -9.543 -7.040 -20.776 1.00131.38 C
ANISOU 3030 CG LEU A 301 17113 18128 14676 -1672 -402 1405 C
ATOM 3031 CD1 LEU A 301 -10.752 -6.949 -19.872 1.00131.10 C
ANISOU 3031 CD1 LEU A 301 17034 17955 14821 -1603 -442 1409 C
ATOM 3032 CD2 LEU A 301 -9.918 -7.723 -22.084 1.00135.20 C
ANISOU 3032 CD2 LEU A 301 17631 18780 14959 -1814 -430 1401 C
ATOM 3033 N CYS A 302 -7.631 -5.587 -23.708 1.00130.89 N
ANISOU 3033 N CYS A 302 16997 18451 14283 -1940 -509 1710 N
ATOM 3034 CA CYS A 302 -7.465 -5.126 -25.090 1.00132.50 C
ANISOU 3034 CA CYS A 302 17171 18842 14332 -2084 -582 1854 C
ATOM 3035 C CYS A 302 -8.458 -3.999 -25.415 1.00137.63 C
ANISOU 3035 C CYS A 302 17713 19481 15099 -2148 -753 2067 C
ATOM 3036 O CYS A 302 -8.079 -3.030 -26.077 1.00138.18 O
ANISOU 3036 O CYS A 302 17719 19641 15143 -2227 -832 2243 O
ATOM 3037 CB CYS A 302 -7.611 -6.291 -26.066 1.00133.68 C
ANISOU 3037 CB CYS A 302 17402 19159 14232 -2188 -533 1746 C
ATOM 3038 N LYS A 303 -9.720 -4.131 -24.951 1.00134.17 N
ANISOU 3038 N LYS A 303 17250 18934 14795 -2118 -809 2057 N
ATOM 3039 CA LYS A 303 -10.789 -3.155 -25.177 1.00134.88 C
ANISOU 3039 CA LYS A 303 17230 18990 15030 -2169 -971 2251 C
ATOM 3040 C LYS A 303 -10.971 -2.242 -23.942 1.00137.94 C
ANISOU 3040 C LYS A 303 17537 19168 15706 -2037 -1001 2295 C
ATOM 3041 O LYS A 303 -12.087 -2.087 -23.435 1.00137.37 O
ANISOU 3041 O LYS A 303 17415 18982 15797 -2002 -1059 2313 O
ATOM 3042 CB LYS A 303 -12.103 -3.876 -25.543 1.00137.92 C
ANISOU 3042 CB LYS A 303 17627 19397 15381 -2234 -1025 2227 C
ATOM 3043 N SER A 304 -9.859 -1.635 -23.468 1.00133.89 N
ANISOU 3043 N SER A 304 17011 18603 15259 -1963 -958 2305 N
ATOM 3044 CA SER A 304 -9.840 -0.718 -22.320 1.00132.75 C
ANISOU 3044 CA SER A 304 16800 18263 15374 -1831 -977 2321 C
ATOM 3045 C SER A 304 -8.660 0.247 -22.388 1.00136.60 C
ANISOU 3045 C SER A 304 17244 18745 15915 -1810 -989 2413 C
ATOM 3046 O SER A 304 -8.792 1.390 -21.946 1.00136.10 O
ANISOU 3046 O SER A 304 17085 18551 16076 -1749 -1067 2508 O
ATOM 3047 CB SER A 304 -9.800 -1.483 -21.001 1.00134.58 C
ANISOU 3047 CB SER A 304 17113 18372 15652 -1691 -847 2107 C
ATOM 3048 OG SER A 304 -9.883 -0.595 -19.897 1.00141.98 O
ANISOU 3048 OG SER A 304 17986 19126 16835 -1573 -875 2110 O
ATOM 3049 N PHE A 305 -7.508 -0.229 -22.926 1.00133.29 N
ANISOU 3049 N PHE A 305 16891 18458 15293 -1855 -907 2376 N
ATOM 3050 CA PHE A 305 -6.234 0.486 -23.104 1.00164.26 C
ANISOU 3050 CA PHE A 305 20786 22410 19214 -1852 -899 2456 C
ATOM 3051 C PHE A 305 -5.709 1.046 -21.781 1.00192.59 C
ANISOU 3051 C PHE A 305 24353 25803 23017 -1698 -871 2401 C
ATOM 3052 O PHE A 305 -5.550 0.296 -20.823 1.00152.64 O
ANISOU 3052 O PHE A 305 19372 20652 17971 -1591 -764 2216 O
ATOM 3053 CB PHE A 305 -6.358 1.613 -24.143 1.00167.63 C
ANISOU 3053 CB PHE A 305 21103 22939 19651 -1978 -1044 2708 C
TER 3054 PHE A 305
HETATM 3055 OAI 6AT A1201 -15.253 -8.614 18.681 1.00 83.20 O
HETATM 3056 PBE 6AT A1201 -15.967 -7.455 17.805 1.00 82.82 P
HETATM 3057 OAH 6AT A1201 -17.415 -7.741 17.788 1.00 83.71 O
HETATM 3058 OAC 6AT A1201 -15.478 -6.136 18.276 1.00 83.02 O
HETATM 3059 OAS 6AT A1201 -15.417 -7.693 16.309 1.00 79.35 O
HETATM 3060 PBG 6AT A1201 -16.009 -6.797 15.110 1.00 75.95 P
HETATM 3061 OAK 6AT A1201 -14.889 -6.804 13.966 1.00 76.13 O
HETATM 3062 OAE 6AT A1201 -16.323 -5.412 15.525 1.00 76.06 O
HETATM 3063 OAT 6AT A1201 -17.328 -7.568 14.565 1.00 72.86 O
HETATM 3064 PBF 6AT A1201 -17.329 -8.890 13.622 1.00 70.11 P
HETATM 3065 OAJ 6AT A1201 -17.621 -10.136 14.592 1.00 69.82 O
HETATM 3066 OAD 6AT A1201 -16.099 -9.083 12.828 1.00 70.33 O
HETATM 3067 O5' 6AT A1201 -18.623 -8.793 12.662 1.00 68.72 O
HETATM 3068 C5' 6AT A1201 -19.741 -7.948 12.961 1.00 67.58 C
HETATM 3069 C4' 6AT A1201 -21.026 -8.528 12.351 1.00 66.55 C
HETATM 3070 O4' 6AT A1201 -20.801 -9.226 11.098 1.00 65.97 O
HETATM 3071 C3' 6AT A1201 -21.699 -9.490 13.314 1.00 66.03 C
HETATM 3072 O3' 6AT A1201 -23.119 -9.237 13.328 1.00 66.15 O
HETATM 3073 C2' 6AT A1201 -21.387 -10.852 12.729 1.00 65.38 C
HETATM 3074 O2' 6AT A1201 -22.443 -11.789 12.972 1.00 65.15 O
HETATM 3075 C1' 6AT A1201 -21.232 -10.599 11.235 1.00 65.10 C
HETATM 3076 N9 6AT A1201 -20.192 -11.473 10.602 1.00 64.02 N
HETATM 3077 C8 6AT A1201 -18.988 -11.769 11.094 1.00 63.69 C
HETATM 3078 N7 6AT A1201 -18.361 -12.556 10.229 1.00 63.42 N
HETATM 3079 C5 6AT A1201 -19.159 -12.727 9.178 1.00 63.20 C
HETATM 3080 C4 6AT A1201 -20.294 -12.051 9.404 1.00 63.39 C
HETATM 3081 N3 6AT A1201 -21.281 -12.058 8.479 1.00 62.93 N
HETATM 3082 C2 6AT A1201 -21.138 -12.750 7.331 1.00 62.82 C
HETATM 3083 S2 6AT A1201 -22.466 -12.737 6.137 1.00 62.93 S
HETATM 3084 CAA 6AT A1201 -21.719 -13.469 4.692 1.00 62.93 C
HETATM 3085 N1 6AT A1201 -19.990 -13.427 7.109 1.00 62.66 N
HETATM 3086 C6 6AT A1201 -19.014 -13.412 8.036 1.00 62.81 C
HETATM 3087 N6 6AT A1201 -17.866 -14.067 7.861 1.00 62.76 N
HETATM 3088 C9 OLC A1202 0.116 -7.598 8.236 1.00 75.48 C
HETATM 3089 C8 OLC A1202 -0.251 -7.998 9.665 1.00 75.68 C
HETATM 3090 C24 OLC A1202 -0.866 -5.211 22.460 1.00 82.52 C
HETATM 3091 C7 OLC A1202 0.082 -6.848 10.617 1.00 76.18 C
HETATM 3092 C6 OLC A1202 -0.658 -7.049 11.942 1.00 76.73 C
HETATM 3093 C5 OLC A1202 0.267 -6.694 13.109 1.00 77.18 C
HETATM 3094 C4 OLC A1202 -0.455 -5.751 14.075 1.00 77.56 C
HETATM 3095 C3 OLC A1202 -0.649 -6.457 15.417 1.00 78.21 C
HETATM 3096 C2 OLC A1202 -0.807 -5.423 16.539 1.00 79.18 C
HETATM 3097 C21 OLC A1202 -0.558 -5.080 19.965 1.00 81.84 C
HETATM 3098 C1 OLC A1202 -0.930 -6.121 17.906 1.00 80.39 C
HETATM 3099 C22 OLC A1202 0.003 -5.657 21.273 1.00 82.28 C
HETATM 3100 O19 OLC A1202 -1.811 -6.958 18.117 1.00 80.71 O
HETATM 3101 O25 OLC A1202 -2.045 -6.020 22.567 1.00 82.55 O
HETATM 3102 O23 OLC A1202 0.065 -7.087 21.209 1.00 82.37 O
HETATM 3103 O20 OLC A1202 0.013 -5.753 18.827 1.00 81.20 O
HETATM 3104 C9 OLC A1203 -2.396 -3.316 7.038 1.00 92.31 C
HETATM 3105 C8 OLC A1203 -3.172 -2.540 8.107 1.00 92.25 C
HETATM 3106 C24 OLC A1203 -1.179 -1.317 20.098 1.00 95.24 C
HETATM 3107 C7 OLC A1203 -2.284 -1.454 8.731 1.00 92.28 C
HETATM 3108 C6 OLC A1203 -1.495 -2.019 9.921 1.00 92.52 C
HETATM 3109 C5 OLC A1203 -2.143 -1.585 11.239 1.00 92.74 C
HETATM 3110 C4 OLC A1203 -1.097 -1.585 12.358 1.00 92.94 C
HETATM 3111 C3 OLC A1203 -1.711 -2.163 13.637 1.00 93.26 C
HETATM 3112 C2 OLC A1203 -1.834 -1.061 14.695 1.00 93.59 C
HETATM 3113 C21 OLC A1203 -2.405 -0.758 17.990 1.00 94.74 C
HETATM 3114 C1 OLC A1203 -2.808 -1.491 15.806 1.00 94.03 C
HETATM 3115 C22 OLC A1203 -2.536 -1.374 19.385 1.00 95.04 C
HETATM 3116 O19 OLC A1203 -4.019 -1.569 15.586 1.00 94.09 O
HETATM 3117 O25 OLC A1203 -1.319 -1.727 21.463 1.00 95.33 O
HETATM 3118 O23 OLC A1203 -3.513 -0.642 20.134 1.00 95.06 O
HETATM 3119 O20 OLC A1203 -2.228 -1.794 17.007 1.00 94.42 O
HETATM 3120 O HOH A1301 -14.275 -16.110 8.134 1.00 31.45 O
CONECT 19 2783
CONECT 652 1214
CONECT 1214 652
CONECT 2783 19
CONECT 3055 3056
CONECT 3056 3055 3057 3058 3059
CONECT 3057 3056
CONECT 3058 3056
CONECT 3059 3056 3060
CONECT 3060 3059 3061 3062 3063
CONECT 3061 3060
CONECT 3062 3060
CONECT 3063 3060 3064
CONECT 3064 3063 3065 3066 3067
CONECT 3065 3064
CONECT 3066 3064
CONECT 3067 3064 3068
CONECT 3068 3067 3069
CONECT 3069 3068 3070 3071
CONECT 3070 3069 3075
CONECT 3071 3069 3072 3073
CONECT 3072 3071
CONECT 3073 3071 3074 3075
CONECT 3074 3073
CONECT 3075 3070 3073 3076
CONECT 3076 3075 3077 3080
CONECT 3077 3076 3078
CONECT 3078 3077 3079
CONECT 3079 3078 3080 3086
CONECT 3080 3076 3079 3081
CONECT 3081 3080 3082
CONECT 3082 3081 3083 3085
CONECT 3083 3082 3084
CONECT 3084 3083
CONECT 3085 3082 3086
CONECT 3086 3079 3085 3087
CONECT 3087 3086
CONECT 3088 3089
CONECT 3089 3088 3091
CONECT 3090 3099 3101
CONECT 3091 3089 3092
CONECT 3092 3091 3093
CONECT 3093 3092 3094
CONECT 3094 3093 3095
CONECT 3095 3094 3096
CONECT 3096 3095 3098
CONECT 3097 3099 3103
CONECT 3098 3096 3100 3103
CONECT 3099 3090 3097 3102
CONECT 3100 3098
CONECT 3101 3090
CONECT 3102 3099
CONECT 3103 3097 3098
CONECT 3104 3105
CONECT 3105 3104 3107
CONECT 3106 3115 3117
CONECT 3107 3105 3108
CONECT 3108 3107 3109
CONECT 3109 3108 3110
CONECT 3110 3109 3111
CONECT 3111 3110 3112
CONECT 3112 3111 3114
CONECT 3113 3115 3119
CONECT 3114 3112 3116 3119
CONECT 3115 3106 3113 3118
CONECT 3116 3114
CONECT 3117 3106
CONECT 3118 3115
CONECT 3119 3113 3114
MASTER 416 0 3 19 0 0 8 6 3112 1 69 36
END