HEADER SIGNALING PROTEIN 11-FEB-18 5ZBH
TITLE THE CRYSTAL STRUCTURE OF HUMAN NEUROPEPTIDE Y Y1 RECEPTOR WITH BMS-
TITLE 2 193885
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPEPTIDE Y RECEPTOR TYPE 1,T4 LYSOZYME,NEUROPEPTIDE Y
COMPND 3 RECEPTOR TYPE 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 2-241,UNP RESIDUES 2-161,UNP RESIDUES 250-358;
COMPND 6 SYNONYM: NPY1-R,LYSIS PROTEIN,LYSOZYME,MURAMIDASE,NPY1-R;
COMPND 7 EC: 3.2.1.17;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4T;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 857277;
SOURCE 5 GENE: NPY1R, NPYR, NPYY1, E, T4TP126;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS G PROTEIN-COUPLED RECEPTOR NEUROPEPTIDE Y Y1 RECEPTOR INHIBITOR
KEYWDS 2 COMPLEX STRUCTURE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.YANG,S.HAN,Q.ZHAO,B.WU
REVDAT 3 09-MAY-18 5ZBH 1 JRNL
REVDAT 2 02-MAY-18 5ZBH 1 JRNL
REVDAT 1 25-APR-18 5ZBH 0
JRNL AUTH Z.YANG,S.HAN,M.KELLER,A.KAISER,B.J.BENDER,M.BOSSE,K.BURKERT,
JRNL AUTH 2 L.M.KOGLER,D.WIFLING,G.BERNHARDT,N.PLANK,T.LITTMANN,
JRNL AUTH 3 P.SCHMIDT,C.YI,B.LI,S.YE,R.ZHANG,B.XU,D.LARHAMMAR,
JRNL AUTH 4 R.C.STEVENS,D.HUSTER,J.MEILER,Q.ZHAO,A.G.BECK-SICKINGER,
JRNL AUTH 5 A.BUSCHAUER,B.WU
JRNL TITL STRUCTURAL BASIS OF LIGAND BINDING MODES AT THE NEUROPEPTIDE
JRNL TITL 2 Y Y1RECEPTOR
JRNL REF NATURE V. 556 520 2018
JRNL REFN ESSN 1476-4687
JRNL PMID 29670288
JRNL DOI 10.1038/S41586-018-0046-X
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 15600
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 : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 797
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.95
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2458
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2720
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2349
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.43
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 117.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.44550
REMARK 3 B22 (A**2) : -20.77820
REMARK 3 B33 (A**2) : 13.33270
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.520
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.258
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.366
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.454
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.375
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 : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3785 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5154 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1291 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 77 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 575 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3785 ; 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 : 509 ; 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 : 4443 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.11
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.17
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4450 29.2797 -27.7696
REMARK 3 T TENSOR
REMARK 3 T11: -0.1576 T22: 0.1686
REMARK 3 T33: -0.2744 T12: -0.0165
REMARK 3 T13: -0.0325 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 1.4362
REMARK 3 L33: 2.1889 L12: 0.0027
REMARK 3 L13: 0.0512 L23: 1.3400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0516 S12: -0.0527 S13: 0.0061
REMARK 3 S21: 0.1753 S22: 0.0239 S23: 0.0281
REMARK 3 S31: 0.1989 S32: 0.3511 S33: 0.0277
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ZBH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2-7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15601
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.2-7.6, 20% PEG400, PH
REMARK 280 7.4, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.91000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.91000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.29000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.12000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.29000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.12000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.91000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.29000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.12000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.91000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.29000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.12000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 PRO A 1
REMARK 465 ASN A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 PHE A 6
REMARK 465 SER A 7
REMARK 465 GLN A 8
REMARK 465 VAL A 9
REMARK 465 GLU A 10
REMARK 465 ASN A 11
REMARK 465 HIS A 12
REMARK 465 SER A 13
REMARK 465 VAL A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 ASN A 17
REMARK 465 PHE A 18
REMARK 465 SER A 19
REMARK 465 GLU A 20
REMARK 465 LYS A 21
REMARK 465 ASN A 22
REMARK 465 ALA A 23
REMARK 465 GLN A 24
REMARK 465 LEU A 25
REMARK 465 LEU A 26
REMARK 465 ALA A 27
REMARK 465 PHE A 28
REMARK 465 GLU A 29
REMARK 465 ASN A 30
REMARK 465 PHE A 340
REMARK 465 ARG A 341
REMARK 465 SER A 342
REMARK 465 ARG A 343
REMARK 465 ASP A 344
REMARK 465 ASP A 345
REMARK 465 ASP A 346
REMARK 465 TYR A 347
REMARK 465 GLU A 348
REMARK 465 THR A 349
REMARK 465 ILE A 350
REMARK 465 ALA A 351
REMARK 465 MET A 352
REMARK 465 SER A 353
REMARK 465 THR A 354
REMARK 465 MET A 355
REMARK 465 HIS A 356
REMARK 465 THR A 357
REMARK 465 ASP A 358
REMARK 465 GLU A 359
REMARK 465 PHE A 360
REMARK 465 LEU A 361
REMARK 465 GLU A 362
REMARK 465 VAL A 363
REMARK 465 LEU A 364
REMARK 465 PHE A 365
REMARK 465 GLN A 366
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 ASP A 31 CG OD1 OD2
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 HIS A 34 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 71 CG SD CE
REMARK 470 ARG A 149 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 189 CG CD1 CD2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 ASP A 250 CG OD1 OD2
REMARK 470 ASN A 251 CG OD1 ND2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 333 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 334 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 335 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 337 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 HIS A 34 103.56 -162.48
REMARK 500 GLU A 70 -10.66 84.35
REMARK 500 ASN A 152 -13.31 -49.83
REMARK 500 GLU A 182 78.14 -108.01
REMARK 500 TYR A 220 -71.50 -113.74
REMARK 500 ASP A1009 -68.54 -91.83
REMARK 500 PHE A1113 43.84 -90.76
REMARK 500 THR A1141 76.60 -113.57
REMARK 500 TYR A1160 68.81 -102.90
REMARK 500 ASN A 289 56.87 -109.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9AF A 1201
DBREF 5ZBH A 2 241 UNP P25929 NPY1R_HUMAN 2 241
DBREF 5ZBH A 1001 1160 UNP D9IEF7 D9IEF7_BPT4 2 161
DBREF 5ZBH A 250 358 UNP P25929 NPY1R_HUMAN 250 358
SEQADV 5ZBH ASP A -8 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH TYR A -7 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH LYS A -6 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH ASP A -5 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH ASP A -4 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH ASP A -3 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH ASP A -2 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH GLY A -1 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH ALA A 0 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH PRO A 1 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH TRP A 129 UNP P25929 PHE 129 ENGINEERED MUTATION
SEQADV 5ZBH THR A 1053 UNP D9IEF7 CYS 54 ENGINEERED MUTATION
SEQADV 5ZBH ALA A 1096 UNP D9IEF7 CYS 97 ENGINEERED MUTATION
SEQADV 5ZBH GLU A 359 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH PHE A 360 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH LEU A 361 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH GLU A 362 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH VAL A 363 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH LEU A 364 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH PHE A 365 UNP P25929 EXPRESSION TAG
SEQADV 5ZBH GLN A 366 UNP P25929 EXPRESSION TAG
SEQRES 1 A 527 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ASN SER THR
SEQRES 2 A 527 LEU PHE SER GLN VAL GLU ASN HIS SER VAL HIS SER ASN
SEQRES 3 A 527 PHE SER GLU LYS ASN ALA GLN LEU LEU ALA PHE GLU ASN
SEQRES 4 A 527 ASP ASP CYS HIS LEU PRO LEU ALA MET ILE PHE THR LEU
SEQRES 5 A 527 ALA LEU ALA TYR GLY ALA VAL ILE ILE LEU GLY VAL SER
SEQRES 6 A 527 GLY ASN LEU ALA LEU ILE ILE ILE ILE LEU LYS GLN LYS
SEQRES 7 A 527 GLU MET ARG ASN VAL THR ASN ILE LEU ILE VAL ASN LEU
SEQRES 8 A 527 SER PHE SER ASP LEU LEU VAL ALA ILE MET CYS LEU PRO
SEQRES 9 A 527 PHE THR PHE VAL TYR THR LEU MET ASP HIS TRP VAL PHE
SEQRES 10 A 527 GLY GLU ALA MET CYS LYS LEU ASN PRO PHE VAL GLN CYS
SEQRES 11 A 527 VAL SER ILE THR VAL SER ILE TRP SER LEU VAL LEU ILE
SEQRES 12 A 527 ALA VAL GLU ARG HIS GLN LEU ILE ILE ASN PRO ARG GLY
SEQRES 13 A 527 TRP ARG PRO ASN ASN ARG HIS ALA TYR VAL GLY ILE ALA
SEQRES 14 A 527 VAL ILE TRP VAL LEU ALA VAL ALA SER SER LEU PRO PHE
SEQRES 15 A 527 LEU ILE TYR GLN VAL MET THR ASP GLU PRO PHE GLN ASN
SEQRES 16 A 527 VAL THR LEU ASP ALA TYR LYS ASP LYS TYR VAL CYS PHE
SEQRES 17 A 527 ASP GLN PHE PRO SER ASP SER HIS ARG LEU SER TYR THR
SEQRES 18 A 527 THR LEU LEU LEU VAL LEU GLN TYR PHE GLY PRO LEU CYS
SEQRES 19 A 527 PHE ILE PHE ILE CYS TYR PHE LYS ILE TYR ILE ARG LEU
SEQRES 20 A 527 LYS ARG ARG ASN ILE PHE GLU MET LEU ARG ILE ASP GLU
SEQRES 21 A 527 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR
SEQRES 22 A 527 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO
SEQRES 23 A 527 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE
SEQRES 24 A 527 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA
SEQRES 25 A 527 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG
SEQRES 26 A 527 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP
SEQRES 27 A 527 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET
SEQRES 28 A 527 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR
SEQRES 29 A 527 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU
SEQRES 30 A 527 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN
SEQRES 31 A 527 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG
SEQRES 32 A 527 THR GLY THR TRP ASP ALA TYR ASP ASN LYS TYR ARG SER
SEQRES 33 A 527 SER GLU THR LYS ARG ILE ASN ILE MET LEU LEU SER ILE
SEQRES 34 A 527 VAL VAL ALA PHE ALA VAL CYS TRP LEU PRO LEU THR ILE
SEQRES 35 A 527 PHE ASN THR VAL PHE ASP TRP ASN HIS GLN ILE ILE ALA
SEQRES 36 A 527 THR CYS ASN HIS ASN LEU LEU PHE LEU LEU CYS HIS LEU
SEQRES 37 A 527 THR ALA MET ILE SER THR CYS VAL ASN PRO ILE PHE TYR
SEQRES 38 A 527 GLY PHE LEU ASN LYS ASN PHE GLN ARG ASP LEU GLN PHE
SEQRES 39 A 527 PHE PHE ASN PHE CYS ASP PHE ARG SER ARG ASP ASP ASP
SEQRES 40 A 527 TYR GLU THR ILE ALA MET SER THR MET HIS THR ASP GLU
SEQRES 41 A 527 PHE LEU GLU VAL LEU PHE GLN
HET 9AF A1201 43
HETNAM 9AF DIMETHYL 4-{3-[({3-[4-(3-METHOXYPHENYL)PIPERIDIN-1-
HETNAM 2 9AF YL]PROPYL}CARBAMOYL)AMINO]PHENYL}-2,6-DIMETHYL-1,4-
HETNAM 3 9AF DIHYDROPYRIDINE-3,5-DICARBOXYLATE
FORMUL 2 9AF C33 H42 N4 O6
HELIX 1 AA1 PRO A 36 GLN A 68 1 33
HELIX 2 AA2 ASN A 73 CYS A 93 1 21
HELIX 3 AA3 CYS A 93 LEU A 102 1 10
HELIX 4 AA4 PHE A 108 ASN A 144 1 37
HELIX 5 AA5 ASN A 152 TYR A 176 1 25
HELIX 6 AA6 SER A 204 TYR A 220 1 17
HELIX 7 AA7 TYR A 220 GLU A 1010 1 32
HELIX 8 AA8 SER A 1037 ILE A 1049 1 13
HELIX 9 AA9 THR A 1058 ASN A 1080 1 23
HELIX 10 AB1 LEU A 1083 LEU A 1090 1 8
HELIX 11 AB2 ASP A 1091 GLY A 1106 1 16
HELIX 12 AB3 GLY A 1106 GLY A 1112 1 7
HELIX 13 AB4 PHE A 1113 GLN A 1122 1 10
HELIX 14 AB5 ARG A 1124 LEU A 1132 1 9
HELIX 15 AB6 SER A 1135 THR A 1141 1 7
HELIX 16 AB7 THR A 1141 GLY A 1155 1 15
HELIX 17 AB8 THR A 1156 TYR A 1160 5 5
HELIX 18 AB9 TYR A 253 ASN A 289 1 37
HELIX 19 AC1 THR A 295 ILE A 311 1 17
HELIX 20 AC2 ILE A 311 TYR A 320 1 10
HELIX 21 AC3 ASN A 324 ASN A 336 1 13
SHEET 1 AA1 2 GLN A 177 THR A 180 0
SHEET 2 AA1 2 VAL A 197 ASP A 200 -1 O PHE A 199 N VAL A 178
SHEET 1 AA2 3 ARG A1013 LYS A1018 0
SHEET 2 AA2 3 TYR A1024 GLY A1027 -1 O THR A1025 N TYR A1017
SHEET 3 AA2 3 HIS A1030 THR A1033 -1 O LEU A1032 N TYR A1024
SSBOND 1 CYS A 33 CYS A 296 1555 1555 2.04
SSBOND 2 CYS A 113 CYS A 198 1555 1555 2.04
SITE 1 AC1 20 PRO A 117 GLN A 120 CYS A 121 ILE A 124
SITE 2 AC1 20 PHE A 173 ASP A 200 THR A 212 LEU A 215
SITE 3 AC1 20 GLN A 219 TYR A 220 THR A 280 PHE A 282
SITE 4 AC1 20 ASN A 283 THR A 284 PHE A 286 ASP A 287
SITE 5 AC1 20 ALA A 294 HIS A 298 ASN A 299 PHE A 302
CRYST1 76.580 126.240 169.820 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013058 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005889 0.00000
ATOM 1 N ASP A 31 28.995 25.860 -73.864 1.00147.75 N
ANISOU 1 N ASP A 31 20450 21047 14641 -2593 1930 -710 N
ATOM 2 CA ASP A 31 28.517 26.270 -72.545 1.00146.31 C
ANISOU 2 CA ASP A 31 20107 20909 14576 -2496 1799 -661 C
ATOM 3 C ASP A 31 29.431 27.311 -71.869 1.00151.49 C
ANISOU 3 C ASP A 31 20654 21724 15181 -2742 1951 -787 C
ATOM 4 O ASP A 31 28.986 27.978 -70.930 1.00150.45 O
ANISOU 4 O ASP A 31 20523 21551 15092 -2733 1860 -736 O
ATOM 5 CB ASP A 31 28.308 25.046 -71.635 1.00146.45 C
ANISOU 5 CB ASP A 31 19766 21097 14781 -2202 1663 -635 C
ATOM 6 N ASP A 32 30.704 27.441 -72.346 1.00149.52 N
ANISOU 6 N ASP A 32 20306 21663 14841 -2966 2186 -961 N
ATOM 7 CA ASP A 32 31.746 28.361 -71.847 1.00150.58 C
ANISOU 7 CA ASP A 32 20313 21984 14916 -3235 2369 -1121 C
ATOM 8 C ASP A 32 31.946 28.276 -70.321 1.00152.69 C
ANISOU 8 C ASP A 32 20212 22466 15338 -3107 2276 -1148 C
ATOM 9 O ASP A 32 32.269 29.280 -69.677 1.00152.92 O
ANISOU 9 O ASP A 32 20240 22529 15334 -3278 2328 -1195 O
ATOM 10 CB ASP A 32 31.477 29.809 -72.310 1.00153.47 C
ANISOU 10 CB ASP A 32 21103 22109 15101 -3520 2456 -1096 C
ATOM 11 N CYS A 33 31.759 27.059 -69.757 1.00147.09 N
ANISOU 11 N CYS A 33 19210 21893 14786 -2807 2138 -1121 N
ATOM 12 CA CYS A 33 31.832 26.768 -68.321 1.00145.23 C
ANISOU 12 CA CYS A 33 18642 21839 14699 -2631 2021 -1130 C
ATOM 13 C CYS A 33 33.220 26.312 -67.847 1.00150.74 C
ANISOU 13 C CYS A 33 18933 22906 15436 -2655 2141 -1345 C
ATOM 14 O CYS A 33 33.914 25.579 -68.563 1.00151.77 O
ANISOU 14 O CYS A 33 18951 23173 15541 -2651 2242 -1456 O
ATOM 15 CB CYS A 33 30.746 25.768 -67.922 1.00142.60 C
ANISOU 15 CB CYS A 33 18278 21403 14500 -2290 1788 -966 C
ATOM 16 SG CYS A 33 30.271 25.829 -66.170 1.00144.28 S
ANISOU 16 SG CYS A 33 18296 21664 14860 -2110 1604 -893 S
ATOM 17 N HIS A 34 33.611 26.759 -66.627 1.00146.76 N
ANISOU 17 N HIS A 34 18206 22565 14992 -2672 2120 -1410 N
ATOM 18 CA HIS A 34 34.878 26.437 -65.959 1.00147.66 C
ANISOU 18 CA HIS A 34 17914 23038 15153 -2674 2200 -1624 C
ATOM 19 C HIS A 34 34.826 26.738 -64.449 1.00149.73 C
ANISOU 19 C HIS A 34 17980 23397 15515 -2575 2077 -1613 C
ATOM 20 O HIS A 34 34.893 27.906 -64.049 1.00149.72 O
ANISOU 20 O HIS A 34 18064 23355 15466 -2780 2129 -1622 O
ATOM 21 CB HIS A 34 36.069 27.159 -66.626 1.00151.17 C
ANISOU 21 CB HIS A 34 18336 23634 15469 -3027 2467 -1840 C
ATOM 22 N LEU A 35 34.688 25.677 -63.618 1.00144.30 N
ANISOU 22 N LEU A 35 17052 22822 14954 -2259 1913 -1589 N
ATOM 23 CA LEU A 35 34.672 25.771 -62.151 1.00142.84 C
ANISOU 23 CA LEU A 35 16667 22740 14864 -2128 1787 -1584 C
ATOM 24 C LEU A 35 36.081 25.418 -61.620 1.00147.76 C
ANISOU 24 C LEU A 35 16893 23738 15512 -2114 1857 -1835 C
ATOM 25 O LEU A 35 36.641 24.401 -62.047 1.00148.68 O
ANISOU 25 O LEU A 35 16841 24006 15643 -1971 1867 -1934 O
ATOM 26 CB LEU A 35 33.593 24.859 -61.536 1.00140.45 C
ANISOU 26 CB LEU A 35 16393 22300 14671 -1796 1559 -1397 C
ATOM 27 CG LEU A 35 33.246 25.094 -60.056 1.00143.78 C
ANISOU 27 CG LEU A 35 16717 22733 15178 -1679 1418 -1337 C
ATOM 28 CD1 LEU A 35 32.440 26.379 -59.860 1.00142.94 C
ANISOU 28 CD1 LEU A 35 16872 22396 15043 -1845 1405 -1206 C
ATOM 29 CD2 LEU A 35 32.462 23.932 -59.502 1.00144.51 C
ANISOU 29 CD2 LEU A 35 16775 22765 15369 -1348 1228 -1213 C
ATOM 30 N PRO A 36 36.698 26.255 -60.747 1.00143.58 N
ANISOU 30 N PRO A 36 16209 23365 14980 -2264 1909 -1955 N
ATOM 31 CA PRO A 36 38.078 25.966 -60.308 1.00144.75 C
ANISOU 31 CA PRO A 36 15967 23884 15146 -2260 1978 -2224 C
ATOM 32 C PRO A 36 38.214 24.889 -59.242 1.00145.99 C
ANISOU 32 C PRO A 36 15858 24199 15413 -1897 1786 -2246 C
ATOM 33 O PRO A 36 37.329 24.755 -58.396 1.00144.35 O
ANISOU 33 O PRO A 36 15728 23846 15272 -1715 1612 -2073 O
ATOM 34 CB PRO A 36 38.595 27.322 -59.801 1.00147.74 C
ANISOU 34 CB PRO A 36 16308 24345 15482 -2549 2087 -2327 C
ATOM 35 CG PRO A 36 37.456 28.303 -59.974 1.00151.07 C
ANISOU 35 CG PRO A 36 17129 24423 15847 -2712 2088 -2111 C
ATOM 36 CD PRO A 36 36.206 27.516 -60.160 1.00144.34 C
ANISOU 36 CD PRO A 36 16477 23315 15051 -2446 1909 -1869 C
ATOM 37 N LEU A 37 39.349 24.153 -59.252 1.00141.94 N
ANISOU 37 N LEU A 37 15034 23987 14910 -1794 1821 -2474 N
ATOM 38 CA LEU A 37 39.638 23.114 -58.258 1.00140.59 C
ANISOU 38 CA LEU A 37 14611 23984 14822 -1439 1638 -2530 C
ATOM 39 C LEU A 37 40.043 23.732 -56.905 1.00143.36 C
ANISOU 39 C LEU A 37 14761 24495 15213 -1439 1576 -2622 C
ATOM 40 O LEU A 37 40.071 23.034 -55.887 1.00142.49 O
ANISOU 40 O LEU A 37 14511 24461 15166 -1145 1395 -2620 O
ATOM 41 CB LEU A 37 40.696 22.125 -58.773 1.00142.40 C
ANISOU 41 CB LEU A 37 14587 24477 15042 -1310 1682 -2753 C
ATOM 42 CG LEU A 37 40.588 20.691 -58.246 1.00146.21 C
ANISOU 42 CG LEU A 37 14956 25013 15586 -885 1470 -2733 C
ATOM 43 CD1 LEU A 37 39.467 19.927 -58.932 1.00144.16 C
ANISOU 43 CD1 LEU A 37 14991 24452 15333 -727 1381 -2477 C
ATOM 44 CD2 LEU A 37 41.888 19.946 -58.438 1.00150.98 C
ANISOU 44 CD2 LEU A 37 15235 25952 16178 -769 1509 -3024 C
ATOM 45 N ALA A 38 40.312 25.060 -56.901 1.00139.49 N
ANISOU 45 N ALA A 38 14290 24034 14677 -1774 1723 -2692 N
ATOM 46 CA ALA A 38 40.636 25.872 -55.726 1.00138.84 C
ANISOU 46 CA ALA A 38 14061 24073 14620 -1838 1690 -2768 C
ATOM 47 C ALA A 38 39.373 26.079 -54.878 1.00138.15 C
ANISOU 47 C ALA A 38 14199 23709 14582 -1713 1518 -2494 C
ATOM 48 O ALA A 38 39.480 26.325 -53.677 1.00137.65 O
ANISOU 48 O ALA A 38 14004 23731 14567 -1612 1408 -2516 O
ATOM 49 CB ALA A 38 41.190 27.221 -56.163 1.00141.21 C
ANISOU 49 CB ALA A 38 14380 24435 14839 -2261 1916 -2900 C
ATOM 50 N MET A 39 38.184 25.991 -55.514 1.00131.05 N
ANISOU 50 N MET A 39 13635 22487 13670 -1722 1497 -2249 N
ATOM 51 CA MET A 39 36.872 26.132 -54.875 1.00127.69 C
ANISOU 51 CA MET A 39 13441 21785 13292 -1611 1346 -1992 C
ATOM 52 C MET A 39 36.354 24.749 -54.495 1.00126.72 C
ANISOU 52 C MET A 39 13297 21610 13239 -1239 1158 -1886 C
ATOM 53 O MET A 39 35.883 24.567 -53.375 1.00124.34 O
ANISOU 53 O MET A 39 12986 21262 12995 -1065 1008 -1797 O
ATOM 54 CB MET A 39 35.859 26.812 -55.820 1.00129.41 C
ANISOU 54 CB MET A 39 14025 21689 13455 -1799 1412 -1807 C
ATOM 55 CG MET A 39 36.311 28.151 -56.383 1.00135.22 C
ANISOU 55 CG MET A 39 14859 22425 14093 -2180 1607 -1894 C
ATOM 56 SD MET A 39 35.586 29.587 -55.549 1.00139.11 S
ANISOU 56 SD MET A 39 15530 22747 14579 -2336 1569 -1774 S
ATOM 57 CE MET A 39 35.963 30.877 -56.757 1.00137.56 C
ANISOU 57 CE MET A 39 15564 22473 14229 -2775 1816 -1849 C
ATOM 58 N ILE A 40 36.455 23.779 -55.437 1.00122.11 N
ANISOU 58 N ILE A 40 12722 21033 12642 -1127 1174 -1901 N
ATOM 59 CA ILE A 40 36.017 22.380 -55.328 1.00120.30 C
ANISOU 59 CA ILE A 40 12504 20745 12458 -794 1021 -1812 C
ATOM 60 C ILE A 40 36.619 21.681 -54.107 1.00123.76 C
ANISOU 60 C ILE A 40 12694 21390 12939 -531 883 -1922 C
ATOM 61 O ILE A 40 35.865 21.092 -53.331 1.00121.81 O
ANISOU 61 O ILE A 40 12534 21013 12736 -310 723 -1780 O
ATOM 62 CB ILE A 40 36.269 21.604 -56.661 1.00123.98 C
ANISOU 62 CB ILE A 40 13001 21221 12885 -767 1097 -1853 C
ATOM 63 CG1 ILE A 40 35.267 22.054 -57.748 1.00123.15 C
ANISOU 63 CG1 ILE A 40 13218 20831 12741 -952 1174 -1681 C
ATOM 64 CG2 ILE A 40 36.221 20.073 -56.470 1.00124.22 C
ANISOU 64 CG2 ILE A 40 12986 21261 12950 -410 945 -1822 C
ATOM 65 CD1 ILE A 40 35.737 21.902 -59.191 1.00131.00 C
ANISOU 65 CD1 ILE A 40 14245 21864 13666 -1083 1330 -1771 C
ATOM 66 N PHE A 41 37.956 21.752 -53.931 1.00122.01 N
ANISOU 66 N PHE A 41 12173 21486 12699 -556 943 -2185 N
ATOM 67 CA PHE A 41 38.620 21.122 -52.789 1.00122.34 C
ANISOU 67 CA PHE A 41 11971 21742 12770 -295 802 -2320 C
ATOM 68 C PHE A 41 38.278 21.803 -51.463 1.00122.44 C
ANISOU 68 C PHE A 41 11989 21715 12817 -296 710 -2255 C
ATOM 69 O PHE A 41 38.050 21.104 -50.478 1.00121.32 O
ANISOU 69 O PHE A 41 11833 21559 12704 -21 537 -2209 O
ATOM 70 CB PHE A 41 40.133 21.006 -52.989 1.00127.53 C
ANISOU 70 CB PHE A 41 12291 22764 13402 -315 885 -2641 C
ATOM 71 CG PHE A 41 40.714 19.793 -52.299 1.00130.91 C
ANISOU 71 CG PHE A 41 12525 23371 13844 60 714 -2767 C
ATOM 72 CD1 PHE A 41 41.026 19.824 -50.941 1.00134.95 C
ANISOU 72 CD1 PHE A 41 12890 24005 14379 227 570 -2841 C
ATOM 73 CD2 PHE A 41 40.944 18.615 -53.004 1.00134.25 C
ANISOU 73 CD2 PHE A 41 12932 23831 14247 258 689 -2813 C
ATOM 74 CE1 PHE A 41 41.543 18.695 -50.297 1.00137.07 C
ANISOU 74 CE1 PHE A 41 13015 24421 14643 594 396 -2959 C
ATOM 75 CE2 PHE A 41 41.477 17.490 -52.363 1.00138.38 C
ANISOU 75 CE2 PHE A 41 13303 24506 14768 624 519 -2933 C
ATOM 76 CZ PHE A 41 41.772 17.538 -51.014 1.00136.97 C
ANISOU 76 CZ PHE A 41 12996 24440 14606 793 370 -3006 C
ATOM 77 N THR A 42 38.208 23.158 -51.454 1.00116.65 N
ANISOU 77 N THR A 42 11305 20944 12072 -606 826 -2243 N
ATOM 78 CA THR A 42 37.842 23.992 -50.297 1.00114.26 C
ANISOU 78 CA THR A 42 11032 20585 11797 -657 763 -2173 C
ATOM 79 C THR A 42 36.420 23.639 -49.833 1.00113.53 C
ANISOU 79 C THR A 42 11204 20187 11744 -497 623 -1897 C
ATOM 80 O THR A 42 36.164 23.590 -48.629 1.00112.50 O
ANISOU 80 O THR A 42 11057 20042 11647 -351 493 -1850 O
ATOM 81 CB THR A 42 37.987 25.482 -50.660 1.00118.70 C
ANISOU 81 CB THR A 42 11644 21136 12320 -1042 937 -2208 C
ATOM 82 OG1 THR A 42 39.332 25.733 -51.065 1.00117.42 O
ANISOU 82 OG1 THR A 42 11216 21277 12120 -1193 1074 -2488 O
ATOM 83 CG2 THR A 42 37.609 26.417 -49.513 1.00115.57 C
ANISOU 83 CG2 THR A 42 11301 20665 11947 -1113 880 -2128 C
ATOM 84 N LEU A 43 35.511 23.376 -50.794 1.00107.20 N
ANISOU 84 N LEU A 43 10645 19149 10938 -526 653 -1727 N
ATOM 85 CA LEU A 43 34.132 22.977 -50.522 1.00103.98 C
ANISOU 85 CA LEU A 43 10482 18458 10569 -390 537 -1484 C
ATOM 86 C LEU A 43 34.086 21.536 -50.020 1.00106.04 C
ANISOU 86 C LEU A 43 10704 18738 10850 -50 388 -1469 C
ATOM 87 O LEU A 43 33.329 21.258 -49.098 1.00104.16 O
ANISOU 87 O LEU A 43 10565 18367 10644 96 267 -1342 O
ATOM 88 CB LEU A 43 33.236 23.148 -51.764 1.00102.80 C
ANISOU 88 CB LEU A 43 10588 18069 10404 -525 612 -1335 C
ATOM 89 CG LEU A 43 32.729 24.562 -52.044 1.00106.68 C
ANISOU 89 CG LEU A 43 11243 18417 10874 -813 702 -1263 C
ATOM 90 CD1 LEU A 43 32.519 24.780 -53.523 1.00106.89 C
ANISOU 90 CD1 LEU A 43 11448 18317 10849 -979 818 -1225 C
ATOM 91 CD2 LEU A 43 31.440 24.842 -51.304 1.00107.35 C
ANISOU 91 CD2 LEU A 43 11504 18275 11008 -758 591 -1072 C
ATOM 92 N ALA A 44 34.908 20.630 -50.602 1.00102.99 N
ANISOU 92 N ALA A 44 10182 18515 10436 76 401 -1607 N
ATOM 93 CA ALA A 44 34.979 19.222 -50.196 1.00102.78 C
ANISOU 93 CA ALA A 44 10131 18513 10408 410 259 -1613 C
ATOM 94 C ALA A 44 35.472 19.091 -48.751 1.00108.09 C
ANISOU 94 C ALA A 44 10657 19327 11087 588 130 -1703 C
ATOM 95 O ALA A 44 34.999 18.214 -48.023 1.00107.02 O
ANISOU 95 O ALA A 44 10622 19090 10951 836 -13 -1614 O
ATOM 96 CB ALA A 44 35.884 18.448 -51.134 1.00105.04 C
ANISOU 96 CB ALA A 44 10282 18971 10656 487 308 -1773 C
ATOM 97 N LEU A 45 36.396 19.992 -48.338 1.00106.44 N
ANISOU 97 N LEU A 45 10228 19341 10875 449 184 -1878 N
ATOM 98 CA LEU A 45 36.936 20.085 -46.980 1.00107.15 C
ANISOU 98 CA LEU A 45 10162 19582 10968 580 72 -1984 C
ATOM 99 C LEU A 45 35.819 20.585 -46.056 1.00109.56 C
ANISOU 99 C LEU A 45 10666 19657 11305 551 7 -1777 C
ATOM 100 O LEU A 45 35.565 19.968 -45.019 1.00109.09 O
ANISOU 100 O LEU A 45 10655 19551 11243 784 -141 -1731 O
ATOM 101 CB LEU A 45 38.143 21.054 -46.922 1.00109.26 C
ANISOU 101 CB LEU A 45 10148 20138 11227 382 174 -2226 C
ATOM 102 CG LEU A 45 39.474 20.596 -47.554 1.00116.56 C
ANISOU 102 CG LEU A 45 10794 21371 12123 440 219 -2502 C
ATOM 103 CD1 LEU A 45 40.328 21.789 -47.940 1.00118.24 C
ANISOU 103 CD1 LEU A 45 10812 21788 12327 109 402 -2692 C
ATOM 104 CD2 LEU A 45 40.260 19.702 -46.617 1.00120.51 C
ANISOU 104 CD2 LEU A 45 11105 22073 12611 773 42 -2669 C
ATOM 105 N ALA A 46 35.125 21.674 -46.464 1.00104.93 N
ANISOU 105 N ALA A 46 10215 18915 10740 272 117 -1654 N
ATOM 106 CA ALA A 46 34.013 22.285 -45.730 1.00102.80 C
ANISOU 106 CA ALA A 46 10133 18424 10504 212 75 -1465 C
ATOM 107 C ALA A 46 32.823 21.334 -45.540 1.00105.48 C
ANISOU 107 C ALA A 46 10703 18515 10861 406 -28 -1266 C
ATOM 108 O ALA A 46 32.266 21.304 -44.450 1.00104.53 O
ANISOU 108 O ALA A 46 10657 18303 10756 508 -126 -1183 O
ATOM 109 CB ALA A 46 33.573 23.572 -46.408 1.00102.80 C
ANISOU 109 CB ALA A 46 10238 18313 10509 -110 213 -1396 C
ATOM 110 N TYR A 47 32.455 20.539 -46.572 1.00102.07 N
ANISOU 110 N TYR A 47 10382 17978 10421 455 -4 -1200 N
ATOM 111 CA TYR A 47 31.359 19.563 -46.493 1.00100.46 C
ANISOU 111 CA TYR A 47 10394 17547 10230 626 -88 -1030 C
ATOM 112 C TYR A 47 31.741 18.383 -45.603 1.00104.76 C
ANISOU 112 C TYR A 47 10904 18159 10741 931 -225 -1082 C
ATOM 113 O TYR A 47 30.941 17.976 -44.762 1.00103.10 O
ANISOU 113 O TYR A 47 10850 17789 10536 1050 -313 -961 O
ATOM 114 CB TYR A 47 30.917 19.088 -47.882 1.00101.35 C
ANISOU 114 CB TYR A 47 10626 17543 10339 585 -22 -961 C
ATOM 115 CG TYR A 47 29.891 19.990 -48.533 1.00102.31 C
ANISOU 115 CG TYR A 47 10917 17465 10493 354 57 -824 C
ATOM 116 CD1 TYR A 47 30.276 20.991 -49.420 1.00105.04 C
ANISOU 116 CD1 TYR A 47 11225 17864 10823 111 185 -882 C
ATOM 117 CD2 TYR A 47 28.530 19.824 -48.287 1.00101.40 C
ANISOU 117 CD2 TYR A 47 11007 17104 10416 382 3 -646 C
ATOM 118 CE1 TYR A 47 29.335 21.819 -50.030 1.00104.94 C
ANISOU 118 CE1 TYR A 47 11395 17655 10824 -80 240 -761 C
ATOM 119 CE2 TYR A 47 27.579 20.638 -48.902 1.00101.16 C
ANISOU 119 CE2 TYR A 47 11127 16896 10412 196 57 -537 C
ATOM 120 CZ TYR A 47 27.987 21.635 -49.773 1.00108.86 C
ANISOU 120 CZ TYR A 47 12081 17916 11363 -24 167 -592 C
ATOM 121 OH TYR A 47 27.066 22.450 -50.379 1.00108.99 O
ANISOU 121 OH TYR A 47 12272 17748 11392 -188 205 -490 O
ATOM 122 N GLY A 48 32.977 17.898 -45.756 1.00103.25 N
ANISOU 122 N GLY A 48 10513 18208 10511 1051 -242 -1273 N
ATOM 123 CA GLY A 48 33.546 16.821 -44.948 1.00103.84 C
ANISOU 123 CA GLY A 48 10540 18378 10536 1361 -386 -1362 C
ATOM 124 C GLY A 48 33.646 17.180 -43.475 1.00106.19 C
ANISOU 124 C GLY A 48 10809 18709 10831 1430 -483 -1380 C
ATOM 125 O GLY A 48 33.491 16.311 -42.612 1.00105.83 O
ANISOU 125 O GLY A 48 10876 18591 10744 1671 -614 -1344 O
ATOM 126 N ALA A 49 33.889 18.472 -43.180 1.00101.54 N
ANISOU 126 N ALA A 49 10090 18215 10276 1212 -415 -1432 N
ATOM 127 CA ALA A 49 33.958 18.999 -41.817 1.00101.19 C
ANISOU 127 CA ALA A 49 10012 18202 10233 1236 -492 -1446 C
ATOM 128 C ALA A 49 32.558 19.010 -41.187 1.00102.69 C
ANISOU 128 C ALA A 49 10469 18104 10445 1231 -527 -1219 C
ATOM 129 O ALA A 49 32.414 18.657 -40.019 1.00102.18 O
ANISOU 129 O ALA A 49 10477 17996 10352 1398 -641 -1197 O
ATOM 130 CB ALA A 49 34.536 20.405 -41.829 1.00102.45 C
ANISOU 130 CB ALA A 49 9987 18518 10422 970 -389 -1550 C
ATOM 131 N VAL A 50 31.530 19.382 -41.983 1.00 97.29 N
ANISOU 131 N VAL A 50 9937 17224 9805 1045 -431 -1062 N
ATOM 132 CA VAL A 50 30.122 19.440 -41.580 1.00 94.94 C
ANISOU 132 CA VAL A 50 9875 16659 9539 1009 -444 -861 C
ATOM 133 C VAL A 50 29.547 18.006 -41.431 1.00 99.05 C
ANISOU 133 C VAL A 50 10584 17027 10024 1241 -526 -775 C
ATOM 134 O VAL A 50 28.546 17.821 -40.738 1.00 97.64 O
ANISOU 134 O VAL A 50 10587 16660 9853 1270 -563 -646 O
ATOM 135 CB VAL A 50 29.308 20.380 -42.516 1.00 97.27 C
ANISOU 135 CB VAL A 50 10248 16820 9889 742 -324 -756 C
ATOM 136 CG1 VAL A 50 27.817 20.372 -42.191 1.00 95.57 C
ANISOU 136 CG1 VAL A 50 10258 16342 9713 718 -341 -571 C
ATOM 137 CG2 VAL A 50 29.842 21.810 -42.449 1.00 97.30 C
ANISOU 137 CG2 VAL A 50 10112 16950 9909 518 -251 -836 C
ATOM 138 N ILE A 51 30.216 16.990 -42.023 1.00 97.20 N
ANISOU 138 N ILE A 51 10310 16879 9743 1405 -555 -856 N
ATOM 139 CA ILE A 51 29.819 15.587 -41.873 1.00 97.14 C
ANISOU 139 CA ILE A 51 10490 16736 9682 1636 -637 -792 C
ATOM 140 C ILE A 51 30.368 15.090 -40.536 1.00103.36 C
ANISOU 140 C ILE A 51 11284 17588 10400 1869 -773 -865 C
ATOM 141 O ILE A 51 29.594 14.640 -39.698 1.00102.81 O
ANISOU 141 O ILE A 51 11425 17338 10302 1952 -829 -756 O
ATOM 142 CB ILE A 51 30.273 14.681 -43.058 1.00100.77 C
ANISOU 142 CB ILE A 51 10930 17246 10111 1732 -620 -845 C
ATOM 143 CG1 ILE A 51 29.553 15.051 -44.362 1.00 99.70 C
ANISOU 143 CG1 ILE A 51 10853 16995 10035 1519 -498 -747 C
ATOM 144 CG2 ILE A 51 30.067 13.188 -42.738 1.00101.89 C
ANISOU 144 CG2 ILE A 51 11267 17273 10175 2004 -726 -808 C
ATOM 145 CD1 ILE A 51 30.375 14.768 -45.616 1.00107.59 C
ANISOU 145 CD1 ILE A 51 11729 18132 11017 1521 -441 -853 C
ATOM 146 N ILE A 52 31.697 15.195 -40.329 1.00102.43 N
ANISOU 146 N ILE A 52 10939 17729 10251 1968 -825 -1058 N
ATOM 147 CA ILE A 52 32.375 14.722 -39.114 1.00104.08 C
ANISOU 147 CA ILE A 52 11133 18028 10383 2217 -974 -1161 C
ATOM 148 C ILE A 52 31.943 15.511 -37.865 1.00106.94 C
ANISOU 148 C ILE A 52 11551 18321 10761 2142 -1000 -1098 C
ATOM 149 O ILE A 52 31.997 14.954 -36.776 1.00106.85 O
ANISOU 149 O ILE A 52 11670 18253 10677 2344 -1121 -1095 O
ATOM 150 CB ILE A 52 33.931 14.618 -39.254 1.00109.95 C
ANISOU 150 CB ILE A 52 11593 19089 11093 2354 -1032 -1414 C
ATOM 151 CG1 ILE A 52 34.631 16.002 -39.301 1.00111.08 C
ANISOU 151 CG1 ILE A 52 11451 19451 11302 2116 -942 -1538 C
ATOM 152 CG2 ILE A 52 34.334 13.736 -40.459 1.00111.61 C
ANISOU 152 CG2 ILE A 52 11776 19355 11276 2466 -1019 -1477 C
ATOM 153 CD1 ILE A 52 36.142 15.981 -38.888 1.00121.08 C
ANISOU 153 CD1 ILE A 52 12427 21045 12533 2265 -1026 -1813 C
ATOM 154 N LEU A 53 31.498 16.774 -38.018 1.00102.79 N
ANISOU 154 N LEU A 53 10950 17787 10320 1861 -891 -1044 N
ATOM 155 CA LEU A 53 31.012 17.587 -36.897 1.00102.17 C
ANISOU 155 CA LEU A 53 10925 17633 10261 1772 -904 -978 C
ATOM 156 C LEU A 53 29.520 17.316 -36.656 1.00105.48 C
ANISOU 156 C LEU A 53 11629 17755 10694 1730 -880 -770 C
ATOM 157 O LEU A 53 29.072 17.296 -35.508 1.00105.09 O
ANISOU 157 O LEU A 53 11716 17600 10613 1795 -940 -714 O
ATOM 158 CB LEU A 53 31.242 19.084 -37.160 1.00101.78 C
ANISOU 158 CB LEU A 53 10689 17696 10286 1492 -799 -1017 C
ATOM 159 CG LEU A 53 31.495 19.943 -35.929 1.00106.83 C
ANISOU 159 CG LEU A 53 11259 18405 10926 1454 -843 -1060 C
ATOM 160 CD1 LEU A 53 32.553 20.985 -36.204 1.00108.33 C
ANISOU 160 CD1 LEU A 53 11175 18842 11145 1288 -781 -1222 C
ATOM 161 CD2 LEU A 53 30.223 20.594 -35.430 1.00106.48 C
ANISOU 161 CD2 LEU A 53 11397 18134 10925 1308 -801 -881 C
ATOM 162 N GLY A 54 28.780 17.127 -37.746 1.00101.39 N
ANISOU 162 N GLY A 54 11193 17111 10221 1616 -790 -670 N
ATOM 163 CA GLY A 54 27.350 16.863 -37.732 1.00 99.89 C
ANISOU 163 CA GLY A 54 11241 16657 10055 1555 -752 -495 C
ATOM 164 C GLY A 54 27.016 15.456 -37.303 1.00104.84 C
ANISOU 164 C GLY A 54 12092 17144 10598 1775 -827 -449 C
ATOM 165 O GLY A 54 26.545 15.264 -36.183 1.00104.64 O
ANISOU 165 O GLY A 54 12222 17004 10534 1835 -873 -396 O
ATOM 166 N VAL A 55 27.271 14.466 -38.187 1.00102.12 N
ANISOU 166 N VAL A 55 11781 16804 10217 1890 -836 -470 N
ATOM 167 CA VAL A 55 26.995 13.034 -37.986 1.00102.75 C
ANISOU 167 CA VAL A 55 12096 16740 10204 2098 -900 -428 C
ATOM 168 C VAL A 55 27.433 12.554 -36.598 1.00109.75 C
ANISOU 168 C VAL A 55 13087 17629 10984 2313 -1026 -477 C
ATOM 169 O VAL A 55 26.635 11.909 -35.915 1.00109.75 O
ANISOU 169 O VAL A 55 13352 17424 10925 2369 -1044 -383 O
ATOM 170 CB VAL A 55 27.562 12.137 -39.123 1.00107.36 C
ANISOU 170 CB VAL A 55 12651 17387 10753 2218 -908 -485 C
ATOM 171 CG1 VAL A 55 27.264 10.658 -38.877 1.00107.66 C
ANISOU 171 CG1 VAL A 55 12963 17262 10682 2433 -978 -440 C
ATOM 172 CG2 VAL A 55 27.025 12.565 -40.488 1.00106.04 C
ANISOU 172 CG2 VAL A 55 12424 17185 10680 2006 -786 -424 C
ATOM 173 N SER A 56 28.668 12.903 -36.168 1.00107.96 N
ANISOU 173 N SER A 56 12661 17629 10730 2422 -1108 -629 N
ATOM 174 CA SER A 56 29.193 12.507 -34.856 1.00108.86 C
ANISOU 174 CA SER A 56 12862 17763 10737 2645 -1246 -696 C
ATOM 175 C SER A 56 28.513 13.249 -33.700 1.00111.67 C
ANISOU 175 C SER A 56 13307 18011 11112 2528 -1231 -614 C
ATOM 176 O SER A 56 28.136 12.608 -32.723 1.00111.68 O
ANISOU 176 O SER A 56 13562 17854 11018 2654 -1295 -562 O
ATOM 177 CB SER A 56 30.710 12.662 -34.796 1.00113.65 C
ANISOU 177 CB SER A 56 13205 18660 11315 2800 -1344 -905 C
ATOM 178 OG SER A 56 31.094 13.989 -34.477 1.00120.91 O
ANISOU 178 OG SER A 56 13888 19741 12313 2631 -1309 -968 O
ATOM 179 N GLY A 57 28.362 14.571 -33.833 1.00107.04 N
ANISOU 179 N GLY A 57 12531 17503 10636 2288 -1145 -606 N
ATOM 180 CA GLY A 57 27.734 15.442 -32.840 1.00105.90 C
ANISOU 180 CA GLY A 57 12433 17278 10526 2151 -1119 -536 C
ATOM 181 C GLY A 57 26.277 15.119 -32.566 1.00108.36 C
ANISOU 181 C GLY A 57 13016 17314 10843 2061 -1052 -370 C
ATOM 182 O GLY A 57 25.859 15.072 -31.406 1.00107.75 O
ANISOU 182 O GLY A 57 13105 17121 10713 2096 -1084 -327 O
ATOM 183 N ASN A 58 25.494 14.897 -33.637 1.00104.16 N
ANISOU 183 N ASN A 58 12526 16678 10372 1938 -955 -287 N
ATOM 184 CA ASN A 58 24.075 14.538 -33.565 1.00102.69 C
ANISOU 184 CA ASN A 58 12570 16246 10203 1837 -880 -150 C
ATOM 185 C ASN A 58 23.903 13.123 -33.001 1.00107.44 C
ANISOU 185 C ASN A 58 13459 16693 10670 2035 -939 -124 C
ATOM 186 O ASN A 58 22.938 12.877 -32.279 1.00107.35 O
ANISOU 186 O ASN A 58 13665 16494 10631 1986 -903 -43 O
ATOM 187 CB ASN A 58 23.404 14.650 -34.938 1.00100.62 C
ANISOU 187 CB ASN A 58 12260 15936 10034 1680 -780 -92 C
ATOM 188 CG ASN A 58 23.113 16.052 -35.409 1.00118.00 C
ANISOU 188 CG ASN A 58 14281 18196 12358 1447 -702 -78 C
ATOM 189 OD1 ASN A 58 22.750 16.946 -34.634 1.00109.87 O
ANISOU 189 OD1 ASN A 58 13239 17140 11367 1338 -684 -52 O
ATOM 190 ND2 ASN A 58 23.193 16.252 -36.717 1.00109.87 N
ANISOU 190 ND2 ASN A 58 13134 17227 11385 1365 -653 -89 N
ATOM 191 N LEU A 59 24.836 12.204 -33.320 1.00104.20 N
ANISOU 191 N LEU A 59 13062 16360 10171 2257 -1028 -201 N
ATOM 192 CA LEU A 59 24.797 10.837 -32.813 1.00104.94 C
ANISOU 192 CA LEU A 59 13453 16306 10114 2469 -1100 -188 C
ATOM 193 C LEU A 59 25.255 10.808 -31.350 1.00111.87 C
ANISOU 193 C LEU A 59 14443 17180 10881 2623 -1208 -233 C
ATOM 194 O LEU A 59 24.796 9.956 -30.590 1.00112.44 O
ANISOU 194 O LEU A 59 14832 17058 10832 2718 -1234 -183 O
ATOM 195 CB LEU A 59 25.647 9.904 -33.688 1.00105.79 C
ANISOU 195 CB LEU A 59 13535 16499 10160 2666 -1167 -263 C
ATOM 196 CG LEU A 59 25.269 8.420 -33.716 1.00110.91 C
ANISOU 196 CG LEU A 59 14517 16946 10677 2821 -1194 -214 C
ATOM 197 CD1 LEU A 59 23.881 8.202 -34.289 1.00109.88 C
ANISOU 197 CD1 LEU A 59 14525 16615 10608 2614 -1054 -83 C
ATOM 198 CD2 LEU A 59 26.255 7.633 -34.547 1.00113.70 C
ANISOU 198 CD2 LEU A 59 14812 17421 10969 3043 -1281 -312 C
ATOM 199 N ALA A 60 26.123 11.766 -30.946 1.00109.61 N
ANISOU 199 N ALA A 60 13912 17101 10632 2634 -1266 -330 N
ATOM 200 CA ALA A 60 26.612 11.889 -29.568 1.00110.90 C
ANISOU 200 CA ALA A 60 14151 17283 10702 2774 -1377 -384 C
ATOM 201 C ALA A 60 25.510 12.434 -28.664 1.00114.36 C
ANISOU 201 C ALA A 60 14739 17549 11165 2592 -1295 -273 C
ATOM 202 O ALA A 60 25.350 11.951 -27.546 1.00115.11 O
ANISOU 202 O ALA A 60 15087 17510 11138 2703 -1353 -256 O
ATOM 203 CB ALA A 60 27.829 12.801 -29.513 1.00112.37 C
ANISOU 203 CB ALA A 60 14005 17756 10936 2811 -1450 -531 C
ATOM 204 N LEU A 61 24.746 13.428 -29.162 1.00109.21 N
ANISOU 204 N LEU A 61 13939 16893 10663 2317 -1161 -204 N
ATOM 205 CA LEU A 61 23.621 14.075 -28.481 1.00107.63 C
ANISOU 205 CA LEU A 61 13832 16548 10515 2116 -1066 -109 C
ATOM 206 C LEU A 61 22.543 13.030 -28.152 1.00110.95 C
ANISOU 206 C LEU A 61 14598 16703 10854 2114 -1009 -14 C
ATOM 207 O LEU A 61 22.067 12.989 -27.019 1.00109.96 O
ANISOU 207 O LEU A 61 14672 16444 10665 2097 -998 23 O
ATOM 208 CB LEU A 61 23.059 15.179 -29.401 1.00105.91 C
ANISOU 208 CB LEU A 61 13385 16387 10469 1857 -949 -71 C
ATOM 209 CG LEU A 61 22.448 16.426 -28.762 1.00109.31 C
ANISOU 209 CG LEU A 61 13747 16800 10984 1660 -886 -33 C
ATOM 210 CD1 LEU A 61 23.514 17.364 -28.256 1.00109.82 C
ANISOU 210 CD1 LEU A 61 13605 17065 11056 1689 -961 -124 C
ATOM 211 CD2 LEU A 61 21.652 17.194 -29.786 1.00110.54 C
ANISOU 211 CD2 LEU A 61 13772 16945 11283 1432 -774 19 C
ATOM 212 N ILE A 62 22.215 12.150 -29.135 1.00107.98 N
ANISOU 212 N ILE A 62 14303 16254 10471 2133 -972 16 N
ATOM 213 CA ILE A 62 21.241 11.054 -29.017 1.00108.06 C
ANISOU 213 CA ILE A 62 14638 16020 10399 2122 -909 93 C
ATOM 214 C ILE A 62 21.699 10.069 -27.927 1.00114.33 C
ANISOU 214 C ILE A 62 15742 16708 10991 2354 -1013 69 C
ATOM 215 O ILE A 62 20.999 9.910 -26.926 1.00113.69 O
ANISOU 215 O ILE A 62 15912 16448 10837 2298 -967 118 O
ATOM 216 CB ILE A 62 20.976 10.357 -30.402 1.00110.47 C
ANISOU 216 CB ILE A 62 14931 16299 10742 2102 -859 117 C
ATOM 217 CG1 ILE A 62 20.161 11.264 -31.349 1.00109.03 C
ANISOU 217 CG1 ILE A 62 14531 16151 10744 1847 -741 159 C
ATOM 218 CG2 ILE A 62 20.279 8.998 -30.240 1.00111.58 C
ANISOU 218 CG2 ILE A 62 15435 16201 10758 2145 -821 171 C
ATOM 219 CD1 ILE A 62 20.218 10.905 -32.871 1.00115.31 C
ANISOU 219 CD1 ILE A 62 15213 16998 11600 1837 -717 158 C
ATOM 220 N ILE A 63 22.893 9.454 -28.118 1.00113.10 N
ANISOU 220 N ILE A 63 15567 16665 10741 2616 -1156 -17 N
ATOM 221 CA ILE A 63 23.514 8.456 -27.237 1.00115.24 C
ANISOU 221 CA ILE A 63 16129 16852 10804 2891 -1292 -60 C
ATOM 222 C ILE A 63 23.585 8.936 -25.780 1.00120.57 C
ANISOU 222 C ILE A 63 16914 17489 11410 2914 -1340 -70 C
ATOM 223 O ILE A 63 23.224 8.171 -24.883 1.00121.30 O
ANISOU 223 O ILE A 63 17380 17368 11340 2989 -1354 -34 O
ATOM 224 CB ILE A 63 24.890 7.999 -27.811 1.00119.57 C
ANISOU 224 CB ILE A 63 16538 17592 11300 3166 -1449 -182 C
ATOM 225 CG1 ILE A 63 24.672 6.994 -28.969 1.00120.09 C
ANISOU 225 CG1 ILE A 63 16679 17596 11354 3199 -1411 -156 C
ATOM 226 CG2 ILE A 63 25.819 7.407 -26.731 1.00122.04 C
ANISOU 226 CG2 ILE A 63 17059 17893 11416 3479 -1635 -268 C
ATOM 227 CD1 ILE A 63 25.832 6.853 -29.987 1.00128.86 C
ANISOU 227 CD1 ILE A 63 17521 18945 12495 3366 -1504 -272 C
ATOM 228 N ILE A 64 24.004 10.201 -25.555 1.00117.16 N
ANISOU 228 N ILE A 64 16176 17247 11092 2836 -1357 -116 N
ATOM 229 CA ILE A 64 24.117 10.794 -24.219 1.00117.65 C
ANISOU 229 CA ILE A 64 16299 17297 11105 2847 -1404 -130 C
ATOM 230 C ILE A 64 22.738 10.867 -23.541 1.00122.10 C
ANISOU 230 C ILE A 64 17110 17620 11663 2633 -1257 -16 C
ATOM 231 O ILE A 64 22.566 10.222 -22.512 1.00122.66 O
ANISOU 231 O ILE A 64 17529 17509 11566 2731 -1290 3 O
ATOM 232 CB ILE A 64 24.903 12.143 -24.234 1.00120.00 C
ANISOU 232 CB ILE A 64 16199 17862 11532 2795 -1446 -212 C
ATOM 233 CG1 ILE A 64 26.421 11.846 -24.350 1.00122.10 C
ANISOU 233 CG1 ILE A 64 16318 18343 11730 3079 -1630 -365 C
ATOM 234 CG2 ILE A 64 24.604 13.005 -22.989 1.00120.04 C
ANISOU 234 CG2 ILE A 64 16244 17827 11538 2698 -1433 -190 C
ATOM 235 CD1 ILE A 64 27.312 12.912 -24.961 1.00128.00 C
ANISOU 235 CD1 ILE A 64 16627 19391 12615 3023 -1651 -472 C
ATOM 236 N ILE A 65 21.756 11.568 -24.151 1.00118.01 N
ANISOU 236 N ILE A 65 16433 17093 11314 2352 -1098 51 N
ATOM 237 CA ILE A 65 20.393 11.734 -23.621 1.00117.43 C
ANISOU 237 CA ILE A 65 16531 16824 11264 2126 -946 138 C
ATOM 238 C ILE A 65 19.675 10.378 -23.419 1.00124.64 C
ANISOU 238 C ILE A 65 17851 17478 12028 2149 -886 189 C
ATOM 239 O ILE A 65 19.043 10.183 -22.376 1.00124.88 O
ANISOU 239 O ILE A 65 18153 17329 11965 2084 -826 222 O
ATOM 240 CB ILE A 65 19.564 12.741 -24.479 1.00118.11 C
ANISOU 240 CB ILE A 65 16336 16976 11563 1854 -811 175 C
ATOM 241 CG1 ILE A 65 20.177 14.165 -24.404 1.00117.66 C
ANISOU 241 CG1 ILE A 65 15946 17135 11624 1806 -857 130 C
ATOM 242 CG2 ILE A 65 18.085 12.766 -24.061 1.00117.82 C
ANISOU 242 CG2 ILE A 65 16466 16744 11555 1628 -651 242 C
ATOM 243 CD1 ILE A 65 19.850 15.116 -25.576 1.00122.91 C
ANISOU 243 CD1 ILE A 65 16301 17919 12481 1614 -779 141 C
ATOM 244 N LEU A 66 19.800 9.445 -24.389 1.00123.06 N
ANISOU 244 N LEU A 66 17707 17256 11796 2237 -900 189 N
ATOM 245 CA LEU A 66 19.154 8.131 -24.318 1.00124.40 C
ANISOU 245 CA LEU A 66 18267 17181 11820 2253 -841 233 C
ATOM 246 C LEU A 66 19.621 7.254 -23.150 1.00132.17 C
ANISOU 246 C LEU A 66 19647 18014 12557 2473 -945 215 C
ATOM 247 O LEU A 66 18.786 6.879 -22.323 1.00132.49 O
ANISOU 247 O LEU A 66 20014 17833 12492 2370 -849 259 O
ATOM 248 CB LEU A 66 19.266 7.360 -25.642 1.00124.27 C
ANISOU 248 CB LEU A 66 18213 17181 11823 2307 -841 236 C
ATOM 249 CG LEU A 66 18.377 7.801 -26.805 1.00127.00 C
ANISOU 249 CG LEU A 66 18332 17561 12363 2061 -700 275 C
ATOM 250 CD1 LEU A 66 18.442 6.787 -27.921 1.00127.32 C
ANISOU 250 CD1 LEU A 66 18419 17580 12378 2143 -710 278 C
ATOM 251 CD2 LEU A 66 16.921 7.970 -26.379 1.00128.84 C
ANISOU 251 CD2 LEU A 66 18711 17612 12629 1797 -523 328 C
ATOM 252 N LYS A 67 20.934 6.926 -23.077 1.00131.35 N
ANISOU 252 N LYS A 67 19524 18027 12355 2775 -1141 140 N
ATOM 253 CA LYS A 67 21.488 6.073 -22.011 1.00133.90 C
ANISOU 253 CA LYS A 67 20232 18213 12429 3031 -1275 109 C
ATOM 254 C LYS A 67 21.507 6.764 -20.643 1.00139.47 C
ANISOU 254 C LYS A 67 21014 18892 13088 3010 -1298 102 C
ATOM 255 O LYS A 67 21.396 6.085 -19.618 1.00140.31 O
ANISOU 255 O LYS A 67 21542 18782 12988 3093 -1321 118 O
ATOM 256 CB LYS A 67 22.872 5.496 -22.378 1.00137.46 C
ANISOU 256 CB LYS A 67 20629 18808 12791 3379 -1490 9 C
ATOM 257 CG LYS A 67 22.879 4.511 -23.569 1.00146.06 C
ANISOU 257 CG LYS A 67 21752 19877 13868 3448 -1483 15 C
ATOM 258 CD LYS A 67 21.975 3.267 -23.411 1.00153.18 C
ANISOU 258 CD LYS A 67 23127 20461 14612 3391 -1379 97 C
ATOM 259 CE LYS A 67 22.581 2.157 -22.586 1.00162.07 C
ANISOU 259 CE LYS A 67 24730 21401 15449 3682 -1524 67 C
ATOM 260 NZ LYS A 67 21.659 0.998 -22.481 1.00169.52 N
ANISOU 260 NZ LYS A 67 26137 22032 16242 3584 -1398 147 N
ATOM 261 N GLN A 68 21.618 8.107 -20.632 1.00135.88 N
ANISOU 261 N GLN A 68 20173 18641 12815 2887 -1286 82 N
ATOM 262 CA GLN A 68 21.586 8.918 -19.417 1.00136.25 C
ANISOU 262 CA GLN A 68 20241 18682 12846 2838 -1296 77 C
ATOM 263 C GLN A 68 20.107 9.191 -19.092 1.00139.98 C
ANISOU 263 C GLN A 68 20839 18972 13374 2519 -1075 168 C
ATOM 264 O GLN A 68 19.544 10.213 -19.494 1.00137.56 O
ANISOU 264 O GLN A 68 20230 18768 13270 2286 -963 192 O
ATOM 265 CB GLN A 68 22.405 10.212 -19.610 1.00136.80 C
ANISOU 265 CB GLN A 68 19847 19049 13082 2840 -1373 9 C
ATOM 266 CG GLN A 68 22.633 11.065 -18.368 1.00155.64 C
ANISOU 266 CG GLN A 68 22229 21463 15444 2837 -1422 -14 C
ATOM 267 CD GLN A 68 23.320 12.372 -18.708 1.00177.04 C
ANISOU 267 CD GLN A 68 24473 24460 18333 2785 -1465 -77 C
ATOM 268 OE1 GLN A 68 22.936 13.096 -19.640 1.00171.22 O
ANISOU 268 OE1 GLN A 68 23439 23831 17787 2579 -1356 -51 O
ATOM 269 NE2 GLN A 68 24.343 12.717 -17.942 1.00171.52 N
ANISOU 269 NE2 GLN A 68 23718 23884 17568 2967 -1627 -168 N
ATOM 270 N LYS A 69 19.469 8.222 -18.413 1.00138.91 N
ANISOU 270 N LYS A 69 21164 18563 13052 2510 -1011 210 N
ATOM 271 CA LYS A 69 18.068 8.281 -17.986 1.00138.66 C
ANISOU 271 CA LYS A 69 21309 18340 13037 2217 -796 274 C
ATOM 272 C LYS A 69 17.909 9.373 -16.923 1.00142.62 C
ANISOU 272 C LYS A 69 21725 18878 13585 2112 -773 270 C
ATOM 273 O LYS A 69 18.834 9.605 -16.135 1.00143.21 O
ANISOU 273 O LYS A 69 21818 19022 13575 2309 -932 227 O
ATOM 274 CB LYS A 69 17.598 6.923 -17.433 1.00143.54 C
ANISOU 274 CB LYS A 69 22478 18653 13408 2248 -742 303 C
ATOM 275 CG LYS A 69 17.808 5.738 -18.378 1.00162.56 C
ANISOU 275 CG LYS A 69 25033 20996 15735 2375 -776 306 C
ATOM 276 CD LYS A 69 17.651 4.407 -17.640 1.00176.00 C
ANISOU 276 CD LYS A 69 27334 22395 17144 2471 -771 324 C
ATOM 277 CE LYS A 69 18.598 3.336 -18.133 1.00187.46 C
ANISOU 277 CE LYS A 69 28962 23823 18441 2781 -941 296 C
ATOM 278 NZ LYS A 69 19.975 3.515 -17.597 1.00195.50 N
ANISOU 278 NZ LYS A 69 29929 24980 19373 3126 -1199 223 N
ATOM 279 N GLU A 70 16.738 10.046 -16.917 1.00138.06 N
ANISOU 279 N GLU A 70 21047 18264 13146 1809 -581 305 N
ATOM 280 CA GLU A 70 16.340 11.178 -16.050 1.00137.26 C
ANISOU 280 CA GLU A 70 20833 18196 13122 1655 -520 305 C
ATOM 281 C GLU A 70 16.840 12.525 -16.619 1.00138.66 C
ANISOU 281 C GLU A 70 20513 18653 13518 1636 -588 279 C
ATOM 282 O GLU A 70 16.401 13.590 -16.173 1.00137.27 O
ANISOU 282 O GLU A 70 20184 18531 13442 1492 -534 280 O
ATOM 283 CB GLU A 70 16.689 10.990 -14.553 1.00140.47 C
ANISOU 283 CB GLU A 70 21587 18467 13320 1772 -586 296 C
ATOM 284 CG GLU A 70 16.035 9.777 -13.895 1.00154.99 C
ANISOU 284 CG GLU A 70 23953 20001 14935 1736 -484 323 C
ATOM 285 CD GLU A 70 14.589 9.480 -14.259 1.00181.00 C
ANISOU 285 CD GLU A 70 27315 23159 18296 1427 -235 351 C
ATOM 286 OE1 GLU A 70 13.713 10.331 -13.981 1.00180.01 O
ANISOU 286 OE1 GLU A 70 27037 23057 18303 1187 -92 350 O
ATOM 287 OE2 GLU A 70 14.335 8.392 -14.825 1.00176.93 O
ANISOU 287 OE2 GLU A 70 27002 22520 17702 1429 -185 364 O
ATOM 288 N MET A 71 17.718 12.457 -17.643 1.00134.08 N
ANISOU 288 N MET A 71 19696 18242 13005 1771 -695 254 N
ATOM 289 CA MET A 71 18.215 13.584 -18.433 1.00131.86 C
ANISOU 289 CA MET A 71 18963 18217 12921 1739 -743 226 C
ATOM 290 C MET A 71 17.391 13.563 -19.723 1.00132.39 C
ANISOU 290 C MET A 71 18871 18291 13139 1562 -616 258 C
ATOM 291 O MET A 71 17.469 14.484 -20.535 1.00130.35 O
ANISOU 291 O MET A 71 18268 18205 13054 1479 -612 248 O
ATOM 292 CB MET A 71 19.709 13.429 -18.751 1.00135.04 C
ANISOU 292 CB MET A 71 19233 18800 13277 2010 -941 158 C
ATOM 293 N ARG A 72 16.589 12.489 -19.885 1.00128.20 N
ANISOU 293 N ARG A 72 18618 17562 12530 1501 -511 292 N
ATOM 294 CA ARG A 72 15.670 12.250 -20.994 1.00126.38 C
ANISOU 294 CA ARG A 72 18311 17294 12412 1334 -383 317 C
ATOM 295 C ARG A 72 14.263 12.799 -20.656 1.00127.38 C
ANISOU 295 C ARG A 72 18431 17331 12636 1054 -202 331 C
ATOM 296 O ARG A 72 13.318 12.037 -20.420 1.00127.92 O
ANISOU 296 O ARG A 72 18752 17213 12638 934 -71 342 O
ATOM 297 CB ARG A 72 15.653 10.755 -21.421 1.00128.03 C
ANISOU 297 CB ARG A 72 18815 17352 12477 1435 -379 331 C
ATOM 298 CG ARG A 72 15.583 9.745 -20.270 1.00142.56 C
ANISOU 298 CG ARG A 72 21121 18969 14078 1520 -378 340 C
ATOM 299 CD ARG A 72 15.002 8.401 -20.681 1.00155.39 C
ANISOU 299 CD ARG A 72 23065 20393 15584 1498 -294 362 C
ATOM 300 NE ARG A 72 13.536 8.418 -20.740 1.00165.14 N
ANISOU 300 NE ARG A 72 24342 21507 16895 1199 -79 375 N
ATOM 301 CZ ARG A 72 12.730 8.169 -19.709 1.00180.94 C
ANISOU 301 CZ ARG A 72 26634 23321 18795 1051 53 376 C
ATOM 302 NH1 ARG A 72 13.236 7.893 -18.512 1.00168.79 N
ANISOU 302 NH1 ARG A 72 25395 21674 17064 1177 -11 378 N
ATOM 303 NH2 ARG A 72 11.414 8.205 -19.865 1.00167.98 N
ANISOU 303 NH2 ARG A 72 24984 21601 17240 775 250 364 N
ATOM 304 N ASN A 73 14.147 14.139 -20.599 1.00120.24 N
ANISOU 304 N ASN A 73 17238 16563 11884 951 -197 320 N
ATOM 305 CA ASN A 73 12.879 14.826 -20.343 1.00118.01 C
ANISOU 305 CA ASN A 73 16888 16234 11715 705 -48 315 C
ATOM 306 C ASN A 73 12.199 15.196 -21.680 1.00118.60 C
ANISOU 306 C ASN A 73 16701 16386 11977 570 15 309 C
ATOM 307 O ASN A 73 12.814 15.031 -22.738 1.00117.91 O
ANISOU 307 O ASN A 73 16478 16395 11928 666 -62 316 O
ATOM 308 CB ASN A 73 13.079 16.039 -19.434 1.00116.28 C
ANISOU 308 CB ASN A 73 16543 16101 11539 680 -82 304 C
ATOM 309 CG ASN A 73 13.990 17.089 -20.002 1.00131.26 C
ANISOU 309 CG ASN A 73 18106 18217 13549 751 -203 293 C
ATOM 310 OD1 ASN A 73 13.561 17.993 -20.720 1.00123.52 O
ANISOU 310 OD1 ASN A 73 16867 17332 12734 625 -167 287 O
ATOM 311 ND2 ASN A 73 15.266 16.998 -19.681 1.00123.16 N
ANISOU 311 ND2 ASN A 73 17090 17276 12429 955 -351 280 N
ATOM 312 N VAL A 74 10.934 15.676 -21.631 1.00112.53 N
ANISOU 312 N VAL A 74 15865 15574 11317 355 150 287 N
ATOM 313 CA VAL A 74 10.109 16.035 -22.799 1.00109.87 C
ANISOU 313 CA VAL A 74 15304 15289 11151 221 211 266 C
ATOM 314 C VAL A 74 10.886 16.886 -23.816 1.00108.81 C
ANISOU 314 C VAL A 74 14868 15342 11134 295 94 276 C
ATOM 315 O VAL A 74 10.834 16.586 -25.009 1.00107.94 O
ANISOU 315 O VAL A 74 14663 15265 11086 300 85 279 O
ATOM 316 CB VAL A 74 8.748 16.681 -22.410 1.00113.68 C
ANISOU 316 CB VAL A 74 15730 15728 11737 4 348 216 C
ATOM 317 CG1 VAL A 74 7.841 16.831 -23.628 1.00112.81 C
ANISOU 317 CG1 VAL A 74 15435 15648 11780 -114 404 178 C
ATOM 318 CG2 VAL A 74 8.035 15.877 -21.322 1.00114.83 C
ANISOU 318 CG2 VAL A 74 16185 15692 11752 -87 478 195 C
ATOM 319 N THR A 75 11.631 17.909 -23.337 1.00102.00 N
ANISOU 319 N THR A 75 13873 14595 10289 348 9 279 N
ATOM 320 CA THR A 75 12.446 18.802 -24.174 1.00 99.44 C
ANISOU 320 CA THR A 75 13280 14447 10056 399 -91 280 C
ATOM 321 C THR A 75 13.594 18.026 -24.847 1.00100.64 C
ANISOU 321 C THR A 75 13443 14661 10134 576 -188 291 C
ATOM 322 O THR A 75 13.796 18.151 -26.054 1.00 99.64 O
ANISOU 322 O THR A 75 13154 14619 10085 578 -212 290 O
ATOM 323 CB THR A 75 12.943 20.018 -23.352 1.00104.67 C
ANISOU 323 CB THR A 75 13829 15205 10737 398 -146 270 C
ATOM 324 OG1 THR A 75 11.836 20.645 -22.697 1.00105.51 O
ANISOU 324 OG1 THR A 75 13949 15241 10899 246 -53 255 O
ATOM 325 CG2 THR A 75 13.691 21.044 -24.195 1.00 99.84 C
ANISOU 325 CG2 THR A 75 12948 14765 10220 407 -224 262 C
ATOM 326 N ASN A 76 14.314 17.212 -24.062 1.00 95.94 N
ANISOU 326 N ASN A 76 13052 14019 9382 728 -244 294 N
ATOM 327 CA ASN A 76 15.459 16.420 -24.507 1.00 95.34 C
ANISOU 327 CA ASN A 76 13008 14002 9215 927 -351 287 C
ATOM 328 C ASN A 76 15.075 15.284 -25.462 1.00 96.59 C
ANISOU 328 C ASN A 76 13271 14073 9354 940 -308 304 C
ATOM 329 O ASN A 76 15.861 14.957 -26.349 1.00 96.06 O
ANISOU 329 O ASN A 76 13118 14099 9283 1058 -381 294 O
ATOM 330 CB ASN A 76 16.262 15.910 -23.303 1.00 97.56 C
ANISOU 330 CB ASN A 76 13498 14247 9324 1103 -438 274 C
ATOM 331 CG ASN A 76 17.136 16.944 -22.607 1.00120.07 C
ANISOU 331 CG ASN A 76 16191 17248 12183 1164 -536 239 C
ATOM 332 OD1 ASN A 76 18.316 16.711 -22.357 1.00118.01 O
ANISOU 332 OD1 ASN A 76 15927 17079 11833 1358 -665 198 O
ATOM 333 ND2 ASN A 76 16.592 18.098 -22.244 1.00110.55 N
ANISOU 333 ND2 ASN A 76 14855 16072 11077 1007 -483 243 N
ATOM 334 N ILE A 77 13.869 14.707 -25.300 1.00 91.62 N
ANISOU 334 N ILE A 77 12820 13275 8718 810 -184 321 N
ATOM 335 CA ILE A 77 13.341 13.647 -26.169 1.00 91.11 C
ANISOU 335 CA ILE A 77 12863 13114 8640 789 -125 333 C
ATOM 336 C ILE A 77 13.072 14.229 -27.572 1.00 93.16 C
ANISOU 336 C ILE A 77 12847 13482 9066 708 -117 329 C
ATOM 337 O ILE A 77 13.345 13.566 -28.575 1.00 92.10 O
ANISOU 337 O ILE A 77 12702 13366 8925 780 -146 336 O
ATOM 338 CB ILE A 77 12.101 12.965 -25.520 1.00 94.66 C
ANISOU 338 CB ILE A 77 13569 13362 9036 643 19 333 C
ATOM 339 CG1 ILE A 77 12.539 12.063 -24.361 1.00 96.82 C
ANISOU 339 CG1 ILE A 77 14193 13498 9098 764 -2 344 C
ATOM 340 CG2 ILE A 77 11.261 12.167 -26.530 1.00 94.88 C
ANISOU 340 CG2 ILE A 77 13628 13312 9111 544 109 329 C
ATOM 341 CD1 ILE A 77 11.513 11.896 -23.293 1.00106.29 C
ANISOU 341 CD1 ILE A 77 15613 14534 10239 607 132 333 C
ATOM 342 N LEU A 78 12.588 15.485 -27.627 1.00 89.24 N
ANISOU 342 N LEU A 78 12142 13056 8710 569 -86 315 N
ATOM 343 CA LEU A 78 12.323 16.208 -28.873 1.00 88.38 C
ANISOU 343 CA LEU A 78 11791 13040 8750 490 -87 308 C
ATOM 344 C LEU A 78 13.625 16.675 -29.549 1.00 91.90 C
ANISOU 344 C LEU A 78 12055 13654 9207 605 -197 308 C
ATOM 345 O LEU A 78 13.651 16.853 -30.768 1.00 90.43 O
ANISOU 345 O LEU A 78 11732 13527 9100 581 -206 307 O
ATOM 346 CB LEU A 78 11.378 17.393 -28.627 1.00 87.91 C
ANISOU 346 CB LEU A 78 11599 12988 8815 322 -30 285 C
ATOM 347 CG LEU A 78 9.890 17.070 -28.429 1.00 93.12 C
ANISOU 347 CG LEU A 78 12354 13514 9513 170 94 256 C
ATOM 348 CD1 LEU A 78 9.208 18.154 -27.607 1.00 93.09 C
ANISOU 348 CD1 LEU A 78 12270 13518 9582 52 136 223 C
ATOM 349 CD2 LEU A 78 9.165 16.888 -29.770 1.00 95.00 C
ANISOU 349 CD2 LEU A 78 12506 13740 9849 102 126 237 C
ATOM 350 N ILE A 79 14.701 16.867 -28.752 1.00 89.29 N
ANISOU 350 N ILE A 79 11728 13402 8795 726 -278 298 N
ATOM 351 CA ILE A 79 16.039 17.253 -29.220 1.00 88.98 C
ANISOU 351 CA ILE A 79 11519 13539 8751 838 -378 272 C
ATOM 352 C ILE A 79 16.705 16.038 -29.910 1.00 93.87 C
ANISOU 352 C ILE A 79 12215 14163 9287 995 -425 267 C
ATOM 353 O ILE A 79 17.378 16.208 -30.928 1.00 93.58 O
ANISOU 353 O ILE A 79 12017 14251 9289 1031 -463 245 O
ATOM 354 CB ILE A 79 16.865 17.884 -28.052 1.00 92.30 C
ANISOU 354 CB ILE A 79 11906 14045 9117 904 -448 244 C
ATOM 355 CG1 ILE A 79 16.439 19.358 -27.770 1.00 91.60 C
ANISOU 355 CG1 ILE A 79 11662 14004 9137 744 -416 243 C
ATOM 356 CG2 ILE A 79 18.379 17.754 -28.224 1.00 93.71 C
ANISOU 356 CG2 ILE A 79 11985 14387 9232 1078 -562 192 C
ATOM 357 CD1 ILE A 79 16.845 20.476 -28.827 1.00 96.11 C
ANISOU 357 CD1 ILE A 79 11980 14721 9817 664 -430 223 C
ATOM 358 N VAL A 80 16.465 14.816 -29.377 1.00 91.06 N
ANISOU 358 N VAL A 80 12123 13664 8813 1079 -414 283 N
ATOM 359 CA VAL A 80 16.933 13.529 -29.913 1.00 91.45 C
ANISOU 359 CA VAL A 80 12304 13678 8763 1233 -454 282 C
ATOM 360 C VAL A 80 16.244 13.281 -31.271 1.00 95.63 C
ANISOU 360 C VAL A 80 12775 14175 9385 1133 -386 304 C
ATOM 361 O VAL A 80 16.892 12.832 -32.221 1.00 95.63 O
ANISOU 361 O VAL A 80 12716 14246 9374 1230 -431 291 O
ATOM 362 CB VAL A 80 16.681 12.390 -28.880 1.00 96.13 C
ANISOU 362 CB VAL A 80 13241 14091 9194 1319 -447 298 C
ATOM 363 CG1 VAL A 80 16.712 11.001 -29.519 1.00 96.50 C
ANISOU 363 CG1 VAL A 80 13477 14043 9147 1427 -453 309 C
ATOM 364 CG2 VAL A 80 17.677 12.471 -27.729 1.00 96.95 C
ANISOU 364 CG2 VAL A 80 13407 14246 9184 1483 -555 265 C
ATOM 365 N ASN A 81 14.937 13.614 -31.354 1.00 91.92 N
ANISOU 365 N ASN A 81 12312 13608 9007 942 -282 327 N
ATOM 366 CA ASN A 81 14.110 13.506 -32.557 1.00 90.97 C
ANISOU 366 CA ASN A 81 12131 13449 8984 830 -218 338 C
ATOM 367 C ASN A 81 14.580 14.514 -33.605 1.00 94.68 C
ANISOU 367 C ASN A 81 12334 14075 9564 802 -258 325 C
ATOM 368 O ASN A 81 14.562 14.209 -34.799 1.00 94.31 O
ANISOU 368 O ASN A 81 12240 14041 9551 805 -256 329 O
ATOM 369 CB ASN A 81 12.639 13.763 -32.210 1.00 89.51 C
ANISOU 369 CB ASN A 81 11988 13148 8872 640 -110 337 C
ATOM 370 CG ASN A 81 11.685 13.528 -33.356 1.00 99.88 C
ANISOU 370 CG ASN A 81 13266 14408 10276 533 -49 332 C
ATOM 371 OD1 ASN A 81 11.418 12.389 -33.748 1.00 93.59 O
ANISOU 371 OD1 ASN A 81 12624 13516 9421 557 -16 339 O
ATOM 372 ND2 ASN A 81 11.130 14.599 -33.896 1.00 85.67 N
ANISOU 372 ND2 ASN A 81 11275 12661 8614 415 -36 314 N
ATOM 373 N LEU A 82 14.992 15.714 -33.149 1.00 91.18 N
ANISOU 373 N LEU A 82 11736 13741 9168 766 -289 309 N
ATOM 374 CA LEU A 82 15.482 16.798 -33.994 1.00 90.76 C
ANISOU 374 CA LEU A 82 11455 13828 9202 719 -318 292 C
ATOM 375 C LEU A 82 16.831 16.446 -34.621 1.00 96.29 C
ANISOU 375 C LEU A 82 12079 14660 9845 859 -387 264 C
ATOM 376 O LEU A 82 17.014 16.676 -35.815 1.00 95.89 O
ANISOU 376 O LEU A 82 11916 14671 9847 826 -383 257 O
ATOM 377 CB LEU A 82 15.599 18.084 -33.177 1.00 90.66 C
ANISOU 377 CB LEU A 82 11335 13883 9228 648 -330 278 C
ATOM 378 CG LEU A 82 15.100 19.339 -33.857 1.00 94.83 C
ANISOU 378 CG LEU A 82 11704 14454 9873 506 -311 274 C
ATOM 379 CD1 LEU A 82 14.407 20.223 -32.870 1.00 94.71 C
ANISOU 379 CD1 LEU A 82 11690 14390 9907 399 -281 275 C
ATOM 380 CD2 LEU A 82 16.239 20.090 -34.528 1.00 98.36 C
ANISOU 380 CD2 LEU A 82 11985 15068 10320 524 -359 244 C
ATOM 381 N SER A 83 17.765 15.873 -33.828 1.00 94.07 N
ANISOU 381 N SER A 83 11867 14423 9453 1021 -451 238 N
ATOM 382 CA SER A 83 19.085 15.471 -34.316 1.00 94.77 C
ANISOU 382 CA SER A 83 11877 14650 9480 1177 -525 186 C
ATOM 383 C SER A 83 19.051 14.144 -35.098 1.00100.13 C
ANISOU 383 C SER A 83 12683 15257 10105 1276 -524 200 C
ATOM 384 O SER A 83 20.015 13.832 -35.799 1.00100.51 O
ANISOU 384 O SER A 83 12639 15422 10127 1380 -569 154 O
ATOM 385 CB SER A 83 20.114 15.450 -33.187 1.00 98.45 C
ANISOU 385 CB SER A 83 12351 15205 9850 1328 -613 132 C
ATOM 386 OG SER A 83 19.999 14.301 -32.368 1.00106.12 O
ANISOU 386 OG SER A 83 13578 16038 10704 1451 -638 153 O
ATOM 387 N PHE A 84 17.948 13.380 -34.999 1.00 97.37 N
ANISOU 387 N PHE A 84 12539 14721 9738 1235 -467 253 N
ATOM 388 CA PHE A 84 17.799 12.148 -35.764 1.00 98.40 C
ANISOU 388 CA PHE A 84 12803 14766 9818 1308 -457 270 C
ATOM 389 C PHE A 84 17.475 12.505 -37.217 1.00100.53 C
ANISOU 389 C PHE A 84 12931 15069 10198 1196 -414 281 C
ATOM 390 O PHE A 84 17.936 11.817 -38.130 1.00 99.95 O
ANISOU 390 O PHE A 84 12860 15021 10096 1281 -432 272 O
ATOM 391 CB PHE A 84 16.721 11.224 -35.169 1.00101.60 C
ANISOU 391 CB PHE A 84 13483 14960 10161 1278 -398 313 C
ATOM 392 CG PHE A 84 16.449 10.009 -36.030 1.00105.15 C
ANISOU 392 CG PHE A 84 14077 15312 10563 1327 -378 332 C
ATOM 393 CD1 PHE A 84 17.255 8.878 -35.942 1.00110.62 C
ANISOU 393 CD1 PHE A 84 14914 15999 11119 1536 -450 315 C
ATOM 394 CD2 PHE A 84 15.419 10.017 -36.971 1.00107.82 C
ANISOU 394 CD2 PHE A 84 14400 15571 10994 1174 -296 358 C
ATOM 395 CE1 PHE A 84 17.030 7.771 -36.773 1.00112.39 C
ANISOU 395 CE1 PHE A 84 15276 16132 11296 1583 -432 333 C
ATOM 396 CE2 PHE A 84 15.201 8.913 -37.810 1.00111.34 C
ANISOU 396 CE2 PHE A 84 14974 15933 11399 1216 -278 372 C
ATOM 397 CZ PHE A 84 16.004 7.796 -37.701 1.00110.75 C
ANISOU 397 CZ PHE A 84 15051 15845 11184 1415 -343 364 C
ATOM 398 N SER A 85 16.659 13.562 -37.428 1.00 96.35 N
ANISOU 398 N SER A 85 12291 14530 9787 1015 -361 297 N
ATOM 399 CA SER A 85 16.285 14.044 -38.767 1.00 95.28 C
ANISOU 399 CA SER A 85 12037 14414 9752 906 -330 305 C
ATOM 400 C SER A 85 17.498 14.678 -39.457 1.00 97.62 C
ANISOU 400 C SER A 85 12147 14888 10057 941 -370 264 C
ATOM 401 O SER A 85 17.673 14.508 -40.661 1.00 97.10 O
ANISOU 401 O SER A 85 12035 14847 10011 934 -361 261 O
ATOM 402 CB SER A 85 15.113 15.025 -38.698 1.00 98.71 C
ANISOU 402 CB SER A 85 12422 14787 10295 728 -281 319 C
ATOM 403 OG SER A 85 15.483 16.340 -38.309 1.00108.37 O
ANISOU 403 OG SER A 85 13497 16115 11562 668 -300 300 O
ATOM 404 N ASP A 86 18.351 15.367 -38.670 1.00 93.59 N
ANISOU 404 N ASP A 86 11535 14502 9523 973 -410 224 N
ATOM 405 CA ASP A 86 19.585 16.020 -39.112 1.00 93.36 C
ANISOU 405 CA ASP A 86 11318 14661 9494 991 -439 162 C
ATOM 406 C ASP A 86 20.699 14.996 -39.429 1.00 97.09 C
ANISOU 406 C ASP A 86 11785 15227 9876 1177 -490 107 C
ATOM 407 O ASP A 86 21.729 15.351 -40.009 1.00 96.91 O
ANISOU 407 O ASP A 86 11600 15370 9852 1192 -502 38 O
ATOM 408 CB ASP A 86 20.042 17.076 -38.080 1.00 95.41 C
ANISOU 408 CB ASP A 86 11472 15019 9762 950 -461 128 C
ATOM 409 CG ASP A 86 19.085 18.246 -37.857 1.00104.55 C
ANISOU 409 CG ASP A 86 12611 16107 11008 770 -416 168 C
ATOM 410 OD1 ASP A 86 18.336 18.602 -38.806 1.00104.15 O
ANISOU 410 OD1 ASP A 86 12556 15990 11027 656 -374 199 O
ATOM 411 OD2 ASP A 86 19.126 18.842 -36.756 1.00110.57 O
ANISOU 411 OD2 ASP A 86 13361 16886 11766 751 -432 161 O
ATOM 412 N LEU A 87 20.474 13.727 -39.054 1.00 93.70 N
ANISOU 412 N LEU A 87 11543 14690 9367 1314 -516 130 N
ATOM 413 CA LEU A 87 21.361 12.601 -39.325 1.00 94.62 C
ANISOU 413 CA LEU A 87 11703 14861 9388 1514 -574 83 C
ATOM 414 C LEU A 87 20.993 12.072 -40.707 1.00 97.69 C
ANISOU 414 C LEU A 87 12113 15197 9806 1479 -528 112 C
ATOM 415 O LEU A 87 21.884 11.690 -41.461 1.00 98.71 O
ANISOU 415 O LEU A 87 12155 15442 9907 1568 -551 54 O
ATOM 416 CB LEU A 87 21.133 11.501 -38.284 1.00 95.64 C
ANISOU 416 CB LEU A 87 12077 14856 9406 1661 -617 107 C
ATOM 417 CG LEU A 87 22.358 10.869 -37.653 1.00102.12 C
ANISOU 417 CG LEU A 87 12922 15776 10104 1902 -726 26 C
ATOM 418 CD1 LEU A 87 22.568 11.393 -36.252 1.00102.36 C
ANISOU 418 CD1 LEU A 87 12946 15840 10106 1925 -773 2 C
ATOM 419 CD2 LEU A 87 22.193 9.367 -37.575 1.00106.20 C
ANISOU 419 CD2 LEU A 87 13716 16139 10498 2066 -759 53 C
ATOM 420 N LEU A 88 19.675 12.070 -41.045 1.00 91.85 N
ANISOU 420 N LEU A 88 11482 14290 9126 1345 -464 190 N
ATOM 421 CA LEU A 88 19.138 11.628 -42.338 1.00 90.20 C
ANISOU 421 CA LEU A 88 11309 14008 8953 1293 -421 223 C
ATOM 422 C LEU A 88 19.572 12.530 -43.486 1.00 91.45 C
ANISOU 422 C LEU A 88 11279 14284 9182 1195 -397 195 C
ATOM 423 O LEU A 88 20.070 12.015 -44.478 1.00 91.28 O
ANISOU 423 O LEU A 88 11237 14307 9138 1251 -396 173 O
ATOM 424 CB LEU A 88 17.605 11.532 -42.315 1.00 89.31 C
ANISOU 424 CB LEU A 88 11326 13709 8897 1160 -363 289 C
ATOM 425 CG LEU A 88 17.002 10.295 -41.683 1.00 94.45 C
ANISOU 425 CG LEU A 88 12214 14203 9468 1230 -355 318 C
ATOM 426 CD1 LEU A 88 15.613 10.584 -41.210 1.00 94.34 C
ANISOU 426 CD1 LEU A 88 12271 14060 9513 1079 -295 350 C
ATOM 427 CD2 LEU A 88 16.968 9.129 -42.658 1.00 96.58 C
ANISOU 427 CD2 LEU A 88 12599 14395 9702 1284 -343 335 C
ATOM 428 N VAL A 89 19.383 13.865 -43.362 1.00 86.09 N
ANISOU 428 N VAL A 89 10482 13651 8579 1047 -374 193 N
ATOM 429 CA VAL A 89 19.764 14.842 -44.394 1.00 85.46 C
ANISOU 429 CA VAL A 89 10256 13665 8550 933 -344 167 C
ATOM 430 C VAL A 89 21.301 14.824 -44.625 1.00 91.05 C
ANISOU 430 C VAL A 89 10822 14573 9201 1021 -363 76 C
ATOM 431 O VAL A 89 21.743 14.989 -45.763 1.00 91.02 O
ANISOU 431 O VAL A 89 10748 14633 9202 979 -330 46 O
ATOM 432 CB VAL A 89 19.175 16.261 -44.130 1.00 88.16 C
ANISOU 432 CB VAL A 89 10539 13988 8969 760 -320 185 C
ATOM 433 CG1 VAL A 89 19.547 16.791 -42.754 1.00 88.26 C
ANISOU 433 CG1 VAL A 89 10495 14074 8966 775 -346 158 C
ATOM 434 CG2 VAL A 89 19.548 17.259 -45.223 1.00 87.66 C
ANISOU 434 CG2 VAL A 89 10378 13992 8938 635 -285 161 C
ATOM 435 N ALA A 90 22.091 14.541 -43.566 1.00 88.22 N
ANISOU 435 N ALA A 90 10428 14309 8781 1153 -417 22 N
ATOM 436 CA ALA A 90 23.547 14.434 -43.648 1.00 89.33 C
ANISOU 436 CA ALA A 90 10419 14656 8868 1261 -448 -91 C
ATOM 437 C ALA A 90 23.989 13.177 -44.413 1.00 94.73 C
ANISOU 437 C ALA A 90 11153 15350 9489 1419 -469 -119 C
ATOM 438 O ALA A 90 24.985 13.229 -45.130 1.00 95.25 O
ANISOU 438 O ALA A 90 11076 15577 9537 1447 -459 -211 O
ATOM 439 CB ALA A 90 24.153 14.438 -42.254 1.00 90.86 C
ANISOU 439 CB ALA A 90 10578 14934 9011 1377 -519 -146 C
ATOM 440 N ILE A 91 23.255 12.060 -44.269 1.00 91.95 N
ANISOU 440 N ILE A 91 11006 14828 9101 1514 -491 -47 N
ATOM 441 CA ILE A 91 23.584 10.804 -44.945 1.00 93.28 C
ANISOU 441 CA ILE A 91 11258 14982 9201 1672 -516 -64 C
ATOM 442 C ILE A 91 22.938 10.716 -46.346 1.00 98.85 C
ANISOU 442 C ILE A 91 12004 15597 9957 1561 -448 -8 C
ATOM 443 O ILE A 91 23.655 10.604 -47.336 1.00 99.43 O
ANISOU 443 O ILE A 91 11987 15775 10018 1587 -431 -66 O
ATOM 444 CB ILE A 91 23.274 9.552 -44.060 1.00 96.96 C
ANISOU 444 CB ILE A 91 11952 15315 9574 1851 -581 -30 C
ATOM 445 CG1 ILE A 91 24.083 9.558 -42.743 1.00 98.25 C
ANISOU 445 CG1 ILE A 91 12081 15582 9666 2002 -668 -104 C
ATOM 446 CG2 ILE A 91 23.520 8.245 -44.836 1.00 98.95 C
ANISOU 446 CG2 ILE A 91 12323 15522 9751 2006 -604 -37 C
ATOM 447 CD1 ILE A 91 23.494 8.678 -41.607 1.00104.12 C
ANISOU 447 CD1 ILE A 91 13084 16152 10324 2109 -715 -49 C
ATOM 448 N MET A 92 21.598 10.757 -46.415 1.00 95.66 N
ANISOU 448 N MET A 92 11734 15007 9607 1442 -411 91 N
ATOM 449 CA MET A 92 20.789 10.610 -47.634 1.00 95.45 C
ANISOU 449 CA MET A 92 11772 14868 9627 1344 -361 146 C
ATOM 450 C MET A 92 20.817 11.780 -48.631 1.00 99.08 C
ANISOU 450 C MET A 92 12101 15387 10158 1174 -309 136 C
ATOM 451 O MET A 92 20.557 11.544 -49.811 1.00 98.94 O
ANISOU 451 O MET A 92 12120 15320 10153 1137 -280 154 O
ATOM 452 CB MET A 92 19.313 10.315 -47.276 1.00 97.27 C
ANISOU 452 CB MET A 92 12172 14892 9893 1271 -344 231 C
ATOM 453 CG MET A 92 19.118 9.348 -46.123 1.00101.88 C
ANISOU 453 CG MET A 92 12919 15389 10401 1391 -377 248 C
ATOM 454 SD MET A 92 19.482 7.645 -46.572 1.00107.73 S
ANISOU 454 SD MET A 92 13835 16071 11026 1589 -409 244 S
ATOM 455 CE MET A 92 17.856 7.092 -47.027 1.00103.75 C
ANISOU 455 CE MET A 92 13519 15339 10564 1463 -349 323 C
ATOM 456 N CYS A 93 21.061 13.029 -48.176 1.00 95.30 N
ANISOU 456 N CYS A 93 11497 14994 9720 1064 -297 111 N
ATOM 457 CA CYS A 93 20.990 14.196 -49.065 1.00 94.52 C
ANISOU 457 CA CYS A 93 11321 14919 9674 889 -246 106 C
ATOM 458 C CYS A 93 22.313 14.941 -49.283 1.00 97.05 C
ANISOU 458 C CYS A 93 11465 15443 9968 852 -217 9 C
ATOM 459 O CYS A 93 22.620 15.258 -50.431 1.00 97.18 O
ANISOU 459 O CYS A 93 11450 15496 9978 777 -168 -17 O
ATOM 460 CB CYS A 93 19.902 15.158 -48.597 1.00 94.39 C
ANISOU 460 CB CYS A 93 11338 14796 9729 750 -242 162 C
ATOM 461 SG CYS A 93 18.336 14.359 -48.154 1.00 97.91 S
ANISOU 461 SG CYS A 93 11959 15031 10211 773 -262 243 S
ATOM 462 N LEU A 94 23.055 15.268 -48.199 1.00 91.79 N
ANISOU 462 N LEU A 94 10690 14904 9283 891 -243 -50 N
ATOM 463 CA LEU A 94 24.295 16.057 -48.230 1.00 91.38 C
ANISOU 463 CA LEU A 94 10451 15060 9210 838 -213 -161 C
ATOM 464 C LEU A 94 25.338 15.607 -49.292 1.00 95.24 C
ANISOU 464 C LEU A 94 10847 15687 9652 880 -176 -256 C
ATOM 465 O LEU A 94 25.703 16.457 -50.107 1.00 94.87 O
ANISOU 465 O LEU A 94 10733 15703 9612 719 -99 -297 O
ATOM 466 CB LEU A 94 24.950 16.151 -46.829 1.00 91.66 C
ANISOU 466 CB LEU A 94 10393 15214 9221 934 -271 -223 C
ATOM 467 CG LEU A 94 26.099 17.168 -46.635 1.00 96.51 C
ANISOU 467 CG LEU A 94 10802 16041 9826 849 -242 -344 C
ATOM 468 CD1 LEU A 94 26.216 17.576 -45.201 1.00 96.59 C
ANISOU 468 CD1 LEU A 94 10772 16091 9838 888 -299 -359 C
ATOM 469 CD2 LEU A 94 27.434 16.599 -47.053 1.00 99.48 C
ANISOU 469 CD2 LEU A 94 11027 16624 10148 958 -240 -488 C
ATOM 470 N PRO A 95 25.900 14.369 -49.285 1.00 91.96 N
ANISOU 470 N PRO A 95 10428 15332 9182 1085 -222 -305 N
ATOM 471 CA PRO A 95 26.954 14.057 -50.267 1.00 92.79 C
ANISOU 471 CA PRO A 95 10419 15592 9246 1115 -180 -416 C
ATOM 472 C PRO A 95 26.484 13.900 -51.708 1.00 96.49 C
ANISOU 472 C PRO A 95 10986 15952 9723 1028 -115 -360 C
ATOM 473 O PRO A 95 27.223 14.245 -52.634 1.00 97.64 O
ANISOU 473 O PRO A 95 11036 16212 9851 938 -39 -442 O
ATOM 474 CB PRO A 95 27.578 12.770 -49.724 1.00 95.50 C
ANISOU 474 CB PRO A 95 10751 16011 9524 1384 -270 -482 C
ATOM 475 CG PRO A 95 26.492 12.121 -48.964 1.00 99.01 C
ANISOU 475 CG PRO A 95 11399 16251 9968 1475 -338 -356 C
ATOM 476 CD PRO A 95 25.646 13.218 -48.391 1.00 93.45 C
ANISOU 476 CD PRO A 95 10726 15448 9331 1296 -313 -272 C
ATOM 477 N PHE A 96 25.256 13.392 -51.891 1.00 90.52 N
ANISOU 477 N PHE A 96 10423 14979 8991 1046 -142 -230 N
ATOM 478 CA PHE A 96 24.653 13.139 -53.195 1.00 88.77 C
ANISOU 478 CA PHE A 96 10321 14630 8779 983 -101 -168 C
ATOM 479 C PHE A 96 24.359 14.433 -53.957 1.00 91.28 C
ANISOU 479 C PHE A 96 10640 14911 9131 751 -27 -149 C
ATOM 480 O PHE A 96 24.595 14.471 -55.159 1.00 91.33 O
ANISOU 480 O PHE A 96 10666 14920 9116 684 32 -169 O
ATOM 481 CB PHE A 96 23.429 12.222 -53.046 1.00 89.26 C
ANISOU 481 CB PHE A 96 10576 14482 8858 1064 -154 -53 C
ATOM 482 CG PHE A 96 23.795 10.958 -52.297 1.00 91.31 C
ANISOU 482 CG PHE A 96 10870 14766 9058 1290 -223 -76 C
ATOM 483 CD1 PHE A 96 24.551 9.963 -52.905 1.00 95.05 C
ANISOU 483 CD1 PHE A 96 11342 15303 9468 1435 -231 -132 C
ATOM 484 CD2 PHE A 96 23.467 10.804 -50.956 1.00 93.17 C
ANISOU 484 CD2 PHE A 96 11147 14966 9289 1365 -281 -52 C
ATOM 485 CE1 PHE A 96 24.935 8.818 -52.200 1.00 96.38 C
ANISOU 485 CE1 PHE A 96 11566 15488 9566 1661 -306 -161 C
ATOM 486 CE2 PHE A 96 23.850 9.656 -50.253 1.00 96.44 C
ANISOU 486 CE2 PHE A 96 11627 15389 9627 1582 -351 -77 C
ATOM 487 CZ PHE A 96 24.575 8.669 -50.882 1.00 95.20 C
ANISOU 487 CZ PHE A 96 11482 15286 9404 1734 -368 -131 C
ATOM 488 N THR A 97 23.949 15.510 -53.254 1.00 86.80 N
ANISOU 488 N THR A 97 10057 14319 8605 632 -29 -123 N
ATOM 489 CA THR A 97 23.688 16.823 -53.857 1.00 86.29 C
ANISOU 489 CA THR A 97 10018 14212 8558 418 31 -110 C
ATOM 490 C THR A 97 24.994 17.514 -54.302 1.00 92.11 C
ANISOU 490 C THR A 97 10612 15140 9245 309 119 -233 C
ATOM 491 O THR A 97 25.028 18.109 -55.379 1.00 92.82 O
ANISOU 491 O THR A 97 10762 15195 9312 160 191 -239 O
ATOM 492 CB THR A 97 22.833 17.693 -52.929 1.00 92.70 C
ANISOU 492 CB THR A 97 10869 14931 9423 343 -6 -48 C
ATOM 493 OG1 THR A 97 21.693 16.948 -52.499 1.00 93.87 O
ANISOU 493 OG1 THR A 97 11130 14923 9613 442 -74 41 O
ATOM 494 CG2 THR A 97 22.360 18.969 -53.599 1.00 90.13 C
ANISOU 494 CG2 THR A 97 10623 14515 9107 147 34 -21 C
ATOM 495 N PHE A 98 26.058 17.422 -53.484 1.00 89.03 N
ANISOU 495 N PHE A 98 10043 14951 8835 380 114 -340 N
ATOM 496 CA PHE A 98 27.367 18.009 -53.769 1.00 89.77 C
ANISOU 496 CA PHE A 98 9964 15260 8885 279 201 -488 C
ATOM 497 C PHE A 98 28.009 17.348 -54.982 1.00 95.07 C
ANISOU 497 C PHE A 98 10614 16000 9509 301 265 -558 C
ATOM 498 O PHE A 98 28.463 18.053 -55.884 1.00 95.80 O
ANISOU 498 O PHE A 98 10692 16141 9566 119 374 -619 O
ATOM 499 CB PHE A 98 28.284 17.916 -52.536 1.00 92.10 C
ANISOU 499 CB PHE A 98 10063 15757 9174 387 157 -599 C
ATOM 500 CG PHE A 98 29.687 18.461 -52.696 1.00 95.27 C
ANISOU 500 CG PHE A 98 10250 16411 9536 291 242 -782 C
ATOM 501 CD1 PHE A 98 29.902 19.749 -53.175 1.00 98.50 C
ANISOU 501 CD1 PHE A 98 10653 16841 9931 28 355 -817 C
ATOM 502 CD2 PHE A 98 30.789 17.716 -52.294 1.00 98.94 C
ANISOU 502 CD2 PHE A 98 10522 17097 9974 463 207 -931 C
ATOM 503 CE1 PHE A 98 31.197 20.264 -53.293 1.00101.06 C
ANISOU 503 CE1 PHE A 98 10775 17407 10217 -86 449 -1002 C
ATOM 504 CE2 PHE A 98 32.083 18.234 -52.407 1.00103.33 C
ANISOU 504 CE2 PHE A 98 10853 17907 10500 367 288 -1125 C
ATOM 505 CZ PHE A 98 32.278 19.504 -52.907 1.00101.58 C
ANISOU 505 CZ PHE A 98 10620 17707 10267 81 418 -1161 C
ATOM 506 N VAL A 99 28.015 16.000 -55.020 1.00 91.07 N
ANISOU 506 N VAL A 99 10125 15485 8992 516 201 -548 N
ATOM 507 CA VAL A 99 28.594 15.229 -56.121 1.00 91.29 C
ANISOU 507 CA VAL A 99 10137 15573 8975 569 250 -612 C
ATOM 508 C VAL A 99 27.807 15.457 -57.414 1.00 93.84 C
ANISOU 508 C VAL A 99 10648 15711 9295 429 308 -517 C
ATOM 509 O VAL A 99 28.432 15.695 -58.448 1.00 95.38 O
ANISOU 509 O VAL A 99 10815 15978 9446 313 411 -594 O
ATOM 510 CB VAL A 99 28.792 13.726 -55.776 1.00 95.47 C
ANISOU 510 CB VAL A 99 10660 16129 9484 849 155 -626 C
ATOM 511 CG1 VAL A 99 29.324 12.941 -56.973 1.00 96.09 C
ANISOU 511 CG1 VAL A 99 10736 16257 9516 904 204 -687 C
ATOM 512 CG2 VAL A 99 29.729 13.554 -54.582 1.00 96.33 C
ANISOU 512 CG2 VAL A 99 10584 16439 9579 996 92 -748 C
ATOM 513 N TYR A 100 26.453 15.442 -57.358 1.00 87.16 N
ANISOU 513 N TYR A 100 9992 14633 8493 431 245 -363 N
ATOM 514 CA TYR A 100 25.619 15.668 -58.547 1.00 85.47 C
ANISOU 514 CA TYR A 100 9965 14232 8276 320 277 -276 C
ATOM 515 C TYR A 100 25.841 17.038 -59.152 1.00 88.53 C
ANISOU 515 C TYR A 100 10380 14623 8635 78 373 -308 C
ATOM 516 O TYR A 100 25.834 17.151 -60.377 1.00 88.72 O
ANISOU 516 O TYR A 100 10512 14582 8616 -15 437 -305 O
ATOM 517 CB TYR A 100 24.122 15.449 -58.261 1.00 85.01 C
ANISOU 517 CB TYR A 100 10075 13948 8278 365 185 -132 C
ATOM 518 CG TYR A 100 23.203 15.621 -59.460 1.00 86.06 C
ANISOU 518 CG TYR A 100 10400 13888 8412 279 192 -54 C
ATOM 519 CD1 TYR A 100 23.417 14.911 -60.638 1.00 88.69 C
ANISOU 519 CD1 TYR A 100 10797 14200 8703 312 226 -64 C
ATOM 520 CD2 TYR A 100 22.084 16.445 -59.393 1.00 85.64 C
ANISOU 520 CD2 TYR A 100 10468 13672 8400 182 153 24 C
ATOM 521 CE1 TYR A 100 22.575 15.063 -61.739 1.00 89.35 C
ANISOU 521 CE1 TYR A 100 11065 14103 8781 243 222 4 C
ATOM 522 CE2 TYR A 100 21.228 16.594 -60.483 1.00 86.00 C
ANISOU 522 CE2 TYR A 100 10693 13542 8442 125 140 83 C
ATOM 523 CZ TYR A 100 21.471 15.894 -61.653 1.00 93.75 C
ANISOU 523 CZ TYR A 100 11740 14501 9378 155 173 75 C
ATOM 524 OH TYR A 100 20.627 16.025 -62.734 1.00 92.78 O
ANISOU 524 OH TYR A 100 11803 14202 9247 108 151 129 O
ATOM 525 N THR A 101 26.037 18.075 -58.308 1.00 84.11 N
ANISOU 525 N THR A 101 9742 14128 8089 -26 384 -337 N
ATOM 526 CA THR A 101 26.256 19.451 -58.766 1.00 84.29 C
ANISOU 526 CA THR A 101 9810 14145 8070 -267 477 -370 C
ATOM 527 C THR A 101 27.511 19.541 -59.656 1.00 89.72 C
ANISOU 527 C THR A 101 10408 15000 8681 -377 613 -510 C
ATOM 528 O THR A 101 27.465 20.179 -60.710 1.00 90.43 O
ANISOU 528 O THR A 101 10639 15007 8712 -553 700 -509 O
ATOM 529 CB THR A 101 26.241 20.428 -57.578 1.00 92.07 C
ANISOU 529 CB THR A 101 10724 15172 9086 -335 454 -376 C
ATOM 530 OG1 THR A 101 24.968 20.335 -56.936 1.00 90.19 O
ANISOU 530 OG1 THR A 101 10597 14757 8915 -250 341 -248 O
ATOM 531 CG2 THR A 101 26.472 21.877 -57.999 1.00 91.91 C
ANISOU 531 CG2 THR A 101 10771 15140 9011 -590 552 -413 C
ATOM 532 N LEU A 102 28.590 18.834 -59.266 1.00 86.06 N
ANISOU 532 N LEU A 102 9723 14764 8212 -262 628 -635 N
ATOM 533 CA LEU A 102 29.870 18.791 -59.977 1.00 86.69 C
ANISOU 533 CA LEU A 102 9666 15044 8227 -345 757 -801 C
ATOM 534 C LEU A 102 29.858 17.840 -61.193 1.00 91.60 C
ANISOU 534 C LEU A 102 10375 15615 8815 -277 786 -793 C
ATOM 535 O LEU A 102 30.895 17.652 -61.834 1.00 93.38 O
ANISOU 535 O LEU A 102 10493 16002 8985 -336 897 -934 O
ATOM 536 CB LEU A 102 31.022 18.435 -59.005 1.00 87.36 C
ANISOU 536 CB LEU A 102 9460 15409 8324 -230 744 -963 C
ATOM 537 CG LEU A 102 31.100 19.145 -57.637 1.00 90.85 C
ANISOU 537 CG LEU A 102 9792 15922 8806 -238 689 -977 C
ATOM 538 CD1 LEU A 102 32.240 18.591 -56.815 1.00 92.05 C
ANISOU 538 CD1 LEU A 102 9672 16340 8962 -73 652 -1141 C
ATOM 539 CD2 LEU A 102 31.266 20.653 -57.775 1.00 92.95 C
ANISOU 539 CD2 LEU A 102 10083 16192 9040 -528 799 -1013 C
ATOM 540 N MET A 103 28.689 17.261 -61.521 1.00 87.06 N
ANISOU 540 N MET A 103 9989 14820 8270 -163 692 -638 N
ATOM 541 CA MET A 103 28.513 16.346 -62.654 1.00 87.31 C
ANISOU 541 CA MET A 103 10131 14771 8272 -91 704 -609 C
ATOM 542 C MET A 103 27.306 16.753 -63.493 1.00 90.80 C
ANISOU 542 C MET A 103 10848 14942 8708 -190 687 -467 C
ATOM 543 O MET A 103 26.392 17.402 -62.977 1.00 88.85 O
ANISOU 543 O MET A 103 10700 14558 8501 -237 623 -372 O
ATOM 544 CB MET A 103 28.281 14.907 -62.161 1.00 89.16 C
ANISOU 544 CB MET A 103 10328 15002 8545 188 584 -569 C
ATOM 545 CG MET A 103 29.461 14.276 -61.457 1.00 93.88 C
ANISOU 545 CG MET A 103 10683 15853 9136 341 573 -715 C
ATOM 546 SD MET A 103 29.031 12.618 -60.869 1.00 97.35 S
ANISOU 546 SD MET A 103 11160 16229 9598 668 421 -645 S
ATOM 547 CE MET A 103 29.398 11.666 -62.314 1.00 94.88 C
ANISOU 547 CE MET A 103 10905 15916 9228 727 477 -683 C
ATOM 548 N ASP A 104 27.281 16.336 -64.779 1.00 88.88 N
ANISOU 548 N ASP A 104 10731 14623 8415 -206 735 -457 N
ATOM 549 CA ASP A 104 26.139 16.598 -65.664 1.00 88.08 C
ANISOU 549 CA ASP A 104 10900 14263 8303 -269 701 -332 C
ATOM 550 C ASP A 104 25.200 15.372 -65.743 1.00 90.80 C
ANISOU 550 C ASP A 104 11327 14471 8700 -63 578 -226 C
ATOM 551 O ASP A 104 24.382 15.274 -66.663 1.00 89.65 O
ANISOU 551 O ASP A 104 11385 14136 8543 -79 548 -146 O
ATOM 552 CB ASP A 104 26.565 17.135 -67.060 1.00 91.32 C
ANISOU 552 CB ASP A 104 11449 14636 8611 -457 832 -379 C
ATOM 553 CG ASP A 104 27.586 16.351 -67.886 1.00102.54 C
ANISOU 553 CG ASP A 104 12783 16202 9975 -430 935 -489 C
ATOM 554 OD1 ASP A 104 27.685 15.116 -67.704 1.00103.50 O
ANISOU 554 OD1 ASP A 104 12805 16387 10134 -220 873 -492 O
ATOM 555 OD2 ASP A 104 28.195 16.955 -68.802 1.00106.78 O
ANISOU 555 OD2 ASP A 104 13386 16765 10422 -621 1076 -566 O
ATOM 556 N HIS A 105 25.311 14.456 -64.744 1.00 87.32 N
ANISOU 556 N HIS A 105 10741 14125 8312 128 506 -233 N
ATOM 557 CA HIS A 105 24.526 13.223 -64.635 1.00 86.37 C
ANISOU 557 CA HIS A 105 10690 13894 8233 321 401 -148 C
ATOM 558 C HIS A 105 24.545 12.597 -63.221 1.00 90.89 C
ANISOU 558 C HIS A 105 11137 14542 8855 490 318 -146 C
ATOM 559 O HIS A 105 25.541 12.689 -62.492 1.00 91.58 O
ANISOU 559 O HIS A 105 11041 14825 8932 524 342 -244 O
ATOM 560 CB HIS A 105 24.922 12.187 -65.715 1.00 87.69 C
ANISOU 560 CB HIS A 105 10899 14071 8349 403 436 -176 C
ATOM 561 CG HIS A 105 26.349 11.729 -65.673 1.00 92.41 C
ANISOU 561 CG HIS A 105 11304 14908 8899 466 509 -318 C
ATOM 562 ND1 HIS A 105 26.671 10.409 -65.414 1.00 94.38 N
ANISOU 562 ND1 HIS A 105 11493 15225 9143 686 457 -345 N
ATOM 563 CD2 HIS A 105 27.491 12.420 -65.897 1.00 95.38 C
ANISOU 563 CD2 HIS A 105 11544 15467 9228 336 627 -451 C
ATOM 564 CE1 HIS A 105 27.990 10.344 -65.466 1.00 95.21 C
ANISOU 564 CE1 HIS A 105 11413 15558 9203 701 533 -497 C
ATOM 565 NE2 HIS A 105 28.527 11.531 -65.749 1.00 96.24 N
ANISOU 565 NE2 HIS A 105 11482 15774 9312 485 642 -571 N
ATOM 566 N TRP A 106 23.411 11.968 -62.854 1.00 86.35 N
ANISOU 566 N TRP A 106 10673 13805 8330 589 220 -41 N
ATOM 567 CA TRP A 106 23.140 11.295 -61.581 1.00 85.37 C
ANISOU 567 CA TRP A 106 10504 13688 8244 741 137 -14 C
ATOM 568 C TRP A 106 23.649 9.849 -61.627 1.00 90.20 C
ANISOU 568 C TRP A 106 11104 14356 8812 940 114 -47 C
ATOM 569 O TRP A 106 23.175 9.041 -62.431 1.00 90.28 O
ANISOU 569 O TRP A 106 11240 14257 8806 987 106 -4 O
ATOM 570 CB TRP A 106 21.628 11.335 -61.300 1.00 82.61 C
ANISOU 570 CB TRP A 106 10299 13129 7959 724 63 99 C
ATOM 571 CG TRP A 106 21.240 10.783 -59.969 1.00 82.98 C
ANISOU 571 CG TRP A 106 10327 13161 8040 838 -6 129 C
ATOM 572 CD1 TRP A 106 20.749 9.541 -59.708 1.00 85.69 C
ANISOU 572 CD1 TRP A 106 10760 13416 8381 975 -58 172 C
ATOM 573 CD2 TRP A 106 21.346 11.447 -58.708 1.00 82.54 C
ANISOU 573 CD2 TRP A 106 10172 13176 8014 816 -23 114 C
ATOM 574 NE1 TRP A 106 20.538 9.390 -58.358 1.00 84.73 N
ANISOU 574 NE1 TRP A 106 10614 13300 8281 1036 -102 185 N
ATOM 575 CE2 TRP A 106 20.896 10.546 -57.720 1.00 86.07 C
ANISOU 575 CE2 TRP A 106 10662 13568 8473 947 -85 151 C
ATOM 576 CE3 TRP A 106 21.761 12.727 -58.316 1.00 83.95 C
ANISOU 576 CE3 TRP A 106 10245 13450 8204 692 11 73 C
ATOM 577 CZ2 TRP A 106 20.852 10.882 -56.364 1.00 85.29 C
ANISOU 577 CZ2 TRP A 106 10502 13507 8397 962 -116 149 C
ATOM 578 CZ3 TRP A 106 21.722 13.059 -56.971 1.00 85.33 C
ANISOU 578 CZ3 TRP A 106 10346 13668 8408 711 -24 71 C
ATOM 579 CH2 TRP A 106 21.266 12.145 -56.012 1.00 85.66 C
ANISOU 579 CH2 TRP A 106 10431 13653 8461 847 -88 110 C
ATOM 580 N VAL A 107 24.622 9.532 -60.772 1.00 87.23 N
ANISOU 580 N VAL A 107 10583 14149 8413 1063 98 -129 N
ATOM 581 CA VAL A 107 25.246 8.206 -60.720 1.00 87.78 C
ANISOU 581 CA VAL A 107 10637 14289 8427 1278 63 -180 C
ATOM 582 C VAL A 107 24.818 7.361 -59.504 1.00 92.05 C
ANISOU 582 C VAL A 107 11240 14766 8967 1450 -36 -134 C
ATOM 583 O VAL A 107 25.470 6.356 -59.209 1.00 93.28 O
ANISOU 583 O VAL A 107 11381 14998 9064 1648 -80 -191 O
ATOM 584 CB VAL A 107 26.789 8.320 -60.811 1.00 93.00 C
ANISOU 584 CB VAL A 107 11090 15207 9038 1317 116 -343 C
ATOM 585 CG1 VAL A 107 27.238 8.575 -62.244 1.00 93.55 C
ANISOU 585 CG1 VAL A 107 11153 15314 9077 1197 221 -393 C
ATOM 586 CG2 VAL A 107 27.337 9.385 -59.860 1.00 92.98 C
ANISOU 586 CG2 VAL A 107 10914 15355 9060 1236 130 -415 C
ATOM 587 N PHE A 108 23.713 7.730 -58.828 1.00 86.76 N
ANISOU 587 N PHE A 108 10657 13952 8354 1378 -71 -37 N
ATOM 588 CA PHE A 108 23.276 7.042 -57.608 1.00 85.86 C
ANISOU 588 CA PHE A 108 10618 13771 8235 1505 -147 4 C
ATOM 589 C PHE A 108 21.934 6.260 -57.725 1.00 88.66 C
ANISOU 589 C PHE A 108 11186 13896 8605 1515 -177 114 C
ATOM 590 O PHE A 108 21.509 5.632 -56.743 1.00 88.34 O
ANISOU 590 O PHE A 108 11240 13781 8544 1610 -227 146 O
ATOM 591 CB PHE A 108 23.240 8.040 -56.434 1.00 87.02 C
ANISOU 591 CB PHE A 108 10669 13970 8426 1428 -159 -1 C
ATOM 592 CG PHE A 108 24.459 8.936 -56.345 1.00 88.89 C
ANISOU 592 CG PHE A 108 10693 14427 8654 1381 -119 -115 C
ATOM 593 CD1 PHE A 108 25.638 8.479 -55.768 1.00 92.50 C
ANISOU 593 CD1 PHE A 108 11026 15065 9053 1547 -153 -227 C
ATOM 594 CD2 PHE A 108 24.431 10.228 -56.859 1.00 90.21 C
ANISOU 594 CD2 PHE A 108 10791 14621 8862 1172 -50 -122 C
ATOM 595 CE1 PHE A 108 26.758 9.308 -55.684 1.00 94.00 C
ANISOU 595 CE1 PHE A 108 11002 15474 9240 1491 -111 -352 C
ATOM 596 CE2 PHE A 108 25.558 11.050 -56.789 1.00 93.49 C
ANISOU 596 CE2 PHE A 108 11019 15240 9263 1105 2 -237 C
ATOM 597 CZ PHE A 108 26.710 10.586 -56.195 1.00 92.65 C
ANISOU 597 CZ PHE A 108 10765 15327 9111 1259 -25 -356 C
ATOM 598 N GLY A 109 21.323 6.267 -58.914 1.00 84.10 N
ANISOU 598 N GLY A 109 10689 13212 8053 1417 -145 160 N
ATOM 599 CA GLY A 109 20.089 5.537 -59.196 1.00 83.03 C
ANISOU 599 CA GLY A 109 10737 12875 7935 1412 -167 242 C
ATOM 600 C GLY A 109 18.798 6.252 -58.853 1.00 85.84 C
ANISOU 600 C GLY A 109 11135 13102 8377 1266 -176 303 C
ATOM 601 O GLY A 109 18.806 7.248 -58.130 1.00 84.42 O
ANISOU 601 O GLY A 109 10860 12975 8240 1187 -174 294 O
ATOM 602 N GLU A 110 17.671 5.729 -59.379 1.00 83.21 N
ANISOU 602 N GLU A 110 10942 12603 8070 1231 -186 356 N
ATOM 603 CA GLU A 110 16.314 6.266 -59.199 1.00 82.83 C
ANISOU 603 CA GLU A 110 10936 12427 8107 1104 -201 394 C
ATOM 604 C GLU A 110 15.913 6.358 -57.732 1.00 88.05 C
ANISOU 604 C GLU A 110 11586 13076 8792 1101 -215 402 C
ATOM 605 O GLU A 110 15.233 7.316 -57.345 1.00 87.53 O
ANISOU 605 O GLU A 110 11472 12984 8800 989 -220 407 O
ATOM 606 CB GLU A 110 15.289 5.431 -59.996 1.00 84.04 C
ANISOU 606 CB GLU A 110 11236 12423 8271 1094 -212 425 C
ATOM 607 CG GLU A 110 13.914 6.071 -60.142 1.00 93.74 C
ANISOU 607 CG GLU A 110 12483 13540 9593 961 -234 436 C
ATOM 608 CD GLU A 110 12.981 5.444 -61.163 1.00114.08 C
ANISOU 608 CD GLU A 110 15176 15982 12186 940 -251 446 C
ATOM 609 OE1 GLU A 110 12.963 4.196 -61.276 1.00100.55 O
ANISOU 609 OE1 GLU A 110 13568 14217 10419 1018 -241 457 O
ATOM 610 OE2 GLU A 110 12.239 6.206 -61.826 1.00110.64 O
ANISOU 610 OE2 GLU A 110 14736 15489 11813 849 -280 436 O
ATOM 611 N ALA A 111 16.341 5.362 -56.925 1.00 85.59 N
ANISOU 611 N ALA A 111 11335 12777 8410 1231 -223 399 N
ATOM 612 CA ALA A 111 16.059 5.257 -55.495 1.00 85.34 C
ANISOU 612 CA ALA A 111 11330 12721 8374 1248 -232 405 C
ATOM 613 C ALA A 111 16.605 6.456 -54.731 1.00 88.83 C
ANISOU 613 C ALA A 111 11613 13291 8847 1207 -236 379 C
ATOM 614 O ALA A 111 15.842 7.116 -54.025 1.00 87.30 O
ANISOU 614 O ALA A 111 11399 13055 8715 1110 -234 392 O
ATOM 615 CB ALA A 111 16.644 3.965 -54.947 1.00 87.07 C
ANISOU 615 CB ALA A 111 11670 12930 8481 1419 -250 401 C
ATOM 616 N MET A 112 17.907 6.768 -54.915 1.00 86.68 N
ANISOU 616 N MET A 112 11221 13180 8534 1273 -237 333 N
ATOM 617 CA MET A 112 18.569 7.903 -54.265 1.00 86.93 C
ANISOU 617 CA MET A 112 11092 13351 8587 1231 -236 294 C
ATOM 618 C MET A 112 18.135 9.253 -54.838 1.00 90.81 C
ANISOU 618 C MET A 112 11505 13841 9158 1054 -210 302 C
ATOM 619 O MET A 112 18.252 10.274 -54.156 1.00 90.72 O
ANISOU 619 O MET A 112 11398 13892 9180 982 -209 287 O
ATOM 620 CB MET A 112 20.100 7.764 -54.317 1.00 90.36 C
ANISOU 620 CB MET A 112 11413 13969 8950 1351 -240 218 C
ATOM 621 CG MET A 112 20.676 6.720 -53.358 1.00 95.09 C
ANISOU 621 CG MET A 112 12069 14597 9462 1548 -291 192 C
ATOM 622 SD MET A 112 20.178 6.790 -51.605 1.00 99.19 S
ANISOU 622 SD MET A 112 12645 15063 9978 1568 -328 216 S
ATOM 623 CE MET A 112 20.614 8.468 -51.179 1.00 95.55 C
ANISOU 623 CE MET A 112 11962 14754 9588 1434 -310 175 C
ATOM 624 N CYS A 113 17.649 9.252 -56.092 1.00 87.21 N
ANISOU 624 N CYS A 113 11106 13307 8723 991 -196 322 N
ATOM 625 CA CYS A 113 17.180 10.439 -56.801 1.00 86.58 C
ANISOU 625 CA CYS A 113 11002 13195 8700 841 -185 328 C
ATOM 626 C CYS A 113 15.874 10.955 -56.201 1.00 88.56 C
ANISOU 626 C CYS A 113 11288 13331 9029 756 -213 359 C
ATOM 627 O CYS A 113 15.820 12.105 -55.761 1.00 87.92 O
ANISOU 627 O CYS A 113 11138 13283 8986 668 -215 350 O
ATOM 628 CB CYS A 113 17.051 10.163 -58.298 1.00 87.16 C
ANISOU 628 CB CYS A 113 11151 13207 8757 822 -172 336 C
ATOM 629 SG CYS A 113 16.299 11.515 -59.242 1.00 90.79 S
ANISOU 629 SG CYS A 113 11646 13582 9268 658 -179 347 S
ATOM 630 N LYS A 114 14.839 10.097 -56.169 1.00 83.71 N
ANISOU 630 N LYS A 114 10780 12588 8438 780 -231 386 N
ATOM 631 CA LYS A 114 13.524 10.414 -55.620 1.00 82.49 C
ANISOU 631 CA LYS A 114 10652 12330 8360 703 -251 394 C
ATOM 632 C LYS A 114 13.581 10.766 -54.127 1.00 87.08 C
ANISOU 632 C LYS A 114 11175 12957 8953 700 -246 389 C
ATOM 633 O LYS A 114 12.858 11.664 -53.693 1.00 87.16 O
ANISOU 633 O LYS A 114 11148 12939 9031 612 -259 380 O
ATOM 634 CB LYS A 114 12.553 9.253 -55.851 1.00 84.10 C
ANISOU 634 CB LYS A 114 10977 12406 8573 726 -253 404 C
ATOM 635 CG LYS A 114 12.014 9.167 -57.264 1.00 85.37 C
ANISOU 635 CG LYS A 114 11195 12488 8752 697 -273 403 C
ATOM 636 CD LYS A 114 10.885 8.165 -57.331 1.00 90.15 C
ANISOU 636 CD LYS A 114 11903 12969 9381 692 -274 398 C
ATOM 637 CE LYS A 114 10.027 8.331 -58.557 1.00 99.28 C
ANISOU 637 CE LYS A 114 13096 14039 10586 640 -312 379 C
ATOM 638 NZ LYS A 114 9.060 9.446 -58.402 1.00103.62 N
ANISOU 638 NZ LYS A 114 13583 14560 11226 551 -355 339 N
ATOM 639 N LEU A 115 14.440 10.071 -53.351 1.00 83.52 N
ANISOU 639 N LEU A 115 10724 12577 8432 804 -235 388 N
ATOM 640 CA LEU A 115 14.590 10.295 -51.909 1.00 82.76 C
ANISOU 640 CA LEU A 115 10594 12521 8329 819 -236 382 C
ATOM 641 C LEU A 115 15.199 11.637 -51.553 1.00 85.13 C
ANISOU 641 C LEU A 115 10755 12937 8653 759 -240 361 C
ATOM 642 O LEU A 115 14.806 12.212 -50.549 1.00 83.78 O
ANISOU 642 O LEU A 115 10555 12759 8518 711 -244 361 O
ATOM 643 CB LEU A 115 15.386 9.165 -51.233 1.00 83.48 C
ANISOU 643 CB LEU A 115 10746 12648 8323 970 -241 379 C
ATOM 644 CG LEU A 115 14.660 7.835 -50.993 1.00 88.28 C
ANISOU 644 CG LEU A 115 11535 13118 8891 1019 -231 402 C
ATOM 645 CD1 LEU A 115 15.614 6.795 -50.455 1.00 89.37 C
ANISOU 645 CD1 LEU A 115 11754 13292 8912 1191 -251 395 C
ATOM 646 CD2 LEU A 115 13.476 7.990 -50.039 1.00 89.85 C
ANISOU 646 CD2 LEU A 115 11787 13214 9139 921 -208 410 C
ATOM 647 N ASN A 116 16.152 12.132 -52.366 1.00 82.21 N
ANISOU 647 N ASN A 116 10306 12671 8260 753 -232 338 N
ATOM 648 CA ASN A 116 16.868 13.399 -52.144 1.00 81.77 C
ANISOU 648 CA ASN A 116 10125 12733 8211 681 -223 308 C
ATOM 649 C ASN A 116 15.945 14.594 -51.758 1.00 83.38 C
ANISOU 649 C ASN A 116 10317 12873 8490 554 -234 321 C
ATOM 650 O ASN A 116 16.115 15.073 -50.633 1.00 82.09 O
ANISOU 650 O ASN A 116 10094 12762 8335 544 -239 312 O
ATOM 651 CB ASN A 116 17.778 13.751 -53.322 1.00 81.50 C
ANISOU 651 CB ASN A 116 10039 12787 8141 652 -192 275 C
ATOM 652 CG ASN A 116 19.002 14.500 -52.892 1.00102.44 C
ANISOU 652 CG ASN A 116 12552 15609 10763 627 -169 217 C
ATOM 653 OD1 ASN A 116 18.983 15.720 -52.704 1.00 94.09 O
ANISOU 653 OD1 ASN A 116 11448 14569 9732 508 -159 210 O
ATOM 654 ND2 ASN A 116 20.085 13.769 -52.681 1.00 97.77 N
ANISOU 654 ND2 ASN A 116 11891 15147 10110 744 -165 165 N
ATOM 655 N PRO A 117 14.952 15.057 -52.584 1.00 78.40 N
ANISOU 655 N PRO A 117 9745 12131 7911 471 -249 336 N
ATOM 656 CA PRO A 117 14.095 16.171 -52.131 1.00 77.40 C
ANISOU 656 CA PRO A 117 9606 11951 7850 376 -273 334 C
ATOM 657 C PRO A 117 13.117 15.786 -51.014 1.00 81.69 C
ANISOU 657 C PRO A 117 10167 12428 8442 389 -284 340 C
ATOM 658 O PRO A 117 12.805 16.622 -50.165 1.00 81.61 O
ANISOU 658 O PRO A 117 10112 12428 8468 338 -292 330 O
ATOM 659 CB PRO A 117 13.360 16.591 -53.403 1.00 78.57 C
ANISOU 659 CB PRO A 117 9828 11998 8027 318 -301 335 C
ATOM 660 CG PRO A 117 13.283 15.358 -54.208 1.00 83.02 C
ANISOU 660 CG PRO A 117 10459 12517 8567 388 -294 347 C
ATOM 661 CD PRO A 117 14.560 14.614 -53.942 1.00 79.34 C
ANISOU 661 CD PRO A 117 9948 12168 8029 471 -254 346 C
ATOM 662 N PHE A 118 12.640 14.526 -51.012 1.00 77.53 N
ANISOU 662 N PHE A 118 9716 11832 7910 450 -275 350 N
ATOM 663 CA PHE A 118 11.704 14.018 -50.024 1.00 76.77 C
ANISOU 663 CA PHE A 118 9661 11663 7846 446 -265 346 C
ATOM 664 C PHE A 118 12.317 14.004 -48.617 1.00 82.67 C
ANISOU 664 C PHE A 118 10378 12479 8553 483 -248 350 C
ATOM 665 O PHE A 118 11.850 14.759 -47.768 1.00 83.29 O
ANISOU 665 O PHE A 118 10414 12555 8676 422 -250 338 O
ATOM 666 CB PHE A 118 11.186 12.642 -50.442 1.00 78.34 C
ANISOU 666 CB PHE A 118 9968 11773 8024 492 -248 352 C
ATOM 667 CG PHE A 118 10.227 12.021 -49.461 1.00 79.69 C
ANISOU 667 CG PHE A 118 10204 11862 8213 466 -216 338 C
ATOM 668 CD1 PHE A 118 8.919 12.477 -49.359 1.00 82.40 C
ANISOU 668 CD1 PHE A 118 10527 12136 8645 370 -217 295 C
ATOM 669 CD2 PHE A 118 10.631 10.981 -48.634 1.00 82.05 C
ANISOU 669 CD2 PHE A 118 10592 12151 8431 539 -184 356 C
ATOM 670 CE1 PHE A 118 8.031 11.900 -48.452 1.00 83.67 C
ANISOU 670 CE1 PHE A 118 10744 12228 8820 325 -169 267 C
ATOM 671 CE2 PHE A 118 9.743 10.404 -47.728 1.00 85.12 C
ANISOU 671 CE2 PHE A 118 11070 12451 8820 496 -140 340 C
ATOM 672 CZ PHE A 118 8.448 10.866 -47.642 1.00 83.20 C
ANISOU 672 CZ PHE A 118 10793 12149 8672 378 -123 293 C
ATOM 673 N VAL A 119 13.390 13.202 -48.391 1.00 79.34 N
ANISOU 673 N VAL A 119 9979 12121 8046 592 -241 361 N
ATOM 674 CA VAL A 119 14.129 13.059 -47.119 1.00 79.13 C
ANISOU 674 CA VAL A 119 9941 12164 7962 662 -242 357 C
ATOM 675 C VAL A 119 14.655 14.421 -46.598 1.00 84.02 C
ANISOU 675 C VAL A 119 10428 12888 8606 604 -255 339 C
ATOM 676 O VAL A 119 14.750 14.602 -45.383 1.00 84.16 O
ANISOU 676 O VAL A 119 10438 12926 8612 614 -257 335 O
ATOM 677 CB VAL A 119 15.238 11.971 -47.210 1.00 83.02 C
ANISOU 677 CB VAL A 119 10474 12716 8353 814 -254 353 C
ATOM 678 CG1 VAL A 119 16.066 11.886 -45.932 1.00 83.38 C
ANISOU 678 CG1 VAL A 119 10509 12839 8332 906 -276 337 C
ATOM 679 CG2 VAL A 119 14.636 10.609 -47.535 1.00 82.84 C
ANISOU 679 CG2 VAL A 119 10612 12570 8295 866 -240 374 C
ATOM 680 N GLN A 120 14.946 15.380 -47.504 1.00 81.02 N
ANISOU 680 N GLN A 120 9967 12563 8255 536 -259 328 N
ATOM 681 CA GLN A 120 15.375 16.732 -47.125 1.00 80.67 C
ANISOU 681 CA GLN A 120 9819 12603 8229 458 -263 309 C
ATOM 682 C GLN A 120 14.158 17.514 -46.596 1.00 84.47 C
ANISOU 682 C GLN A 120 10313 12994 8786 364 -272 316 C
ATOM 683 O GLN A 120 14.254 18.131 -45.536 1.00 84.17 O
ANISOU 683 O GLN A 120 10231 12996 8755 341 -275 308 O
ATOM 684 CB GLN A 120 16.049 17.462 -48.303 1.00 81.64 C
ANISOU 684 CB GLN A 120 9888 12791 8340 399 -254 290 C
ATOM 685 CG GLN A 120 16.690 18.790 -47.928 1.00 84.52 C
ANISOU 685 CG GLN A 120 10155 13259 8699 317 -246 261 C
ATOM 686 CD GLN A 120 17.777 19.171 -48.890 1.00102.61 C
ANISOU 686 CD GLN A 120 12390 15655 10941 280 -214 224 C
ATOM 687 OE1 GLN A 120 18.936 18.790 -48.729 1.00102.25 O
ANISOU 687 OE1 GLN A 120 12262 15747 10843 345 -198 179 O
ATOM 688 NE2 GLN A 120 17.432 19.932 -49.914 1.00 92.32 N
ANISOU 688 NE2 GLN A 120 11136 14292 9648 176 -203 230 N
ATOM 689 N CYS A 121 13.013 17.441 -47.311 1.00 80.77 N
ANISOU 689 N CYS A 121 9905 12410 8375 320 -280 320 N
ATOM 690 CA CYS A 121 11.758 18.102 -46.943 1.00 80.49 C
ANISOU 690 CA CYS A 121 9873 12291 8417 244 -296 304 C
ATOM 691 C CYS A 121 11.219 17.593 -45.598 1.00 84.02 C
ANISOU 691 C CYS A 121 10343 12707 8875 255 -271 299 C
ATOM 692 O CYS A 121 10.875 18.410 -44.741 1.00 83.25 O
ANISOU 692 O CYS A 121 10205 12613 8813 204 -274 284 O
ATOM 693 CB CYS A 121 10.723 17.958 -48.055 1.00 80.94 C
ANISOU 693 CB CYS A 121 9983 12246 8526 218 -319 289 C
ATOM 694 SG CYS A 121 9.268 19.017 -47.854 1.00 84.83 S
ANISOU 694 SG CYS A 121 10456 12658 9116 139 -360 239 S
ATOM 695 N VAL A 122 11.186 16.244 -45.409 1.00 80.48 N
ANISOU 695 N VAL A 122 9975 12221 8384 321 -242 312 N
ATOM 696 CA VAL A 122 10.749 15.551 -44.183 1.00 79.91 C
ANISOU 696 CA VAL A 122 9972 12099 8291 333 -204 309 C
ATOM 697 C VAL A 122 11.557 16.088 -42.990 1.00 83.75 C
ANISOU 697 C VAL A 122 10415 12670 8738 358 -210 317 C
ATOM 698 O VAL A 122 10.971 16.416 -41.962 1.00 83.16 O
ANISOU 698 O VAL A 122 10345 12565 8688 308 -191 303 O
ATOM 699 CB VAL A 122 10.867 13.996 -44.301 1.00 83.79 C
ANISOU 699 CB VAL A 122 10592 12536 8709 415 -178 327 C
ATOM 700 CG1 VAL A 122 10.520 13.307 -42.983 1.00 84.13 C
ANISOU 700 CG1 VAL A 122 10746 12517 8702 423 -134 326 C
ATOM 701 CG2 VAL A 122 9.992 13.448 -45.418 1.00 83.32 C
ANISOU 701 CG2 VAL A 122 10578 12389 8690 381 -169 314 C
ATOM 702 N SER A 123 12.898 16.193 -43.161 1.00 80.79 N
ANISOU 702 N SER A 123 9989 12407 8302 432 -236 327 N
ATOM 703 CA SER A 123 13.871 16.679 -42.178 1.00 80.66 C
ANISOU 703 CA SER A 123 9913 12495 8239 470 -254 320 C
ATOM 704 C SER A 123 13.609 18.134 -41.740 1.00 82.58 C
ANISOU 704 C SER A 123 10064 12768 8543 366 -261 307 C
ATOM 705 O SER A 123 13.638 18.407 -40.537 1.00 82.39 O
ANISOU 705 O SER A 123 10038 12762 8506 366 -260 303 O
ATOM 706 CB SER A 123 15.290 16.520 -42.713 1.00 85.21 C
ANISOU 706 CB SER A 123 10424 13200 8753 556 -278 306 C
ATOM 707 OG SER A 123 16.242 16.997 -41.777 1.00 99.05 O
ANISOU 707 OG SER A 123 12107 15067 10462 599 -301 282 O
ATOM 708 N ILE A 124 13.357 19.055 -42.708 1.00 76.76 N
ANISOU 708 N ILE A 124 9274 12028 7864 282 -271 301 N
ATOM 709 CA ILE A 124 13.050 20.471 -42.448 1.00 75.05 C
ANISOU 709 CA ILE A 124 8997 11821 7697 186 -285 287 C
ATOM 710 C ILE A 124 11.739 20.531 -41.636 1.00 79.62 C
ANISOU 710 C ILE A 124 9613 12302 8336 143 -273 275 C
ATOM 711 O ILE A 124 11.686 21.211 -40.609 1.00 79.41 O
ANISOU 711 O ILE A 124 9558 12296 8319 112 -273 267 O
ATOM 712 CB ILE A 124 12.963 21.317 -43.768 1.00 76.91 C
ANISOU 712 CB ILE A 124 9215 12046 7960 118 -306 280 C
ATOM 713 CG1 ILE A 124 14.244 21.213 -44.611 1.00 77.01 C
ANISOU 713 CG1 ILE A 124 9194 12158 7910 141 -297 280 C
ATOM 714 CG2 ILE A 124 12.638 22.791 -43.484 1.00 76.69 C
ANISOU 714 CG2 ILE A 124 9156 12013 7968 28 -328 265 C
ATOM 715 CD1 ILE A 124 14.028 21.405 -46.073 1.00 80.46 C
ANISOU 715 CD1 ILE A 124 9671 12547 8354 101 -305 280 C
ATOM 716 N THR A 125 10.711 19.769 -42.085 1.00 76.35 N
ANISOU 716 N THR A 125 9261 11788 7959 140 -258 265 N
ATOM 717 CA THR A 125 9.373 19.693 -41.490 1.00 75.89 C
ANISOU 717 CA THR A 125 9229 11643 7964 87 -233 229 C
ATOM 718 C THR A 125 9.418 19.130 -40.052 1.00 79.92 C
ANISOU 718 C THR A 125 9792 12144 8431 102 -186 234 C
ATOM 719 O THR A 125 8.887 19.784 -39.150 1.00 79.86 O
ANISOU 719 O THR A 125 9759 12125 8459 46 -173 209 O
ATOM 720 CB THR A 125 8.408 18.948 -42.432 1.00 82.83 C
ANISOU 720 CB THR A 125 10153 12435 8885 76 -225 203 C
ATOM 721 OG1 THR A 125 8.429 19.577 -43.719 1.00 82.18 O
ANISOU 721 OG1 THR A 125 10039 12357 8828 72 -279 201 O
ATOM 722 CG2 THR A 125 6.987 18.951 -41.926 1.00 81.52 C
ANISOU 722 CG2 THR A 125 9982 12197 8795 5 -198 136 C
ATOM 723 N VAL A 126 10.062 17.950 -39.838 1.00 75.86 N
ANISOU 723 N VAL A 126 9365 11628 7831 183 -165 265 N
ATOM 724 CA VAL A 126 10.217 17.315 -38.520 1.00 75.44 C
ANISOU 724 CA VAL A 126 9407 11550 7708 216 -128 273 C
ATOM 725 C VAL A 126 10.893 18.296 -37.558 1.00 79.84 C
ANISOU 725 C VAL A 126 9896 12189 8249 220 -155 278 C
ATOM 726 O VAL A 126 10.369 18.532 -36.471 1.00 79.36 O
ANISOU 726 O VAL A 126 9867 12091 8195 173 -123 263 O
ATOM 727 CB VAL A 126 10.924 15.930 -38.599 1.00 79.32 C
ANISOU 727 CB VAL A 126 10022 12023 8093 330 -125 302 C
ATOM 728 CG1 VAL A 126 11.545 15.514 -37.268 1.00 79.61 C
ANISOU 728 CG1 VAL A 126 10160 12058 8029 402 -121 315 C
ATOM 729 CG2 VAL A 126 9.962 14.862 -39.081 1.00 79.22 C
ANISOU 729 CG2 VAL A 126 10118 11895 8087 299 -74 292 C
ATOM 730 N SER A 127 12.005 18.925 -37.998 1.00 77.18 N
ANISOU 730 N SER A 127 9463 11966 7895 260 -207 290 N
ATOM 731 CA SER A 127 12.737 19.922 -37.215 1.00 77.14 C
ANISOU 731 CA SER A 127 9380 12055 7875 255 -235 285 C
ATOM 732 C SER A 127 11.839 21.107 -36.843 1.00 81.81 C
ANISOU 732 C SER A 127 9921 12616 8548 143 -227 266 C
ATOM 733 O SER A 127 11.844 21.507 -35.684 1.00 81.80 O
ANISOU 733 O SER A 127 9923 12624 8533 129 -220 261 O
ATOM 734 CB SER A 127 13.984 20.394 -37.955 1.00 79.55 C
ANISOU 734 CB SER A 127 9583 12489 8155 286 -275 282 C
ATOM 735 OG SER A 127 14.860 19.320 -38.260 1.00 87.44 O
ANISOU 735 OG SER A 127 10614 13532 9078 405 -289 284 O
ATOM 736 N ILE A 128 11.018 21.605 -37.795 1.00 78.78 N
ANISOU 736 N ILE A 128 9502 12189 8243 74 -232 249 N
ATOM 737 CA ILE A 128 10.084 22.719 -37.587 1.00 78.60 C
ANISOU 737 CA ILE A 128 9435 12131 8298 -13 -240 216 C
ATOM 738 C ILE A 128 9.035 22.383 -36.508 1.00 83.68 C
ANISOU 738 C ILE A 128 10126 12700 8968 -48 -188 186 C
ATOM 739 O ILE A 128 8.855 23.175 -35.583 1.00 82.75 O
ANISOU 739 O ILE A 128 9983 12595 8865 -87 -185 171 O
ATOM 740 CB ILE A 128 9.469 23.201 -38.936 1.00 81.35 C
ANISOU 740 CB ILE A 128 9759 12443 8709 -49 -274 195 C
ATOM 741 CG1 ILE A 128 10.201 24.443 -39.431 1.00 81.89 C
ANISOU 741 CG1 ILE A 128 9780 12579 8756 -69 -319 210 C
ATOM 742 CG2 ILE A 128 7.965 23.476 -38.861 1.00 82.44 C
ANISOU 742 CG2 ILE A 128 9882 12506 8934 -107 -278 135 C
ATOM 743 CD1 ILE A 128 10.481 24.440 -40.894 1.00 94.69 C
ANISOU 743 CD1 ILE A 128 11417 14178 10381 -70 -347 212 C
ATOM 744 N TRP A 129 8.384 21.207 -36.608 1.00 81.93 N
ANISOU 744 N TRP A 129 9981 12403 8746 -44 -140 172 N
ATOM 745 CA TRP A 129 7.363 20.783 -35.653 1.00 82.60 C
ANISOU 745 CA TRP A 129 10125 12413 8847 -101 -69 129 C
ATOM 746 C TRP A 129 7.928 20.396 -34.307 1.00 85.57 C
ANISOU 746 C TRP A 129 10589 12789 9134 -71 -34 158 C
ATOM 747 O TRP A 129 7.272 20.630 -33.295 1.00 85.31 O
ANISOU 747 O TRP A 129 10579 12720 9115 -134 15 124 O
ATOM 748 CB TRP A 129 6.490 19.667 -36.220 1.00 82.40 C
ANISOU 748 CB TRP A 129 10164 12306 8840 -124 -18 96 C
ATOM 749 CG TRP A 129 5.664 20.059 -37.406 1.00 83.83 C
ANISOU 749 CG TRP A 129 10261 12474 9117 -158 -54 44 C
ATOM 750 CD1 TRP A 129 5.659 19.458 -38.627 1.00 86.99 C
ANISOU 750 CD1 TRP A 129 10676 12855 9523 -128 -75 51 C
ATOM 751 CD2 TRP A 129 4.687 21.112 -37.472 1.00 83.83 C
ANISOU 751 CD2 TRP A 129 10161 12475 9215 -215 -82 -31 C
ATOM 752 NE1 TRP A 129 4.749 20.072 -39.456 1.00 86.78 N
ANISOU 752 NE1 TRP A 129 10569 12814 9590 -162 -118 -15 N
ATOM 753 CE2 TRP A 129 4.134 21.088 -38.771 1.00 88.10 C
ANISOU 753 CE2 TRP A 129 10665 12995 9815 -209 -128 -70 C
ATOM 754 CE3 TRP A 129 4.218 22.071 -36.556 1.00 85.33 C
ANISOU 754 CE3 TRP A 129 10296 12681 9446 -262 -79 -76 C
ATOM 755 CZ2 TRP A 129 3.143 21.989 -39.181 1.00 87.44 C
ANISOU 755 CZ2 TRP A 129 10495 12905 9824 -235 -182 -157 C
ATOM 756 CZ3 TRP A 129 3.243 22.969 -36.967 1.00 86.91 C
ANISOU 756 CZ3 TRP A 129 10404 12878 9741 -290 -127 -161 C
ATOM 757 CH2 TRP A 129 2.720 22.927 -38.266 1.00 87.59 C
ANISOU 757 CH2 TRP A 129 10459 12942 9880 -271 -184 -203 C
ATOM 758 N SER A 130 9.142 19.818 -34.286 1.00 81.89 N
ANISOU 758 N SER A 130 10177 12365 8573 30 -63 212 N
ATOM 759 CA SER A 130 9.822 19.451 -33.043 1.00 82.11 C
ANISOU 759 CA SER A 130 10301 12397 8500 89 -56 236 C
ATOM 760 C SER A 130 10.213 20.717 -32.284 1.00 84.60 C
ANISOU 760 C SER A 130 10525 12788 8833 67 -90 233 C
ATOM 761 O SER A 130 10.073 20.748 -31.066 1.00 84.26 O
ANISOU 761 O SER A 130 10551 12711 8754 50 -59 227 O
ATOM 762 CB SER A 130 11.038 18.577 -33.320 1.00 86.38 C
ANISOU 762 CB SER A 130 10900 12979 8940 224 -100 274 C
ATOM 763 OG SER A 130 10.646 17.371 -33.956 1.00 95.54 O
ANISOU 763 OG SER A 130 12165 14060 10077 244 -66 278 O
ATOM 764 N LEU A 131 10.636 21.776 -33.010 1.00 80.42 N
ANISOU 764 N LEU A 131 9855 12346 8354 55 -147 235 N
ATOM 765 CA LEU A 131 10.963 23.080 -32.428 1.00 79.99 C
ANISOU 765 CA LEU A 131 9713 12359 8319 17 -179 229 C
ATOM 766 C LEU A 131 9.684 23.770 -31.918 1.00 85.12 C
ANISOU 766 C LEU A 131 10350 12943 9047 -83 -142 189 C
ATOM 767 O LEU A 131 9.739 24.430 -30.876 1.00 85.49 O
ANISOU 767 O LEU A 131 10392 13006 9084 -107 -140 183 O
ATOM 768 CB LEU A 131 11.720 23.992 -33.418 1.00 79.34 C
ANISOU 768 CB LEU A 131 9515 12373 8259 9 -236 234 C
ATOM 769 CG LEU A 131 13.188 23.654 -33.720 1.00 83.62 C
ANISOU 769 CG LEU A 131 10024 13024 8725 95 -274 249 C
ATOM 770 CD1 LEU A 131 13.688 24.444 -34.899 1.00 83.27 C
ANISOU 770 CD1 LEU A 131 9884 13048 8705 53 -301 243 C
ATOM 771 CD2 LEU A 131 14.087 23.909 -32.530 1.00 86.86 C
ANISOU 771 CD2 LEU A 131 10420 13511 9070 139 -299 243 C
ATOM 772 N VAL A 132 8.535 23.593 -32.636 1.00 81.39 N
ANISOU 772 N VAL A 132 9870 12402 8651 -136 -115 151 N
ATOM 773 CA VAL A 132 7.212 24.118 -32.250 1.00 80.95 C
ANISOU 773 CA VAL A 132 9788 12292 8678 -221 -79 85 C
ATOM 774 C VAL A 132 6.840 23.498 -30.895 1.00 85.16 C
ANISOU 774 C VAL A 132 10421 12770 9166 -250 3 70 C
ATOM 775 O VAL A 132 6.555 24.232 -29.953 1.00 85.18 O
ANISOU 775 O VAL A 132 10405 12774 9184 -295 19 45 O
ATOM 776 CB VAL A 132 6.108 23.843 -33.324 1.00 84.78 C
ANISOU 776 CB VAL A 132 10242 12726 9246 -255 -72 28 C
ATOM 777 CG1 VAL A 132 4.704 24.029 -32.754 1.00 84.97 C
ANISOU 777 CG1 VAL A 132 10243 12698 9344 -337 -16 -66 C
ATOM 778 CG2 VAL A 132 6.286 24.712 -34.558 1.00 84.08 C
ANISOU 778 CG2 VAL A 132 10074 12671 9201 -239 -158 31 C
ATOM 779 N LEU A 133 6.885 22.150 -30.806 1.00 81.74 N
ANISOU 779 N LEU A 133 10111 12281 8666 -223 56 87 N
ATOM 780 CA LEU A 133 6.556 21.364 -29.618 1.00 82.22 C
ANISOU 780 CA LEU A 133 10318 12263 8657 -253 144 76 C
ATOM 781 C LEU A 133 7.395 21.694 -28.392 1.00 86.14 C
ANISOU 781 C LEU A 133 10873 12787 9070 -208 124 115 C
ATOM 782 O LEU A 133 6.868 21.656 -27.280 1.00 86.60 O
ANISOU 782 O LEU A 133 11015 12787 9102 -268 194 87 O
ATOM 783 CB LEU A 133 6.627 19.873 -29.938 1.00 82.95 C
ANISOU 783 CB LEU A 133 10559 12284 8675 -219 187 95 C
ATOM 784 CG LEU A 133 5.280 19.210 -30.152 1.00 88.47 C
ANISOU 784 CG LEU A 133 11300 12895 9421 -330 289 20 C
ATOM 785 CD1 LEU A 133 4.756 19.454 -31.560 1.00 88.27 C
ANISOU 785 CD1 LEU A 133 11137 12899 9504 -345 250 -16 C
ATOM 786 CD2 LEU A 133 5.359 17.731 -29.864 1.00 92.33 C
ANISOU 786 CD2 LEU A 133 12009 13282 9791 -319 362 40 C
ATOM 787 N ILE A 134 8.696 22.006 -28.593 1.00 81.79 N
ANISOU 787 N ILE A 134 10275 12327 8475 -109 33 168 N
ATOM 788 CA ILE A 134 9.633 22.405 -27.539 1.00 81.45 C
ANISOU 788 CA ILE A 134 10258 12333 8355 -53 -8 196 C
ATOM 789 C ILE A 134 9.154 23.747 -26.959 1.00 87.33 C
ANISOU 789 C ILE A 134 10908 13103 9172 -138 -5 166 C
ATOM 790 O ILE A 134 9.030 23.859 -25.741 1.00 88.42 O
ANISOU 790 O ILE A 134 11122 13209 9265 -156 26 160 O
ATOM 791 CB ILE A 134 11.107 22.435 -28.064 1.00 83.65 C
ANISOU 791 CB ILE A 134 10474 12725 8584 65 -105 232 C
ATOM 792 CG1 ILE A 134 11.727 21.020 -28.042 1.00 83.80 C
ANISOU 792 CG1 ILE A 134 10640 12710 8490 184 -114 256 C
ATOM 793 CG2 ILE A 134 11.985 23.431 -27.289 1.00 84.11 C
ANISOU 793 CG2 ILE A 134 10464 12878 8615 89 -164 235 C
ATOM 794 CD1 ILE A 134 13.003 20.818 -28.888 1.00 84.32 C
ANISOU 794 CD1 ILE A 134 10627 12889 8522 301 -197 269 C
ATOM 795 N ALA A 135 8.815 24.724 -27.837 1.00 83.63 N
ANISOU 795 N ALA A 135 10294 12678 8805 -188 -38 145 N
ATOM 796 CA ALA A 135 8.315 26.062 -27.481 1.00 83.15 C
ANISOU 796 CA ALA A 135 10144 12637 8814 -259 -48 111 C
ATOM 797 C ALA A 135 7.011 26.034 -26.677 1.00 86.06 C
ANISOU 797 C ALA A 135 10552 12924 9222 -345 38 49 C
ATOM 798 O ALA A 135 6.803 26.908 -25.832 1.00 85.55 O
ANISOU 798 O ALA A 135 10465 12869 9172 -384 42 28 O
ATOM 799 CB ALA A 135 8.131 26.905 -28.735 1.00 83.56 C
ANISOU 799 CB ALA A 135 10076 12724 8948 -281 -105 96 C
ATOM 800 N VAL A 136 6.134 25.044 -26.957 1.00 81.99 N
ANISOU 800 N VAL A 136 10093 12335 8726 -382 112 9 N
ATOM 801 CA VAL A 136 4.847 24.850 -26.275 1.00 81.52 C
ANISOU 801 CA VAL A 136 10067 12204 8703 -482 217 -73 C
ATOM 802 C VAL A 136 5.111 24.240 -24.890 1.00 85.78 C
ANISOU 802 C VAL A 136 10774 12688 9131 -491 288 -51 C
ATOM 803 O VAL A 136 4.470 24.646 -23.920 1.00 86.08 O
ANISOU 803 O VAL A 136 10826 12698 9181 -565 351 -101 O
ATOM 804 CB VAL A 136 3.829 24.030 -27.127 1.00 84.82 C
ANISOU 804 CB VAL A 136 10478 12571 9177 -532 275 -138 C
ATOM 805 CG1 VAL A 136 2.512 23.833 -26.393 1.00 85.35 C
ANISOU 805 CG1 VAL A 136 10568 12581 9282 -654 399 -247 C
ATOM 806 CG2 VAL A 136 3.571 24.703 -28.465 1.00 83.87 C
ANISOU 806 CG2 VAL A 136 10207 12500 9159 -511 191 -165 C
ATOM 807 N GLU A 137 6.076 23.297 -24.799 1.00 82.45 N
ANISOU 807 N GLU A 137 10486 12247 8595 -405 270 21 N
ATOM 808 CA GLU A 137 6.473 22.637 -23.550 1.00 83.43 C
ANISOU 808 CA GLU A 137 10809 12305 8586 -381 314 50 C
ATOM 809 C GLU A 137 7.135 23.621 -22.581 1.00 88.21 C
ANISOU 809 C GLU A 137 11389 12964 9161 -347 257 75 C
ATOM 810 O GLU A 137 6.843 23.584 -21.384 1.00 88.29 O
ANISOU 810 O GLU A 137 11521 12912 9113 -391 321 59 O
ATOM 811 CB GLU A 137 7.392 21.436 -23.829 1.00 85.21 C
ANISOU 811 CB GLU A 137 11175 12504 8696 -264 277 111 C
ATOM 812 CG GLU A 137 7.609 20.514 -22.635 1.00 96.71 C
ANISOU 812 CG GLU A 137 12895 13853 9997 -237 330 129 C
ATOM 813 CD GLU A 137 6.409 19.740 -22.112 1.00120.20 C
ANISOU 813 CD GLU A 137 16037 16690 12944 -373 486 74 C
ATOM 814 OE1 GLU A 137 5.413 19.579 -22.856 1.00110.75 O
ANISOU 814 OE1 GLU A 137 14761 15478 11841 -473 554 17 O
ATOM 815 OE2 GLU A 137 6.494 19.245 -20.965 1.00118.39 O
ANISOU 815 OE2 GLU A 137 16031 16364 12589 -380 541 80 O
ATOM 816 N ARG A 138 8.008 24.509 -23.106 1.00 84.81 N
ANISOU 816 N ARG A 138 10810 12648 8766 -281 144 109 N
ATOM 817 CA ARG A 138 8.700 25.547 -22.333 1.00 84.51 C
ANISOU 817 CA ARG A 138 10724 12678 8708 -256 82 127 C
ATOM 818 C ARG A 138 7.700 26.578 -21.806 1.00 89.38 C
ANISOU 818 C ARG A 138 11271 13281 9408 -366 129 73 C
ATOM 819 O ARG A 138 7.847 27.054 -20.679 1.00 89.48 O
ANISOU 819 O ARG A 138 11328 13291 9380 -376 132 74 O
ATOM 820 CB ARG A 138 9.801 26.237 -23.170 1.00 82.46 C
ANISOU 820 CB ARG A 138 10318 12545 8469 -188 -31 159 C
ATOM 821 CG ARG A 138 10.919 25.319 -23.686 1.00 88.39 C
ANISOU 821 CG ARG A 138 11108 13337 9138 -65 -89 197 C
ATOM 822 CD ARG A 138 11.555 24.449 -22.615 1.00 96.79 C
ANISOU 822 CD ARG A 138 12348 14363 10065 30 -98 215 C
ATOM 823 NE ARG A 138 12.307 25.244 -21.646 1.00103.09 N
ANISOU 823 NE ARG A 138 13120 15229 10821 62 -158 216 N
ATOM 824 CZ ARG A 138 12.764 24.779 -20.490 1.00116.47 C
ANISOU 824 CZ ARG A 138 14968 16890 12397 142 -179 223 C
ATOM 825 NH1 ARG A 138 12.552 23.514 -20.144 1.00104.68 N
ANISOU 825 NH1 ARG A 138 13685 15283 10804 197 -142 233 N
ATOM 826 NH2 ARG A 138 13.434 25.574 -19.668 1.00102.96 N
ANISOU 826 NH2 ARG A 138 13214 15249 10656 168 -240 216 N
ATOM 827 N HIS A 139 6.672 26.896 -22.617 1.00 86.23 N
ANISOU 827 N HIS A 139 10768 12873 9122 -439 159 18 N
ATOM 828 CA HIS A 139 5.609 27.833 -22.269 1.00 86.37 C
ANISOU 828 CA HIS A 139 10706 12881 9229 -529 197 -56 C
ATOM 829 C HIS A 139 4.710 27.284 -21.181 1.00 90.60 C
ANISOU 829 C HIS A 139 11359 13330 9736 -613 324 -112 C
ATOM 830 O HIS A 139 4.194 28.060 -20.377 1.00 90.52 O
ANISOU 830 O HIS A 139 11325 13317 9750 -668 355 -157 O
ATOM 831 CB HIS A 139 4.793 28.231 -23.505 1.00 87.19 C
ANISOU 831 CB HIS A 139 10673 13001 9453 -558 176 -115 C
ATOM 832 CG HIS A 139 3.762 29.285 -23.242 1.00 90.97 C
ANISOU 832 CG HIS A 139 11056 13484 10024 -621 187 -204 C
ATOM 833 ND1 HIS A 139 4.104 30.515 -22.707 1.00 92.78 N
ANISOU 833 ND1 HIS A 139 11241 13754 10256 -613 127 -190 N
ATOM 834 CD2 HIS A 139 2.429 29.263 -23.459 1.00 93.30 C
ANISOU 834 CD2 HIS A 139 11289 13753 10409 -686 245 -317 C
ATOM 835 CE1 HIS A 139 2.975 31.196 -22.616 1.00 92.40 C
ANISOU 835 CE1 HIS A 139 11116 13697 10295 -662 145 -290 C
ATOM 836 NE2 HIS A 139 1.943 30.488 -23.066 1.00 93.13 N
ANISOU 836 NE2 HIS A 139 11184 13757 10446 -704 213 -376 N
ATOM 837 N GLN A 140 4.510 25.953 -21.155 1.00 87.38 N
ANISOU 837 N GLN A 140 11087 12845 9268 -629 406 -115 N
ATOM 838 CA GLN A 140 3.694 25.318 -20.127 1.00 87.86 C
ANISOU 838 CA GLN A 140 11296 12809 9279 -728 548 -171 C
ATOM 839 C GLN A 140 4.457 25.277 -18.803 1.00 93.23 C
ANISOU 839 C GLN A 140 12144 13453 9828 -689 546 -113 C
ATOM 840 O GLN A 140 3.849 25.443 -17.746 1.00 93.27 O
ANISOU 840 O GLN A 140 12229 13402 9808 -777 641 -162 O
ATOM 841 CB GLN A 140 3.205 23.931 -20.570 1.00 89.27 C
ANISOU 841 CB GLN A 140 11591 12905 9422 -771 639 -194 C
ATOM 842 CG GLN A 140 2.088 23.342 -19.700 1.00 95.54 C
ANISOU 842 CG GLN A 140 12512 13600 10187 -922 815 -288 C
ATOM 843 CD GLN A 140 1.027 24.331 -19.255 1.00107.24 C
ANISOU 843 CD GLN A 140 13852 15119 11777 -1030 875 -402 C
ATOM 844 OE1 GLN A 140 0.436 25.071 -20.048 1.00 98.64 O
ANISOU 844 OE1 GLN A 140 12547 14105 10826 -1039 831 -471 O
ATOM 845 NE2 GLN A 140 0.706 24.304 -17.977 1.00103.26 N
ANISOU 845 NE2 GLN A 140 13478 14552 11204 -1112 980 -434 N
ATOM 846 N LEU A 141 5.795 25.126 -18.876 1.00 90.49 N
ANISOU 846 N LEU A 141 11835 13146 9400 -555 433 -21 N
ATOM 847 CA LEU A 141 6.689 25.122 -17.721 1.00 91.06 C
ANISOU 847 CA LEU A 141 12049 13202 9346 -485 394 31 C
ATOM 848 C LEU A 141 6.791 26.490 -17.051 1.00 96.72 C
ANISOU 848 C LEU A 141 12660 13983 10106 -505 354 21 C
ATOM 849 O LEU A 141 6.859 26.536 -15.832 1.00 97.45 O
ANISOU 849 O LEU A 141 12887 14023 10118 -520 390 22 O
ATOM 850 CB LEU A 141 8.081 24.602 -18.093 1.00 90.88 C
ANISOU 850 CB LEU A 141 12068 13226 9236 -325 275 105 C
ATOM 851 CG LEU A 141 8.251 23.094 -18.031 1.00 96.24 C
ANISOU 851 CG LEU A 141 12980 13800 9787 -271 312 127 C
ATOM 852 CD1 LEU A 141 9.228 22.614 -19.072 1.00 96.20 C
ANISOU 852 CD1 LEU A 141 12923 13863 9764 -137 207 171 C
ATOM 853 CD2 LEU A 141 8.667 22.639 -16.641 1.00 99.47 C
ANISOU 853 CD2 LEU A 141 13642 14119 10034 -223 323 147 C
ATOM 854 N ILE A 142 6.794 27.596 -17.816 1.00 93.77 N
ANISOU 854 N ILE A 142 12069 13710 9849 -509 281 12 N
ATOM 855 CA ILE A 142 6.881 28.942 -17.219 1.00 94.02 C
ANISOU 855 CA ILE A 142 12012 13795 9917 -532 241 2 C
ATOM 856 C ILE A 142 5.544 29.374 -16.582 1.00 99.20 C
ANISOU 856 C ILE A 142 12661 14396 10636 -654 351 -83 C
ATOM 857 O ILE A 142 5.562 30.135 -15.613 1.00 99.55 O
ANISOU 857 O ILE A 142 12713 14445 10667 -678 351 -92 O
ATOM 858 CB ILE A 142 7.464 30.028 -18.170 1.00 96.53 C
ANISOU 858 CB ILE A 142 12141 14226 10310 -497 125 23 C
ATOM 859 CG1 ILE A 142 6.708 30.111 -19.508 1.00 96.78 C
ANISOU 859 CG1 ILE A 142 12051 14270 10451 -524 123 -12 C
ATOM 860 CG2 ILE A 142 8.950 29.785 -18.416 1.00 97.48 C
ANISOU 860 CG2 ILE A 142 12267 14422 10350 -388 22 90 C
ATOM 861 CD1 ILE A 142 5.605 31.115 -19.589 1.00105.99 C
ANISOU 861 CD1 ILE A 142 13113 15430 11729 -603 149 -91 C
ATOM 862 N ILE A 143 4.399 28.893 -17.122 1.00 95.96 N
ANISOU 862 N ILE A 143 12226 13941 10293 -732 444 -156 N
ATOM 863 CA ILE A 143 3.051 29.181 -16.608 1.00 96.27 C
ANISOU 863 CA ILE A 143 12236 13943 10399 -853 559 -268 C
ATOM 864 C ILE A 143 2.799 28.414 -15.293 1.00102.64 C
ANISOU 864 C ILE A 143 13259 14646 11092 -923 691 -283 C
ATOM 865 O ILE A 143 2.275 28.986 -14.329 1.00102.23 O
ANISOU 865 O ILE A 143 13220 14577 11044 -994 755 -338 O
ATOM 866 CB ILE A 143 1.960 28.893 -17.690 1.00 98.89 C
ANISOU 866 CB ILE A 143 12448 14281 10844 -909 604 -360 C
ATOM 867 CG1 ILE A 143 1.945 29.994 -18.769 1.00 98.16 C
ANISOU 867 CG1 ILE A 143 12152 14276 10868 -857 480 -374 C
ATOM 868 CG2 ILE A 143 0.562 28.717 -17.067 1.00100.55 C
ANISOU 868 CG2 ILE A 143 12667 14443 11095 -1049 762 -498 C
ATOM 869 CD1 ILE A 143 1.154 29.652 -19.998 1.00104.15 C
ANISOU 869 CD1 ILE A 143 12807 15046 11720 -868 480 -441 C
ATOM 870 N ASN A 144 3.186 27.121 -15.271 1.00100.87 N
ANISOU 870 N ASN A 144 13228 14352 10747 -878 709 -218 N
ATOM 871 CA ASN A 144 3.006 26.218 -14.140 1.00102.33 C
ANISOU 871 CA ASN A 144 13672 14409 10798 -942 837 -229 C
ATOM 872 C ASN A 144 4.262 25.317 -13.907 1.00108.46 C
ANISOU 872 C ASN A 144 14673 15130 11406 -815 770 -122 C
ATOM 873 O ASN A 144 4.250 24.163 -14.323 1.00108.60 O
ANISOU 873 O ASN A 144 14863 15061 11340 -814 823 -110 O
ATOM 874 CB ASN A 144 1.736 25.385 -14.374 1.00102.16 C
ANISOU 874 CB ASN A 144 13684 14323 10810 -1076 991 -324 C
ATOM 875 CG ASN A 144 1.285 24.590 -13.186 1.00125.70 C
ANISOU 875 CG ASN A 144 16932 17166 13664 -1193 1159 -364 C
ATOM 876 OD1 ASN A 144 1.734 23.464 -12.963 1.00121.23 O
ANISOU 876 OD1 ASN A 144 16607 16494 12961 -1178 1200 -320 O
ATOM 877 ND2 ASN A 144 0.350 25.144 -12.430 1.00118.12 N
ANISOU 877 ND2 ASN A 144 15946 16200 12736 -1310 1260 -452 N
ATOM 878 N PRO A 145 5.346 25.797 -13.241 1.00106.14 N
ANISOU 878 N PRO A 145 14383 14888 11059 -702 647 -55 N
ATOM 879 CA PRO A 145 6.522 24.919 -13.031 1.00107.02 C
ANISOU 879 CA PRO A 145 14683 14965 11013 -554 558 27 C
ATOM 880 C PRO A 145 6.393 23.949 -11.862 1.00114.49 C
ANISOU 880 C PRO A 145 15965 15748 11788 -582 657 25 C
ATOM 881 O PRO A 145 6.980 22.864 -11.891 1.00114.50 O
ANISOU 881 O PRO A 145 16171 15680 11653 -478 619 71 O
ATOM 882 CB PRO A 145 7.672 25.900 -12.806 1.00108.04 C
ANISOU 882 CB PRO A 145 14702 15203 11144 -453 415 68 C
ATOM 883 CG PRO A 145 7.024 27.151 -12.313 1.00111.93 C
ANISOU 883 CG PRO A 145 15076 15720 11734 -573 473 15 C
ATOM 884 CD PRO A 145 5.565 27.146 -12.675 1.00107.10 C
ANISOU 884 CD PRO A 145 14346 15098 11251 -703 583 -61 C
ATOM 885 N ARG A 146 5.634 24.359 -10.833 1.00113.70 N
ANISOU 885 N ARG A 146 15930 15584 11688 -722 786 -33 N
ATOM 886 CA ARG A 146 5.404 23.622 -9.594 1.00115.90 C
ANISOU 886 CA ARG A 146 16546 15697 11794 -773 896 -40 C
ATOM 887 C ARG A 146 4.701 22.277 -9.802 1.00122.59 C
ANISOU 887 C ARG A 146 17590 16416 12574 -858 1031 -70 C
ATOM 888 O ARG A 146 5.235 21.246 -9.392 1.00123.19 O
ANISOU 888 O ARG A 146 17918 16398 12492 -753 990 -14 O
ATOM 889 CB ARG A 146 4.651 24.494 -8.576 1.00116.96 C
ANISOU 889 CB ARG A 146 16673 15809 11958 -916 1009 -107 C
ATOM 890 CG ARG A 146 5.370 25.789 -8.218 1.00127.41 C
ANISOU 890 CG ARG A 146 17834 17245 13330 -832 875 -74 C
ATOM 891 CD ARG A 146 4.718 26.505 -7.052 1.00136.61 C
ANISOU 891 CD ARG A 146 19065 18365 14477 -941 971 -123 C
ATOM 892 NE ARG A 146 5.146 27.902 -6.992 1.00140.24 N
ANISOU 892 NE ARG A 146 19288 18959 15038 -889 851 -109 N
ATOM 893 CZ ARG A 146 4.413 28.932 -7.400 1.00151.34 C
ANISOU 893 CZ ARG A 146 20440 20454 16607 -973 877 -174 C
ATOM 894 NH1 ARG A 146 3.189 28.738 -7.880 1.00138.36 N
ANISOU 894 NH1 ARG A 146 18709 18798 15063 -1114 1016 -274 N
ATOM 895 NH2 ARG A 146 4.889 30.165 -7.317 1.00136.05 N
ANISOU 895 NH2 ARG A 146 18338 18622 14732 -911 755 -148 N
ATOM 896 N GLY A 147 3.529 22.304 -10.445 1.00120.26 N
ANISOU 896 N GLY A 147 17170 16126 12398 -1037 1178 -164 N
ATOM 897 CA GLY A 147 2.721 21.115 -10.706 1.00121.65 C
ANISOU 897 CA GLY A 147 17530 16177 12515 -1165 1340 -217 C
ATOM 898 C GLY A 147 2.877 20.458 -12.066 1.00125.97 C
ANISOU 898 C GLY A 147 18021 16745 13095 -1103 1290 -191 C
ATOM 899 O GLY A 147 2.180 19.476 -12.343 1.00126.36 O
ANISOU 899 O GLY A 147 18251 16682 13078 -1206 1421 -230 O
ATOM 900 N TRP A 148 3.777 20.971 -12.931 1.00122.00 N
ANISOU 900 N TRP A 148 17282 16384 12690 -947 1111 -130 N
ATOM 901 CA TRP A 148 3.989 20.381 -14.255 1.00121.64 C
ANISOU 901 CA TRP A 148 17167 16371 12680 -875 1049 -101 C
ATOM 902 C TRP A 148 4.971 19.211 -14.207 1.00127.17 C
ANISOU 902 C TRP A 148 18174 16963 13182 -733 990 -19 C
ATOM 903 O TRP A 148 6.189 19.406 -14.249 1.00126.76 O
ANISOU 903 O TRP A 148 18145 16957 13062 -550 833 55 O
ATOM 904 CB TRP A 148 4.383 21.443 -15.296 1.00118.76 C
ANISOU 904 CB TRP A 148 16468 16186 12470 -765 886 -68 C
ATOM 905 CG TRP A 148 4.453 20.946 -16.708 1.00119.21 C
ANISOU 905 CG TRP A 148 16404 16290 12600 -727 843 -60 C
ATOM 906 CD1 TRP A 148 5.568 20.863 -17.489 1.00121.52 C
ANISOU 906 CD1 TRP A 148 16636 16654 12881 -560 693 17 C
ATOM 907 CD2 TRP A 148 3.363 20.480 -17.516 1.00119.11 C
ANISOU 907 CD2 TRP A 148 16307 16263 12686 -860 951 -141 C
ATOM 908 NE1 TRP A 148 5.241 20.390 -18.737 1.00120.47 N
ANISOU 908 NE1 TRP A 148 16402 16542 12828 -580 703 -1 N
ATOM 909 CE2 TRP A 148 3.897 20.125 -18.775 1.00122.26 C
ANISOU 909 CE2 TRP A 148 16614 16717 13124 -759 855 -96 C
ATOM 910 CE3 TRP A 148 1.984 20.314 -17.292 1.00121.00 C
ANISOU 910 CE3 TRP A 148 16533 16457 12985 -1057 1122 -261 C
ATOM 911 CZ2 TRP A 148 3.103 19.610 -19.806 1.00121.40 C
ANISOU 911 CZ2 TRP A 148 16412 16608 13107 -842 916 -158 C
ATOM 912 CZ3 TRP A 148 1.198 19.806 -18.315 1.00122.40 C
ANISOU 912 CZ3 TRP A 148 16600 16646 13259 -1141 1182 -334 C
ATOM 913 CH2 TRP A 148 1.756 19.462 -19.555 1.00122.26 C
ANISOU 913 CH2 TRP A 148 16504 16674 13275 -1030 1075 -278 C
ATOM 914 N ARG A 149 4.418 17.993 -14.090 1.00125.04 N
ANISOU 914 N ARG A 149 18147 16549 12814 -821 1119 -45 N
ATOM 915 CA ARG A 149 5.149 16.732 -14.050 1.00125.86 C
ANISOU 915 CA ARG A 149 18591 16519 12711 -694 1077 21 C
ATOM 916 C ARG A 149 4.660 15.922 -15.253 1.00129.42 C
ANISOU 916 C ARG A 149 19038 16947 13188 -720 1114 10 C
ATOM 917 O ARG A 149 3.729 15.123 -15.116 1.00130.71 O
ANISOU 917 O ARG A 149 19495 16945 13223 -814 1244 -13 O
ATOM 918 CB ARG A 149 4.890 15.998 -12.722 1.00128.23 C
ANISOU 918 CB ARG A 149 19289 16618 12816 -799 1223 -2 C
ATOM 919 N PRO A 150 5.209 16.164 -16.465 1.00124.00 N
ANISOU 919 N PRO A 150 18037 16418 12661 -643 1003 26 N
ATOM 920 CA PRO A 150 4.683 15.463 -17.641 1.00123.52 C
ANISOU 920 CA PRO A 150 17901 16358 12673 -702 1052 -2 C
ATOM 921 C PRO A 150 5.245 14.072 -17.890 1.00128.37 C
ANISOU 921 C PRO A 150 18806 16853 13117 -591 1023 53 C
ATOM 922 O PRO A 150 6.467 13.880 -17.938 1.00127.59 O
ANISOU 922 O PRO A 150 18718 16803 12959 -373 856 128 O
ATOM 923 CB PRO A 150 4.996 16.423 -18.796 1.00123.49 C
ANISOU 923 CB PRO A 150 17517 16551 12854 -609 908 18 C
ATOM 924 CG PRO A 150 6.201 17.186 -18.344 1.00127.55 C
ANISOU 924 CG PRO A 150 18016 17138 13311 -421 744 92 C
ATOM 925 CD PRO A 150 6.284 17.111 -16.838 1.00124.17 C
ANISOU 925 CD PRO A 150 17806 16609 12765 -470 812 82 C
ATOM 926 N ASN A 151 4.337 13.095 -18.060 1.00126.29 N
ANISOU 926 N ASN A 151 18779 16435 12770 -742 1188 5 N
ATOM 927 CA ASN A 151 4.693 11.728 -18.417 1.00126.98 C
ANISOU 927 CA ASN A 151 19112 16411 12722 -660 1173 46 C
ATOM 928 C ASN A 151 5.040 11.792 -19.911 1.00130.35 C
ANISOU 928 C ASN A 151 19250 16982 13294 -560 1057 70 C
ATOM 929 O ASN A 151 4.226 12.261 -20.717 1.00129.08 O
ANISOU 929 O ASN A 151 18790 16930 13326 -676 1097 12 O
ATOM 930 CB ASN A 151 3.527 10.766 -18.146 1.00128.54 C
ANISOU 930 CB ASN A 151 19566 16435 12838 -892 1396 -29 C
ATOM 931 CG ASN A 151 3.833 9.301 -18.366 1.00153.39 C
ANISOU 931 CG ASN A 151 23010 19443 15828 -824 1395 10 C
ATOM 932 OD1 ASN A 151 4.985 8.878 -18.519 1.00147.42 O
ANISOU 932 OD1 ASN A 151 22270 18722 15020 -587 1220 92 O
ATOM 933 ND2 ASN A 151 2.790 8.487 -18.369 1.00147.32 N
ANISOU 933 ND2 ASN A 151 22479 18518 14979 -1039 1595 -59 N
ATOM 934 N ASN A 152 6.270 11.376 -20.262 1.00127.02 N
ANISOU 934 N ASN A 152 18929 16559 12773 -339 911 146 N
ATOM 935 CA ASN A 152 6.844 11.422 -21.611 1.00125.38 C
ANISOU 935 CA ASN A 152 18462 16494 12684 -218 786 176 C
ATOM 936 C ASN A 152 5.970 10.838 -22.740 1.00128.11 C
ANISOU 936 C ASN A 152 18705 16836 13136 -348 875 131 C
ATOM 937 O ASN A 152 6.273 11.086 -23.908 1.00127.22 O
ANISOU 937 O ASN A 152 18304 16864 13170 -299 791 138 O
ATOM 938 CB ASN A 152 8.225 10.755 -21.628 1.00127.30 C
ANISOU 938 CB ASN A 152 18875 16720 12774 42 629 247 C
ATOM 939 CG ASN A 152 9.262 11.383 -20.728 1.00154.25 C
ANISOU 939 CG ASN A 152 22230 20230 16149 224 475 282 C
ATOM 940 OD1 ASN A 152 10.203 10.717 -20.286 1.00152.88 O
ANISOU 940 OD1 ASN A 152 22212 20042 15834 443 345 318 O
ATOM 941 ND2 ASN A 152 9.169 12.687 -20.493 1.00144.68 N
ANISOU 941 ND2 ASN A 152 20790 19123 15060 144 480 262 N
ATOM 942 N ARG A 153 4.894 10.094 -22.408 1.00124.04 N
ANISOU 942 N ARG A 153 18428 16160 12540 -519 1044 80 N
ATOM 943 CA ARG A 153 3.999 9.481 -23.399 1.00122.96 C
ANISOU 943 CA ARG A 153 18229 16009 12483 -637 1127 31 C
ATOM 944 C ARG A 153 3.394 10.495 -24.385 1.00122.51 C
ANISOU 944 C ARG A 153 17749 16127 12674 -713 1109 -26 C
ATOM 945 O ARG A 153 3.276 10.179 -25.569 1.00121.10 O
ANISOU 945 O ARG A 153 17422 16010 12581 -672 1054 -20 O
ATOM 946 CB ARG A 153 2.910 8.615 -22.737 1.00125.78 C
ANISOU 946 CB ARG A 153 18874 16181 12734 -865 1344 -46 C
ATOM 947 CG ARG A 153 3.431 7.505 -21.802 1.00140.67 C
ANISOU 947 CG ARG A 153 21246 17855 14348 -809 1378 4 C
ATOM 948 CD ARG A 153 4.487 6.592 -22.425 1.00151.45 C
ANISOU 948 CD ARG A 153 22756 19193 15594 -554 1218 100 C
ATOM 949 NE ARG A 153 5.109 5.710 -21.433 1.00162.20 N
ANISOU 949 NE ARG A 153 24577 20363 16687 -446 1205 149 N
ATOM 950 CZ ARG A 153 6.144 6.040 -20.664 1.00175.68 C
ANISOU 950 CZ ARG A 153 26391 22070 18291 -278 1092 198 C
ATOM 951 NH1 ARG A 153 6.638 5.166 -19.796 1.00165.41 N
ANISOU 951 NH1 ARG A 153 25545 20573 16729 -175 1077 233 N
ATOM 952 NH2 ARG A 153 6.688 7.248 -20.750 1.00159.26 N
ANISOU 952 NH2 ARG A 153 23985 20172 16353 -208 988 208 N
ATOM 953 N HIS A 154 3.085 11.728 -23.914 1.00116.66 N
ANISOU 953 N HIS A 154 16825 15461 12040 -806 1141 -78 N
ATOM 954 CA HIS A 154 2.552 12.806 -24.753 1.00114.16 C
ANISOU 954 CA HIS A 154 16128 15302 11944 -854 1103 -134 C
ATOM 955 C HIS A 154 3.609 13.320 -25.752 1.00114.65 C
ANISOU 955 C HIS A 154 15982 15499 12079 -657 912 -52 C
ATOM 956 O HIS A 154 3.243 13.824 -26.818 1.00113.30 O
ANISOU 956 O HIS A 154 15565 15423 12061 -679 875 -89 O
ATOM 957 CB HIS A 154 1.923 13.936 -23.904 1.00114.67 C
ANISOU 957 CB HIS A 154 16058 15420 12091 -960 1155 -201 C
ATOM 958 CG HIS A 154 2.866 15.035 -23.509 1.00116.84 C
ANISOU 958 CG HIS A 154 16182 15809 12403 -813 1005 -130 C
ATOM 959 ND1 HIS A 154 2.943 16.208 -24.234 1.00117.11 N
ANISOU 959 ND1 HIS A 154 15899 15993 12604 -771 901 -139 N
ATOM 960 CD2 HIS A 154 3.717 15.112 -22.461 1.00118.78 C
ANISOU 960 CD2 HIS A 154 16557 16038 12535 -706 943 -59 C
ATOM 961 CE1 HIS A 154 3.848 16.950 -23.624 1.00115.92 C
ANISOU 961 CE1 HIS A 154 15690 15914 12440 -659 793 -75 C
ATOM 962 NE2 HIS A 154 4.343 16.334 -22.550 1.00117.22 N
ANISOU 962 NE2 HIS A 154 16109 15988 12443 -615 813 -29 N
ATOM 963 N ALA A 155 4.918 13.164 -25.411 1.00109.35 N
ANISOU 963 N ALA A 155 15415 14838 11296 -469 793 45 N
ATOM 964 CA ALA A 155 6.031 13.545 -26.283 1.00107.24 C
ANISOU 964 CA ALA A 155 14977 14698 11073 -289 627 113 C
ATOM 965 C ALA A 155 6.184 12.501 -27.381 1.00109.67 C
ANISOU 965 C ALA A 155 15340 14974 11357 -234 610 133 C
ATOM 966 O ALA A 155 6.360 12.877 -28.541 1.00107.78 O
ANISOU 966 O ALA A 155 14884 14834 11234 -205 544 135 O
ATOM 967 CB ALA A 155 7.319 13.669 -25.486 1.00108.08 C
ANISOU 967 CB ALA A 155 15165 14835 11064 -110 512 183 C
ATOM 968 N TYR A 156 6.070 11.190 -27.025 1.00107.19 N
ANISOU 968 N TYR A 156 15365 14500 10862 -210 668 153 N
ATOM 969 CA TYR A 156 6.136 10.062 -27.969 1.00107.21 C
ANISOU 969 CA TYR A 156 15479 14442 10815 -169 670 168 C
ATOM 970 C TYR A 156 4.968 10.139 -28.965 1.00108.93 C
ANISOU 970 C TYR A 156 15525 14678 11186 -336 753 96 C
ATOM 971 O TYR A 156 5.127 9.767 -30.128 1.00107.78 O
ANISOU 971 O TYR A 156 15315 14560 11078 -284 707 110 O
ATOM 972 CB TYR A 156 6.130 8.693 -27.241 1.00110.69 C
ANISOU 972 CB TYR A 156 16331 14686 11040 -164 746 182 C
ATOM 973 CG TYR A 156 7.254 8.465 -26.243 1.00114.20 C
ANISOU 973 CG TYR A 156 16994 15088 11310 18 655 241 C
ATOM 974 CD1 TYR A 156 8.590 8.509 -26.640 1.00115.90 C
ANISOU 974 CD1 TYR A 156 17119 15415 11502 258 478 297 C
ATOM 975 CD2 TYR A 156 6.979 8.104 -24.926 1.00116.57 C
ANISOU 975 CD2 TYR A 156 17614 15228 11451 -45 748 231 C
ATOM 976 CE1 TYR A 156 9.625 8.280 -25.729 1.00117.85 C
ANISOU 976 CE1 TYR A 156 17557 15633 11586 442 380 331 C
ATOM 977 CE2 TYR A 156 8.004 7.878 -24.006 1.00118.50 C
ANISOU 977 CE2 TYR A 156 18077 15424 11523 139 649 278 C
ATOM 978 CZ TYR A 156 9.326 7.963 -24.412 1.00126.55 C
ANISOU 978 CZ TYR A 156 18980 16570 12533 390 458 325 C
ATOM 979 OH TYR A 156 10.333 7.730 -23.503 1.00129.30 O
ANISOU 979 OH TYR A 156 19536 16882 12712 586 348 353 O
ATOM 980 N VAL A 157 3.797 10.632 -28.490 1.00104.72 N
ANISOU 980 N VAL A 157 14914 14134 10739 -532 872 6 N
ATOM 981 CA VAL A 157 2.580 10.856 -29.283 1.00103.41 C
ANISOU 981 CA VAL A 157 14558 14003 10730 -695 947 -95 C
ATOM 982 C VAL A 157 2.870 11.989 -30.273 1.00104.70 C
ANISOU 982 C VAL A 157 14394 14330 11057 -608 809 -81 C
ATOM 983 O VAL A 157 2.587 11.844 -31.465 1.00104.07 O
ANISOU 983 O VAL A 157 14200 14283 11057 -606 779 -100 O
ATOM 984 CB VAL A 157 1.337 11.120 -28.374 1.00107.45 C
ANISOU 984 CB VAL A 157 15073 14474 11280 -912 1107 -212 C
ATOM 985 CG1 VAL A 157 0.233 11.897 -29.095 1.00106.49 C
ANISOU 985 CG1 VAL A 157 14650 14453 11360 -1033 1129 -332 C
ATOM 986 CG2 VAL A 157 0.787 9.815 -27.817 1.00108.88 C
ANISOU 986 CG2 VAL A 157 15583 14479 11309 -1048 1274 -250 C
ATOM 987 N GLY A 158 3.488 13.061 -29.765 1.00 99.13 N
ANISOU 987 N GLY A 158 13570 13714 10381 -534 726 -44 N
ATOM 988 CA GLY A 158 3.883 14.233 -30.535 1.00 96.94 C
ANISOU 988 CA GLY A 158 13023 13580 10231 -457 600 -25 C
ATOM 989 C GLY A 158 4.807 13.897 -31.687 1.00 98.80 C
ANISOU 989 C GLY A 158 13227 13862 10452 -313 491 47 C
ATOM 990 O GLY A 158 4.462 14.168 -32.839 1.00 98.37 O
ANISOU 990 O GLY A 158 13014 13857 10504 -326 454 21 O
ATOM 991 N ILE A 159 5.953 13.238 -31.393 1.00 93.78 N
ANISOU 991 N ILE A 159 12754 13202 9675 -172 441 127 N
ATOM 992 CA ILE A 159 6.960 12.849 -32.394 1.00 92.19 C
ANISOU 992 CA ILE A 159 12533 13053 9443 -21 341 187 C
ATOM 993 C ILE A 159 6.357 11.937 -33.495 1.00 94.29 C
ANISOU 993 C ILE A 159 12840 13257 9730 -64 383 165 C
ATOM 994 O ILE A 159 6.720 12.090 -34.663 1.00 93.21 O
ANISOU 994 O ILE A 159 12576 13190 9650 -1 309 185 O
ATOM 995 CB ILE A 159 8.281 12.267 -31.777 1.00 95.63 C
ANISOU 995 CB ILE A 159 13136 13481 9717 154 272 253 C
ATOM 996 CG1 ILE A 159 8.086 10.896 -31.098 1.00 97.39 C
ANISOU 996 CG1 ILE A 159 13686 13538 9778 155 350 258 C
ATOM 997 CG2 ILE A 159 8.957 13.258 -30.821 1.00 95.26 C
ANISOU 997 CG2 ILE A 159 13009 13522 9664 208 210 268 C
ATOM 998 CD1 ILE A 159 8.595 9.703 -31.894 1.00104.09 C
ANISOU 998 CD1 ILE A 159 14683 14332 10535 265 322 289 C
ATOM 999 N ALA A 160 5.420 11.031 -33.126 1.00 90.24 N
ANISOU 999 N ALA A 160 12503 12613 9170 -185 506 118 N
ATOM 1000 CA ALA A 160 4.750 10.127 -34.067 1.00 89.88 C
ANISOU 1000 CA ALA A 160 12509 12500 9140 -249 561 83 C
ATOM 1001 C ALA A 160 3.848 10.908 -35.013 1.00 91.63 C
ANISOU 1001 C ALA A 160 12473 12799 9543 -342 551 11 C
ATOM 1002 O ALA A 160 3.911 10.690 -36.220 1.00 90.91 O
ANISOU 1002 O ALA A 160 12314 12732 9496 -300 501 19 O
ATOM 1003 CB ALA A 160 3.950 9.077 -33.319 1.00 92.05 C
ANISOU 1003 CB ALA A 160 13036 12620 9317 -384 711 34 C
ATOM 1004 N VAL A 161 3.053 11.851 -34.471 1.00 87.03 N
ANISOU 1004 N VAL A 161 11752 12257 9060 -452 588 -62 N
ATOM 1005 CA VAL A 161 2.168 12.729 -35.240 1.00 85.83 C
ANISOU 1005 CA VAL A 161 11357 12180 9076 -521 560 -146 C
ATOM 1006 C VAL A 161 3.027 13.626 -36.169 1.00 88.57 C
ANISOU 1006 C VAL A 161 11540 12635 9479 -386 411 -79 C
ATOM 1007 O VAL A 161 2.728 13.704 -37.362 1.00 87.74 O
ANISOU 1007 O VAL A 161 11332 12555 9450 -377 362 -103 O
ATOM 1008 CB VAL A 161 1.194 13.515 -34.314 1.00 89.75 C
ANISOU 1008 CB VAL A 161 11759 12693 9650 -655 632 -249 C
ATOM 1009 CG1 VAL A 161 0.462 14.625 -35.062 1.00 89.03 C
ANISOU 1009 CG1 VAL A 161 11414 12690 9725 -681 567 -337 C
ATOM 1010 CG2 VAL A 161 0.188 12.575 -33.656 1.00 90.77 C
ANISOU 1010 CG2 VAL A 161 12041 12717 9731 -820 799 -339 C
ATOM 1011 N ILE A 162 4.130 14.220 -35.637 1.00 84.54 N
ANISOU 1011 N ILE A 162 11024 12181 8916 -286 345 1 N
ATOM 1012 CA ILE A 162 5.095 15.055 -36.375 1.00 83.48 C
ANISOU 1012 CA ILE A 162 10758 12150 8810 -175 223 61 C
ATOM 1013 C ILE A 162 5.638 14.308 -37.604 1.00 87.47 C
ANISOU 1013 C ILE A 162 11295 12655 9286 -90 178 105 C
ATOM 1014 O ILE A 162 5.616 14.865 -38.699 1.00 86.78 O
ANISOU 1014 O ILE A 162 11081 12618 9274 -75 113 100 O
ATOM 1015 CB ILE A 162 6.259 15.534 -35.458 1.00 86.60 C
ANISOU 1015 CB ILE A 162 11173 12602 9129 -89 179 127 C
ATOM 1016 CG1 ILE A 162 5.784 16.553 -34.409 1.00 87.23 C
ANISOU 1016 CG1 ILE A 162 11186 12701 9256 -167 204 87 C
ATOM 1017 CG2 ILE A 162 7.439 16.090 -36.270 1.00 86.46 C
ANISOU 1017 CG2 ILE A 162 11051 12690 9110 22 72 184 C
ATOM 1018 CD1 ILE A 162 6.726 16.664 -33.175 1.00 96.24 C
ANISOU 1018 CD1 ILE A 162 12413 13859 10294 -102 192 138 C
ATOM 1019 N TRP A 163 6.127 13.060 -37.415 1.00 84.47 N
ANISOU 1019 N TRP A 163 11100 12208 8785 -31 210 146 N
ATOM 1020 CA TRP A 163 6.684 12.239 -38.493 1.00 84.19 C
ANISOU 1020 CA TRP A 163 11114 12166 8707 59 172 187 C
ATOM 1021 C TRP A 163 5.647 11.829 -39.539 1.00 86.84 C
ANISOU 1021 C TRP A 163 11425 12451 9119 -23 202 132 C
ATOM 1022 O TRP A 163 5.981 11.785 -40.721 1.00 86.12 O
ANISOU 1022 O TRP A 163 11275 12394 9053 34 142 153 O
ATOM 1023 CB TRP A 163 7.437 11.018 -37.949 1.00 84.16 C
ANISOU 1023 CB TRP A 163 11333 12099 8546 158 189 236 C
ATOM 1024 CG TRP A 163 8.858 11.304 -37.544 1.00 85.50 C
ANISOU 1024 CG TRP A 163 11491 12356 8638 309 106 291 C
ATOM 1025 CD1 TRP A 163 9.309 11.595 -36.290 1.00 88.85 C
ANISOU 1025 CD1 TRP A 163 11968 12792 8999 342 101 301 C
ATOM 1026 CD2 TRP A 163 10.020 11.284 -38.392 1.00 85.13 C
ANISOU 1026 CD2 TRP A 163 11376 12404 8566 446 18 327 C
ATOM 1027 NE1 TRP A 163 10.674 11.777 -36.307 1.00 88.34 N
ANISOU 1027 NE1 TRP A 163 11857 12831 8876 495 8 335 N
ATOM 1028 CE2 TRP A 163 11.134 11.600 -37.584 1.00 89.12 C
ANISOU 1028 CE2 TRP A 163 11875 12988 8999 556 -39 347 C
ATOM 1029 CE3 TRP A 163 10.226 11.041 -39.761 1.00 86.12 C
ANISOU 1029 CE3 TRP A 163 11440 12560 8722 483 -15 336 C
ATOM 1030 CZ2 TRP A 163 12.431 11.681 -38.095 1.00 88.39 C
ANISOU 1030 CZ2 TRP A 163 11700 13014 8869 695 -122 361 C
ATOM 1031 CZ3 TRP A 163 11.515 11.116 -40.265 1.00 87.56 C
ANISOU 1031 CZ3 TRP A 163 11555 12851 8861 617 -90 360 C
ATOM 1032 CH2 TRP A 163 12.599 11.435 -39.436 1.00 88.48 C
ANISOU 1032 CH2 TRP A 163 11650 13057 8913 718 -141 366 C
ATOM 1033 N VAL A 164 4.393 11.554 -39.122 1.00 82.72 N
ANISOU 1033 N VAL A 164 10943 11853 8632 -161 298 52 N
ATOM 1034 CA VAL A 164 3.324 11.187 -40.065 1.00 81.76 C
ANISOU 1034 CA VAL A 164 10781 11693 8590 -249 328 -25 C
ATOM 1035 C VAL A 164 2.917 12.421 -40.893 1.00 82.56 C
ANISOU 1035 C VAL A 164 10658 11879 8833 -256 242 -70 C
ATOM 1036 O VAL A 164 2.799 12.313 -42.115 1.00 82.11 O
ANISOU 1036 O VAL A 164 10554 11828 8817 -227 189 -76 O
ATOM 1037 CB VAL A 164 2.131 10.447 -39.397 1.00 86.53 C
ANISOU 1037 CB VAL A 164 11487 12202 9187 -409 465 -120 C
ATOM 1038 CG1 VAL A 164 1.020 10.160 -40.404 1.00 86.76 C
ANISOU 1038 CG1 VAL A 164 11436 12216 9314 -502 486 -223 C
ATOM 1039 CG2 VAL A 164 2.592 9.144 -38.755 1.00 87.10 C
ANISOU 1039 CG2 VAL A 164 11833 12165 9095 -392 541 -67 C
ATOM 1040 N LEU A 165 2.779 13.593 -40.227 1.00 76.71 N
ANISOU 1040 N LEU A 165 9800 11195 8150 -283 222 -97 N
ATOM 1041 CA LEU A 165 2.477 14.907 -40.813 1.00 75.05 C
ANISOU 1041 CA LEU A 165 9408 11055 8052 -277 132 -136 C
ATOM 1042 C LEU A 165 3.588 15.304 -41.819 1.00 77.06 C
ANISOU 1042 C LEU A 165 9634 11363 8284 -161 28 -47 C
ATOM 1043 O LEU A 165 3.284 15.837 -42.883 1.00 75.66 O
ANISOU 1043 O LEU A 165 9373 11201 8174 -147 -44 -75 O
ATOM 1044 CB LEU A 165 2.441 15.945 -39.673 1.00 74.95 C
ANISOU 1044 CB LEU A 165 9329 11085 8062 -307 136 -151 C
ATOM 1045 CG LEU A 165 1.551 17.184 -39.796 1.00 79.54 C
ANISOU 1045 CG LEU A 165 9750 11707 8764 -351 89 -248 C
ATOM 1046 CD1 LEU A 165 1.418 17.864 -38.448 1.00 79.36 C
ANISOU 1046 CD1 LEU A 165 9704 11706 8744 -398 130 -268 C
ATOM 1047 CD2 LEU A 165 2.118 18.204 -40.778 1.00 82.44 C
ANISOU 1047 CD2 LEU A 165 10034 12126 9164 -269 -38 -209 C
ATOM 1048 N ALA A 166 4.867 15.054 -41.464 1.00 73.36 N
ANISOU 1048 N ALA A 166 9237 10922 7714 -77 21 50 N
ATOM 1049 CA ALA A 166 6.026 15.386 -42.291 1.00 72.70 C
ANISOU 1049 CA ALA A 166 9122 10904 7598 19 -56 121 C
ATOM 1050 C ALA A 166 6.132 14.542 -43.547 1.00 77.15 C
ANISOU 1050 C ALA A 166 9733 11435 8144 62 -72 137 C
ATOM 1051 O ALA A 166 6.416 15.089 -44.610 1.00 76.38 O
ANISOU 1051 O ALA A 166 9573 11372 8075 90 -137 148 O
ATOM 1052 CB ALA A 166 7.306 15.276 -41.482 1.00 73.46 C
ANISOU 1052 CB ALA A 166 9265 11052 7594 98 -57 190 C
ATOM 1053 N VAL A 167 5.934 13.213 -43.425 1.00 74.65 N
ANISOU 1053 N VAL A 167 9547 11046 7769 65 -11 140 N
ATOM 1054 CA VAL A 167 6.000 12.269 -44.544 1.00 74.44 C
ANISOU 1054 CA VAL A 167 9588 10979 7717 105 -18 154 C
ATOM 1055 C VAL A 167 4.877 12.602 -45.531 1.00 77.93 C
ANISOU 1055 C VAL A 167 9951 11394 8266 37 -44 80 C
ATOM 1056 O VAL A 167 5.151 12.736 -46.723 1.00 77.83 O
ANISOU 1056 O VAL A 167 9911 11394 8266 82 -104 98 O
ATOM 1057 CB VAL A 167 5.987 10.784 -44.070 1.00 79.06 C
ANISOU 1057 CB VAL A 167 10360 11479 8202 119 56 170 C
ATOM 1058 CG1 VAL A 167 5.813 9.822 -45.243 1.00 79.06 C
ANISOU 1058 CG1 VAL A 167 10430 11425 8185 143 53 173 C
ATOM 1059 CG2 VAL A 167 7.256 10.438 -43.286 1.00 78.96 C
ANISOU 1059 CG2 VAL A 167 10435 11498 8069 231 48 240 C
ATOM 1060 N ALA A 168 3.647 12.824 -45.020 1.00 74.15 N
ANISOU 1060 N ALA A 168 9427 10884 7863 -68 -4 -12 N
ATOM 1061 CA ALA A 168 2.467 13.172 -45.815 1.00 73.92 C
ANISOU 1061 CA ALA A 168 9306 10839 7942 -127 -37 -113 C
ATOM 1062 C ALA A 168 2.651 14.465 -46.616 1.00 78.39 C
ANISOU 1062 C ALA A 168 9763 11457 8565 -77 -151 -110 C
ATOM 1063 O ALA A 168 2.491 14.430 -47.833 1.00 78.46 O
ANISOU 1063 O ALA A 168 9768 11448 8597 -45 -212 -123 O
ATOM 1064 CB ALA A 168 1.238 13.267 -44.925 1.00 74.97 C
ANISOU 1064 CB ALA A 168 9389 10956 8142 -243 30 -228 C
ATOM 1065 N SER A 169 3.025 15.584 -45.952 1.00 75.14 N
ANISOU 1065 N SER A 169 9287 11101 8163 -69 -180 -90 N
ATOM 1066 CA SER A 169 3.232 16.897 -46.579 1.00 75.05 C
ANISOU 1066 CA SER A 169 9204 11126 8186 -34 -281 -86 C
ATOM 1067 C SER A 169 4.392 16.936 -47.583 1.00 81.03 C
ANISOU 1067 C SER A 169 10008 11905 8876 39 -325 5 C
ATOM 1068 O SER A 169 4.365 17.758 -48.504 1.00 81.14 O
ANISOU 1068 O SER A 169 10004 11917 8910 58 -405 -4 O
ATOM 1069 CB SER A 169 3.422 17.981 -45.522 1.00 78.44 C
ANISOU 1069 CB SER A 169 9573 11604 8628 -55 -285 -85 C
ATOM 1070 OG SER A 169 4.556 17.740 -44.704 1.00 88.07 O
ANISOU 1070 OG SER A 169 10834 12865 9764 -32 -237 2 O
ATOM 1071 N SER A 170 5.402 16.056 -47.405 1.00 77.86 N
ANISOU 1071 N SER A 170 9674 11521 8387 81 -274 82 N
ATOM 1072 CA SER A 170 6.579 15.972 -48.274 1.00 77.26 C
ANISOU 1072 CA SER A 170 9631 11483 8243 147 -299 154 C
ATOM 1073 C SER A 170 6.395 15.018 -49.459 1.00 81.31 C
ANISOU 1073 C SER A 170 10211 11941 8742 178 -305 156 C
ATOM 1074 O SER A 170 7.175 15.091 -50.410 1.00 80.88 O
ANISOU 1074 O SER A 170 10177 11910 8644 222 -333 198 O
ATOM 1075 CB SER A 170 7.809 15.551 -47.473 1.00 80.15 C
ANISOU 1075 CB SER A 170 10020 11912 8520 198 -256 218 C
ATOM 1076 OG SER A 170 8.068 16.422 -46.384 1.00 86.37 O
ANISOU 1076 OG SER A 170 10749 12753 9314 173 -253 219 O
ATOM 1077 N LEU A 171 5.377 14.129 -49.408 1.00 78.15 N
ANISOU 1077 N LEU A 171 9847 11470 8375 144 -273 104 N
ATOM 1078 CA LEU A 171 5.117 13.109 -50.433 1.00 78.35 C
ANISOU 1078 CA LEU A 171 9944 11437 8387 164 -271 99 C
ATOM 1079 C LEU A 171 5.232 13.575 -51.894 1.00 81.64 C
ANISOU 1079 C LEU A 171 10357 11845 8816 198 -351 103 C
ATOM 1080 O LEU A 171 5.938 12.877 -52.627 1.00 81.07 O
ANISOU 1080 O LEU A 171 10353 11769 8681 252 -343 155 O
ATOM 1081 CB LEU A 171 3.780 12.392 -50.232 1.00 78.96 C
ANISOU 1081 CB LEU A 171 10037 11445 8521 92 -230 11 C
ATOM 1082 CG LEU A 171 3.833 11.148 -49.357 1.00 84.20 C
ANISOU 1082 CG LEU A 171 10806 12068 9117 72 -130 27 C
ATOM 1083 CD1 LEU A 171 2.440 10.705 -48.972 1.00 84.99 C
ANISOU 1083 CD1 LEU A 171 10899 12115 9280 -41 -71 -82 C
ATOM 1084 CD2 LEU A 171 4.622 10.014 -50.025 1.00 86.57 C
ANISOU 1084 CD2 LEU A 171 11230 12336 9328 145 -118 93 C
ATOM 1085 N PRO A 172 4.614 14.712 -52.349 1.00 77.63 N
ANISOU 1085 N PRO A 172 9792 11329 8375 177 -429 49 N
ATOM 1086 CA PRO A 172 4.734 15.102 -53.773 1.00 76.97 C
ANISOU 1086 CA PRO A 172 9747 11216 8281 212 -505 55 C
ATOM 1087 C PRO A 172 6.151 15.212 -54.336 1.00 79.68 C
ANISOU 1087 C PRO A 172 10137 11605 8534 253 -494 144 C
ATOM 1088 O PRO A 172 6.327 14.989 -55.530 1.00 78.20 O
ANISOU 1088 O PRO A 172 10014 11383 8317 281 -523 158 O
ATOM 1089 CB PRO A 172 4.008 16.441 -53.831 1.00 78.70 C
ANISOU 1089 CB PRO A 172 9915 11423 8565 193 -591 -12 C
ATOM 1090 CG PRO A 172 3.012 16.356 -52.745 1.00 83.56 C
ANISOU 1090 CG PRO A 172 10451 12043 9255 145 -562 -92 C
ATOM 1091 CD PRO A 172 3.723 15.650 -51.633 1.00 79.05 C
ANISOU 1091 CD PRO A 172 9886 11515 8634 128 -456 -28 C
ATOM 1092 N PHE A 173 7.153 15.532 -53.486 1.00 76.90 N
ANISOU 1092 N PHE A 173 9749 11334 8137 253 -450 194 N
ATOM 1093 CA PHE A 173 8.560 15.619 -53.894 1.00 76.99 C
ANISOU 1093 CA PHE A 173 9776 11413 8064 284 -427 255 C
ATOM 1094 C PHE A 173 9.072 14.238 -54.313 1.00 83.20 C
ANISOU 1094 C PHE A 173 10620 12199 8794 346 -385 288 C
ATOM 1095 O PHE A 173 9.716 14.121 -55.352 1.00 83.20 O
ANISOU 1095 O PHE A 173 10661 12205 8746 372 -390 309 O
ATOM 1096 CB PHE A 173 9.449 16.223 -52.787 1.00 78.18 C
ANISOU 1096 CB PHE A 173 9858 11662 8186 272 -393 279 C
ATOM 1097 CG PHE A 173 9.448 17.733 -52.679 1.00 79.31 C
ANISOU 1097 CG PHE A 173 9965 11821 8348 213 -431 263 C
ATOM 1098 CD1 PHE A 173 9.775 18.528 -53.774 1.00 82.19 C
ANISOU 1098 CD1 PHE A 173 10378 12170 8680 188 -464 267 C
ATOM 1099 CD2 PHE A 173 9.194 18.359 -51.465 1.00 81.38 C
ANISOU 1099 CD2 PHE A 173 10164 12109 8647 181 -429 247 C
ATOM 1100 CE1 PHE A 173 9.797 19.923 -53.666 1.00 83.04 C
ANISOU 1100 CE1 PHE A 173 10486 12278 8788 130 -498 253 C
ATOM 1101 CE2 PHE A 173 9.227 19.754 -51.357 1.00 84.05 C
ANISOU 1101 CE2 PHE A 173 10485 12457 8994 129 -465 234 C
ATOM 1102 CZ PHE A 173 9.534 20.527 -52.456 1.00 82.16 C
ANISOU 1102 CZ PHE A 173 10307 12194 8716 104 -500 237 C
ATOM 1103 N LEU A 174 8.733 13.197 -53.529 1.00 80.93 N
ANISOU 1103 N LEU A 174 10352 11891 8506 367 -343 286 N
ATOM 1104 CA LEU A 174 9.096 11.803 -53.781 1.00 81.30 C
ANISOU 1104 CA LEU A 174 10480 11918 8491 433 -306 313 C
ATOM 1105 C LEU A 174 8.401 11.298 -55.046 1.00 86.26 C
ANISOU 1105 C LEU A 174 11174 12460 9141 430 -334 294 C
ATOM 1106 O LEU A 174 9.053 10.676 -55.886 1.00 86.98 O
ANISOU 1106 O LEU A 174 11320 12554 9173 486 -328 324 O
ATOM 1107 CB LEU A 174 8.683 10.940 -52.573 1.00 81.50 C
ANISOU 1107 CB LEU A 174 10548 11911 8508 433 -256 305 C
ATOM 1108 CG LEU A 174 9.079 9.469 -52.585 1.00 86.60 C
ANISOU 1108 CG LEU A 174 11311 12521 9072 508 -218 333 C
ATOM 1109 CD1 LEU A 174 10.486 9.272 -52.048 1.00 87.08 C
ANISOU 1109 CD1 LEU A 174 11373 12673 9040 608 -207 373 C
ATOM 1110 CD2 LEU A 174 8.110 8.656 -51.762 1.00 89.58 C
ANISOU 1110 CD2 LEU A 174 11770 12809 9457 458 -168 304 C
ATOM 1111 N ILE A 175 7.080 11.565 -55.171 1.00 82.13 N
ANISOU 1111 N ILE A 175 10638 11866 8702 368 -367 233 N
ATOM 1112 CA ILE A 175 6.239 11.139 -56.294 1.00 81.68 C
ANISOU 1112 CA ILE A 175 10631 11727 8677 362 -406 194 C
ATOM 1113 C ILE A 175 6.676 11.804 -57.607 1.00 85.48 C
ANISOU 1113 C ILE A 175 11137 12204 9136 387 -466 212 C
ATOM 1114 O ILE A 175 6.827 11.110 -58.614 1.00 85.91 O
ANISOU 1114 O ILE A 175 11267 12220 9153 423 -470 229 O
ATOM 1115 CB ILE A 175 4.716 11.371 -56.000 1.00 84.64 C
ANISOU 1115 CB ILE A 175 10956 12049 9153 293 -434 96 C
ATOM 1116 CG1 ILE A 175 4.276 10.724 -54.675 1.00 84.94 C
ANISOU 1116 CG1 ILE A 175 10987 12085 9203 244 -353 71 C
ATOM 1117 CG2 ILE A 175 3.831 10.881 -57.157 1.00 85.90 C
ANISOU 1117 CG2 ILE A 175 11158 12133 9348 292 -483 38 C
ATOM 1118 CD1 ILE A 175 3.157 11.447 -53.966 1.00 90.65 C
ANISOU 1118 CD1 ILE A 175 11613 12809 10021 169 -366 -25 C
ATOM 1119 N TYR A 176 6.884 13.138 -57.590 1.00 80.65 N
ANISOU 1119 N TYR A 176 10481 11625 8538 363 -508 209 N
ATOM 1120 CA TYR A 176 7.196 13.914 -58.783 1.00 79.43 C
ANISOU 1120 CA TYR A 176 10381 11447 8351 368 -562 218 C
ATOM 1121 C TYR A 176 8.685 14.121 -59.080 1.00 82.76 C
ANISOU 1121 C TYR A 176 10819 11945 8682 379 -513 280 C
ATOM 1122 O TYR A 176 8.977 14.744 -60.099 1.00 82.49 O
ANISOU 1122 O TYR A 176 10850 11886 8608 364 -542 285 O
ATOM 1123 CB TYR A 176 6.444 15.243 -58.763 1.00 80.15 C
ANISOU 1123 CB TYR A 176 10453 11504 8495 334 -644 165 C
ATOM 1124 CG TYR A 176 4.951 15.015 -58.837 1.00 82.18 C
ANISOU 1124 CG TYR A 176 10693 11691 8842 335 -709 75 C
ATOM 1125 CD1 TYR A 176 4.375 14.397 -59.944 1.00 84.92 C
ANISOU 1125 CD1 TYR A 176 11108 11963 9193 365 -757 43 C
ATOM 1126 CD2 TYR A 176 4.120 15.356 -57.777 1.00 82.61 C
ANISOU 1126 CD2 TYR A 176 10653 11761 8974 303 -716 11 C
ATOM 1127 CE1 TYR A 176 3.006 14.141 -60.001 1.00 86.03 C
ANISOU 1127 CE1 TYR A 176 11213 12054 9419 363 -814 -60 C
ATOM 1128 CE2 TYR A 176 2.747 15.115 -57.828 1.00 83.77 C
ANISOU 1128 CE2 TYR A 176 10761 11862 9207 297 -766 -96 C
ATOM 1129 CZ TYR A 176 2.195 14.507 -58.944 1.00 90.65 C
ANISOU 1129 CZ TYR A 176 11689 12667 10085 326 -816 -136 C
ATOM 1130 OH TYR A 176 0.847 14.260 -59.017 1.00 91.35 O
ANISOU 1130 OH TYR A 176 11723 12724 10261 317 -867 -261 O
ATOM 1131 N GLN A 177 9.625 13.553 -58.279 1.00 78.88 N
ANISOU 1131 N GLN A 177 10280 11542 8147 407 -439 316 N
ATOM 1132 CA GLN A 177 11.049 13.627 -58.643 1.00 78.37 C
ANISOU 1132 CA GLN A 177 10209 11568 7999 425 -391 349 C
ATOM 1133 C GLN A 177 11.304 12.486 -59.614 1.00 82.94 C
ANISOU 1133 C GLN A 177 10865 12118 8532 485 -374 365 C
ATOM 1134 O GLN A 177 10.864 11.360 -59.376 1.00 81.96 O
ANISOU 1134 O GLN A 177 10770 11954 8417 533 -366 369 O
ATOM 1135 CB GLN A 177 12.010 13.558 -57.450 1.00 79.14 C
ANISOU 1135 CB GLN A 177 10216 11787 8068 448 -338 362 C
ATOM 1136 CG GLN A 177 13.403 14.114 -57.779 1.00 79.63 C
ANISOU 1136 CG GLN A 177 10234 11964 8058 436 -295 363 C
ATOM 1137 CD GLN A 177 13.473 15.627 -57.852 1.00 88.45 C
ANISOU 1137 CD GLN A 177 11333 13095 9178 336 -305 349 C
ATOM 1138 OE1 GLN A 177 12.579 16.357 -57.412 1.00 86.81 O
ANISOU 1138 OE1 GLN A 177 11128 12827 9027 291 -352 340 O
ATOM 1139 NE2 GLN A 177 14.574 16.139 -58.355 1.00 73.77 N
ANISOU 1139 NE2 GLN A 177 9456 11321 7252 296 -257 337 N
ATOM 1140 N VAL A 178 11.974 12.794 -60.726 1.00 80.64 N
ANISOU 1140 N VAL A 178 10621 11835 8183 472 -366 372 N
ATOM 1141 CA VAL A 178 12.207 11.863 -61.824 1.00 80.71 C
ANISOU 1141 CA VAL A 178 10713 11810 8145 522 -353 384 C
ATOM 1142 C VAL A 178 13.701 11.649 -62.127 1.00 86.20 C
ANISOU 1142 C VAL A 178 11375 12623 8753 550 -282 389 C
ATOM 1143 O VAL A 178 14.514 12.552 -61.914 1.00 85.87 O
ANISOU 1143 O VAL A 178 11269 12674 8684 496 -247 374 O
ATOM 1144 CB VAL A 178 11.387 12.381 -63.049 1.00 83.88 C
ANISOU 1144 CB VAL A 178 11223 12088 8558 481 -418 371 C
ATOM 1145 CG1 VAL A 178 12.040 12.073 -64.396 1.00 84.15 C
ANISOU 1145 CG1 VAL A 178 11352 12107 8516 495 -393 383 C
ATOM 1146 CG2 VAL A 178 9.949 11.876 -63.001 1.00 83.20 C
ANISOU 1146 CG2 VAL A 178 11166 11895 8551 497 -485 346 C
ATOM 1147 N MET A 179 14.044 10.432 -62.614 1.00 83.93 N
ANISOU 1147 N MET A 179 11131 12336 8422 634 -259 398 N
ATOM 1148 CA MET A 179 15.381 10.058 -63.082 1.00 84.39 C
ANISOU 1148 CA MET A 179 11162 12504 8399 679 -197 385 C
ATOM 1149 C MET A 179 15.265 9.462 -64.495 1.00 89.14 C
ANISOU 1149 C MET A 179 11882 13027 8962 699 -197 394 C
ATOM 1150 O MET A 179 15.069 8.250 -64.639 1.00 89.31 O
ANISOU 1150 O MET A 179 11957 13005 8970 787 -205 408 O
ATOM 1151 CB MET A 179 16.106 9.097 -62.119 1.00 86.73 C
ANISOU 1151 CB MET A 179 11388 12901 8665 794 -173 377 C
ATOM 1152 CG MET A 179 17.582 8.947 -62.457 1.00 91.05 C
ANISOU 1152 CG MET A 179 11860 13599 9134 840 -115 333 C
ATOM 1153 SD MET A 179 18.359 7.358 -62.063 1.00 95.85 S
ANISOU 1153 SD MET A 179 12464 14280 9676 1032 -111 315 S
ATOM 1154 CE MET A 179 17.410 6.245 -63.086 1.00 92.48 C
ANISOU 1154 CE MET A 179 12218 13677 9244 1071 -137 363 C
ATOM 1155 N THR A 180 15.350 10.320 -65.531 1.00 85.57 N
ANISOU 1155 N THR A 180 11490 12542 8482 613 -189 385 N
ATOM 1156 CA THR A 180 15.277 9.869 -66.920 1.00 85.63 C
ANISOU 1156 CA THR A 180 11623 12468 8444 623 -188 392 C
ATOM 1157 C THR A 180 16.591 10.132 -67.655 1.00 90.27 C
ANISOU 1157 C THR A 180 12198 13157 8942 588 -100 361 C
ATOM 1158 O THR A 180 17.272 11.114 -67.362 1.00 89.58 O
ANISOU 1158 O THR A 180 12045 13158 8833 502 -52 331 O
ATOM 1159 CB THR A 180 14.036 10.428 -67.648 1.00 94.90 C
ANISOU 1159 CB THR A 180 12926 13478 9654 567 -269 404 C
ATOM 1160 OG1 THR A 180 13.910 9.792 -68.924 1.00 97.71 O
ANISOU 1160 OG1 THR A 180 13411 13750 9966 594 -277 411 O
ATOM 1161 CG2 THR A 180 14.077 11.930 -67.843 1.00 92.89 C
ANISOU 1161 CG2 THR A 180 12700 13208 9386 457 -277 390 C
ATOM 1162 N ASP A 181 16.931 9.253 -68.625 1.00 88.42 N
ANISOU 1162 N ASP A 181 12032 12910 8655 646 -73 359 N
ATOM 1163 CA ASP A 181 18.133 9.344 -69.469 1.00 89.22 C
ANISOU 1163 CA ASP A 181 12129 13105 8667 616 21 316 C
ATOM 1164 C ASP A 181 17.927 10.273 -70.663 1.00 92.95 C
ANISOU 1164 C ASP A 181 12749 13477 9092 490 36 317 C
ATOM 1165 O ASP A 181 18.765 10.305 -71.562 1.00 92.80 O
ANISOU 1165 O ASP A 181 12764 13503 8991 445 120 281 O
ATOM 1166 CB ASP A 181 18.597 7.951 -69.938 1.00 91.66 C
ANISOU 1166 CB ASP A 181 12455 13437 8934 743 41 310 C
ATOM 1167 CG ASP A 181 17.700 7.280 -70.961 1.00104.94 C
ANISOU 1167 CG ASP A 181 14309 14947 10615 772 -14 355 C
ATOM 1168 OD1 ASP A 181 16.528 6.986 -70.627 1.00105.35 O
ANISOU 1168 OD1 ASP A 181 14410 14883 10734 799 -98 395 O
ATOM 1169 OD2 ASP A 181 18.184 7.003 -72.080 1.00113.55 O
ANISOU 1169 OD2 ASP A 181 15480 16027 11637 769 32 340 O
ATOM 1170 N GLU A 182 16.814 11.029 -70.656 1.00 90.22 N
ANISOU 1170 N GLU A 182 12498 12992 8791 436 -48 349 N
ATOM 1171 CA GLU A 182 16.418 11.991 -71.683 1.00 91.13 C
ANISOU 1171 CA GLU A 182 12792 12977 8857 334 -68 352 C
ATOM 1172 C GLU A 182 16.587 13.429 -71.144 1.00 96.35 C
ANISOU 1172 C GLU A 182 13433 13664 9512 214 -52 335 C
ATOM 1173 O GLU A 182 15.589 14.052 -70.762 1.00 95.03 O
ANISOU 1173 O GLU A 182 13303 13402 9402 209 -148 353 O
ATOM 1174 CB GLU A 182 14.949 11.758 -72.113 1.00 92.14 C
ANISOU 1174 CB GLU A 182 13055 12919 9035 387 -199 386 C
ATOM 1175 CG GLU A 182 14.657 10.424 -72.781 1.00104.47 C
ANISOU 1175 CG GLU A 182 14667 14430 10595 488 -218 402 C
ATOM 1176 CD GLU A 182 13.218 9.946 -72.702 1.00129.86 C
ANISOU 1176 CD GLU A 182 17930 17518 13894 556 -341 418 C
ATOM 1177 OE1 GLU A 182 12.297 10.793 -72.623 1.00122.99 O
ANISOU 1177 OE1 GLU A 182 17097 16562 13071 525 -431 408 O
ATOM 1178 OE2 GLU A 182 13.012 8.711 -72.739 1.00128.81 O
ANISOU 1178 OE2 GLU A 182 17798 17371 13773 639 -346 429 O
ATOM 1179 N PRO A 183 17.819 13.993 -71.093 1.00 95.25 N
ANISOU 1179 N PRO A 183 13230 13655 9304 116 67 289 N
ATOM 1180 CA PRO A 183 17.961 15.369 -70.605 1.00 95.88 C
ANISOU 1180 CA PRO A 183 13311 13749 9370 -10 85 272 C
ATOM 1181 C PRO A 183 17.375 16.408 -71.559 1.00102.64 C
ANISOU 1181 C PRO A 183 14419 14420 10160 -105 42 286 C
ATOM 1182 O PRO A 183 17.405 16.264 -72.785 1.00102.96 O
ANISOU 1182 O PRO A 183 14636 14362 10122 -125 56 289 O
ATOM 1183 CB PRO A 183 19.478 15.551 -70.456 1.00 98.39 C
ANISOU 1183 CB PRO A 183 13502 14261 9622 -98 237 202 C
ATOM 1184 CG PRO A 183 20.072 14.199 -70.622 1.00102.76 C
ANISOU 1184 CG PRO A 183 13949 14919 10175 17 278 181 C
ATOM 1185 CD PRO A 183 19.129 13.445 -71.484 1.00 97.81 C
ANISOU 1185 CD PRO A 183 13479 14126 9559 105 194 238 C
ATOM 1186 N PHE A 184 16.828 17.454 -70.948 1.00100.30 N
ANISOU 1186 N PHE A 184 14149 14072 9890 -153 -18 293 N
ATOM 1187 CA PHE A 184 16.224 18.662 -71.510 1.00100.91 C
ANISOU 1187 CA PHE A 184 14462 13976 9905 -231 -81 300 C
ATOM 1188 C PHE A 184 17.279 19.478 -72.263 1.00106.35 C
ANISOU 1188 C PHE A 184 15293 14669 10446 -405 53 265 C
ATOM 1189 O PHE A 184 16.952 20.174 -73.225 1.00106.71 O
ANISOU 1189 O PHE A 184 15609 14542 10395 -466 21 270 O
ATOM 1190 CB PHE A 184 15.682 19.516 -70.338 1.00102.50 C
ANISOU 1190 CB PHE A 184 14591 14179 10174 -239 -152 303 C
ATOM 1191 CG PHE A 184 16.395 19.275 -69.015 1.00103.84 C
ANISOU 1191 CG PHE A 184 14492 14552 10410 -241 -79 287 C
ATOM 1192 CD1 PHE A 184 17.652 19.824 -68.769 1.00107.82 C
ANISOU 1192 CD1 PHE A 184 14924 15195 10846 -370 58 244 C
ATOM 1193 CD2 PHE A 184 15.829 18.468 -68.036 1.00104.74 C
ANISOU 1193 CD2 PHE A 184 14431 14720 10647 -116 -146 306 C
ATOM 1194 CE1 PHE A 184 18.324 19.567 -67.571 1.00108.32 C
ANISOU 1194 CE1 PHE A 184 14739 15450 10967 -356 111 219 C
ATOM 1195 CE2 PHE A 184 16.499 18.224 -66.835 1.00107.25 C
ANISOU 1195 CE2 PHE A 184 14526 15212 11012 -106 -88 291 C
ATOM 1196 CZ PHE A 184 17.738 18.779 -66.609 1.00106.11 C
ANISOU 1196 CZ PHE A 184 14308 15207 10803 -216 32 247 C
ATOM 1197 N GLN A 185 18.544 19.391 -71.802 1.00103.78 N
ANISOU 1197 N GLN A 185 14789 14542 10099 -485 202 217 N
ATOM 1198 CA GLN A 185 19.705 20.117 -72.314 1.00105.01 C
ANISOU 1198 CA GLN A 185 15022 14753 10124 -676 364 157 C
ATOM 1199 C GLN A 185 20.856 19.173 -72.714 1.00107.74 C
ANISOU 1199 C GLN A 185 15221 15273 10442 -682 504 99 C
ATOM 1200 O GLN A 185 20.918 18.035 -72.237 1.00106.39 O
ANISOU 1200 O GLN A 185 14845 15216 10361 -533 477 103 O
ATOM 1201 CB GLN A 185 20.186 21.099 -71.234 1.00106.84 C
ANISOU 1201 CB GLN A 185 15151 15085 10359 -792 414 123 C
ATOM 1202 CG GLN A 185 20.644 22.443 -71.783 1.00128.74 C
ANISOU 1202 CG GLN A 185 18157 17776 12982 -1011 511 86 C
ATOM 1203 CD GLN A 185 21.413 23.255 -70.767 1.00151.75 C
ANISOU 1203 CD GLN A 185 20940 20828 15891 -1146 597 34 C
ATOM 1204 OE1 GLN A 185 21.220 23.142 -69.545 1.00145.88 O
ANISOU 1204 OE1 GLN A 185 19977 20190 15261 -1063 538 43 O
ATOM 1205 NE2 GLN A 185 22.303 24.107 -71.259 1.00146.40 N
ANISOU 1205 NE2 GLN A 185 20407 20147 15071 -1368 743 -28 N
ATOM 1206 N ASN A 186 21.773 19.664 -73.576 1.00104.45 N
ANISOU 1206 N ASN A 186 14920 14875 9892 -856 656 37 N
ATOM 1207 CA ASN A 186 22.935 18.919 -74.070 1.00104.48 C
ANISOU 1207 CA ASN A 186 14797 15049 9851 -888 807 -44 C
ATOM 1208 C ASN A 186 23.963 18.623 -72.971 1.00106.37 C
ANISOU 1208 C ASN A 186 14695 15565 10156 -872 882 -127 C
ATOM 1209 O ASN A 186 24.547 19.537 -72.387 1.00106.33 O
ANISOU 1209 O ASN A 186 14615 15653 10134 -1006 950 -181 O
ATOM 1210 CB ASN A 186 23.591 19.636 -75.266 1.00106.83 C
ANISOU 1210 CB ASN A 186 15322 15288 9982 -1107 962 -103 C
ATOM 1211 CG ASN A 186 22.974 19.350 -76.617 1.00125.91 C
ANISOU 1211 CG ASN A 186 18031 17491 12319 -1083 923 -51 C
ATOM 1212 OD1 ASN A 186 21.783 19.050 -76.742 1.00117.64 O
ANISOU 1212 OD1 ASN A 186 17102 16270 11325 -936 751 40 O
ATOM 1213 ND2 ASN A 186 23.772 19.469 -77.674 1.00118.91 N
ANISOU 1213 ND2 ASN A 186 17271 16612 11299 -1237 1085 -118 N
ATOM 1214 N VAL A 187 24.165 17.327 -72.706 1.00101.06 N
ANISOU 1214 N VAL A 187 13829 15017 9553 -698 862 -140 N
ATOM 1215 CA VAL A 187 25.099 16.763 -71.725 1.00100.14 C
ANISOU 1215 CA VAL A 187 13393 15159 9496 -621 903 -223 C
ATOM 1216 C VAL A 187 26.315 16.201 -72.516 1.00103.75 C
ANISOU 1216 C VAL A 187 13763 15779 9880 -659 1054 -342 C
ATOM 1217 O VAL A 187 26.178 15.928 -73.712 1.00103.39 O
ANISOU 1217 O VAL A 187 13898 15620 9767 -680 1086 -323 O
ATOM 1218 CB VAL A 187 24.342 15.693 -70.875 1.00102.32 C
ANISOU 1218 CB VAL A 187 13561 15421 9895 -377 746 -144 C
ATOM 1219 CG1 VAL A 187 25.272 14.876 -69.991 1.00102.41 C
ANISOU 1219 CG1 VAL A 187 13284 15676 9952 -252 767 -226 C
ATOM 1220 CG2 VAL A 187 23.247 16.337 -70.029 1.00100.84 C
ANISOU 1220 CG2 VAL A 187 13433 15101 9779 -364 619 -53 C
ATOM 1221 N THR A 188 27.503 16.090 -71.875 1.00100.58 N
ANISOU 1221 N THR A 188 13088 15641 9485 -672 1147 -475 N
ATOM 1222 CA THR A 188 28.734 15.568 -72.500 1.00101.75 C
ANISOU 1222 CA THR A 188 13105 15983 9571 -699 1292 -621 C
ATOM 1223 C THR A 188 28.558 14.120 -72.971 1.00104.78 C
ANISOU 1223 C THR A 188 13486 16347 9979 -478 1225 -587 C
ATOM 1224 O THR A 188 27.956 13.318 -72.265 1.00103.19 O
ANISOU 1224 O THR A 188 13228 16114 9864 -267 1080 -508 O
ATOM 1225 CB THR A 188 29.959 15.759 -71.597 1.00112.23 C
ANISOU 1225 CB THR A 188 14117 17608 10916 -731 1376 -785 C
ATOM 1226 OG1 THR A 188 29.690 15.227 -70.300 1.00115.12 O
ANISOU 1226 OG1 THR A 188 14306 18044 11390 -517 1232 -748 O
ATOM 1227 CG2 THR A 188 30.366 17.214 -71.473 1.00111.27 C
ANISOU 1227 CG2 THR A 188 14022 17516 10740 -1003 1492 -848 C
ATOM 1228 N LEU A 189 29.045 13.805 -74.181 1.00102.48 N
ANISOU 1228 N LEU A 189 13278 16057 9602 -537 1335 -645 N
ATOM 1229 CA LEU A 189 28.893 12.492 -74.807 1.00101.76 C
ANISOU 1229 CA LEU A 189 13221 15929 9516 -349 1284 -614 C
ATOM 1230 C LEU A 189 29.690 11.365 -74.138 1.00105.37 C
ANISOU 1230 C LEU A 189 13396 16618 10020 -134 1260 -711 C
ATOM 1231 O LEU A 189 30.866 11.538 -73.818 1.00106.27 O
ANISOU 1231 O LEU A 189 13277 16982 10120 -179 1361 -875 O
ATOM 1232 CB LEU A 189 29.215 12.565 -76.310 1.00102.95 C
ANISOU 1232 CB LEU A 189 13553 16013 9552 -488 1418 -654 C
ATOM 1233 N ASP A 190 29.018 10.213 -73.924 1.00100.57 N
ANISOU 1233 N ASP A 190 12824 15923 9466 103 1118 -616 N
ATOM 1234 CA ASP A 190 29.557 8.958 -73.382 1.00100.67 C
ANISOU 1234 CA ASP A 190 12648 16093 9508 351 1061 -679 C
ATOM 1235 C ASP A 190 28.786 7.792 -74.009 1.00102.98 C
ANISOU 1235 C ASP A 190 13118 16211 9800 515 971 -570 C
ATOM 1236 O ASP A 190 27.731 7.395 -73.515 1.00100.84 O
ANISOU 1236 O ASP A 190 12948 15779 9588 624 834 -436 O
ATOM 1237 CB ASP A 190 29.522 8.910 -71.840 1.00101.98 C
ANISOU 1237 CB ASP A 190 12642 16352 9753 481 953 -676 C
ATOM 1238 CG ASP A 190 30.208 7.701 -71.212 1.00113.20 C
ANISOU 1238 CG ASP A 190 13875 17952 11184 739 895 -767 C
ATOM 1239 OD1 ASP A 190 31.012 7.035 -71.912 1.00114.41 O
ANISOU 1239 OD1 ASP A 190 13989 18198 11283 815 951 -861 O
ATOM 1240 OD2 ASP A 190 29.975 7.445 -70.012 1.00119.63 O
ANISOU 1240 OD2 ASP A 190 14590 18813 12051 868 793 -753 O
ATOM 1241 N ALA A 191 29.315 7.280 -75.129 1.00100.27 N
ANISOU 1241 N ALA A 191 12814 15900 9385 515 1059 -636 N
ATOM 1242 CA ALA A 191 28.741 6.213 -75.947 1.00 99.41 C
ANISOU 1242 CA ALA A 191 12878 15637 9255 644 1002 -554 C
ATOM 1243 C ALA A 191 28.602 4.851 -75.275 1.00102.91 C
ANISOU 1243 C ALA A 191 13264 16099 9737 925 872 -526 C
ATOM 1244 O ALA A 191 27.794 4.047 -75.740 1.00101.65 O
ANISOU 1244 O ALA A 191 13283 15759 9579 1022 793 -418 O
ATOM 1245 CB ALA A 191 29.550 6.065 -77.221 1.00101.70 C
ANISOU 1245 CB ALA A 191 13190 15999 9453 569 1147 -661 C
ATOM 1246 N TYR A 192 29.389 4.575 -74.211 1.00100.26 N
ANISOU 1246 N TYR A 192 12696 15974 9423 1056 849 -630 N
ATOM 1247 CA TYR A 192 29.422 3.269 -73.543 1.00 99.81 C
ANISOU 1247 CA TYR A 192 12598 15948 9379 1335 731 -626 C
ATOM 1248 C TYR A 192 28.429 3.097 -72.384 1.00101.63 C
ANISOU 1248 C TYR A 192 12888 16048 9677 1424 588 -498 C
ATOM 1249 O TYR A 192 28.125 1.956 -72.025 1.00101.01 O
ANISOU 1249 O TYR A 192 12876 15908 9595 1631 487 -452 O
ATOM 1250 CB TYR A 192 30.849 2.929 -73.087 1.00103.01 C
ANISOU 1250 CB TYR A 192 12739 16648 9754 1465 767 -824 C
ATOM 1251 CG TYR A 192 31.911 3.229 -74.126 1.00107.12 C
ANISOU 1251 CG TYR A 192 13154 17334 10211 1345 931 -986 C
ATOM 1252 CD1 TYR A 192 31.875 2.632 -75.385 1.00109.39 C
ANISOU 1252 CD1 TYR A 192 13582 17540 10440 1347 985 -975 C
ATOM 1253 CD2 TYR A 192 32.953 4.108 -73.852 1.00109.61 C
ANISOU 1253 CD2 TYR A 192 13231 17894 10523 1220 1040 -1159 C
ATOM 1254 CE1 TYR A 192 32.832 2.928 -76.353 1.00111.82 C
ANISOU 1254 CE1 TYR A 192 13805 17997 10685 1219 1150 -1129 C
ATOM 1255 CE2 TYR A 192 33.934 4.388 -74.803 1.00112.57 C
ANISOU 1255 CE2 TYR A 192 13506 18429 10835 1088 1210 -1324 C
ATOM 1256 CZ TYR A 192 33.869 3.795 -76.054 1.00120.24 C
ANISOU 1256 CZ TYR A 192 14629 19311 11747 1087 1267 -1308 C
ATOM 1257 OH TYR A 192 34.832 4.068 -76.996 1.00123.18 O
ANISOU 1257 OH TYR A 192 14910 19840 12052 944 1447 -1479 O
ATOM 1258 N LYS A 193 27.910 4.205 -71.821 1.00 96.64 N
ANISOU 1258 N LYS A 193 12249 15369 9101 1266 584 -442 N
ATOM 1259 CA LYS A 193 26.937 4.175 -70.727 1.00 94.55 C
ANISOU 1259 CA LYS A 193 12037 14985 8904 1322 465 -329 C
ATOM 1260 C LYS A 193 25.794 5.157 -70.986 1.00 97.21 C
ANISOU 1260 C LYS A 193 12521 15128 9288 1128 457 -211 C
ATOM 1261 O LYS A 193 26.007 6.180 -71.636 1.00 96.84 O
ANISOU 1261 O LYS A 193 12483 15091 9219 936 548 -239 O
ATOM 1262 CB LYS A 193 27.623 4.493 -69.389 1.00 97.10 C
ANISOU 1262 CB LYS A 193 12148 15494 9252 1380 442 -413 C
ATOM 1263 N ASP A 194 24.583 4.850 -70.482 1.00 92.92 N
ANISOU 1263 N ASP A 194 12099 14408 8800 1178 350 -89 N
ATOM 1264 CA ASP A 194 23.433 5.746 -70.622 1.00 91.55 C
ANISOU 1264 CA ASP A 194 12050 14058 8677 1024 320 9 C
ATOM 1265 C ASP A 194 23.408 6.733 -69.453 1.00 93.36 C
ANISOU 1265 C ASP A 194 12160 14355 8959 948 309 0 C
ATOM 1266 O ASP A 194 23.305 6.321 -68.297 1.00 92.47 O
ANISOU 1266 O ASP A 194 11969 14284 8880 1060 247 6 O
ATOM 1267 CB ASP A 194 22.105 4.975 -70.766 1.00 92.76 C
ANISOU 1267 CB ASP A 194 12380 13998 8868 1096 220 121 C
ATOM 1268 CG ASP A 194 21.570 4.957 -72.195 1.00106.60 C
ANISOU 1268 CG ASP A 194 14316 15597 10592 1033 229 164 C
ATOM 1269 OD1 ASP A 194 21.232 6.048 -72.726 1.00105.76 O
ANISOU 1269 OD1 ASP A 194 14274 15431 10480 873 261 171 O
ATOM 1270 OD2 ASP A 194 21.480 3.856 -72.779 1.00115.92 O
ANISOU 1270 OD2 ASP A 194 15592 16703 11749 1146 198 190 O
ATOM 1271 N LYS A 195 23.578 8.030 -69.759 1.00 88.99 N
ANISOU 1271 N LYS A 195 11604 13809 8400 757 373 -19 N
ATOM 1272 CA LYS A 195 23.612 9.109 -68.772 1.00 87.81 C
ANISOU 1272 CA LYS A 195 11353 13720 8290 660 374 -32 C
ATOM 1273 C LYS A 195 22.201 9.490 -68.349 1.00 91.21 C
ANISOU 1273 C LYS A 195 11900 13964 8793 629 276 78 C
ATOM 1274 O LYS A 195 21.373 9.820 -69.201 1.00 91.04 O
ANISOU 1274 O LYS A 195 12046 13776 8770 549 255 134 O
ATOM 1275 CB LYS A 195 24.352 10.337 -69.330 1.00 89.85 C
ANISOU 1275 CB LYS A 195 11586 14057 8496 457 492 -106 C
ATOM 1276 CG LYS A 195 25.848 10.140 -69.499 1.00 86.29 C
ANISOU 1276 CG LYS A 195 10961 13841 7986 463 603 -250 C
ATOM 1277 CD LYS A 195 26.504 11.413 -69.956 1.00 82.54 C
ANISOU 1277 CD LYS A 195 10461 13441 7460 233 730 -329 C
ATOM 1278 CE LYS A 195 27.955 11.446 -69.578 1.00 82.81 C
ANISOU 1278 CE LYS A 195 10246 13754 7463 231 828 -498 C
ATOM 1279 NZ LYS A 195 28.466 12.835 -69.522 1.00 83.09 N
ANISOU 1279 NZ LYS A 195 10231 13872 7469 -4 939 -573 N
ATOM 1280 N TYR A 196 21.933 9.437 -67.035 1.00 87.37 N
ANISOU 1280 N TYR A 196 11325 13507 8365 701 213 97 N
ATOM 1281 CA TYR A 196 20.645 9.773 -66.425 1.00 86.04 C
ANISOU 1281 CA TYR A 196 11229 13191 8272 679 126 180 C
ATOM 1282 C TYR A 196 20.747 11.105 -65.693 1.00 90.30 C
ANISOU 1282 C TYR A 196 11689 13782 8838 555 140 163 C
ATOM 1283 O TYR A 196 21.789 11.394 -65.111 1.00 90.52 O
ANISOU 1283 O TYR A 196 11563 13985 8845 546 193 91 O
ATOM 1284 CB TYR A 196 20.226 8.686 -65.413 1.00 86.58 C
ANISOU 1284 CB TYR A 196 11276 13244 8378 838 55 212 C
ATOM 1285 CG TYR A 196 19.849 7.358 -66.031 1.00 88.16 C
ANISOU 1285 CG TYR A 196 11591 13351 8555 956 26 244 C
ATOM 1286 CD1 TYR A 196 20.791 6.346 -66.182 1.00 91.21 C
ANISOU 1286 CD1 TYR A 196 11936 13842 8879 1090 52 195 C
ATOM 1287 CD2 TYR A 196 18.540 7.098 -66.431 1.00 87.89 C
ANISOU 1287 CD2 TYR A 196 11704 13129 8562 938 -32 312 C
ATOM 1288 CE1 TYR A 196 20.450 5.116 -66.745 1.00 92.48 C
ANISOU 1288 CE1 TYR A 196 12219 13909 9009 1200 25 226 C
ATOM 1289 CE2 TYR A 196 18.183 5.867 -66.983 1.00 88.92 C
ANISOU 1289 CE2 TYR A 196 11945 13173 8668 1036 -54 338 C
ATOM 1290 CZ TYR A 196 19.145 4.881 -67.147 1.00 98.62 C
ANISOU 1290 CZ TYR A 196 13150 14495 9827 1165 -24 301 C
ATOM 1291 OH TYR A 196 18.815 3.662 -67.698 1.00100.74 O
ANISOU 1291 OH TYR A 196 13543 14670 10062 1262 -46 327 O
ATOM 1292 N VAL A 197 19.658 11.895 -65.692 1.00 86.64 N
ANISOU 1292 N VAL A 197 11327 13172 8420 468 87 219 N
ATOM 1293 CA VAL A 197 19.568 13.178 -64.980 1.00 86.26 C
ANISOU 1293 CA VAL A 197 11231 13145 8399 356 86 212 C
ATOM 1294 C VAL A 197 18.469 13.123 -63.918 1.00 90.68 C
ANISOU 1294 C VAL A 197 11785 13624 9046 405 -5 264 C
ATOM 1295 O VAL A 197 17.392 12.574 -64.181 1.00 89.67 O
ANISOU 1295 O VAL A 197 11758 13356 8958 455 -72 311 O
ATOM 1296 CB VAL A 197 19.455 14.437 -65.889 1.00 89.84 C
ANISOU 1296 CB VAL A 197 11810 13517 8807 189 118 208 C
ATOM 1297 CG1 VAL A 197 20.744 14.675 -66.670 1.00 90.70 C
ANISOU 1297 CG1 VAL A 197 11895 13744 8822 103 241 135 C
ATOM 1298 CG2 VAL A 197 18.244 14.377 -66.820 1.00 89.04 C
ANISOU 1298 CG2 VAL A 197 11907 13207 8717 192 41 266 C
ATOM 1299 N CYS A 198 18.750 13.674 -62.716 1.00 87.97 N
ANISOU 1299 N CYS A 198 11319 13374 8730 386 -3 245 N
ATOM 1300 CA CYS A 198 17.811 13.709 -61.587 1.00 86.92 C
ANISOU 1300 CA CYS A 198 11168 13184 8675 419 -74 283 C
ATOM 1301 C CYS A 198 17.185 15.101 -61.492 1.00 89.37 C
ANISOU 1301 C CYS A 198 11521 13422 9014 293 -100 293 C
ATOM 1302 O CYS A 198 17.873 16.054 -61.116 1.00 90.19 O
ANISOU 1302 O CYS A 198 11558 13616 9093 206 -57 260 O
ATOM 1303 CB CYS A 198 18.512 13.310 -60.289 1.00 87.74 C
ANISOU 1303 CB CYS A 198 11127 13429 8782 500 -63 256 C
ATOM 1304 SG CYS A 198 17.414 13.179 -58.851 1.00 91.08 S
ANISOU 1304 SG CYS A 198 11542 13778 9285 542 -133 299 S
ATOM 1305 N PHE A 199 15.895 15.227 -61.860 1.00 83.61 N
ANISOU 1305 N PHE A 199 10905 12530 8333 287 -175 327 N
ATOM 1306 CA PHE A 199 15.177 16.506 -61.832 1.00 82.89 C
ANISOU 1306 CA PHE A 199 10876 12353 8267 195 -222 329 C
ATOM 1307 C PHE A 199 13.723 16.366 -61.359 1.00 85.35 C
ANISOU 1307 C PHE A 199 11210 12551 8670 238 -315 344 C
ATOM 1308 O PHE A 199 13.173 15.265 -61.389 1.00 84.73 O
ANISOU 1308 O PHE A 199 11136 12433 8626 319 -337 356 O
ATOM 1309 CB PHE A 199 15.234 17.187 -63.217 1.00 85.47 C
ANISOU 1309 CB PHE A 199 11360 12592 8524 114 -217 324 C
ATOM 1310 CG PHE A 199 14.476 16.457 -64.305 1.00 87.29 C
ANISOU 1310 CG PHE A 199 11719 12693 8756 172 -269 341 C
ATOM 1311 CD1 PHE A 199 13.124 16.710 -64.527 1.00 89.96 C
ANISOU 1311 CD1 PHE A 199 12150 12884 9148 193 -377 346 C
ATOM 1312 CD2 PHE A 199 15.111 15.513 -65.105 1.00 89.86 C
ANISOU 1312 CD2 PHE A 199 12065 13049 9027 210 -214 342 C
ATOM 1313 CE1 PHE A 199 12.418 16.010 -65.504 1.00 90.71 C
ANISOU 1313 CE1 PHE A 199 12353 12867 9246 249 -431 351 C
ATOM 1314 CE2 PHE A 199 14.407 14.827 -66.090 1.00 92.38 C
ANISOU 1314 CE2 PHE A 199 12507 13247 9346 263 -264 358 C
ATOM 1315 CZ PHE A 199 13.066 15.078 -66.283 1.00 90.11 C
ANISOU 1315 CZ PHE A 199 12308 12816 9115 280 -373 362 C
ATOM 1316 N ASP A 200 13.098 17.494 -60.952 1.00 81.24 N
ANISOU 1316 N ASP A 200 10708 11978 8182 180 -366 334 N
ATOM 1317 CA ASP A 200 11.694 17.558 -60.525 1.00 79.95 C
ANISOU 1317 CA ASP A 200 10553 11718 8107 209 -455 323 C
ATOM 1318 C ASP A 200 10.765 17.656 -61.747 1.00 81.14 C
ANISOU 1318 C ASP A 200 10847 11723 8258 223 -537 309 C
ATOM 1319 O ASP A 200 10.976 18.503 -62.616 1.00 81.12 O
ANISOU 1319 O ASP A 200 10967 11666 8189 173 -551 306 O
ATOM 1320 CB ASP A 200 11.454 18.722 -59.536 1.00 81.95 C
ANISOU 1320 CB ASP A 200 10756 11989 8393 156 -479 308 C
ATOM 1321 CG ASP A 200 11.756 20.110 -60.075 1.00 96.79 C
ANISOU 1321 CG ASP A 200 12739 13827 10211 71 -494 299 C
ATOM 1322 OD1 ASP A 200 12.949 20.412 -60.310 1.00 98.41 O
ANISOU 1322 OD1 ASP A 200 12948 14109 10336 5 -414 306 O
ATOM 1323 OD2 ASP A 200 10.802 20.904 -60.236 1.00105.00 O
ANISOU 1323 OD2 ASP A 200 13859 14759 11277 69 -586 275 O
ATOM 1324 N GLN A 201 9.759 16.771 -61.820 1.00 75.27 N
ANISOU 1324 N GLN A 201 10102 10916 7582 286 -589 292 N
ATOM 1325 CA GLN A 201 8.804 16.718 -62.924 1.00 74.37 C
ANISOU 1325 CA GLN A 201 10106 10672 7478 315 -680 262 C
ATOM 1326 C GLN A 201 7.359 16.686 -62.406 1.00 76.65 C
ANISOU 1326 C GLN A 201 10344 10905 7873 346 -767 201 C
ATOM 1327 O GLN A 201 6.645 15.688 -62.574 1.00 76.13 O
ANISOU 1327 O GLN A 201 10266 10805 7855 386 -785 175 O
ATOM 1328 CB GLN A 201 9.120 15.528 -63.845 1.00 75.79 C
ANISOU 1328 CB GLN A 201 10344 10835 7617 357 -646 286 C
ATOM 1329 CG GLN A 201 8.597 15.684 -65.267 1.00 93.42 C
ANISOU 1329 CG GLN A 201 12737 12941 9817 374 -726 267 C
ATOM 1330 CD GLN A 201 8.933 14.489 -66.120 1.00115.38 C
ANISOU 1330 CD GLN A 201 15574 15708 12558 415 -689 292 C
ATOM 1331 OE1 GLN A 201 8.607 13.341 -65.799 1.00110.92 O
ANISOU 1331 OE1 GLN A 201 14947 15161 12035 459 -668 293 O
ATOM 1332 NE2 GLN A 201 9.576 14.738 -67.245 1.00110.35 N
ANISOU 1332 NE2 GLN A 201 15073 15026 11830 395 -679 308 N
ATOM 1333 N PHE A 202 6.934 17.803 -61.778 1.00 72.32 N
ANISOU 1333 N PHE A 202 9767 10353 7359 321 -817 167 N
ATOM 1334 CA PHE A 202 5.586 18.001 -61.221 1.00 71.81 C
ANISOU 1334 CA PHE A 202 9636 10252 7395 344 -899 87 C
ATOM 1335 C PHE A 202 4.490 18.050 -62.321 1.00 77.20 C
ANISOU 1335 C PHE A 202 10412 10821 8101 400 -1026 14 C
ATOM 1336 O PHE A 202 4.855 18.209 -63.491 1.00 78.33 O
ANISOU 1336 O PHE A 202 10700 10898 8165 414 -1056 39 O
ATOM 1337 CB PHE A 202 5.573 19.268 -60.349 1.00 73.13 C
ANISOU 1337 CB PHE A 202 9762 10447 7576 310 -920 72 C
ATOM 1338 CG PHE A 202 6.009 19.014 -58.924 1.00 73.97 C
ANISOU 1338 CG PHE A 202 9729 10662 7713 274 -824 100 C
ATOM 1339 CD1 PHE A 202 7.359 18.945 -58.592 1.00 76.33 C
ANISOU 1339 CD1 PHE A 202 10009 11049 7943 239 -726 174 C
ATOM 1340 CD2 PHE A 202 5.071 18.822 -57.917 1.00 75.59 C
ANISOU 1340 CD2 PHE A 202 9822 10885 8012 276 -832 43 C
ATOM 1341 CE1 PHE A 202 7.760 18.698 -57.279 1.00 76.38 C
ANISOU 1341 CE1 PHE A 202 9900 11151 7971 222 -652 194 C
ATOM 1342 CE2 PHE A 202 5.476 18.567 -56.606 1.00 77.68 C
ANISOU 1342 CE2 PHE A 202 9986 11236 8293 245 -744 71 C
ATOM 1343 CZ PHE A 202 6.817 18.513 -56.295 1.00 75.28 C
ANISOU 1343 CZ PHE A 202 9676 11011 7916 226 -663 150 C
ATOM 1344 N PRO A 203 3.163 17.920 -62.017 1.00 73.21 N
ANISOU 1344 N PRO A 203 9830 10292 7696 432 -1103 -88 N
ATOM 1345 CA PRO A 203 2.155 17.976 -63.093 1.00 73.40 C
ANISOU 1345 CA PRO A 203 9933 10217 7739 499 -1238 -175 C
ATOM 1346 C PRO A 203 2.295 19.187 -64.025 1.00 77.42 C
ANISOU 1346 C PRO A 203 10620 10632 8164 535 -1345 -174 C
ATOM 1347 O PRO A 203 2.151 19.048 -65.244 1.00 77.83 O
ANISOU 1347 O PRO A 203 10810 10594 8167 582 -1417 -185 O
ATOM 1348 CB PRO A 203 0.828 17.991 -62.327 1.00 75.27 C
ANISOU 1348 CB PRO A 203 10025 10477 8099 514 -1296 -304 C
ATOM 1349 CG PRO A 203 1.118 17.287 -61.077 1.00 79.25 C
ANISOU 1349 CG PRO A 203 10393 11075 8642 446 -1157 -268 C
ATOM 1350 CD PRO A 203 2.509 17.716 -60.708 1.00 74.62 C
ANISOU 1350 CD PRO A 203 9846 10535 7971 407 -1070 -143 C
ATOM 1351 N SER A 204 2.609 20.357 -63.444 1.00 72.96 N
ANISOU 1351 N SER A 204 10071 10079 7570 507 -1351 -158 N
ATOM 1352 CA SER A 204 2.827 21.616 -64.141 1.00 73.42 C
ANISOU 1352 CA SER A 204 10325 10041 7529 523 -1436 -151 C
ATOM 1353 C SER A 204 3.580 22.572 -63.222 1.00 78.53 C
ANISOU 1353 C SER A 204 10955 10742 8140 449 -1370 -101 C
ATOM 1354 O SER A 204 3.798 22.249 -62.053 1.00 77.59 O
ANISOU 1354 O SER A 204 10662 10733 8085 405 -1279 -82 O
ATOM 1355 CB SER A 204 1.497 22.231 -64.556 1.00 77.70 C
ANISOU 1355 CB SER A 204 10927 10487 8108 629 -1627 -278 C
ATOM 1356 OG SER A 204 0.902 22.934 -63.479 1.00 87.12 O
ANISOU 1356 OG SER A 204 11998 11725 9378 642 -1669 -350 O
ATOM 1357 N ASP A 205 3.949 23.758 -63.741 1.00 77.29 N
ANISOU 1357 N ASP A 205 10995 10498 7873 435 -1419 -83 N
ATOM 1358 CA ASP A 205 4.655 24.790 -62.987 1.00 77.83 C
ANISOU 1358 CA ASP A 205 11082 10600 7891 356 -1364 -43 C
ATOM 1359 C ASP A 205 3.764 25.391 -61.908 1.00 82.02 C
ANISOU 1359 C ASP A 205 11492 11156 8514 397 -1438 -117 C
ATOM 1360 O ASP A 205 4.277 25.722 -60.844 1.00 81.39 O
ANISOU 1360 O ASP A 205 11308 11165 8450 329 -1353 -83 O
ATOM 1361 CB ASP A 205 5.214 25.877 -63.911 1.00 81.45 C
ANISOU 1361 CB ASP A 205 11819 10935 8194 321 -1398 -17 C
ATOM 1362 CG ASP A 205 6.257 25.373 -64.896 1.00 99.32 C
ANISOU 1362 CG ASP A 205 14194 13191 10353 249 -1290 57 C
ATOM 1363 OD1 ASP A 205 5.915 25.211 -66.097 1.00100.84 O
ANISOU 1363 OD1 ASP A 205 14563 13266 10485 301 -1365 41 O
ATOM 1364 OD2 ASP A 205 7.418 25.151 -64.472 1.00107.42 O
ANISOU 1364 OD2 ASP A 205 15127 14333 11354 146 -1134 120 O
ATOM 1365 N SER A 206 2.433 25.494 -62.162 1.00 79.08 N
ANISOU 1365 N SER A 206 11122 10717 8208 510 -1594 -230 N
ATOM 1366 CA SER A 206 1.459 26.002 -61.186 1.00 78.84 C
ANISOU 1366 CA SER A 206 10960 10718 8277 560 -1671 -328 C
ATOM 1367 C SER A 206 1.281 24.992 -60.057 1.00 81.22 C
ANISOU 1367 C SER A 206 10998 11157 8704 519 -1561 -335 C
ATOM 1368 O SER A 206 1.178 25.398 -58.906 1.00 80.71 O
ANISOU 1368 O SER A 206 10814 11160 8691 489 -1528 -351 O
ATOM 1369 CB SER A 206 0.115 26.301 -61.843 1.00 84.14 C
ANISOU 1369 CB SER A 206 11691 11295 8983 702 -1871 -469 C
ATOM 1370 OG SER A 206 -0.616 25.119 -62.130 1.00 95.14 O
ANISOU 1370 OG SER A 206 12954 12722 10474 745 -1886 -539 O
ATOM 1371 N HIS A 207 1.267 23.679 -60.388 1.00 76.65 N
ANISOU 1371 N HIS A 207 10350 10611 8163 513 -1500 -322 N
ATOM 1372 CA HIS A 207 1.167 22.596 -59.411 1.00 75.36 C
ANISOU 1372 CA HIS A 207 9984 10556 8094 466 -1385 -321 C
ATOM 1373 C HIS A 207 2.389 22.620 -58.501 1.00 78.67 C
ANISOU 1373 C HIS A 207 10355 11063 8472 375 -1238 -207 C
ATOM 1374 O HIS A 207 2.231 22.596 -57.278 1.00 78.38 O
ANISOU 1374 O HIS A 207 10181 11102 8499 342 -1183 -223 O
ATOM 1375 CB HIS A 207 1.012 21.233 -60.102 1.00 75.94 C
ANISOU 1375 CB HIS A 207 10045 10623 8186 478 -1354 -321 C
ATOM 1376 CG HIS A 207 -0.368 21.001 -60.641 1.00 79.91 C
ANISOU 1376 CG HIS A 207 10513 11081 8769 555 -1479 -466 C
ATOM 1377 ND1 HIS A 207 -0.687 21.289 -61.953 1.00 82.17 N
ANISOU 1377 ND1 HIS A 207 10949 11263 9010 638 -1614 -508 N
ATOM 1378 CD2 HIS A 207 -1.474 20.537 -60.014 1.00 81.68 C
ANISOU 1378 CD2 HIS A 207 10569 11356 9111 555 -1484 -587 C
ATOM 1379 CE1 HIS A 207 -1.968 20.988 -62.085 1.00 82.19 C
ANISOU 1379 CE1 HIS A 207 10854 11265 9110 697 -1708 -658 C
ATOM 1380 NE2 HIS A 207 -2.483 20.528 -60.946 1.00 82.27 N
ANISOU 1380 NE2 HIS A 207 10665 11371 9221 642 -1627 -715 N
ATOM 1381 N ARG A 208 3.597 22.757 -59.092 1.00 74.50 N
ANISOU 1381 N ARG A 208 9945 10527 7835 335 -1180 -105 N
ATOM 1382 CA ARG A 208 4.847 22.837 -58.338 1.00 73.46 C
ANISOU 1382 CA ARG A 208 9767 10488 7657 255 -1052 -14 C
ATOM 1383 C ARG A 208 4.894 24.104 -57.501 1.00 77.50 C
ANISOU 1383 C ARG A 208 10270 11015 8163 223 -1072 -25 C
ATOM 1384 O ARG A 208 5.187 24.015 -56.313 1.00 76.52 O
ANISOU 1384 O ARG A 208 10016 10981 8076 185 -997 -6 O
ATOM 1385 CB ARG A 208 6.072 22.773 -59.267 1.00 73.09 C
ANISOU 1385 CB ARG A 208 9841 10436 7494 214 -988 67 C
ATOM 1386 CG ARG A 208 7.394 22.547 -58.522 1.00 77.88 C
ANISOU 1386 CG ARG A 208 10360 11167 8063 145 -850 140 C
ATOM 1387 CD ARG A 208 8.460 23.564 -58.878 1.00 82.85 C
ANISOU 1387 CD ARG A 208 11095 11803 8583 65 -810 178 C
ATOM 1388 NE ARG A 208 9.089 23.296 -60.173 1.00 88.95 N
ANISOU 1388 NE ARG A 208 11996 12536 9264 48 -781 206 N
ATOM 1389 CZ ARG A 208 8.819 23.957 -61.295 1.00101.41 C
ANISOU 1389 CZ ARG A 208 13774 13988 10769 44 -850 192 C
ATOM 1390 NH1 ARG A 208 7.921 24.933 -61.300 1.00 86.37 N
ANISOU 1390 NH1 ARG A 208 11966 11983 8867 69 -966 147 N
ATOM 1391 NH2 ARG A 208 9.448 23.650 -62.419 1.00 92.72 N
ANISOU 1391 NH2 ARG A 208 12790 12856 9582 19 -808 218 N
ATOM 1392 N LEU A 209 4.614 25.278 -58.117 1.00 75.12 N
ANISOU 1392 N LEU A 209 10123 10615 7805 242 -1176 -55 N
ATOM 1393 CA LEU A 209 4.669 26.581 -57.445 1.00 74.99 C
ANISOU 1393 CA LEU A 209 10136 10592 7765 213 -1205 -65 C
ATOM 1394 C LEU A 209 3.670 26.724 -56.329 1.00 78.91 C
ANISOU 1394 C LEU A 209 10484 11124 8374 253 -1250 -145 C
ATOM 1395 O LEU A 209 4.037 27.268 -55.287 1.00 78.09 O
ANISOU 1395 O LEU A 209 10319 11078 8274 203 -1204 -125 O
ATOM 1396 CB LEU A 209 4.572 27.761 -58.417 1.00 75.69 C
ANISOU 1396 CB LEU A 209 10466 10545 7749 232 -1312 -82 C
ATOM 1397 CG LEU A 209 5.904 28.177 -59.017 1.00 80.65 C
ANISOU 1397 CG LEU A 209 11246 11161 8238 128 -1222 4 C
ATOM 1398 CD1 LEU A 209 5.716 28.977 -60.293 1.00 81.87 C
ANISOU 1398 CD1 LEU A 209 11682 11151 8275 154 -1323 -13 C
ATOM 1399 CD2 LEU A 209 6.746 28.937 -58.002 1.00 83.55 C
ANISOU 1399 CD2 LEU A 209 11569 11604 8572 27 -1136 43 C
ATOM 1400 N SER A 210 2.430 26.213 -56.525 1.00 75.24 N
ANISOU 1400 N SER A 210 9954 10633 8001 335 -1333 -243 N
ATOM 1401 CA SER A 210 1.368 26.238 -55.515 1.00 74.66 C
ANISOU 1401 CA SER A 210 9722 10603 8044 365 -1366 -345 C
ATOM 1402 C SER A 210 1.755 25.393 -54.302 1.00 77.49 C
ANISOU 1402 C SER A 210 9909 11078 8457 291 -1217 -301 C
ATOM 1403 O SER A 210 1.588 25.847 -53.174 1.00 76.71 O
ANISOU 1403 O SER A 210 9719 11028 8399 266 -1193 -324 O
ATOM 1404 CB SER A 210 0.056 25.740 -56.103 1.00 78.07 C
ANISOU 1404 CB SER A 210 10114 10994 8556 456 -1475 -476 C
ATOM 1405 OG SER A 210 -0.406 26.650 -57.086 1.00 88.93 O
ANISOU 1405 OG SER A 210 11656 12257 9878 548 -1638 -534 O
ATOM 1406 N TYR A 211 2.304 24.184 -54.543 1.00 73.54 N
ANISOU 1406 N TYR A 211 9386 10612 7945 262 -1121 -236 N
ATOM 1407 CA TYR A 211 2.755 23.257 -53.510 1.00 72.85 C
ANISOU 1407 CA TYR A 211 9179 10615 7884 206 -986 -188 C
ATOM 1408 C TYR A 211 3.885 23.890 -52.709 1.00 78.11 C
ANISOU 1408 C TYR A 211 9842 11344 8491 150 -916 -103 C
ATOM 1409 O TYR A 211 3.789 23.970 -51.489 1.00 78.77 O
ANISOU 1409 O TYR A 211 9829 11486 8615 120 -866 -111 O
ATOM 1410 CB TYR A 211 3.181 21.916 -54.152 1.00 73.77 C
ANISOU 1410 CB TYR A 211 9317 10736 7975 208 -922 -136 C
ATOM 1411 CG TYR A 211 3.880 20.930 -53.238 1.00 74.94 C
ANISOU 1411 CG TYR A 211 9397 10963 8114 169 -791 -70 C
ATOM 1412 CD1 TYR A 211 3.280 20.492 -52.059 1.00 77.17 C
ANISOU 1412 CD1 TYR A 211 9578 11281 8463 141 -737 -115 C
ATOM 1413 CD2 TYR A 211 5.104 20.372 -53.590 1.00 75.30 C
ANISOU 1413 CD2 TYR A 211 9488 11043 8078 165 -723 25 C
ATOM 1414 CE1 TYR A 211 3.918 19.583 -51.214 1.00 77.92 C
ANISOU 1414 CE1 TYR A 211 9647 11429 8531 117 -627 -55 C
ATOM 1415 CE2 TYR A 211 5.744 19.449 -52.762 1.00 75.99 C
ANISOU 1415 CE2 TYR A 211 9528 11197 8146 155 -622 75 C
ATOM 1416 CZ TYR A 211 5.147 19.059 -51.574 1.00 83.03 C
ANISOU 1416 CZ TYR A 211 10347 12108 9094 134 -579 39 C
ATOM 1417 OH TYR A 211 5.770 18.153 -50.754 1.00 82.84 O
ANISOU 1417 OH TYR A 211 10311 12132 9034 134 -490 87 O
ATOM 1418 N THR A 212 4.907 24.398 -53.408 1.00 74.81 N
ANISOU 1418 N THR A 212 9535 10914 7976 129 -913 -33 N
ATOM 1419 CA THR A 212 6.098 25.058 -52.884 1.00 74.42 C
ANISOU 1419 CA THR A 212 9493 10927 7857 65 -848 37 C
ATOM 1420 C THR A 212 5.782 26.340 -52.078 1.00 78.48 C
ANISOU 1420 C THR A 212 9999 11434 8384 46 -893 3 C
ATOM 1421 O THR A 212 6.407 26.549 -51.042 1.00 78.09 O
ANISOU 1421 O THR A 212 9875 11465 8329 -2 -826 36 O
ATOM 1422 CB THR A 212 7.061 25.286 -54.064 1.00 84.94 C
ANISOU 1422 CB THR A 212 10958 12234 9082 37 -835 90 C
ATOM 1423 OG1 THR A 212 7.925 24.153 -54.174 1.00 85.83 O
ANISOU 1423 OG1 THR A 212 11021 12418 9171 32 -741 143 O
ATOM 1424 CG2 THR A 212 7.843 26.610 -53.994 1.00 83.95 C
ANISOU 1424 CG2 THR A 212 10911 12113 8872 -38 -825 116 C
ATOM 1425 N THR A 213 4.846 27.199 -52.548 1.00 75.49 N
ANISOU 1425 N THR A 213 9704 10960 8017 91 -1015 -67 N
ATOM 1426 CA THR A 213 4.539 28.453 -51.851 1.00 75.03 C
ANISOU 1426 CA THR A 213 9660 10887 7962 84 -1068 -103 C
ATOM 1427 C THR A 213 3.739 28.213 -50.588 1.00 79.37 C
ANISOU 1427 C THR A 213 10046 11493 8619 98 -1053 -164 C
ATOM 1428 O THR A 213 4.064 28.841 -49.583 1.00 79.86 O
ANISOU 1428 O THR A 213 10068 11599 8676 56 -1020 -148 O
ATOM 1429 CB THR A 213 3.922 29.509 -52.753 1.00 78.30 C
ANISOU 1429 CB THR A 213 10244 11176 8332 140 -1210 -159 C
ATOM 1430 OG1 THR A 213 2.917 28.900 -53.551 1.00 77.69 O
ANISOU 1430 OG1 THR A 213 10171 11041 8308 230 -1297 -235 O
ATOM 1431 CG2 THR A 213 4.955 30.183 -53.647 1.00 75.54 C
ANISOU 1431 CG2 THR A 213 10090 10768 7842 81 -1197 -88 C
ATOM 1432 N LEU A 214 2.757 27.283 -50.582 1.00 75.49 N
ANISOU 1432 N LEU A 214 9459 11005 8218 141 -1061 -234 N
ATOM 1433 CA LEU A 214 2.059 27.020 -49.323 1.00 75.73 C
ANISOU 1433 CA LEU A 214 9340 11093 8340 128 -1019 -295 C
ATOM 1434 C LEU A 214 2.953 26.194 -48.377 1.00 80.70 C
ANISOU 1434 C LEU A 214 9899 11809 8954 61 -876 -208 C
ATOM 1435 O LEU A 214 2.812 26.300 -47.163 1.00 80.54 O
ANISOU 1435 O LEU A 214 9795 11836 8970 29 -826 -225 O
ATOM 1436 CB LEU A 214 0.629 26.459 -49.458 1.00 76.40 C
ANISOU 1436 CB LEU A 214 9339 11161 8529 175 -1067 -430 C
ATOM 1437 CG LEU A 214 0.389 25.233 -50.318 1.00 81.77 C
ANISOU 1437 CG LEU A 214 10019 11824 9226 190 -1050 -439 C
ATOM 1438 CD1 LEU A 214 0.454 23.960 -49.489 1.00 82.47 C
ANISOU 1438 CD1 LEU A 214 10014 11974 9348 126 -911 -418 C
ATOM 1439 CD2 LEU A 214 -0.960 25.321 -50.995 1.00 83.52 C
ANISOU 1439 CD2 LEU A 214 10215 11999 9520 264 -1170 -590 C
ATOM 1440 N LEU A 215 3.935 25.453 -48.925 1.00 77.44 N
ANISOU 1440 N LEU A 215 9531 11415 8476 47 -817 -118 N
ATOM 1441 CA LEU A 215 4.912 24.707 -48.123 1.00 76.30 C
ANISOU 1441 CA LEU A 215 9339 11351 8300 9 -702 -40 C
ATOM 1442 C LEU A 215 5.777 25.724 -47.390 1.00 79.74 C
ANISOU 1442 C LEU A 215 9774 11838 8686 -33 -685 5 C
ATOM 1443 O LEU A 215 5.860 25.687 -46.169 1.00 79.42 O
ANISOU 1443 O LEU A 215 9664 11848 8664 -56 -636 8 O
ATOM 1444 CB LEU A 215 5.788 23.819 -49.025 1.00 75.94 C
ANISOU 1444 CB LEU A 215 9346 11317 8192 22 -663 28 C
ATOM 1445 CG LEU A 215 6.258 22.497 -48.444 1.00 80.22 C
ANISOU 1445 CG LEU A 215 9846 11909 8725 28 -569 67 C
ATOM 1446 CD1 LEU A 215 5.106 21.510 -48.305 1.00 80.49 C
ANISOU 1446 CD1 LEU A 215 9854 11897 8830 39 -558 2 C
ATOM 1447 CD2 LEU A 215 7.302 21.887 -49.327 1.00 82.77 C
ANISOU 1447 CD2 LEU A 215 10220 12254 8975 50 -541 130 C
ATOM 1448 N LEU A 216 6.351 26.678 -48.135 1.00 76.36 N
ANISOU 1448 N LEU A 216 9437 11387 8191 -50 -728 32 N
ATOM 1449 CA LEU A 216 7.190 27.745 -47.597 1.00 76.30 C
ANISOU 1449 CA LEU A 216 9446 11420 8126 -107 -713 65 C
ATOM 1450 C LEU A 216 6.422 28.653 -46.616 1.00 79.08 C
ANISOU 1450 C LEU A 216 9764 11755 8527 -110 -755 13 C
ATOM 1451 O LEU A 216 6.977 29.025 -45.584 1.00 78.53 O
ANISOU 1451 O LEU A 216 9647 11750 8442 -153 -710 38 O
ATOM 1452 CB LEU A 216 7.834 28.537 -48.759 1.00 76.87 C
ANISOU 1452 CB LEU A 216 9655 11445 8106 -140 -744 90 C
ATOM 1453 CG LEU A 216 8.272 29.971 -48.491 1.00 81.88 C
ANISOU 1453 CG LEU A 216 10362 12072 8677 -207 -760 96 C
ATOM 1454 CD1 LEU A 216 9.720 30.150 -48.766 1.00 81.90 C
ANISOU 1454 CD1 LEU A 216 10395 12142 8583 -292 -680 147 C
ATOM 1455 CD2 LEU A 216 7.450 30.946 -49.302 1.00 85.08 C
ANISOU 1455 CD2 LEU A 216 10920 12345 9062 -178 -874 49 C
ATOM 1456 N VAL A 217 5.150 28.974 -46.916 1.00 74.75 N
ANISOU 1456 N VAL A 217 9232 11129 8040 -58 -845 -70 N
ATOM 1457 CA VAL A 217 4.346 29.866 -46.067 1.00 74.14 C
ANISOU 1457 CA VAL A 217 9120 11037 8011 -47 -895 -139 C
ATOM 1458 C VAL A 217 3.753 29.143 -44.828 1.00 76.96 C
ANISOU 1458 C VAL A 217 9336 11452 8455 -54 -828 -179 C
ATOM 1459 O VAL A 217 3.953 29.616 -43.712 1.00 76.41 O
ANISOU 1459 O VAL A 217 9222 11425 8386 -89 -792 -169 O
ATOM 1460 CB VAL A 217 3.266 30.640 -46.883 1.00 77.92 C
ANISOU 1460 CB VAL A 217 9681 11415 8510 26 -1035 -232 C
ATOM 1461 CG1 VAL A 217 2.286 31.373 -45.972 1.00 77.75 C
ANISOU 1461 CG1 VAL A 217 9596 11390 8554 56 -1088 -327 C
ATOM 1462 CG2 VAL A 217 3.916 31.618 -47.865 1.00 77.90 C
ANISOU 1462 CG2 VAL A 217 9863 11339 8396 15 -1094 -188 C
ATOM 1463 N LEU A 218 3.043 28.020 -45.021 1.00 73.16 N
ANISOU 1463 N LEU A 218 8798 10965 8036 -29 -807 -226 N
ATOM 1464 CA LEU A 218 2.377 27.284 -43.939 1.00 72.87 C
ANISOU 1464 CA LEU A 218 8653 10965 8070 -53 -733 -278 C
ATOM 1465 C LEU A 218 3.266 26.316 -43.135 1.00 76.52 C
ANISOU 1465 C LEU A 218 9098 11485 8492 -96 -612 -191 C
ATOM 1466 O LEU A 218 2.884 25.946 -42.028 1.00 76.35 O
ANISOU 1466 O LEU A 218 9020 11487 8502 -129 -544 -220 O
ATOM 1467 CB LEU A 218 1.132 26.523 -44.460 1.00 73.29 C
ANISOU 1467 CB LEU A 218 8657 10985 8204 -25 -755 -388 C
ATOM 1468 CG LEU A 218 0.149 27.262 -45.379 1.00 78.25 C
ANISOU 1468 CG LEU A 218 9298 11558 8877 46 -893 -500 C
ATOM 1469 CD1 LEU A 218 -0.857 26.304 -45.953 1.00 78.67 C
ANISOU 1469 CD1 LEU A 218 9293 11596 9001 65 -902 -603 C
ATOM 1470 CD2 LEU A 218 -0.565 28.385 -44.653 1.00 81.64 C
ANISOU 1470 CD2 LEU A 218 9678 11991 9349 63 -951 -592 C
ATOM 1471 N GLN A 219 4.403 25.874 -43.679 1.00 73.41 N
ANISOU 1471 N GLN A 219 8757 11111 8024 -91 -586 -97 N
ATOM 1472 CA GLN A 219 5.270 24.924 -42.974 1.00 73.47 C
ANISOU 1472 CA GLN A 219 8758 11173 7985 -103 -492 -27 C
ATOM 1473 C GLN A 219 6.623 25.517 -42.549 1.00 79.20 C
ANISOU 1473 C GLN A 219 9490 11968 8633 -119 -476 49 C
ATOM 1474 O GLN A 219 7.312 24.914 -41.720 1.00 79.55 O
ANISOU 1474 O GLN A 219 9520 12065 8641 -117 -414 89 O
ATOM 1475 CB GLN A 219 5.461 23.636 -43.795 1.00 74.67 C
ANISOU 1475 CB GLN A 219 8947 11310 8115 -73 -463 1 C
ATOM 1476 CG GLN A 219 4.295 22.655 -43.730 1.00 82.54 C
ANISOU 1476 CG GLN A 219 9930 12259 9174 -79 -431 -69 C
ATOM 1477 CD GLN A 219 4.536 21.536 -42.752 1.00 89.85 C
ANISOU 1477 CD GLN A 219 10872 13198 10068 -96 -332 -42 C
ATOM 1478 OE1 GLN A 219 5.185 21.716 -41.712 1.00 87.38 O
ANISOU 1478 OE1 GLN A 219 10559 12928 9714 -104 -295 -1 O
ATOM 1479 NE2 GLN A 219 3.999 20.358 -43.056 1.00 69.30 N
ANISOU 1479 NE2 GLN A 219 8303 10552 7476 -101 -288 -69 N
ATOM 1480 N TYR A 220 6.999 26.694 -43.093 1.00 75.49 N
ANISOU 1480 N TYR A 220 9052 11496 8133 -135 -533 60 N
ATOM 1481 CA TYR A 220 8.257 27.352 -42.743 1.00 74.61 C
ANISOU 1481 CA TYR A 220 8941 11458 7951 -170 -512 113 C
ATOM 1482 C TYR A 220 8.012 28.656 -42.013 1.00 79.35 C
ANISOU 1482 C TYR A 220 9535 12053 8560 -209 -544 88 C
ATOM 1483 O TYR A 220 8.219 28.681 -40.811 1.00 78.68 O
ANISOU 1483 O TYR A 220 9401 12018 8476 -224 -506 97 O
ATOM 1484 CB TYR A 220 9.165 27.511 -43.971 1.00 75.37 C
ANISOU 1484 CB TYR A 220 9093 11567 7978 -183 -521 149 C
ATOM 1485 CG TYR A 220 10.515 28.132 -43.696 1.00 76.15 C
ANISOU 1485 CG TYR A 220 9177 11756 8000 -237 -488 182 C
ATOM 1486 CD1 TYR A 220 11.458 27.479 -42.904 1.00 77.84 C
ANISOU 1486 CD1 TYR A 220 9318 12075 8182 -222 -431 207 C
ATOM 1487 CD2 TYR A 220 10.897 29.313 -44.320 1.00 76.91 C
ANISOU 1487 CD2 TYR A 220 9345 11832 8046 -303 -515 179 C
ATOM 1488 CE1 TYR A 220 12.725 28.015 -42.698 1.00 78.16 C
ANISOU 1488 CE1 TYR A 220 9324 12217 8157 -272 -403 216 C
ATOM 1489 CE2 TYR A 220 12.162 29.860 -44.121 1.00 77.95 C
ANISOU 1489 CE2 TYR A 220 9458 12055 8105 -374 -471 194 C
ATOM 1490 CZ TYR A 220 13.070 29.211 -43.302 1.00 86.11 C
ANISOU 1490 CZ TYR A 220 10385 13210 9121 -358 -416 207 C
ATOM 1491 OH TYR A 220 14.317 29.747 -43.105 1.00 89.59 O
ANISOU 1491 OH TYR A 220 10787 13758 9496 -429 -376 200 O
ATOM 1492 N PHE A 221 7.524 29.714 -42.693 1.00 78.05 N
ANISOU 1492 N PHE A 221 9438 11821 8398 -218 -620 56 N
ATOM 1493 CA PHE A 221 7.251 31.001 -42.042 1.00 79.09 C
ANISOU 1493 CA PHE A 221 9584 11936 8531 -247 -659 29 C
ATOM 1494 C PHE A 221 6.216 30.887 -40.920 1.00 82.45 C
ANISOU 1494 C PHE A 221 9933 12357 9038 -227 -654 -29 C
ATOM 1495 O PHE A 221 6.518 31.264 -39.790 1.00 81.93 O
ANISOU 1495 O PHE A 221 9829 12336 8964 -259 -620 -16 O
ATOM 1496 CB PHE A 221 6.868 32.108 -43.049 1.00 82.24 C
ANISOU 1496 CB PHE A 221 10104 12243 8901 -243 -753 -1 C
ATOM 1497 CG PHE A 221 7.875 32.419 -44.139 1.00 85.55 C
ANISOU 1497 CG PHE A 221 10628 12655 9222 -291 -747 49 C
ATOM 1498 CD1 PHE A 221 9.241 32.458 -43.863 1.00 89.42 C
ANISOU 1498 CD1 PHE A 221 11097 13237 9642 -368 -671 102 C
ATOM 1499 CD2 PHE A 221 7.453 32.737 -45.430 1.00 89.40 C
ANISOU 1499 CD2 PHE A 221 11242 13045 9681 -263 -817 30 C
ATOM 1500 CE1 PHE A 221 10.170 32.756 -44.873 1.00 91.22 C
ANISOU 1500 CE1 PHE A 221 11414 13467 9777 -432 -648 130 C
ATOM 1501 CE2 PHE A 221 8.383 33.048 -46.436 1.00 92.80 C
ANISOU 1501 CE2 PHE A 221 11789 13461 10009 -325 -797 71 C
ATOM 1502 CZ PHE A 221 9.735 33.045 -46.153 1.00 90.90 C
ANISOU 1502 CZ PHE A 221 11513 13320 9703 -416 -704 118 C
ATOM 1503 N GLY A 222 5.046 30.329 -41.234 1.00 78.82 N
ANISOU 1503 N GLY A 222 9447 11848 8653 -182 -680 -98 N
ATOM 1504 CA GLY A 222 3.940 30.128 -40.304 1.00 78.81 C
ANISOU 1504 CA GLY A 222 9366 11844 8735 -175 -662 -179 C
ATOM 1505 C GLY A 222 4.358 29.577 -38.952 1.00 83.79 C
ANISOU 1505 C GLY A 222 9944 12535 9357 -215 -563 -143 C
ATOM 1506 O GLY A 222 4.357 30.327 -37.966 1.00 83.59 O
ANISOU 1506 O GLY A 222 9900 12529 9333 -240 -558 -153 O
ATOM 1507 N PRO A 223 4.783 28.284 -38.874 1.00 80.36 N
ANISOU 1507 N PRO A 223 9505 12126 8902 -216 -487 -98 N
ATOM 1508 CA PRO A 223 5.210 27.729 -37.582 1.00 79.80 C
ANISOU 1508 CA PRO A 223 9418 12098 8804 -240 -402 -65 C
ATOM 1509 C PRO A 223 6.300 28.539 -36.890 1.00 84.51 C
ANISOU 1509 C PRO A 223 10019 12753 9337 -257 -405 -4 C
ATOM 1510 O PRO A 223 6.154 28.785 -35.697 1.00 85.76 O
ANISOU 1510 O PRO A 223 10159 12926 9498 -280 -371 -15 O
ATOM 1511 CB PRO A 223 5.666 26.311 -37.937 1.00 81.27 C
ANISOU 1511 CB PRO A 223 9635 12288 8956 -216 -348 -21 C
ATOM 1512 CG PRO A 223 4.907 25.969 -39.152 1.00 85.82 C
ANISOU 1512 CG PRO A 223 10216 12813 9579 -197 -385 -66 C
ATOM 1513 CD PRO A 223 4.857 27.256 -39.930 1.00 81.69 C
ANISOU 1513 CD PRO A 223 9700 12276 9063 -187 -480 -80 C
ATOM 1514 N LEU A 224 7.346 29.001 -37.623 1.00 79.96 N
ANISOU 1514 N LEU A 224 9468 12211 8702 -257 -440 48 N
ATOM 1515 CA LEU A 224 8.431 29.806 -37.043 1.00 79.49 C
ANISOU 1515 CA LEU A 224 9403 12219 8581 -288 -439 90 C
ATOM 1516 C LEU A 224 7.897 31.035 -36.317 1.00 84.97 C
ANISOU 1516 C LEU A 224 10093 12891 9299 -323 -470 54 C
ATOM 1517 O LEU A 224 8.285 31.254 -35.176 1.00 84.99 O
ANISOU 1517 O LEU A 224 10073 12938 9281 -342 -440 68 O
ATOM 1518 CB LEU A 224 9.488 30.217 -38.082 1.00 79.35 C
ANISOU 1518 CB LEU A 224 9413 12237 8499 -307 -462 126 C
ATOM 1519 CG LEU A 224 10.491 29.155 -38.555 1.00 83.55 C
ANISOU 1519 CG LEU A 224 9930 12833 8982 -276 -424 166 C
ATOM 1520 CD1 LEU A 224 11.268 29.662 -39.738 1.00 83.44 C
ANISOU 1520 CD1 LEU A 224 9947 12839 8916 -312 -440 179 C
ATOM 1521 CD2 LEU A 224 11.469 28.755 -37.453 1.00 86.30 C
ANISOU 1521 CD2 LEU A 224 10230 13278 9282 -259 -385 189 C
ATOM 1522 N CYS A 225 6.954 31.784 -36.933 1.00 82.70 N
ANISOU 1522 N CYS A 225 9834 12533 9057 -319 -534 0 N
ATOM 1523 CA CYS A 225 6.328 32.971 -36.336 1.00 83.48 C
ANISOU 1523 CA CYS A 225 9939 12601 9180 -334 -577 -49 C
ATOM 1524 C CYS A 225 5.715 32.646 -35.000 1.00 85.66 C
ANISOU 1524 C CYS A 225 10154 12890 9503 -338 -524 -85 C
ATOM 1525 O CYS A 225 5.908 33.396 -34.047 1.00 85.53 O
ANISOU 1525 O CYS A 225 10133 12894 9470 -367 -519 -82 O
ATOM 1526 CB CYS A 225 5.300 33.583 -37.277 1.00 85.32 C
ANISOU 1526 CB CYS A 225 10216 12750 9453 -295 -668 -119 C
ATOM 1527 SG CYS A 225 6.020 34.390 -38.726 1.00 90.25 S
ANISOU 1527 SG CYS A 225 10967 13329 9993 -305 -737 -79 S
ATOM 1528 N PHE A 226 5.007 31.509 -34.927 1.00 81.01 N
ANISOU 1528 N PHE A 226 9529 12287 8965 -320 -475 -120 N
ATOM 1529 CA PHE A 226 4.386 30.987 -33.715 1.00 80.55 C
ANISOU 1529 CA PHE A 226 9432 12231 8941 -342 -400 -161 C
ATOM 1530 C PHE A 226 5.459 30.635 -32.653 1.00 85.26 C
ANISOU 1530 C PHE A 226 10050 12880 9466 -360 -339 -84 C
ATOM 1531 O PHE A 226 5.243 30.898 -31.465 1.00 84.91 O
ANISOU 1531 O PHE A 226 9999 12839 9423 -387 -301 -103 O
ATOM 1532 CB PHE A 226 3.524 29.764 -34.067 1.00 82.12 C
ANISOU 1532 CB PHE A 226 9612 12399 9192 -336 -352 -215 C
ATOM 1533 CG PHE A 226 3.014 28.973 -32.892 1.00 83.47 C
ANISOU 1533 CG PHE A 226 9776 12564 9373 -379 -247 -249 C
ATOM 1534 CD1 PHE A 226 3.740 27.896 -32.392 1.00 86.29 C
ANISOU 1534 CD1 PHE A 226 10196 12930 9662 -383 -174 -178 C
ATOM 1535 CD2 PHE A 226 1.803 29.295 -32.290 1.00 85.46 C
ANISOU 1535 CD2 PHE A 226 9974 12800 9698 -415 -221 -363 C
ATOM 1536 CE1 PHE A 226 3.277 27.175 -31.292 1.00 87.51 C
ANISOU 1536 CE1 PHE A 226 10385 13059 9806 -430 -73 -208 C
ATOM 1537 CE2 PHE A 226 1.335 28.565 -31.199 1.00 88.52 C
ANISOU 1537 CE2 PHE A 226 10374 13176 10084 -475 -106 -401 C
ATOM 1538 CZ PHE A 226 2.075 27.511 -30.709 1.00 86.77 C
ANISOU 1538 CZ PHE A 226 10241 12946 9781 -486 -31 -318 C
ATOM 1539 N ILE A 227 6.603 30.036 -33.080 1.00 81.83 N
ANISOU 1539 N ILE A 227 9642 12486 8965 -338 -333 -7 N
ATOM 1540 CA ILE A 227 7.695 29.669 -32.169 1.00 81.57 C
ANISOU 1540 CA ILE A 227 9625 12511 8856 -330 -296 52 C
ATOM 1541 C ILE A 227 8.214 30.914 -31.438 1.00 87.49 C
ANISOU 1541 C ILE A 227 10360 13302 9580 -362 -325 62 C
ATOM 1542 O ILE A 227 8.282 30.910 -30.206 1.00 87.33 O
ANISOU 1542 O ILE A 227 10350 13293 9540 -371 -291 63 O
ATOM 1543 CB ILE A 227 8.819 28.863 -32.865 1.00 83.92 C
ANISOU 1543 CB ILE A 227 9935 12858 9092 -285 -299 109 C
ATOM 1544 CG1 ILE A 227 8.287 27.544 -33.431 1.00 83.90 C
ANISOU 1544 CG1 ILE A 227 9966 12806 9105 -252 -260 102 C
ATOM 1545 CG2 ILE A 227 9.962 28.602 -31.896 1.00 84.70 C
ANISOU 1545 CG2 ILE A 227 10038 13032 9111 -259 -287 150 C
ATOM 1546 CD1 ILE A 227 9.229 26.827 -34.381 1.00 90.96 C
ANISOU 1546 CD1 ILE A 227 10871 13737 9951 -202 -273 146 C
ATOM 1547 N PHE A 228 8.515 31.989 -32.198 1.00 85.29 N
ANISOU 1547 N PHE A 228 10076 13034 9296 -385 -385 65 N
ATOM 1548 CA PHE A 228 8.986 33.266 -31.656 1.00 85.79 C
ANISOU 1548 CA PHE A 228 10141 13127 9330 -429 -414 70 C
ATOM 1549 C PHE A 228 7.921 33.936 -30.771 1.00 91.28 C
ANISOU 1549 C PHE A 228 10836 13771 10077 -445 -417 17 C
ATOM 1550 O PHE A 228 8.278 34.535 -29.751 1.00 91.67 O
ANISOU 1550 O PHE A 228 10885 13848 10097 -473 -412 25 O
ATOM 1551 CB PHE A 228 9.496 34.202 -32.771 1.00 87.67 C
ANISOU 1551 CB PHE A 228 10409 13367 9535 -464 -467 81 C
ATOM 1552 CG PHE A 228 10.621 33.635 -33.618 1.00 89.27 C
ANISOU 1552 CG PHE A 228 10601 13634 9682 -462 -453 120 C
ATOM 1553 CD1 PHE A 228 11.813 33.213 -33.034 1.00 92.32 C
ANISOU 1553 CD1 PHE A 228 10941 14122 10013 -457 -421 147 C
ATOM 1554 CD2 PHE A 228 10.501 33.556 -35.001 1.00 91.14 C
ANISOU 1554 CD2 PHE A 228 10875 13833 9921 -459 -477 120 C
ATOM 1555 CE1 PHE A 228 12.845 32.683 -33.814 1.00 93.20 C
ANISOU 1555 CE1 PHE A 228 11027 14307 10077 -447 -409 164 C
ATOM 1556 CE2 PHE A 228 11.534 33.023 -35.780 1.00 93.99 C
ANISOU 1556 CE2 PHE A 228 11222 14258 10231 -460 -455 148 C
ATOM 1557 CZ PHE A 228 12.700 32.594 -35.181 1.00 92.22 C
ANISOU 1557 CZ PHE A 228 10936 14145 9958 -455 -420 165 C
ATOM 1558 N ILE A 229 6.618 33.779 -31.126 1.00 87.69 N
ANISOU 1558 N ILE A 229 10372 13249 9698 -426 -423 -48 N
ATOM 1559 CA ILE A 229 5.490 34.301 -30.345 1.00 87.62 C
ANISOU 1559 CA ILE A 229 10343 13201 9747 -435 -420 -124 C
ATOM 1560 C ILE A 229 5.514 33.664 -28.957 1.00 92.08 C
ANISOU 1560 C ILE A 229 10902 13786 10299 -456 -334 -117 C
ATOM 1561 O ILE A 229 5.447 34.397 -27.972 1.00 93.04 O
ANISOU 1561 O ILE A 229 11025 13913 10414 -480 -329 -131 O
ATOM 1562 CB ILE A 229 4.125 34.143 -31.082 1.00 90.93 C
ANISOU 1562 CB ILE A 229 10732 13564 10253 -405 -447 -220 C
ATOM 1563 CG1 ILE A 229 3.978 35.210 -32.196 1.00 91.44 C
ANISOU 1563 CG1 ILE A 229 10837 13590 10317 -374 -557 -240 C
ATOM 1564 CG2 ILE A 229 2.926 34.195 -30.108 1.00 91.56 C
ANISOU 1564 CG2 ILE A 229 10761 13627 10400 -419 -407 -322 C
ATOM 1565 CD1 ILE A 229 2.946 34.891 -33.293 1.00 97.26 C
ANISOU 1565 CD1 ILE A 229 11556 14279 11120 -321 -608 -321 C
ATOM 1566 N CYS A 230 5.680 32.320 -28.878 1.00 87.62 N
ANISOU 1566 N CYS A 230 10352 13225 9715 -444 -270 -92 N
ATOM 1567 CA CYS A 230 5.770 31.586 -27.610 1.00 86.97 C
ANISOU 1567 CA CYS A 230 10308 13142 9596 -458 -188 -79 C
ATOM 1568 C CYS A 230 6.931 32.063 -26.764 1.00 90.59 C
ANISOU 1568 C CYS A 230 10789 13654 9976 -455 -205 -17 C
ATOM 1569 O CYS A 230 6.724 32.366 -25.592 1.00 90.37 O
ANISOU 1569 O CYS A 230 10782 13617 9938 -480 -173 -33 O
ATOM 1570 CB CYS A 230 5.847 30.082 -27.840 1.00 87.10 C
ANISOU 1570 CB CYS A 230 10370 13139 9585 -436 -131 -58 C
ATOM 1571 SG CYS A 230 4.337 29.367 -28.516 1.00 91.13 S
ANISOU 1571 SG CYS A 230 10853 13586 10185 -461 -88 -151 S
ATOM 1572 N TYR A 231 8.141 32.162 -27.358 1.00 87.11 N
ANISOU 1572 N TYR A 231 10340 13275 9482 -428 -254 42 N
ATOM 1573 CA TYR A 231 9.348 32.574 -26.641 1.00 87.37 C
ANISOU 1573 CA TYR A 231 10375 13381 9440 -423 -276 85 C
ATOM 1574 C TYR A 231 9.289 34.018 -26.121 1.00 92.18 C
ANISOU 1574 C TYR A 231 10969 13999 10058 -474 -309 68 C
ATOM 1575 O TYR A 231 9.933 34.328 -25.105 1.00 92.22 O
ANISOU 1575 O TYR A 231 10983 14045 10012 -480 -310 85 O
ATOM 1576 CB TYR A 231 10.611 32.304 -27.462 1.00 88.35 C
ANISOU 1576 CB TYR A 231 10473 13584 9512 -392 -311 126 C
ATOM 1577 CG TYR A 231 10.986 30.838 -27.457 1.00 90.30 C
ANISOU 1577 CG TYR A 231 10754 13837 9718 -320 -283 149 C
ATOM 1578 CD1 TYR A 231 11.303 30.181 -26.269 1.00 92.52 C
ANISOU 1578 CD1 TYR A 231 11096 14119 9939 -276 -258 160 C
ATOM 1579 CD2 TYR A 231 11.002 30.099 -28.634 1.00 91.18 C
ANISOU 1579 CD2 TYR A 231 10860 13943 9841 -291 -284 157 C
ATOM 1580 CE1 TYR A 231 11.617 28.823 -26.253 1.00 93.72 C
ANISOU 1580 CE1 TYR A 231 11313 14258 10037 -199 -239 178 C
ATOM 1581 CE2 TYR A 231 11.334 28.745 -28.634 1.00 92.60 C
ANISOU 1581 CE2 TYR A 231 11088 14119 9975 -218 -261 177 C
ATOM 1582 CZ TYR A 231 11.635 28.110 -27.441 1.00101.90 C
ANISOU 1582 CZ TYR A 231 12339 15291 11088 -170 -240 186 C
ATOM 1583 OH TYR A 231 11.941 26.772 -27.442 1.00105.44 O
ANISOU 1583 OH TYR A 231 12866 15720 11476 -89 -225 203 O
ATOM 1584 N PHE A 232 8.470 34.873 -26.772 1.00 88.15 N
ANISOU 1584 N PHE A 232 10444 13441 9607 -501 -342 29 N
ATOM 1585 CA PHE A 232 8.237 36.242 -26.326 1.00 87.64 C
ANISOU 1585 CA PHE A 232 10386 13363 9549 -541 -378 4 C
ATOM 1586 C PHE A 232 7.334 36.163 -25.099 1.00 91.46 C
ANISOU 1586 C PHE A 232 10876 13809 10066 -547 -327 -40 C
ATOM 1587 O PHE A 232 7.660 36.741 -24.064 1.00 91.25 O
ANISOU 1587 O PHE A 232 10865 13802 10004 -570 -323 -30 O
ATOM 1588 CB PHE A 232 7.587 37.082 -27.435 1.00 89.20 C
ANISOU 1588 CB PHE A 232 10594 13509 9789 -545 -440 -34 C
ATOM 1589 CG PHE A 232 7.288 38.504 -27.029 1.00 90.81 C
ANISOU 1589 CG PHE A 232 10829 13684 9992 -572 -486 -64 C
ATOM 1590 CD1 PHE A 232 8.286 39.471 -27.035 1.00 94.01 C
ANISOU 1590 CD1 PHE A 232 11273 14121 10326 -622 -519 -26 C
ATOM 1591 CD2 PHE A 232 6.006 38.879 -26.647 1.00 93.32 C
ANISOU 1591 CD2 PHE A 232 11137 13946 10375 -552 -493 -143 C
ATOM 1592 CE1 PHE A 232 8.010 40.785 -26.653 1.00 95.37 C
ANISOU 1592 CE1 PHE A 232 11496 14256 10486 -648 -562 -52 C
ATOM 1593 CE2 PHE A 232 5.729 40.195 -26.267 1.00 96.61 C
ANISOU 1593 CE2 PHE A 232 11591 14332 10784 -564 -543 -175 C
ATOM 1594 CZ PHE A 232 6.733 41.139 -26.273 1.00 94.81 C
ANISOU 1594 CZ PHE A 232 11423 14122 10478 -611 -579 -123 C
ATOM 1595 N LYS A 233 6.229 35.394 -25.207 1.00 88.05 N
ANISOU 1595 N LYS A 233 10432 13327 9697 -536 -281 -94 N
ATOM 1596 CA LYS A 233 5.262 35.155 -24.137 1.00 88.27 C
ANISOU 1596 CA LYS A 233 10464 13317 9757 -559 -209 -155 C
ATOM 1597 C LYS A 233 5.936 34.527 -22.905 1.00 94.53 C
ANISOU 1597 C LYS A 233 11319 14125 10474 -566 -149 -106 C
ATOM 1598 O LYS A 233 5.550 34.844 -21.779 1.00 94.80 O
ANISOU 1598 O LYS A 233 11377 14140 10504 -597 -106 -137 O
ATOM 1599 CB LYS A 233 4.094 34.291 -24.640 1.00 89.93 C
ANISOU 1599 CB LYS A 233 10645 13485 10039 -561 -159 -231 C
ATOM 1600 CG LYS A 233 3.153 35.021 -25.595 1.00 96.06 C
ANISOU 1600 CG LYS A 233 11359 14240 10898 -541 -227 -315 C
ATOM 1601 CD LYS A 233 1.865 34.241 -25.828 1.00103.13 C
ANISOU 1601 CD LYS A 233 12203 15108 11875 -554 -169 -426 C
ATOM 1602 CE LYS A 233 0.712 35.139 -26.209 1.00110.52 C
ANISOU 1602 CE LYS A 233 13066 16031 12895 -526 -236 -549 C
ATOM 1603 NZ LYS A 233 -0.598 34.537 -25.844 1.00119.33 N
ANISOU 1603 NZ LYS A 233 14107 17141 14091 -561 -155 -691 N
ATOM 1604 N ILE A 234 6.961 33.668 -23.126 1.00 92.40 N
ANISOU 1604 N ILE A 234 11082 13889 10137 -529 -152 -36 N
ATOM 1605 CA ILE A 234 7.765 33.013 -22.082 1.00 93.20 C
ANISOU 1605 CA ILE A 234 11259 14005 10148 -505 -122 10 C
ATOM 1606 C ILE A 234 8.546 34.088 -21.303 1.00100.41 C
ANISOU 1606 C ILE A 234 12164 14969 11017 -513 -171 33 C
ATOM 1607 O ILE A 234 8.451 34.148 -20.078 1.00100.10 O
ANISOU 1607 O ILE A 234 12182 14908 10943 -527 -136 27 O
ATOM 1608 CB ILE A 234 8.673 31.889 -22.686 1.00 95.74 C
ANISOU 1608 CB ILE A 234 11607 14356 10412 -439 -135 62 C
ATOM 1609 CG1 ILE A 234 7.829 30.648 -23.042 1.00 95.82 C
ANISOU 1609 CG1 ILE A 234 11667 14296 10446 -439 -65 39 C
ATOM 1610 CG2 ILE A 234 9.833 31.510 -21.744 1.00 96.45 C
ANISOU 1610 CG2 ILE A 234 11765 14487 10396 -383 -152 105 C
ATOM 1611 CD1 ILE A 234 8.429 29.688 -24.041 1.00101.00 C
ANISOU 1611 CD1 ILE A 234 12335 14972 11070 -376 -85 78 C
ATOM 1612 N TYR A 235 9.272 34.955 -22.032 1.00 99.57 N
ANISOU 1612 N TYR A 235 11997 14927 10909 -517 -245 54 N
ATOM 1613 CA TYR A 235 10.065 36.065 -21.508 1.00100.55 C
ANISOU 1613 CA TYR A 235 12105 15107 10991 -543 -293 69 C
ATOM 1614 C TYR A 235 9.219 37.004 -20.644 1.00103.38 C
ANISOU 1614 C TYR A 235 12482 15415 11382 -589 -279 31 C
ATOM 1615 O TYR A 235 9.631 37.337 -19.534 1.00102.99 O
ANISOU 1615 O TYR A 235 12463 15385 11284 -598 -279 40 O
ATOM 1616 CB TYR A 235 10.731 36.823 -22.682 1.00103.11 C
ANISOU 1616 CB TYR A 235 12376 15486 11316 -568 -353 81 C
ATOM 1617 CG TYR A 235 11.396 38.138 -22.324 1.00107.52 C
ANISOU 1617 CG TYR A 235 12925 16090 11839 -625 -396 82 C
ATOM 1618 CD1 TYR A 235 12.490 38.178 -21.459 1.00110.52 C
ANISOU 1618 CD1 TYR A 235 13296 16549 12149 -622 -408 96 C
ATOM 1619 CD2 TYR A 235 10.983 39.333 -22.909 1.00108.81 C
ANISOU 1619 CD2 TYR A 235 13099 16217 12028 -679 -430 63 C
ATOM 1620 CE1 TYR A 235 13.122 39.382 -21.144 1.00112.45 C
ANISOU 1620 CE1 TYR A 235 13529 16840 12358 -688 -442 89 C
ATOM 1621 CE2 TYR A 235 11.615 40.542 -22.610 1.00110.49 C
ANISOU 1621 CE2 TYR A 235 13325 16461 12194 -744 -463 64 C
ATOM 1622 CZ TYR A 235 12.683 40.562 -21.723 1.00119.88 C
ANISOU 1622 CZ TYR A 235 14491 17736 13321 -757 -464 76 C
ATOM 1623 OH TYR A 235 13.310 41.747 -21.411 1.00122.06 O
ANISOU 1623 OH TYR A 235 14780 18047 13551 -834 -490 68 O
ATOM 1624 N ILE A 236 8.028 37.388 -21.141 1.00 99.53 N
ANISOU 1624 N ILE A 236 11976 14867 10974 -608 -271 -22 N
ATOM 1625 CA ILE A 236 7.095 38.302 -20.481 1.00 99.46 C
ANISOU 1625 CA ILE A 236 11971 14813 11005 -639 -263 -79 C
ATOM 1626 C ILE A 236 6.585 37.723 -19.141 1.00104.97 C
ANISOU 1626 C ILE A 236 12713 15477 11692 -651 -176 -104 C
ATOM 1627 O ILE A 236 6.597 38.441 -18.136 1.00104.88 O
ANISOU 1627 O ILE A 236 12729 15462 11660 -675 -171 -114 O
ATOM 1628 CB ILE A 236 5.964 38.731 -21.470 1.00102.17 C
ANISOU 1628 CB ILE A 236 12275 15111 11435 -633 -292 -148 C
ATOM 1629 CG1 ILE A 236 6.521 39.526 -22.681 1.00102.53 C
ANISOU 1629 CG1 ILE A 236 12320 15170 11465 -630 -382 -121 C
ATOM 1630 CG2 ILE A 236 4.823 39.493 -20.794 1.00103.07 C
ANISOU 1630 CG2 ILE A 236 12379 15183 11601 -646 -281 -235 C
ATOM 1631 CD1 ILE A 236 7.456 40.787 -22.377 1.00111.84 C
ANISOU 1631 CD1 ILE A 236 13538 16382 12576 -671 -434 -81 C
ATOM 1632 N ARG A 237 6.188 36.430 -19.120 1.00102.36 N
ANISOU 1632 N ARG A 237 12407 15116 11369 -643 -105 -115 N
ATOM 1633 CA ARG A 237 5.710 35.740 -17.913 1.00102.94 C
ANISOU 1633 CA ARG A 237 12556 15142 11415 -669 -8 -141 C
ATOM 1634 C ARG A 237 6.860 35.447 -16.930 1.00107.71 C
ANISOU 1634 C ARG A 237 13243 15768 11912 -645 -20 -72 C
ATOM 1635 O ARG A 237 6.617 35.307 -15.728 1.00107.60 O
ANISOU 1635 O ARG A 237 13303 15720 11861 -670 30 -86 O
ATOM 1636 CB ARG A 237 4.911 34.469 -18.287 1.00104.11 C
ANISOU 1636 CB ARG A 237 12735 15244 11579 -678 76 -170 C
ATOM 1637 CG ARG A 237 4.387 33.609 -17.119 1.00118.62 C
ANISOU 1637 CG ARG A 237 14702 17022 13348 -711 183 -177 C
ATOM 1638 CD ARG A 237 3.105 34.130 -16.485 1.00134.56 C
ANISOU 1638 CD ARG A 237 16729 19012 15384 -774 241 -243 C
ATOM 1639 NE ARG A 237 2.483 33.138 -15.597 1.00146.44 N
ANISOU 1639 NE ARG A 237 18290 20449 16901 -852 382 -328 N
ATOM 1640 CZ ARG A 237 2.571 33.143 -14.269 1.00160.13 C
ANISOU 1640 CZ ARG A 237 20150 22127 18567 -906 479 -345 C
ATOM 1641 NH1 ARG A 237 3.256 34.096 -13.644 1.00147.83 N
ANISOU 1641 NH1 ARG A 237 18672 20570 16925 -876 439 -280 N
ATOM 1642 NH2 ARG A 237 1.967 32.205 -13.555 1.00145.87 N
ANISOU 1642 NH2 ARG A 237 18394 20259 16770 -999 622 -434 N
ATOM 1643 N LEU A 238 8.109 35.386 -17.435 1.00104.74 N
ANISOU 1643 N LEU A 238 12859 15453 11485 -592 -88 -8 N
ATOM 1644 CA LEU A 238 9.295 35.155 -16.613 1.00105.12 C
ANISOU 1644 CA LEU A 238 12969 15541 11431 -548 -121 41 C
ATOM 1645 C LEU A 238 9.702 36.407 -15.837 1.00108.75 C
ANISOU 1645 C LEU A 238 13414 16032 11873 -577 -162 40 C
ATOM 1646 O LEU A 238 10.213 36.285 -14.726 1.00108.85 O
ANISOU 1646 O LEU A 238 13507 16039 11813 -561 -156 52 O
ATOM 1647 CB LEU A 238 10.456 34.641 -17.471 1.00105.42 C
ANISOU 1647 CB LEU A 238 12963 15662 11431 -485 -193 85 C
ATOM 1648 CG LEU A 238 11.384 33.615 -16.821 1.00111.47 C
ANISOU 1648 CG LEU A 238 13831 16422 12102 -402 -188 112 C
ATOM 1649 CD1 LEU A 238 10.634 32.342 -16.413 1.00112.19 C
ANISOU 1649 CD1 LEU A 238 14010 16409 12207 -412 -96 97 C
ATOM 1650 CD2 LEU A 238 12.517 33.242 -17.759 1.00114.17 C
ANISOU 1650 CD2 LEU A 238 14105 16865 12411 -331 -264 136 C
ATOM 1651 N LYS A 239 9.456 37.605 -16.416 1.00104.85 N
ANISOU 1651 N LYS A 239 12838 15565 11437 -618 -206 24 N
ATOM 1652 CA LYS A 239 9.727 38.915 -15.808 1.00104.84 C
ANISOU 1652 CA LYS A 239 12833 15588 11414 -652 -245 23 C
ATOM 1653 C LYS A 239 8.824 39.144 -14.587 1.00110.06 C
ANISOU 1653 C LYS A 239 13563 16179 12076 -679 -180 -12 C
ATOM 1654 O LYS A 239 9.277 39.700 -13.584 1.00110.00 O
ANISOU 1654 O LYS A 239 13606 16182 12007 -681 -190 2 O
ATOM 1655 CB LYS A 239 9.484 40.036 -16.829 1.00106.72 C
ANISOU 1655 CB LYS A 239 13008 15833 11708 -694 -294 3 C
ATOM 1656 CG LYS A 239 10.620 40.257 -17.820 1.00117.67 C
ANISOU 1656 CG LYS A 239 14349 17302 13059 -706 -363 36 C
ATOM 1657 CD LYS A 239 10.136 40.938 -19.104 1.00124.82 C
ANISOU 1657 CD LYS A 239 15222 18186 14019 -724 -391 22 C
ATOM 1658 CE LYS A 239 9.885 42.422 -18.956 1.00132.91 C
ANISOU 1658 CE LYS A 239 16263 19204 15031 -783 -442 11 C
ATOM 1659 NZ LYS A 239 9.124 42.964 -20.111 1.00141.20 N
ANISOU 1659 NZ LYS A 239 17330 20174 16146 -777 -462 -31 N
ATOM 1660 N ARG A 240 7.545 38.715 -14.693 1.00107.33 N
ANISOU 1660 N ARG A 240 13214 15766 11799 -702 -110 -67 N
ATOM 1661 CA ARG A 240 6.510 38.829 -13.655 1.00107.68 C
ANISOU 1661 CA ARG A 240 13315 15749 11848 -742 -30 -119 C
ATOM 1662 C ARG A 240 6.692 37.809 -12.538 1.00112.10 C
ANISOU 1662 C ARG A 240 14004 16274 12315 -731 31 -91 C
ATOM 1663 O ARG A 240 6.194 38.023 -11.433 1.00112.32 O
ANISOU 1663 O ARG A 240 14103 16279 12294 -749 51 -94 O
ATOM 1664 CB ARG A 240 5.101 38.678 -14.263 1.00107.34 C
ANISOU 1664 CB ARG A 240 13226 15657 11900 -775 43 -209 C
ATOM 1665 CG ARG A 240 4.661 39.820 -15.175 1.00115.70 C
ANISOU 1665 CG ARG A 240 14186 16728 13048 -778 -16 -268 C
ATOM 1666 CD ARG A 240 4.315 41.118 -14.445 1.00123.81 C
ANISOU 1666 CD ARG A 240 15226 17754 14061 -795 -48 -284 C
ATOM 1667 NE ARG A 240 3.250 40.969 -13.446 1.00129.31 N
ANISOU 1667 NE ARG A 240 15915 18411 14807 -829 30 -388 N
ATOM 1668 CZ ARG A 240 1.950 40.912 -13.722 1.00140.08 C
ANISOU 1668 CZ ARG A 240 17207 19758 16259 -838 80 -495 C
ATOM 1669 NH1 ARG A 240 1.527 40.952 -14.981 1.00127.55 N
ANISOU 1669 NH1 ARG A 240 15563 18181 14719 -812 56 -503 N
ATOM 1670 NH2 ARG A 240 1.063 40.794 -12.745 1.00123.03 N
ANISOU 1670 NH2 ARG A 240 15028 17578 14140 -875 155 -605 N
ATOM 1671 N ARG A 241 7.343 36.675 -12.838 1.00108.26 N
ANISOU 1671 N ARG A 241 13567 15774 11794 -695 55 -64 N
ATOM 1672 CA ARG A 241 7.585 35.631 -11.848 1.00108.50 C
ANISOU 1672 CA ARG A 241 13757 15750 11717 -672 105 -40 C
ATOM 1673 C ARG A 241 8.890 35.903 -11.113 1.00111.68 C
ANISOU 1673 C ARG A 241 14199 16205 12028 -613 15 13 C
ATOM 1674 O ARG A 241 9.059 35.446 -9.981 1.00111.99 O
ANISOU 1674 O ARG A 241 14370 16197 11983 -607 40 18 O
ATOM 1675 CB ARG A 241 7.546 34.238 -12.480 1.00109.17 C
ANISOU 1675 CB ARG A 241 13908 15801 11771 -636 141 -22 C
ATOM 1676 CG ARG A 241 6.495 33.330 -11.841 1.00119.99 C
ANISOU 1676 CG ARG A 241 15419 17059 13113 -701 283 -69 C
ATOM 1677 CD ARG A 241 5.984 32.204 -12.747 1.00127.72 C
ANISOU 1677 CD ARG A 241 16380 18005 14142 -727 348 -99 C
ATOM 1678 NE ARG A 241 7.050 31.506 -13.475 1.00136.08 N
ANISOU 1678 NE ARG A 241 17477 19085 15142 -632 281 -32 N
ATOM 1679 CZ ARG A 241 7.922 30.663 -12.926 1.00152.16 C
ANISOU 1679 CZ ARG A 241 19661 21103 17048 -547 240 24 C
ATOM 1680 NH1 ARG A 241 7.883 30.408 -11.623 1.00141.12 N
ANISOU 1680 NH1 ARG A 241 18401 19658 15562 -550 259 27 N
ATOM 1681 NH2 ARG A 241 8.856 30.089 -13.672 1.00138.85 N
ANISOU 1681 NH2 ARG A 241 17992 19448 15318 -450 172 69 N
ATOM 1682 N ASN A1001 9.794 36.686 -11.744 1.00106.68 N
ANISOU 1682 N ASN A1001 13454 15672 11409 -575 -90 43 N
ATOM 1683 CA ASN A1001 11.062 37.117 -11.154 1.00106.09 C
ANISOU 1683 CA ASN A1001 13389 15669 11253 -525 -179 73 C
ATOM 1684 C ASN A1001 10.760 38.142 -10.067 1.00109.07 C
ANISOU 1684 C ASN A1001 13797 16021 11622 -578 -167 55 C
ATOM 1685 O ASN A1001 11.423 38.141 -9.031 1.00109.35 O
ANISOU 1685 O ASN A1001 13923 16056 11569 -542 -194 67 O
ATOM 1686 CB ASN A1001 11.983 37.719 -12.216 1.00105.61 C
ANISOU 1686 CB ASN A1001 13180 15723 11223 -517 -270 85 C
ATOM 1687 CG ASN A1001 12.984 36.760 -12.816 1.00120.86 C
ANISOU 1687 CG ASN A1001 15102 17725 13095 -424 -328 105 C
ATOM 1688 OD1 ASN A1001 12.986 35.553 -12.545 1.00114.91 O
ANISOU 1688 OD1 ASN A1001 14458 16919 12284 -355 -304 116 O
ATOM 1689 ND2 ASN A1001 13.871 37.289 -13.648 1.00109.21 N
ANISOU 1689 ND2 ASN A1001 13503 16365 11625 -423 -402 103 N
ATOM 1690 N ILE A1002 9.722 38.987 -10.293 1.00104.20 N
ANISOU 1690 N ILE A1002 13113 15382 11095 -653 -134 20 N
ATOM 1691 CA ILE A1002 9.232 39.988 -9.342 1.00103.54 C
ANISOU 1691 CA ILE A1002 13060 15273 11008 -702 -120 -4 C
ATOM 1692 C ILE A1002 8.602 39.281 -8.129 1.00105.68 C
ANISOU 1692 C ILE A1002 13483 15450 11221 -710 -26 -20 C
ATOM 1693 O ILE A1002 8.652 39.820 -7.025 1.00106.05 O
ANISOU 1693 O ILE A1002 13612 15480 11201 -712 -32 -14 O
ATOM 1694 CB ILE A1002 8.288 41.025 -10.032 1.00106.47 C
ANISOU 1694 CB ILE A1002 13337 15633 11485 -762 -111 -51 C
ATOM 1695 CG1 ILE A1002 8.485 42.434 -9.468 1.00107.03 C
ANISOU 1695 CG1 ILE A1002 13402 15725 11541 -793 -162 -55 C
ATOM 1696 CG2 ILE A1002 6.805 40.625 -10.006 1.00107.95 C
ANISOU 1696 CG2 ILE A1002 13543 15739 11733 -803 0 -121 C
ATOM 1697 CD1 ILE A1002 7.929 43.540 -10.369 1.00115.48 C
ANISOU 1697 CD1 ILE A1002 14408 16771 12698 -832 -165 -108 C
ATOM 1698 N PHE A1003 8.037 38.065 -8.343 1.00100.41 N
ANISOU 1698 N PHE A1003 12863 14716 10571 -725 67 -44 N
ATOM 1699 CA PHE A1003 7.422 37.228 -7.312 1.00100.39 C
ANISOU 1699 CA PHE A1003 13029 14611 10504 -757 180 -67 C
ATOM 1700 C PHE A1003 8.467 36.649 -6.371 1.00104.09 C
ANISOU 1700 C PHE A1003 13664 15059 10828 -679 138 -13 C
ATOM 1701 O PHE A1003 8.248 36.645 -5.162 1.00103.69 O
ANISOU 1701 O PHE A1003 13763 14937 10697 -698 186 -20 O
ATOM 1702 CB PHE A1003 6.555 36.121 -7.938 1.00102.14 C
ANISOU 1702 CB PHE A1003 13266 14773 10771 -802 292 -112 C
ATOM 1703 CG PHE A1003 6.035 35.077 -6.975 1.00104.50 C
ANISOU 1703 CG PHE A1003 13780 14960 10966 -829 407 -121 C
ATOM 1704 CD1 PHE A1003 4.872 35.298 -6.244 1.00108.16 C
ANISOU 1704 CD1 PHE A1003 14296 15347 11453 -941 558 -205 C
ATOM 1705 CD2 PHE A1003 6.699 33.864 -6.812 1.00107.05 C
ANISOU 1705 CD2 PHE A1003 14260 15252 11164 -743 366 -58 C
ATOM 1706 CE1 PHE A1003 4.384 34.324 -5.360 1.00110.07 C
ANISOU 1706 CE1 PHE A1003 14762 15473 11586 -987 680 -217 C
ATOM 1707 CE2 PHE A1003 6.220 32.898 -5.921 1.00110.84 C
ANISOU 1707 CE2 PHE A1003 14977 15607 11529 -767 470 -64 C
ATOM 1708 CZ PHE A1003 5.059 33.130 -5.209 1.00109.46 C
ANISOU 1708 CZ PHE A1003 14873 15347 11371 -900 635 -141 C
ATOM 1709 N GLU A1004 9.584 36.144 -6.932 1.00100.71 N
ANISOU 1709 N GLU A1004 13215 14691 10360 -586 43 34 N
ATOM 1710 CA GLU A1004 10.697 35.555 -6.181 1.00101.25 C
ANISOU 1710 CA GLU A1004 13435 14749 10287 -484 -21 70 C
ATOM 1711 C GLU A1004 11.391 36.607 -5.291 1.00104.50 C
ANISOU 1711 C GLU A1004 13847 15203 10654 -471 -94 74 C
ATOM 1712 O GLU A1004 11.848 36.275 -4.193 1.00104.69 O
ANISOU 1712 O GLU A1004 14045 15170 10561 -424 -104 82 O
ATOM 1713 CB GLU A1004 11.722 34.879 -7.128 1.00102.60 C
ANISOU 1713 CB GLU A1004 13537 15008 10438 -375 -126 100 C
ATOM 1714 CG GLU A1004 11.193 33.708 -7.958 1.00114.44 C
ANISOU 1714 CG GLU A1004 15086 16453 11942 -358 -69 105 C
ATOM 1715 CD GLU A1004 10.745 32.432 -7.262 1.00139.08 C
ANISOU 1715 CD GLU A1004 18469 19424 14951 -355 26 104 C
ATOM 1716 OE1 GLU A1004 11.077 32.234 -6.071 1.00141.92 O
ANISOU 1716 OE1 GLU A1004 18974 19718 15233 -370 51 98 O
ATOM 1717 OE2 GLU A1004 10.075 31.610 -7.929 1.00130.47 O
ANISOU 1717 OE2 GLU A1004 17455 18275 13844 -344 78 107 O
ATOM 1718 N MET A1005 11.444 37.875 -5.769 1.00 99.72 N
ANISOU 1718 N MET A1005 13062 14693 10134 -512 -150 67 N
ATOM 1719 CA MET A1005 12.050 39.028 -5.092 1.00 99.25 C
ANISOU 1719 CA MET A1005 12990 14683 10037 -513 -222 67 C
ATOM 1720 C MET A1005 11.301 39.363 -3.809 1.00104.30 C
ANISOU 1720 C MET A1005 13761 15225 10645 -571 -143 48 C
ATOM 1721 O MET A1005 11.924 39.542 -2.763 1.00104.78 O
ANISOU 1721 O MET A1005 13924 15277 10610 -532 -190 57 O
ATOM 1722 CB MET A1005 12.054 40.251 -6.025 1.00100.39 C
ANISOU 1722 CB MET A1005 12938 14928 10277 -568 -276 59 C
ATOM 1723 CG MET A1005 12.925 41.378 -5.530 1.00103.57 C
ANISOU 1723 CG MET A1005 13324 15372 10657 -601 -331 51 C
ATOM 1724 SD MET A1005 12.446 42.973 -6.223 1.00106.34 S
ANISOU 1724 SD MET A1005 13502 15785 11117 -695 -356 37 S
ATOM 1725 CE MET A1005 13.985 43.787 -6.177 1.00103.34 C
ANISOU 1725 CE MET A1005 13080 15515 10670 -700 -467 36 C
ATOM 1726 N LEU A1006 9.968 39.465 -3.905 1.00100.80 N
ANISOU 1726 N LEU A1006 13308 14712 10281 -664 -26 13 N
ATOM 1727 CA LEU A1006 9.102 39.778 -2.782 1.00101.04 C
ANISOU 1727 CA LEU A1006 13452 14653 10285 -730 64 -19 C
ATOM 1728 C LEU A1006 8.934 38.588 -1.833 1.00106.92 C
ANISOU 1728 C LEU A1006 14440 15287 10899 -704 130 -11 C
ATOM 1729 O LEU A1006 8.701 38.805 -0.646 1.00108.35 O
ANISOU 1729 O LEU A1006 14758 15412 10997 -712 146 -13 O
ATOM 1730 CB LEU A1006 7.748 40.307 -3.283 1.00100.63 C
ANISOU 1730 CB LEU A1006 13315 14568 10352 -828 175 -84 C
ATOM 1731 CG LEU A1006 7.563 41.838 -3.432 1.00104.53 C
ANISOU 1731 CG LEU A1006 13635 15137 10945 -855 109 -103 C
ATOM 1732 CD1 LEU A1006 7.773 42.589 -2.105 1.00105.03 C
ANISOU 1732 CD1 LEU A1006 13753 15193 10961 -874 85 -104 C
ATOM 1733 CD2 LEU A1006 8.397 42.422 -4.569 1.00106.02 C
ANISOU 1733 CD2 LEU A1006 13705 15428 11149 -800 -17 -54 C
ATOM 1734 N ARG A1007 9.078 37.343 -2.338 1.00103.48 N
ANISOU 1734 N ARG A1007 14078 14807 10431 -673 168 0 N
ATOM 1735 CA ARG A1007 8.997 36.101 -1.557 1.00104.47 C
ANISOU 1735 CA ARG A1007 14473 14804 10416 -654 238 7 C
ATOM 1736 C ARG A1007 10.102 36.089 -0.487 1.00109.31 C
ANISOU 1736 C ARG A1007 15220 15422 10890 -540 116 46 C
ATOM 1737 O ARG A1007 9.823 35.815 0.680 1.00109.74 O
ANISOU 1737 O ARG A1007 15498 15369 10830 -548 165 42 O
ATOM 1738 CB ARG A1007 9.103 34.879 -2.499 1.00105.05 C
ANISOU 1738 CB ARG A1007 14599 14840 10475 -625 274 17 C
ATOM 1739 CG ARG A1007 9.371 33.528 -1.834 1.00116.28 C
ANISOU 1739 CG ARG A1007 16276 16182 11724 -511 232 55 C
ATOM 1740 CD ARG A1007 9.740 32.472 -2.865 1.00124.77 C
ANISOU 1740 CD ARG A1007 17304 17293 12811 -431 183 79 C
ATOM 1741 NE ARG A1007 8.742 31.404 -2.929 1.00132.93 N
ANISOU 1741 NE ARG A1007 18540 18187 13782 -480 317 67 N
ATOM 1742 CZ ARG A1007 8.813 30.348 -3.735 1.00145.02 C
ANISOU 1742 CZ ARG A1007 20032 19724 15345 -461 328 73 C
ATOM 1743 NH1 ARG A1007 9.839 30.205 -4.565 1.00130.58 N
ANISOU 1743 NH1 ARG A1007 17969 18035 13612 -391 214 93 N
ATOM 1744 NH2 ARG A1007 7.859 29.427 -3.716 1.00131.09 N
ANISOU 1744 NH2 ARG A1007 18473 17822 13512 -521 460 57 N
ATOM 1745 N ILE A1008 11.340 36.426 -0.894 1.00105.75 N
ANISOU 1745 N ILE A1008 14634 15099 10447 -436 -43 72 N
ATOM 1746 CA ILE A1008 12.537 36.495 -0.050 1.00106.32 C
ANISOU 1746 CA ILE A1008 14802 15201 10393 -315 -179 89 C
ATOM 1747 C ILE A1008 12.442 37.655 0.965 1.00110.10 C
ANISOU 1747 C ILE A1008 15291 15677 10864 -372 -181 76 C
ATOM 1748 O ILE A1008 12.902 37.507 2.100 1.00111.02 O
ANISOU 1748 O ILE A1008 15601 15735 10848 -309 -222 80 O
ATOM 1749 CB ILE A1008 13.817 36.552 -0.958 1.00109.23 C
ANISOU 1749 CB ILE A1008 14983 15734 10786 -204 -340 95 C
ATOM 1750 CG1 ILE A1008 14.093 35.176 -1.618 1.00110.22 C
ANISOU 1750 CG1 ILE A1008 15177 15838 10864 -105 -356 108 C
ATOM 1751 CG2 ILE A1008 15.064 37.050 -0.208 1.00110.78 C
ANISOU 1751 CG2 ILE A1008 15181 16016 10896 -103 -493 83 C
ATOM 1752 CD1 ILE A1008 14.867 35.212 -2.973 1.00117.68 C
ANISOU 1752 CD1 ILE A1008 15883 16943 11887 -49 -454 103 C
ATOM 1753 N ASP A1009 11.822 38.785 0.568 1.00105.28 N
ANISOU 1753 N ASP A1009 14493 15121 10388 -484 -140 58 N
ATOM 1754 CA ASP A1009 11.717 39.976 1.409 1.00104.87 C
ANISOU 1754 CA ASP A1009 14430 15075 10342 -542 -145 43 C
ATOM 1755 C ASP A1009 10.451 40.048 2.269 1.00110.89 C
ANISOU 1755 C ASP A1009 15335 15703 11095 -646 13 14 C
ATOM 1756 O ASP A1009 10.571 39.972 3.496 1.00111.99 O
ANISOU 1756 O ASP A1009 15671 15763 11117 -629 22 17 O
ATOM 1757 CB ASP A1009 11.880 41.249 0.570 1.00104.89 C
ANISOU 1757 CB ASP A1009 14180 15201 10472 -596 -200 35 C
ATOM 1758 CG ASP A1009 13.220 41.382 -0.126 1.00106.76 C
ANISOU 1758 CG ASP A1009 14277 15582 10704 -520 -350 48 C
ATOM 1759 OD1 ASP A1009 14.177 40.687 0.282 1.00106.49 O
ANISOU 1759 OD1 ASP A1009 14328 15571 10563 -407 -438 55 O
ATOM 1760 OD2 ASP A1009 13.319 42.200 -1.055 1.00109.38 O
ANISOU 1760 OD2 ASP A1009 14422 16005 11134 -572 -380 42 O
ATOM 1761 N GLU A1010 9.256 40.228 1.656 1.00107.50 N
ANISOU 1761 N GLU A1010 14806 15254 10786 -751 134 -25 N
ATOM 1762 CA GLU A1010 7.996 40.325 2.404 1.00108.47 C
ANISOU 1762 CA GLU A1010 15029 15270 10914 -861 296 -80 C
ATOM 1763 C GLU A1010 7.551 38.984 3.010 1.00114.79 C
ANISOU 1763 C GLU A1010 16081 15931 11603 -881 422 -89 C
ATOM 1764 O GLU A1010 6.824 38.981 4.007 1.00115.13 O
ANISOU 1764 O GLU A1010 16281 15872 11592 -963 547 -128 O
ATOM 1765 CB GLU A1010 6.874 40.977 1.580 1.00109.20 C
ANISOU 1765 CB GLU A1010 14920 15400 11170 -954 372 -144 C
ATOM 1766 CG GLU A1010 6.856 42.496 1.674 1.00120.43 C
ANISOU 1766 CG GLU A1010 16215 16886 12658 -977 311 -161 C
ATOM 1767 CD GLU A1010 5.486 43.152 1.682 1.00140.48 C
ANISOU 1767 CD GLU A1010 18665 19407 15304 -1070 421 -253 C
ATOM 1768 OE1 GLU A1010 4.931 43.389 0.585 1.00133.87 O
ANISOU 1768 OE1 GLU A1010 17654 18623 14587 -1080 414 -291 O
ATOM 1769 OE2 GLU A1010 4.987 43.472 2.785 1.00132.53 O
ANISOU 1769 OE2 GLU A1010 17762 18337 14258 -1125 506 -296 O
ATOM 1770 N GLY A1011 8.011 37.876 2.430 1.00112.39 N
ANISOU 1770 N GLY A1011 15830 15619 11254 -809 388 -54 N
ATOM 1771 CA GLY A1011 7.714 36.539 2.928 1.00113.90 C
ANISOU 1771 CA GLY A1011 16292 15667 11318 -818 493 -55 C
ATOM 1772 C GLY A1011 6.403 35.968 2.441 1.00119.25 C
ANISOU 1772 C GLY A1011 16954 16286 12068 -952 678 -119 C
ATOM 1773 O GLY A1011 5.378 36.654 2.460 1.00118.49 O
ANISOU 1773 O GLY A1011 16732 16207 12081 -1069 782 -191 O
ATOM 1774 N LEU A1012 6.434 34.692 2.027 1.00117.47 N
ANISOU 1774 N LEU A1012 16864 15992 11777 -931 718 -104 N
ATOM 1775 CA LEU A1012 5.276 33.954 1.526 1.00118.06 C
ANISOU 1775 CA LEU A1012 16946 16007 11904 -1059 895 -170 C
ATOM 1776 C LEU A1012 4.656 33.086 2.635 1.00124.91 C
ANISOU 1776 C LEU A1012 18150 16693 12616 -1162 1074 -206 C
ATOM 1777 O LEU A1012 5.291 32.135 3.095 1.00125.85 O
ANISOU 1777 O LEU A1012 18554 16704 12560 -1083 1042 -151 O
ATOM 1778 CB LEU A1012 5.694 33.101 0.305 1.00117.54 C
ANISOU 1778 CB LEU A1012 16815 15981 11864 -980 829 -131 C
ATOM 1779 CG LEU A1012 4.605 32.309 -0.422 1.00122.19 C
ANISOU 1779 CG LEU A1012 17379 16528 12518 -1099 987 -197 C
ATOM 1780 CD1 LEU A1012 3.733 33.212 -1.256 1.00121.29 C
ANISOU 1780 CD1 LEU A1012 16944 16530 12610 -1180 1017 -273 C
ATOM 1781 CD2 LEU A1012 5.217 31.258 -1.312 1.00124.42 C
ANISOU 1781 CD2 LEU A1012 17702 16810 12763 -1000 915 -141 C
ATOM 1782 N ARG A1013 3.423 33.430 3.068 1.00122.53 N
ANISOU 1782 N ARG A1013 17824 16358 12373 -1337 1261 -308 N
ATOM 1783 CA ARG A1013 2.683 32.701 4.106 1.00124.27 C
ANISOU 1783 CA ARG A1013 18351 16410 12457 -1479 1469 -366 C
ATOM 1784 C ARG A1013 1.331 32.233 3.584 1.00128.83 C
ANISOU 1784 C ARG A1013 18850 16974 13125 -1665 1681 -488 C
ATOM 1785 O ARG A1013 0.555 33.034 3.063 1.00127.54 O
ANISOU 1785 O ARG A1013 18393 16926 13142 -1735 1720 -579 O
ATOM 1786 CB ARG A1013 2.536 33.523 5.401 1.00125.44 C
ANISOU 1786 CB ARG A1013 18597 16517 12548 -1527 1511 -389 C
ATOM 1787 CG ARG A1013 3.815 33.578 6.232 1.00137.91 C
ANISOU 1787 CG ARG A1013 20401 18041 13959 -1369 1349 -282 C
ATOM 1788 CD ARG A1013 3.597 34.166 7.613 1.00152.27 C
ANISOU 1788 CD ARG A1013 22385 19781 15688 -1432 1418 -308 C
ATOM 1789 NE ARG A1013 3.025 33.192 8.546 1.00166.86 N
ANISOU 1789 NE ARG A1013 24601 21433 17365 -1566 1625 -353 N
ATOM 1790 CZ ARG A1013 2.888 33.393 9.855 1.00184.66 C
ANISOU 1790 CZ ARG A1013 27107 23571 19484 -1624 1703 -368 C
ATOM 1791 NH1 ARG A1013 3.289 34.533 10.405 1.00171.71 N
ANISOU 1791 NH1 ARG A1013 25381 21996 17865 -1550 1585 -340 N
ATOM 1792 NH2 ARG A1013 2.355 32.452 10.625 1.00174.24 N
ANISOU 1792 NH2 ARG A1013 26140 22064 18000 -1762 1906 -413 N
ATOM 1793 N LEU A1014 1.060 30.928 3.721 1.00127.14 N
ANISOU 1793 N LEU A1014 18908 16619 12781 -1741 1813 -500 N
ATOM 1794 CA LEU A1014 -0.160 30.280 3.234 1.00127.87 C
ANISOU 1794 CA LEU A1014 18965 16686 12934 -1930 2027 -623 C
ATOM 1795 C LEU A1014 -1.352 30.361 4.210 1.00133.79 C
ANISOU 1795 C LEU A1014 19806 17366 13661 -2155 2278 -765 C
ATOM 1796 O LEU A1014 -2.463 29.973 3.846 1.00133.97 O
ANISOU 1796 O LEU A1014 19724 17409 13770 -2329 2461 -904 O
ATOM 1797 CB LEU A1014 0.145 28.822 2.831 1.00128.67 C
ANISOU 1797 CB LEU A1014 19332 16662 12896 -1918 2059 -573 C
ATOM 1798 CG LEU A1014 1.309 28.613 1.839 1.00131.88 C
ANISOU 1798 CG LEU A1014 19664 17134 13312 -1696 1823 -445 C
ATOM 1799 CD1 LEU A1014 1.827 27.191 1.888 1.00133.17 C
ANISOU 1799 CD1 LEU A1014 20204 17130 13266 -1648 1833 -379 C
ATOM 1800 CD2 LEU A1014 0.925 29.007 0.421 1.00132.27 C
ANISOU 1800 CD2 LEU A1014 19333 17345 13580 -1691 1778 -483 C
ATOM 1801 N LYS A1015 -1.131 30.899 5.423 1.00131.54 N
ANISOU 1801 N LYS A1015 19700 17012 13266 -2155 2287 -743 N
ATOM 1802 CA LYS A1015 -2.166 31.063 6.452 1.00133.07 C
ANISOU 1802 CA LYS A1015 20000 17138 13423 -2362 2522 -875 C
ATOM 1803 C LYS A1015 -2.371 32.546 6.791 1.00136.31 C
ANISOU 1803 C LYS A1015 20147 17677 13968 -2338 2463 -919 C
ATOM 1804 O LYS A1015 -1.402 33.309 6.748 1.00134.40 O
ANISOU 1804 O LYS A1015 19813 17504 13750 -2153 2237 -805 O
ATOM 1805 CB LYS A1015 -1.798 30.277 7.725 1.00137.47 C
ANISOU 1805 CB LYS A1015 21053 17472 13707 -2401 2608 -821 C
ATOM 1806 CG LYS A1015 -1.763 28.763 7.542 1.00154.33 C
ANISOU 1806 CG LYS A1015 23517 19446 15675 -2442 2691 -790 C
ATOM 1807 CD LYS A1015 -1.069 28.078 8.708 1.00166.24 C
ANISOU 1807 CD LYS A1015 25537 20730 16896 -2409 2701 -706 C
ATOM 1808 CE LYS A1015 -0.759 26.633 8.409 1.00177.86 C
ANISOU 1808 CE LYS A1015 27352 22039 18189 -2390 2721 -650 C
ATOM 1809 NZ LYS A1015 0.011 26.000 9.510 1.00188.90 N
ANISOU 1809 NZ LYS A1015 29274 23208 19291 -2328 2705 -569 N
ATOM 1810 N ILE A1016 -3.624 32.954 7.129 1.00134.10 N
ANISOU 1810 N ILE A1016 19750 17429 13771 -2527 2667 -1094 N
ATOM 1811 CA ILE A1016 -3.952 34.341 7.504 1.00133.54 C
ANISOU 1811 CA ILE A1016 19450 17469 13819 -2514 2632 -1158 C
ATOM 1812 C ILE A1016 -3.175 34.705 8.773 1.00139.12 C
ANISOU 1812 C ILE A1016 20430 18071 14359 -2451 2573 -1054 C
ATOM 1813 O ILE A1016 -3.367 34.080 9.818 1.00140.50 O
ANISOU 1813 O ILE A1016 20947 18083 14353 -2572 2739 -1074 O
ATOM 1814 CB ILE A1016 -5.481 34.627 7.640 1.00137.46 C
ANISOU 1814 CB ILE A1016 19770 18027 14433 -2726 2870 -1391 C
ATOM 1815 CG1 ILE A1016 -6.228 34.419 6.303 1.00137.38 C
ANISOU 1815 CG1 ILE A1016 19454 18141 14604 -2769 2902 -1509 C
ATOM 1816 CG2 ILE A1016 -5.722 36.046 8.179 1.00137.54 C
ANISOU 1816 CG2 ILE A1016 19588 18132 14538 -2689 2819 -1446 C
ATOM 1817 CD1 ILE A1016 -7.768 34.490 6.381 1.00145.23 C
ANISOU 1817 CD1 ILE A1016 20271 19203 15707 -2985 3149 -1772 C
ATOM 1818 N TYR A1017 -2.276 35.692 8.657 1.00135.12 N
ANISOU 1818 N TYR A1017 19784 17653 13904 -2265 2337 -947 N
ATOM 1819 CA TYR A1017 -1.414 36.147 9.744 1.00135.46 C
ANISOU 1819 CA TYR A1017 20040 17623 13806 -2176 2238 -845 C
ATOM 1820 C TYR A1017 -1.585 37.631 10.050 1.00139.78 C
ANISOU 1820 C TYR A1017 20362 18279 14468 -2148 2173 -883 C
ATOM 1821 O TYR A1017 -1.839 38.425 9.143 1.00138.28 O
ANISOU 1821 O TYR A1017 19831 18242 14467 -2100 2085 -922 O
ATOM 1822 CB TYR A1017 0.064 35.807 9.444 1.00135.77 C
ANISOU 1822 CB TYR A1017 20184 17648 13754 -1965 1996 -667 C
ATOM 1823 CG TYR A1017 0.680 36.543 8.267 1.00135.59 C
ANISOU 1823 CG TYR A1017 19816 17802 13899 -1810 1773 -607 C
ATOM 1824 CD1 TYR A1017 0.406 36.160 6.955 1.00136.77 C
ANISOU 1824 CD1 TYR A1017 19757 18033 14176 -1809 1764 -631 C
ATOM 1825 CD2 TYR A1017 1.606 37.564 8.466 1.00135.35 C
ANISOU 1825 CD2 TYR A1017 19694 17848 13884 -1670 1571 -524 C
ATOM 1826 CE1 TYR A1017 0.983 36.821 5.871 1.00135.50 C
ANISOU 1826 CE1 TYR A1017 19307 18022 14155 -1676 1568 -577 C
ATOM 1827 CE2 TYR A1017 2.203 38.221 7.389 1.00134.60 C
ANISOU 1827 CE2 TYR A1017 19311 17905 13927 -1548 1381 -474 C
ATOM 1828 CZ TYR A1017 1.886 37.847 6.093 1.00140.39 C
ANISOU 1828 CZ TYR A1017 19848 18711 14782 -1551 1381 -499 C
ATOM 1829 OH TYR A1017 2.461 38.495 5.028 1.00139.25 O
ANISOU 1829 OH TYR A1017 19443 18705 14762 -1441 1204 -451 O
ATOM 1830 N LYS A1018 -1.442 37.999 11.331 1.00138.03 N
ANISOU 1830 N LYS A1018 20354 17970 14123 -2174 2212 -873 N
ATOM 1831 CA LYS A1018 -1.532 39.384 11.781 1.00137.74 C
ANISOU 1831 CA LYS A1018 20155 18015 14166 -2145 2150 -901 C
ATOM 1832 C LYS A1018 -0.180 40.051 11.505 1.00141.41 C
ANISOU 1832 C LYS A1018 20554 18546 14631 -1935 1865 -746 C
ATOM 1833 O LYS A1018 0.855 39.556 11.963 1.00140.96 O
ANISOU 1833 O LYS A1018 20744 18401 14412 -1841 1766 -628 O
ATOM 1834 CB LYS A1018 -1.899 39.441 13.278 1.00141.78 C
ANISOU 1834 CB LYS A1018 20937 18398 14535 -2265 2316 -954 C
ATOM 1835 CG LYS A1018 -2.314 40.829 13.766 1.00154.44 C
ANISOU 1835 CG LYS A1018 22359 20086 16236 -2273 2307 -1026 C
ATOM 1836 CD LYS A1018 -2.903 40.804 15.172 1.00165.45 C
ANISOU 1836 CD LYS A1018 24004 21357 17501 -2421 2510 -1106 C
ATOM 1837 CE LYS A1018 -4.410 40.688 15.171 1.00177.21 C
ANISOU 1837 CE LYS A1018 25381 22873 19077 -2630 2781 -1319 C
ATOM 1838 NZ LYS A1018 -4.978 40.853 16.534 1.00187.44 N
ANISOU 1838 NZ LYS A1018 26882 24073 20265 -2773 2973 -1410 N
ATOM 1839 N ASP A1019 -0.188 41.145 10.719 1.00137.96 N
ANISOU 1839 N ASP A1019 19787 18263 14368 -1862 1733 -756 N
ATOM 1840 CA ASP A1019 1.028 41.881 10.359 1.00137.12 C
ANISOU 1840 CA ASP A1019 19586 18237 14276 -1692 1479 -629 C
ATOM 1841 C ASP A1019 1.465 42.868 11.468 1.00142.77 C
ANISOU 1841 C ASP A1019 20393 18931 14921 -1661 1415 -599 C
ATOM 1842 O ASP A1019 0.809 42.946 12.513 1.00143.50 O
ANISOU 1842 O ASP A1019 20628 18943 14954 -1767 1571 -672 O
ATOM 1843 CB ASP A1019 0.879 42.559 8.974 1.00137.49 C
ANISOU 1843 CB ASP A1019 19282 18439 14518 -1634 1366 -647 C
ATOM 1844 CG ASP A1019 0.296 43.963 8.967 1.00146.38 C
ANISOU 1844 CG ASP A1019 20195 19651 15771 -1647 1347 -728 C
ATOM 1845 OD1 ASP A1019 -0.848 44.135 9.437 1.00147.52 O
ANISOU 1845 OD1 ASP A1019 20330 19773 15948 -1760 1517 -860 O
ATOM 1846 OD2 ASP A1019 0.974 44.882 8.459 1.00151.02 O
ANISOU 1846 OD2 ASP A1019 20629 20329 16423 -1545 1166 -668 O
ATOM 1847 N THR A1020 2.585 43.602 11.239 1.00139.31 N
ANISOU 1847 N THR A1020 19878 18568 14486 -1524 1193 -497 N
ATOM 1848 CA THR A1020 3.160 44.590 12.169 1.00139.46 C
ANISOU 1848 CA THR A1020 19963 18582 14442 -1480 1100 -458 C
ATOM 1849 C THR A1020 2.146 45.681 12.546 1.00144.12 C
ANISOU 1849 C THR A1020 20428 19202 15129 -1565 1190 -563 C
ATOM 1850 O THR A1020 2.107 46.104 13.705 1.00144.52 O
ANISOU 1850 O THR A1020 20630 19187 15094 -1596 1232 -575 O
ATOM 1851 CB THR A1020 4.479 45.178 11.621 1.00145.39 C
ANISOU 1851 CB THR A1020 20605 19433 15203 -1337 854 -353 C
ATOM 1852 OG1 THR A1020 4.207 46.006 10.488 1.00143.74 O
ANISOU 1852 OG1 THR A1020 20096 19353 15165 -1325 786 -376 O
ATOM 1853 CG2 THR A1020 5.507 44.102 11.260 1.00143.56 C
ANISOU 1853 CG2 THR A1020 20489 19184 14873 -1237 757 -268 C
ATOM 1854 N GLU A1021 1.311 46.099 11.563 1.00140.31 N
ANISOU 1854 N GLU A1021 19680 18814 14818 -1593 1219 -647 N
ATOM 1855 CA GLU A1021 0.249 47.104 11.695 1.00140.32 C
ANISOU 1855 CA GLU A1021 19525 18861 14931 -1652 1292 -771 C
ATOM 1856 C GLU A1021 -0.855 46.660 12.672 1.00145.82 C
ANISOU 1856 C GLU A1021 20352 19471 15583 -1797 1537 -899 C
ATOM 1857 O GLU A1021 -1.398 47.494 13.400 1.00146.29 O
ANISOU 1857 O GLU A1021 20382 19534 15666 -1838 1595 -983 O
ATOM 1858 CB GLU A1021 -0.376 47.418 10.324 1.00140.89 C
ANISOU 1858 CB GLU A1021 19304 19045 15182 -1630 1256 -840 C
ATOM 1859 CG GLU A1021 0.520 48.157 9.344 1.00150.18 C
ANISOU 1859 CG GLU A1021 20326 20314 16421 -1509 1032 -748 C
ATOM 1860 CD GLU A1021 -0.143 48.456 8.012 1.00167.87 C
ANISOU 1860 CD GLU A1021 22312 22647 18824 -1485 999 -824 C
ATOM 1861 OE1 GLU A1021 0.116 47.714 7.036 1.00153.86 O
ANISOU 1861 OE1 GLU A1021 20469 20905 17087 -1454 957 -784 O
ATOM 1862 OE2 GLU A1021 -0.931 49.427 7.947 1.00163.25 O
ANISOU 1862 OE2 GLU A1021 21604 22099 18326 -1488 1009 -930 O
ATOM 1863 N GLY A1022 -1.173 45.364 12.667 1.00142.62 N
ANISOU 1863 N GLY A1022 20092 18987 15110 -1878 1682 -918 N
ATOM 1864 CA GLY A1022 -2.200 44.775 13.522 1.00143.74 C
ANISOU 1864 CA GLY A1022 20382 19038 15193 -2044 1938 -1045 C
ATOM 1865 C GLY A1022 -3.390 44.218 12.763 1.00147.32 C
ANISOU 1865 C GLY A1022 20664 19543 15768 -2154 2104 -1200 C
ATOM 1866 O GLY A1022 -4.267 43.593 13.367 1.00148.12 O
ANISOU 1866 O GLY A1022 20882 19576 15822 -2316 2339 -1322 O
ATOM 1867 N TYR A1023 -3.428 44.441 11.430 1.00142.37 N
ANISOU 1867 N TYR A1023 19762 19036 15295 -2074 1986 -1206 N
ATOM 1868 CA TYR A1023 -4.497 43.971 10.539 1.00142.14 C
ANISOU 1868 CA TYR A1023 19534 19075 15398 -2153 2106 -1356 C
ATOM 1869 C TYR A1023 -4.150 42.610 9.919 1.00144.96 C
ANISOU 1869 C TYR A1023 19992 19382 15703 -2171 2131 -1288 C
ATOM 1870 O TYR A1023 -2.979 42.223 9.896 1.00143.72 O
ANISOU 1870 O TYR A1023 19996 19170 15440 -2077 2001 -1118 O
ATOM 1871 CB TYR A1023 -4.819 45.015 9.447 1.00142.19 C
ANISOU 1871 CB TYR A1023 19200 19231 15595 -2049 1962 -1416 C
ATOM 1872 CG TYR A1023 -4.724 46.461 9.893 1.00143.57 C
ANISOU 1872 CG TYR A1023 19304 19446 15799 -1970 1848 -1416 C
ATOM 1873 CD1 TYR A1023 -5.589 46.975 10.856 1.00146.75 C
ANISOU 1873 CD1 TYR A1023 19721 19839 16200 -2055 1988 -1556 C
ATOM 1874 CD2 TYR A1023 -3.803 47.329 9.316 1.00142.91 C
ANISOU 1874 CD2 TYR A1023 19137 19416 15748 -1819 1609 -1289 C
ATOM 1875 CE1 TYR A1023 -5.516 48.308 11.256 1.00147.35 C
ANISOU 1875 CE1 TYR A1023 19740 19948 16300 -1977 1881 -1559 C
ATOM 1876 CE2 TYR A1023 -3.719 48.663 9.710 1.00143.57 C
ANISOU 1876 CE2 TYR A1023 19174 19527 15850 -1754 1507 -1291 C
ATOM 1877 CZ TYR A1023 -4.577 49.149 10.681 1.00152.37 C
ANISOU 1877 CZ TYR A1023 20310 20624 16958 -1827 1639 -1423 C
ATOM 1878 OH TYR A1023 -4.496 50.464 11.071 1.00153.39 O
ANISOU 1878 OH TYR A1023 20406 20775 17101 -1758 1536 -1425 O
ATOM 1879 N TYR A1024 -5.168 41.877 9.434 1.00141.67 N
ANISOU 1879 N TYR A1024 19483 18989 15358 -2291 2299 -1432 N
ATOM 1880 CA TYR A1024 -4.974 40.547 8.857 1.00141.22 C
ANISOU 1880 CA TYR A1024 19529 18878 15251 -2326 2345 -1385 C
ATOM 1881 C TYR A1024 -4.481 40.573 7.412 1.00142.32 C
ANISOU 1881 C TYR A1024 19456 19115 15504 -2185 2150 -1307 C
ATOM 1882 O TYR A1024 -5.038 41.292 6.581 1.00140.96 O
ANISOU 1882 O TYR A1024 18989 19068 15500 -2142 2087 -1397 O
ATOM 1883 CB TYR A1024 -6.242 39.694 9.000 1.00144.18 C
ANISOU 1883 CB TYR A1024 19921 19224 15635 -2538 2624 -1576 C
ATOM 1884 CG TYR A1024 -6.579 39.351 10.437 1.00147.91 C
ANISOU 1884 CG TYR A1024 20693 19561 15946 -2701 2842 -1629 C
ATOM 1885 CD1 TYR A1024 -5.937 38.306 11.095 1.00150.62 C
ANISOU 1885 CD1 TYR A1024 21421 19731 16078 -2744 2903 -1514 C
ATOM 1886 CD2 TYR A1024 -7.537 40.075 11.140 1.00149.74 C
ANISOU 1886 CD2 TYR A1024 20838 19832 16226 -2808 2985 -1799 C
ATOM 1887 CE1 TYR A1024 -6.235 37.993 12.421 1.00152.92 C
ANISOU 1887 CE1 TYR A1024 22023 19878 16201 -2896 3104 -1559 C
ATOM 1888 CE2 TYR A1024 -7.848 39.768 12.464 1.00152.33 C
ANISOU 1888 CE2 TYR A1024 21452 20029 16396 -2969 3196 -1851 C
ATOM 1889 CZ TYR A1024 -7.193 38.725 13.102 1.00160.37 C
ANISOU 1889 CZ TYR A1024 22872 20863 17197 -3017 3257 -1727 C
ATOM 1890 OH TYR A1024 -7.494 38.418 14.408 1.00163.25 O
ANISOU 1890 OH TYR A1024 23554 21083 17391 -3179 3466 -1776 O
ATOM 1891 N THR A1025 -3.414 39.791 7.131 1.00137.98 N
ANISOU 1891 N THR A1025 19070 18505 14853 -2105 2049 -1143 N
ATOM 1892 CA THR A1025 -2.778 39.644 5.811 1.00136.31 C
ANISOU 1892 CA THR A1025 18704 18369 14718 -1976 1872 -1052 C
ATOM 1893 C THR A1025 -2.600 38.160 5.427 1.00140.15 C
ANISOU 1893 C THR A1025 19347 18777 15125 -2014 1942 -1012 C
ATOM 1894 O THR A1025 -2.681 37.289 6.297 1.00141.16 O
ANISOU 1894 O THR A1025 19763 18771 15100 -2114 2091 -1014 O
ATOM 1895 CB THR A1025 -1.430 40.400 5.735 1.00142.88 C
ANISOU 1895 CB THR A1025 19531 19237 15521 -1802 1626 -886 C
ATOM 1896 OG1 THR A1025 -0.543 39.906 6.736 1.00143.53 O
ANISOU 1896 OG1 THR A1025 19915 19205 15416 -1779 1615 -779 O
ATOM 1897 CG2 THR A1025 -1.577 41.913 5.853 1.00140.49 C
ANISOU 1897 CG2 THR A1025 19033 19026 15322 -1752 1529 -922 C
ATOM 1898 N ILE A1026 -2.354 37.880 4.125 1.00135.05 N
ANISOU 1898 N ILE A1026 18532 18207 14572 -1936 1834 -976 N
ATOM 1899 CA ILE A1026 -2.138 36.529 3.578 1.00134.82 C
ANISOU 1899 CA ILE A1026 18624 18119 14484 -1951 1875 -934 C
ATOM 1900 C ILE A1026 -1.277 36.580 2.296 1.00136.45 C
ANISOU 1900 C ILE A1026 18673 18412 14759 -1790 1661 -821 C
ATOM 1901 O ILE A1026 -1.508 37.421 1.424 1.00135.19 O
ANISOU 1901 O ILE A1026 18238 18374 14753 -1733 1559 -853 O
ATOM 1902 CB ILE A1026 -3.471 35.729 3.400 1.00139.14 C
ANISOU 1902 CB ILE A1026 19136 18649 15082 -2137 2109 -1107 C
ATOM 1903 CG1 ILE A1026 -3.219 34.272 2.944 1.00139.90 C
ANISOU 1903 CG1 ILE A1026 19403 18660 15091 -2165 2163 -1059 C
ATOM 1904 CG2 ILE A1026 -4.464 36.452 2.486 1.00139.45 C
ANISOU 1904 CG2 ILE A1026 18808 18839 15337 -2148 2099 -1253 C
ATOM 1905 CD1 ILE A1026 -4.009 33.228 3.653 1.00148.07 C
ANISOU 1905 CD1 ILE A1026 20701 19557 16000 -2365 2421 -1150 C
ATOM 1906 N GLY A1027 -0.301 35.681 2.207 1.00132.11 N
ANISOU 1906 N GLY A1027 18315 17794 14086 -1715 1596 -698 N
ATOM 1907 CA GLY A1027 0.606 35.603 1.068 1.00130.30 C
ANISOU 1907 CA GLY A1027 17967 17641 13901 -1568 1409 -594 C
ATOM 1908 C GLY A1027 1.746 36.585 1.201 1.00132.22 C
ANISOU 1908 C GLY A1027 18152 17952 14134 -1426 1204 -489 C
ATOM 1909 O GLY A1027 2.426 36.608 2.230 1.00132.41 O
ANISOU 1909 O GLY A1027 18378 17911 14020 -1384 1167 -423 O
ATOM 1910 N ILE A1028 1.947 37.420 0.171 1.00126.65 N
ANISOU 1910 N ILE A1028 17181 17373 13567 -1356 1071 -480 N
ATOM 1911 CA ILE A1028 3.009 38.425 0.163 1.00125.11 C
ANISOU 1911 CA ILE A1028 16908 17254 13373 -1242 883 -393 C
ATOM 1912 C ILE A1028 2.409 39.837 0.383 1.00127.71 C
ANISOU 1912 C ILE A1028 17083 17640 13802 -1278 877 -463 C
ATOM 1913 O ILE A1028 2.055 40.539 -0.574 1.00126.69 O
ANISOU 1913 O ILE A1028 16736 17596 13806 -1262 820 -503 O
ATOM 1914 CB ILE A1028 3.929 38.291 -1.093 1.00127.13 C
ANISOU 1914 CB ILE A1028 17034 17597 13671 -1132 726 -314 C
ATOM 1915 CG1 ILE A1028 4.607 36.895 -1.137 1.00127.89 C
ANISOU 1915 CG1 ILE A1028 17310 17633 13651 -1078 724 -248 C
ATOM 1916 CG2 ILE A1028 4.982 39.399 -1.129 1.00127.13 C
ANISOU 1916 CG2 ILE A1028 16946 17684 13673 -1042 551 -244 C
ATOM 1917 CD1 ILE A1028 5.273 36.501 -2.474 1.00133.57 C
ANISOU 1917 CD1 ILE A1028 17900 18430 14420 -990 612 -195 C
ATOM 1918 N GLY A1029 2.275 40.195 1.664 1.00123.94 N
ANISOU 1918 N GLY A1029 16742 17103 13247 -1321 936 -480 N
ATOM 1919 CA GLY A1029 1.767 41.477 2.148 1.00123.26 C
ANISOU 1919 CA GLY A1029 16562 17049 13222 -1351 937 -543 C
ATOM 1920 C GLY A1029 0.435 41.946 1.597 1.00126.00 C
ANISOU 1920 C GLY A1029 16711 17443 13719 -1416 1019 -686 C
ATOM 1921 O GLY A1029 0.268 43.142 1.338 1.00125.02 O
ANISOU 1921 O GLY A1029 16433 17387 13681 -1379 932 -716 O
ATOM 1922 N HIS A1030 -0.521 41.014 1.412 1.00122.46 N
ANISOU 1922 N HIS A1030 16270 16961 13297 -1512 1182 -784 N
ATOM 1923 CA HIS A1030 -1.858 41.332 0.902 1.00122.18 C
ANISOU 1923 CA HIS A1030 16035 16982 13405 -1574 1267 -951 C
ATOM 1924 C HIS A1030 -2.832 41.502 2.069 1.00127.08 C
ANISOU 1924 C HIS A1030 16717 17560 14007 -1694 1444 -1083 C
ATOM 1925 O HIS A1030 -3.164 40.523 2.741 1.00127.37 O
ANISOU 1925 O HIS A1030 16930 17510 13953 -1807 1615 -1116 O
ATOM 1926 CB HIS A1030 -2.347 40.265 -0.097 1.00122.78 C
ANISOU 1926 CB HIS A1030 16043 17069 13539 -1612 1335 -1003 C
ATOM 1927 CG HIS A1030 -3.708 40.540 -0.656 1.00126.52 C
ANISOU 1927 CG HIS A1030 16295 17613 14163 -1664 1408 -1191 C
ATOM 1928 ND1 HIS A1030 -3.878 41.316 -1.786 1.00127.49 N
ANISOU 1928 ND1 HIS A1030 16195 17830 14415 -1567 1265 -1219 N
ATOM 1929 CD2 HIS A1030 -4.922 40.137 -0.216 1.00129.63 C
ANISOU 1929 CD2 HIS A1030 16664 18000 14589 -1801 1605 -1369 C
ATOM 1930 CE1 HIS A1030 -5.183 41.362 -1.997 1.00127.79 C
ANISOU 1930 CE1 HIS A1030 16075 17917 14563 -1627 1362 -1415 C
ATOM 1931 NE2 HIS A1030 -5.853 40.671 -1.074 1.00129.44 N
ANISOU 1931 NE2 HIS A1030 16380 18077 14724 -1774 1573 -1517 N
ATOM 1932 N LEU A1031 -3.280 42.748 2.310 1.00123.74 N
ANISOU 1932 N LEU A1031 16163 17193 13659 -1671 1404 -1161 N
ATOM 1933 CA LEU A1031 -4.206 43.069 3.394 1.00124.79 C
ANISOU 1933 CA LEU A1031 16327 17303 13785 -1775 1562 -1300 C
ATOM 1934 C LEU A1031 -5.633 42.710 3.018 1.00130.48 C
ANISOU 1934 C LEU A1031 16890 18071 14616 -1879 1724 -1513 C
ATOM 1935 O LEU A1031 -6.097 43.052 1.925 1.00129.80 O
ANISOU 1935 O LEU A1031 16578 18075 14664 -1818 1647 -1589 O
ATOM 1936 CB LEU A1031 -4.102 44.544 3.798 1.00124.39 C
ANISOU 1936 CB LEU A1031 16201 17293 13767 -1699 1450 -1307 C
ATOM 1937 CG LEU A1031 -4.452 44.844 5.247 1.00129.89 C
ANISOU 1937 CG LEU A1031 17027 17935 14392 -1786 1580 -1372 C
ATOM 1938 CD1 LEU A1031 -3.245 45.357 5.993 1.00129.63 C
ANISOU 1938 CD1 LEU A1031 17195 17836 14223 -1732 1481 -1200 C
ATOM 1939 CD2 LEU A1031 -5.600 45.831 5.338 1.00132.29 C
ANISOU 1939 CD2 LEU A1031 17140 18314 14811 -1771 1583 -1539 C
ATOM 1940 N LEU A1032 -6.323 42.013 3.935 1.00128.91 N
ANISOU 1940 N LEU A1032 16819 17809 14353 -2040 1952 -1617 N
ATOM 1941 CA LEU A1032 -7.701 41.559 3.760 1.00130.21 C
ANISOU 1941 CA LEU A1032 16849 18018 14605 -2176 2145 -1844 C
ATOM 1942 C LEU A1032 -8.700 42.636 4.218 1.00136.53 C
ANISOU 1942 C LEU A1032 17481 18897 15498 -2195 2196 -2038 C
ATOM 1943 O LEU A1032 -9.477 43.127 3.394 1.00136.34 O
ANISOU 1943 O LEU A1032 17189 18989 15626 -2145 2149 -2192 O
ATOM 1944 CB LEU A1032 -7.920 40.209 4.479 1.00131.27 C
ANISOU 1944 CB LEU A1032 17230 18038 14608 -2361 2381 -1864 C
ATOM 1945 CG LEU A1032 -7.067 39.032 3.981 1.00134.75 C
ANISOU 1945 CG LEU A1032 17841 18400 14957 -2339 2341 -1699 C
ATOM 1946 CD1 LEU A1032 -6.886 37.993 5.060 1.00135.75 C
ANISOU 1946 CD1 LEU A1032 18326 18366 14886 -2469 2510 -1645 C
ATOM 1947 CD2 LEU A1032 -7.655 38.412 2.727 1.00137.08 C
ANISOU 1947 CD2 LEU A1032 17952 18765 15368 -2369 2371 -1797 C
ATOM 1948 N THR A1033 -8.648 43.021 5.518 1.00134.67 N
ANISOU 1948 N THR A1033 17407 18598 15165 -2251 2276 -2030 N
ATOM 1949 CA THR A1033 -9.475 44.067 6.146 1.00135.71 C
ANISOU 1949 CA THR A1033 17418 18789 15358 -2264 2325 -2198 C
ATOM 1950 C THR A1033 -8.834 44.612 7.422 1.00139.88 C
ANISOU 1950 C THR A1033 18167 19227 15754 -2259 2314 -2084 C
ATOM 1951 O THR A1033 -8.140 43.881 8.138 1.00139.48 O
ANISOU 1951 O THR A1033 18397 19054 15546 -2319 2372 -1944 O
ATOM 1952 CB THR A1033 -10.935 43.623 6.429 1.00146.23 C
ANISOU 1952 CB THR A1033 18639 20170 16750 -2447 2585 -2478 C
ATOM 1953 OG1 THR A1033 -11.057 42.200 6.429 1.00147.14 O
ANISOU 1953 OG1 THR A1033 18903 20214 16791 -2611 2769 -2482 O
ATOM 1954 CG2 THR A1033 -11.939 44.260 5.477 1.00144.59 C
ANISOU 1954 CG2 THR A1033 18076 20124 16738 -2374 2525 -2696 C
ATOM 1955 N LYS A1034 -9.111 45.895 7.721 1.00136.58 N
ANISOU 1955 N LYS A1034 17632 18867 15395 -2184 2240 -2155 N
ATOM 1956 CA LYS A1034 -8.643 46.580 8.926 1.00136.47 C
ANISOU 1956 CA LYS A1034 17797 18783 15273 -2177 2230 -2076 C
ATOM 1957 C LYS A1034 -9.519 46.210 10.146 1.00142.34 C
ANISOU 1957 C LYS A1034 18651 19480 15953 -2369 2505 -2238 C
ATOM 1958 O LYS A1034 -9.264 46.684 11.259 1.00142.03 O
ANISOU 1958 O LYS A1034 18776 19373 15816 -2389 2535 -2198 O
ATOM 1959 CB LYS A1034 -8.579 48.104 8.694 1.00138.13 C
ANISOU 1959 CB LYS A1034 17850 19067 15565 -2016 2031 -2082 C
ATOM 1960 CG LYS A1034 -7.325 48.553 7.942 1.00146.50 C
ANISOU 1960 CG LYS A1034 18933 20122 16610 -1856 1772 -1861 C
ATOM 1961 CD LYS A1034 -7.572 49.758 7.031 1.00152.48 C
ANISOU 1961 CD LYS A1034 19474 20971 17490 -1702 1581 -1913 C
ATOM 1962 CE LYS A1034 -7.616 49.371 5.569 1.00156.27 C
ANISOU 1962 CE LYS A1034 19782 21518 18074 -1633 1485 -1925 C
ATOM 1963 NZ LYS A1034 -7.539 50.556 4.675 1.00159.07 N
ANISOU 1963 NZ LYS A1034 19989 21935 18517 -1471 1276 -1944 N
ATOM 1964 N SER A1035 -10.537 45.337 9.921 1.00140.45 N
ANISOU 1964 N SER A1035 18328 19272 15763 -2519 2712 -2423 N
ATOM 1965 CA SER A1035 -11.475 44.819 10.922 1.00142.36 C
ANISOU 1965 CA SER A1035 18661 19480 15951 -2739 3010 -2608 C
ATOM 1966 C SER A1035 -10.753 43.864 11.888 1.00147.20 C
ANISOU 1966 C SER A1035 19673 19910 16348 -2858 3131 -2451 C
ATOM 1967 O SER A1035 -9.971 43.021 11.436 1.00145.84 O
ANISOU 1967 O SER A1035 19639 19667 16106 -2830 3066 -2287 O
ATOM 1968 CB SER A1035 -12.643 44.104 10.244 1.00146.43 C
ANISOU 1968 CB SER A1035 18963 20091 16583 -2864 3176 -2845 C
ATOM 1969 OG SER A1035 -13.563 43.576 11.186 1.00155.09 O
ANISOU 1969 OG SER A1035 20145 21159 17624 -3105 3485 -3042 O
ATOM 1970 N PRO A1036 -11.000 43.974 13.216 1.00145.70 N
ANISOU 1970 N PRO A1036 19683 19635 16041 -2984 3302 -2502 N
ATOM 1971 CA PRO A1036 -10.292 43.099 14.167 1.00146.09 C
ANISOU 1971 CA PRO A1036 20149 19494 15866 -3081 3402 -2351 C
ATOM 1972 C PRO A1036 -10.827 41.662 14.271 1.00151.18 C
ANISOU 1972 C PRO A1036 20963 20054 16426 -3305 3666 -2442 C
ATOM 1973 O PRO A1036 -10.167 40.822 14.892 1.00151.26 O
ANISOU 1973 O PRO A1036 21345 19890 16237 -3364 3725 -2304 O
ATOM 1974 CB PRO A1036 -10.390 43.858 15.502 1.00148.72 C
ANISOU 1974 CB PRO A1036 20626 19769 16110 -3123 3475 -2380 C
ATOM 1975 CG PRO A1036 -11.135 45.145 15.206 1.00152.99 C
ANISOU 1975 CG PRO A1036 20814 20478 16836 -3039 3405 -2542 C
ATOM 1976 CD PRO A1036 -11.872 44.926 13.928 1.00148.44 C
ANISOU 1976 CD PRO A1036 19909 20049 16444 -3028 3398 -2692 C
ATOM 1977 N SER A1037 -12.001 41.368 13.669 1.00148.10 N
ANISOU 1977 N SER A1037 20315 19781 16175 -3426 3820 -2678 N
ATOM 1978 CA SER A1037 -12.578 40.023 13.701 1.00149.30 C
ANISOU 1978 CA SER A1037 20608 19864 16255 -3660 4084 -2786 C
ATOM 1979 C SER A1037 -11.937 39.137 12.634 1.00151.52 C
ANISOU 1979 C SER A1037 20924 20115 16530 -3582 3960 -2634 C
ATOM 1980 O SER A1037 -11.880 39.523 11.463 1.00149.64 O
ANISOU 1980 O SER A1037 20387 20012 16458 -3423 3765 -2621 O
ATOM 1981 CB SER A1037 -14.094 40.072 13.530 1.00154.55 C
ANISOU 1981 CB SER A1037 20968 20681 17073 -3830 4302 -3121 C
ATOM 1982 OG SER A1037 -14.694 38.852 13.936 1.00164.83 O
ANISOU 1982 OG SER A1037 22455 21898 18273 -4107 4608 -3248 O
ATOM 1983 N LEU A1038 -11.436 37.955 13.055 1.00148.43 N
ANISOU 1983 N LEU A1038 20921 19538 15937 -3686 4067 -2518 N
ATOM 1984 CA LEU A1038 -10.780 36.957 12.199 1.00147.12 C
ANISOU 1984 CA LEU A1038 20857 19314 15727 -3625 3973 -2370 C
ATOM 1985 C LEU A1038 -11.747 36.374 11.165 1.00151.37 C
ANISOU 1985 C LEU A1038 21133 19967 16412 -3738 4088 -2557 C
ATOM 1986 O LEU A1038 -11.323 36.065 10.053 1.00149.60 O
ANISOU 1986 O LEU A1038 20789 19790 16262 -3610 3923 -2463 O
ATOM 1987 CB LEU A1038 -10.180 35.830 13.058 1.00148.15 C
ANISOU 1987 CB LEU A1038 21500 19204 15586 -3726 4090 -2240 C
ATOM 1988 CG LEU A1038 -8.899 35.178 12.539 1.00151.25 C
ANISOU 1988 CG LEU A1038 22083 19504 15881 -3556 3884 -1996 C
ATOM 1989 CD1 LEU A1038 -7.940 34.899 13.678 1.00151.90 C
ANISOU 1989 CD1 LEU A1038 22615 19386 15715 -3499 3835 -1812 C
ATOM 1990 CD2 LEU A1038 -9.195 33.894 11.798 1.00153.68 C
ANISOU 1990 CD2 LEU A1038 22468 19763 16160 -3688 4023 -2047 C
ATOM 1991 N ASN A1039 -13.037 36.222 11.536 1.00149.80 N
ANISOU 1991 N ASN A1039 20844 19818 16256 -3980 4373 -2830 N
ATOM 1992 CA ASN A1039 -14.100 35.707 10.667 1.00150.30 C
ANISOU 1992 CA ASN A1039 20640 20006 16463 -4116 4513 -3058 C
ATOM 1993 C ASN A1039 -14.470 36.727 9.585 1.00152.76 C
ANISOU 1993 C ASN A1039 20461 20547 17034 -3929 4306 -3154 C
ATOM 1994 O ASN A1039 -14.822 36.332 8.472 1.00152.01 O
ANISOU 1994 O ASN A1039 20150 20547 17060 -3915 4270 -3225 O
ATOM 1995 CB ASN A1039 -15.329 35.316 11.487 1.00152.96 C
ANISOU 1995 CB ASN A1039 21024 20335 16757 -4438 4884 -3339 C
ATOM 1996 CG ASN A1039 -15.066 34.203 12.469 1.00173.63 C
ANISOU 1996 CG ASN A1039 24151 22711 19108 -4653 5114 -3267 C
ATOM 1997 OD1 ASN A1039 -14.950 33.028 12.102 1.00166.95 O
ANISOU 1997 OD1 ASN A1039 23474 21776 18182 -4760 5205 -3242 O
ATOM 1998 ND2 ASN A1039 -14.961 34.553 13.742 1.00166.11 N
ANISOU 1998 ND2 ASN A1039 23476 21637 18002 -4716 5208 -3231 N
ATOM 1999 N ALA A1040 -14.380 38.036 9.914 1.00148.57 N
ANISOU 1999 N ALA A1040 19777 20095 16577 -3781 4165 -3154 N
ATOM 2000 CA ALA A1040 -14.648 39.145 8.995 1.00147.15 C
ANISOU 2000 CA ALA A1040 19184 20109 16616 -3576 3944 -3228 C
ATOM 2001 C ALA A1040 -13.520 39.237 7.964 1.00148.54 C
ANISOU 2001 C ALA A1040 19345 20276 16817 -3334 3638 -2971 C
ATOM 2002 O ALA A1040 -13.780 39.524 6.793 1.00147.41 O
ANISOU 2002 O ALA A1040 18905 20266 16838 -3215 3494 -3031 O
ATOM 2003 CB ALA A1040 -14.760 40.451 9.769 1.00147.87 C
ANISOU 2003 CB ALA A1040 19200 20248 16737 -3491 3884 -3271 C
ATOM 2004 N ALA A1041 -12.274 38.968 8.404 1.00143.93 N
ANISOU 2004 N ALA A1041 19087 19535 16063 -3265 3542 -2698 N
ATOM 2005 CA ALA A1041 -11.081 38.964 7.558 1.00141.55 C
ANISOU 2005 CA ALA A1041 18814 19213 15755 -3056 3273 -2448 C
ATOM 2006 C ALA A1041 -11.054 37.714 6.672 1.00145.39 C
ANISOU 2006 C ALA A1041 19340 19671 16232 -3115 3320 -2427 C
ATOM 2007 O ALA A1041 -10.617 37.798 5.525 1.00143.62 O
ANISOU 2007 O ALA A1041 18966 19508 16094 -2957 3120 -2331 O
ATOM 2008 CB ALA A1041 -9.832 39.029 8.417 1.00141.55 C
ANISOU 2008 CB ALA A1041 19146 19066 15572 -2977 3178 -2204 C
ATOM 2009 N LYS A1042 -11.536 36.563 7.200 1.00143.67 N
ANISOU 2009 N LYS A1042 19332 19354 15903 -3350 3593 -2522 N
ATOM 2010 CA LYS A1042 -11.630 35.280 6.489 1.00143.86 C
ANISOU 2010 CA LYS A1042 19431 19333 15898 -3449 3685 -2528 C
ATOM 2011 C LYS A1042 -12.629 35.388 5.331 1.00148.56 C
ANISOU 2011 C LYS A1042 19623 20111 16712 -3457 3682 -2735 C
ATOM 2012 O LYS A1042 -12.461 34.715 4.313 1.00147.41 O
ANISOU 2012 O LYS A1042 19427 19979 16604 -3416 3614 -2685 O
ATOM 2013 CB LYS A1042 -12.086 34.170 7.448 1.00148.24 C
ANISOU 2013 CB LYS A1042 20308 19738 16277 -3730 4007 -2623 C
ATOM 2014 CG LYS A1042 -10.974 33.324 8.042 1.00158.39 C
ANISOU 2014 CG LYS A1042 22050 20806 17324 -3728 4004 -2396 C
ATOM 2015 CD LYS A1042 -11.518 32.454 9.167 1.00169.30 C
ANISOU 2015 CD LYS A1042 23802 22020 18506 -3988 4308 -2480 C
ATOM 2016 CE LYS A1042 -10.657 31.250 9.449 1.00180.12 C
ANISOU 2016 CE LYS A1042 25622 23172 19645 -4053 4378 -2338 C
ATOM 2017 NZ LYS A1042 -11.461 29.999 9.440 1.00190.08 N
ANISOU 2017 NZ LYS A1042 26857 24436 20929 -4251 4572 -2484 N
ATOM 2018 N SER A1043 -13.668 36.235 5.504 1.00146.65 N
ANISOU 2018 N SER A1043 19099 20012 16610 -3499 3749 -2973 N
ATOM 2019 CA SER A1043 -14.730 36.503 4.531 1.00147.20 C
ANISOU 2019 CA SER A1043 18764 20272 16892 -3492 3741 -3213 C
ATOM 2020 C SER A1043 -14.204 37.237 3.286 1.00149.67 C
ANISOU 2020 C SER A1043 18839 20684 17343 -3212 3413 -3099 C
ATOM 2021 O SER A1043 -14.763 37.070 2.201 1.00148.97 O
ANISOU 2021 O SER A1043 18495 20710 17395 -3183 3369 -3225 O
ATOM 2022 CB SER A1043 -15.850 37.308 5.185 1.00152.36 C
ANISOU 2022 CB SER A1043 19208 21044 17638 -3586 3882 -3495 C
ATOM 2023 OG SER A1043 -17.033 37.298 4.402 1.00162.12 O
ANISOU 2023 OG SER A1043 20088 22456 19056 -3636 3940 -3782 O
ATOM 2024 N GLU A1044 -13.136 38.045 3.446 1.00145.50 N
ANISOU 2024 N GLU A1044 18403 20110 16769 -3014 3190 -2870 N
ATOM 2025 CA GLU A1044 -12.503 38.793 2.355 1.00143.91 C
ANISOU 2025 CA GLU A1044 18027 19982 16669 -2761 2886 -2741 C
ATOM 2026 C GLU A1044 -11.676 37.866 1.465 1.00148.78 C
ANISOU 2026 C GLU A1044 18749 20539 17243 -2707 2791 -2555 C
ATOM 2027 O GLU A1044 -11.645 38.063 0.250 1.00147.37 O
ANISOU 2027 O GLU A1044 18361 20448 17184 -2579 2630 -2557 O
ATOM 2028 CB GLU A1044 -11.633 39.936 2.896 1.00143.94 C
ANISOU 2028 CB GLU A1044 18110 19955 16626 -2600 2704 -2571 C
ATOM 2029 CG GLU A1044 -12.420 41.060 3.546 1.00154.29 C
ANISOU 2029 CG GLU A1044 19275 21345 18005 -2600 2739 -2749 C
ATOM 2030 CD GLU A1044 -13.052 42.039 2.579 1.00172.20 C
ANISOU 2030 CD GLU A1044 21199 23770 20460 -2445 2576 -2899 C
ATOM 2031 OE1 GLU A1044 -14.182 41.768 2.114 1.00166.45 O
ANISOU 2031 OE1 GLU A1044 20245 23149 19850 -2516 2677 -3148 O
ATOM 2032 OE2 GLU A1044 -12.426 43.087 2.300 1.00164.09 O
ANISOU 2032 OE2 GLU A1044 20136 22756 19454 -2253 2346 -2778 O
ATOM 2033 N LEU A1045 -11.012 36.855 2.072 1.00147.22 N
ANISOU 2033 N LEU A1045 18884 20186 16865 -2797 2888 -2401 N
ATOM 2034 CA LEU A1045 -10.194 35.854 1.376 1.00146.90 C
ANISOU 2034 CA LEU A1045 18991 20071 16755 -2754 2819 -2225 C
ATOM 2035 C LEU A1045 -11.074 34.930 0.525 1.00152.17 C
ANISOU 2035 C LEU A1045 19525 20788 17504 -2875 2945 -2388 C
ATOM 2036 O LEU A1045 -10.758 34.695 -0.642 1.00150.25 O
ANISOU 2036 O LEU A1045 19165 20591 17333 -2763 2800 -2323 O
ATOM 2037 CB LEU A1045 -9.349 35.044 2.387 1.00147.59 C
ANISOU 2037 CB LEU A1045 19491 19972 16614 -2822 2906 -2057 C
ATOM 2038 CG LEU A1045 -8.340 34.028 1.822 1.00151.86 C
ANISOU 2038 CG LEU A1045 20233 20417 17049 -2751 2818 -1858 C
ATOM 2039 CD1 LEU A1045 -7.241 34.708 1.012 1.00149.92 C
ANISOU 2039 CD1 LEU A1045 19874 20231 16856 -2502 2518 -1671 C
ATOM 2040 CD2 LEU A1045 -7.722 33.209 2.931 1.00155.53 C
ANISOU 2040 CD2 LEU A1045 21121 20693 17280 -2827 2925 -1742 C
ATOM 2041 N ASP A1046 -12.196 34.446 1.106 1.00151.73 N
ANISOU 2041 N ASP A1046 19477 20732 17440 -3109 3218 -2612 N
ATOM 2042 CA ASP A1046 -13.195 33.592 0.451 1.00153.09 C
ANISOU 2042 CA ASP A1046 19515 20963 17691 -3268 3380 -2816 C
ATOM 2043 C ASP A1046 -13.908 34.347 -0.698 1.00157.63 C
ANISOU 2043 C ASP A1046 19663 21736 18495 -3149 3241 -2985 C
ATOM 2044 O ASP A1046 -14.582 33.721 -1.522 1.00157.98 O
ANISOU 2044 O ASP A1046 19555 21845 18624 -3220 3302 -3126 O
ATOM 2045 CB ASP A1046 -14.217 33.067 1.487 1.00157.16 C
ANISOU 2045 CB ASP A1046 20135 21441 18137 -3561 3717 -3036 C
ATOM 2046 CG ASP A1046 -13.709 31.980 2.425 1.00164.97 C
ANISOU 2046 CG ASP A1046 21582 22215 18884 -3720 3894 -2906 C
ATOM 2047 OD1 ASP A1046 -12.570 32.107 2.927 1.00163.69 O
ANISOU 2047 OD1 ASP A1046 21672 21932 18589 -3586 3758 -2655 O
ATOM 2048 OD2 ASP A1046 -14.475 31.033 2.705 1.00171.57 O
ANISOU 2048 OD2 ASP A1046 22529 23001 19657 -3981 4172 -3069 O
ATOM 2049 N LYS A1047 -13.729 35.689 -0.746 1.00153.63 N
ANISOU 2049 N LYS A1047 18983 21313 18077 -2962 3049 -2970 N
ATOM 2050 CA LYS A1047 -14.276 36.610 -1.744 1.00153.19 C
ANISOU 2050 CA LYS A1047 18565 21425 18217 -2805 2876 -3111 C
ATOM 2051 C LYS A1047 -13.211 36.962 -2.802 1.00154.94 C
ANISOU 2051 C LYS A1047 18765 21641 18463 -2564 2581 -2881 C
ATOM 2052 O LYS A1047 -13.545 37.070 -3.985 1.00154.09 O
ANISOU 2052 O LYS A1047 18433 21629 18484 -2469 2462 -2961 O
ATOM 2053 CB LYS A1047 -14.797 37.880 -1.049 1.00156.33 C
ANISOU 2053 CB LYS A1047 18820 21903 18677 -2757 2858 -3250 C
ATOM 2054 CG LYS A1047 -15.752 38.721 -1.894 1.00171.86 C
ANISOU 2054 CG LYS A1047 20410 24049 20841 -2634 2738 -3486 C
ATOM 2055 CD LYS A1047 -16.261 39.965 -1.149 1.00182.77 C
ANISOU 2055 CD LYS A1047 21671 25502 22272 -2578 2721 -3628 C
ATOM 2056 CE LYS A1047 -15.240 41.076 -0.995 1.00192.27 C
ANISOU 2056 CE LYS A1047 22979 26648 23426 -2374 2490 -3397 C
ATOM 2057 NZ LYS A1047 -14.791 41.627 -2.303 1.00200.27 N
ANISOU 2057 NZ LYS A1047 23879 27698 24516 -2140 2202 -3287 N
ATOM 2058 N ALA A1048 -11.938 37.139 -2.372 1.00150.18 N
ANISOU 2058 N ALA A1048 18397 20929 17736 -2470 2467 -2609 N
ATOM 2059 CA ALA A1048 -10.798 37.462 -3.242 1.00147.98 C
ANISOU 2059 CA ALA A1048 18128 20640 17459 -2263 2207 -2383 C
ATOM 2060 C ALA A1048 -10.422 36.271 -4.126 1.00151.33 C
ANISOU 2060 C ALA A1048 18625 21021 17854 -2282 2207 -2290 C
ATOM 2061 O ALA A1048 -10.191 36.446 -5.325 1.00149.75 O
ANISOU 2061 O ALA A1048 18288 20876 17736 -2145 2032 -2242 O
ATOM 2062 CB ALA A1048 -9.600 37.893 -2.407 1.00147.67 C
ANISOU 2062 CB ALA A1048 18311 20508 17289 -2186 2115 -2154 C
ATOM 2063 N ILE A1049 -10.370 35.065 -3.526 1.00148.87 N
ANISOU 2063 N ILE A1049 18547 20601 17415 -2451 2405 -2265 N
ATOM 2064 CA ILE A1049 -10.062 33.800 -4.202 1.00148.53 C
ANISOU 2064 CA ILE A1049 18618 20496 17319 -2493 2438 -2186 C
ATOM 2065 C ILE A1049 -11.336 33.276 -4.907 1.00153.78 C
ANISOU 2065 C ILE A1049 19073 21249 18106 -2617 2568 -2432 C
ATOM 2066 O ILE A1049 -11.256 32.783 -6.036 1.00152.84 O
ANISOU 2066 O ILE A1049 18868 21161 18045 -2559 2484 -2409 O
ATOM 2067 CB ILE A1049 -9.461 32.758 -3.193 1.00152.14 C
ANISOU 2067 CB ILE A1049 19459 20783 17566 -2611 2587 -2057 C
ATOM 2068 CG1 ILE A1049 -8.236 33.322 -2.401 1.00151.35 C
ANISOU 2068 CG1 ILE A1049 19556 20606 17344 -2479 2449 -1834 C
ATOM 2069 CG2 ILE A1049 -9.132 31.406 -3.855 1.00152.94 C
ANISOU 2069 CG2 ILE A1049 19706 20807 17598 -2656 2631 -1985 C
ATOM 2070 CD1 ILE A1049 -6.900 33.576 -3.176 1.00156.73 C
ANISOU 2070 CD1 ILE A1049 20231 21298 18020 -2256 2183 -1608 C
ATOM 2071 N GLY A1050 -12.484 33.421 -4.237 1.00151.79 N
ANISOU 2071 N GLY A1050 18735 21046 17894 -2785 2768 -2673 N
ATOM 2072 CA GLY A1050 -13.783 32.961 -4.721 1.00152.92 C
ANISOU 2072 CA GLY A1050 18666 21286 18151 -2932 2920 -2950 C
ATOM 2073 C GLY A1050 -13.969 31.484 -4.448 1.00157.23 C
ANISOU 2073 C GLY A1050 19446 21722 18574 -3163 3162 -2967 C
ATOM 2074 O GLY A1050 -14.665 30.786 -5.190 1.00157.63 O
ANISOU 2074 O GLY A1050 19383 21820 18690 -3250 3234 -3099 O
ATOM 2075 N ARG A1051 -13.327 31.008 -3.371 1.00153.43 N
ANISOU 2075 N ARG A1051 19313 21082 17903 -3258 3283 -2833 N
ATOM 2076 CA ARG A1051 -13.307 29.617 -2.929 1.00154.09 C
ANISOU 2076 CA ARG A1051 19719 21011 17816 -3466 3505 -2806 C
ATOM 2077 C ARG A1051 -13.295 29.575 -1.394 1.00158.09 C
ANISOU 2077 C ARG A1051 20513 21395 18159 -3612 3690 -2799 C
ATOM 2078 O ARG A1051 -12.720 30.462 -0.760 1.00156.58 O
ANISOU 2078 O ARG A1051 20366 21190 17939 -3480 3568 -2680 O
ATOM 2079 CB ARG A1051 -12.040 28.940 -3.497 1.00152.45 C
ANISOU 2079 CB ARG A1051 19731 20690 17503 -3319 3341 -2525 C
ATOM 2080 CG ARG A1051 -11.904 27.437 -3.249 1.00162.14 C
ANISOU 2080 CG ARG A1051 21309 21748 18550 -3489 3525 -2475 C
ATOM 2081 CD ARG A1051 -10.535 26.914 -3.655 1.00167.26 C
ANISOU 2081 CD ARG A1051 22174 22290 19087 -3304 3335 -2193 C
ATOM 2082 NE ARG A1051 -9.460 27.425 -2.797 1.00171.05 N
ANISOU 2082 NE ARG A1051 22858 22687 19446 -3157 3206 -1988 N
ATOM 2083 CZ ARG A1051 -8.997 26.804 -1.716 1.00183.02 C
ANISOU 2083 CZ ARG A1051 24774 24023 20744 -3224 3306 -1887 C
ATOM 2084 NH1 ARG A1051 -9.507 25.638 -1.340 1.00172.46 N
ANISOU 2084 NH1 ARG A1051 23703 22553 19270 -3444 3547 -1963 N
ATOM 2085 NH2 ARG A1051 -8.018 27.345 -1.003 1.00166.24 N
ANISOU 2085 NH2 ARG A1051 22796 21842 18524 -3071 3165 -1715 N
ATOM 2086 N ASN A1052 -13.927 28.544 -0.804 1.00156.00 N
ANISOU 2086 N ASN A1052 20460 21033 17778 -3889 3986 -2925 N
ATOM 2087 CA ASN A1052 -13.952 28.341 0.643 1.00156.77 C
ANISOU 2087 CA ASN A1052 20884 20989 17694 -4055 4188 -2923 C
ATOM 2088 C ASN A1052 -12.553 27.883 1.085 1.00158.89 C
ANISOU 2088 C ASN A1052 21569 21056 17747 -3932 4075 -2612 C
ATOM 2089 O ASN A1052 -12.224 26.694 1.016 1.00158.88 O
ANISOU 2089 O ASN A1052 21865 20906 17595 -4014 4159 -2532 O
ATOM 2090 CB ASN A1052 -15.054 27.346 1.034 1.00159.56 C
ANISOU 2090 CB ASN A1052 21341 21300 17984 -4405 4548 -3168 C
ATOM 2091 CG ASN A1052 -16.459 27.915 1.006 1.00180.17 C
ANISOU 2091 CG ASN A1052 23540 24120 20796 -4536 4678 -3510 C
ATOM 2092 OD1 ASN A1052 -16.683 29.132 1.085 1.00172.32 O
ANISOU 2092 OD1 ASN A1052 22267 23267 19940 -4413 4567 -3588 O
ATOM 2093 ND2 ASN A1052 -17.447 27.035 0.954 1.00173.39 N
ANISOU 2093 ND2 ASN A1052 22647 23284 19948 -4798 4927 -3737 N
ATOM 2094 N THR A1053 -11.710 28.866 1.463 1.00153.46 N
ANISOU 2094 N THR A1053 20880 20374 17053 -3715 3861 -2443 N
ATOM 2095 CA THR A1053 -10.303 28.698 1.853 1.00151.77 C
ANISOU 2095 CA THR A1053 20990 20011 16665 -3546 3698 -2159 C
ATOM 2096 C THR A1053 -10.084 28.237 3.294 1.00157.10 C
ANISOU 2096 C THR A1053 22100 20489 17101 -3678 3869 -2115 C
ATOM 2097 O THR A1053 -9.183 27.428 3.528 1.00156.84 O
ANISOU 2097 O THR A1053 22429 20287 16876 -3619 3822 -1932 O
ATOM 2098 CB THR A1053 -9.514 29.991 1.600 1.00154.17 C
ANISOU 2098 CB THR A1053 21084 20422 17073 -3271 3400 -2019 C
ATOM 2099 OG1 THR A1053 -10.132 31.057 2.321 1.00151.83 O
ANISOU 2099 OG1 THR A1053 20636 20203 16848 -3310 3449 -2145 O
ATOM 2100 CG2 THR A1053 -9.412 30.343 0.122 1.00150.98 C
ANISOU 2100 CG2 THR A1053 20334 20171 16859 -3107 3196 -2007 C
ATOM 2101 N ASN A1054 -10.876 28.781 4.256 1.00154.52 N
ANISOU 2101 N ASN A1054 21743 20184 16784 -3842 4054 -2285 N
ATOM 2102 CA ASN A1054 -10.799 28.527 5.709 1.00155.63 C
ANISOU 2102 CA ASN A1054 22278 20147 16708 -3983 4232 -2271 C
ATOM 2103 C ASN A1054 -9.452 28.982 6.320 1.00157.55 C
ANISOU 2103 C ASN A1054 22745 20294 16822 -3753 4007 -2018 C
ATOM 2104 O ASN A1054 -8.939 28.351 7.253 1.00158.22 O
ANISOU 2104 O ASN A1054 23269 20178 16671 -3802 4084 -1922 O
ATOM 2105 CB ASN A1054 -11.137 27.071 6.073 1.00157.62 C
ANISOU 2105 CB ASN A1054 22923 20208 16759 -4234 4501 -2321 C
ATOM 2106 CG ASN A1054 -12.569 26.710 5.806 1.00177.40 C
ANISOU 2106 CG ASN A1054 25241 22800 19364 -4524 4786 -2615 C
ATOM 2107 OD1 ASN A1054 -12.935 26.318 4.696 1.00169.84 O
ANISOU 2107 OD1 ASN A1054 24040 21950 18543 -4536 4770 -2696 O
ATOM 2108 ND2 ASN A1054 -13.409 26.841 6.819 1.00170.50 N
ANISOU 2108 ND2 ASN A1054 24472 21888 18424 -4767 5055 -2792 N
ATOM 2109 N GLY A1055 -8.915 30.085 5.790 1.00151.18 N
ANISOU 2109 N GLY A1055 21640 19634 16168 -3508 3734 -1925 N
ATOM 2110 CA GLY A1055 -7.658 30.681 6.232 1.00149.24 C
ANISOU 2110 CA GLY A1055 21520 19343 15840 -3281 3499 -1708 C
ATOM 2111 C GLY A1055 -6.413 30.161 5.539 1.00150.78 C
ANISOU 2111 C GLY A1055 21822 19494 15973 -3068 3267 -1490 C
ATOM 2112 O GLY A1055 -5.361 30.800 5.612 1.00148.80 O
ANISOU 2112 O GLY A1055 21566 19264 15707 -2856 3035 -1331 O
ATOM 2113 N VAL A1056 -6.518 29.001 4.864 1.00147.30 N
ANISOU 2113 N VAL A1056 21476 18998 15494 -3126 3331 -1492 N
ATOM 2114 CA VAL A1056 -5.401 28.355 4.166 1.00145.70 C
ANISOU 2114 CA VAL A1056 21386 18749 15223 -2935 3132 -1304 C
ATOM 2115 C VAL A1056 -5.565 28.435 2.634 1.00146.88 C
ANISOU 2115 C VAL A1056 21164 19063 15580 -2856 3016 -1327 C
ATOM 2116 O VAL A1056 -6.626 28.094 2.106 1.00147.13 O
ANISOU 2116 O VAL A1056 21040 19150 15714 -3019 3176 -1492 O
ATOM 2117 CB VAL A1056 -5.158 26.898 4.669 1.00151.35 C
ANISOU 2117 CB VAL A1056 22587 19235 15685 -3026 3265 -1251 C
ATOM 2118 CG1 VAL A1056 -3.879 26.306 4.076 1.00150.16 C
ANISOU 2118 CG1 VAL A1056 22567 19038 15450 -2794 3035 -1056 C
ATOM 2119 CG2 VAL A1056 -5.114 26.831 6.198 1.00152.78 C
ANISOU 2119 CG2 VAL A1056 23159 19240 15651 -3119 3394 -1244 C
ATOM 2120 N ILE A1057 -4.503 28.900 1.938 1.00140.49 N
ANISOU 2120 N ILE A1057 20218 18333 14827 -2609 2740 -1169 N
ATOM 2121 CA ILE A1057 -4.418 29.027 0.472 1.00138.11 C
ANISOU 2121 CA ILE A1057 19602 18175 14700 -2497 2591 -1154 C
ATOM 2122 C ILE A1057 -3.193 28.259 -0.064 1.00140.55 C
ANISOU 2122 C ILE A1057 20076 18423 14904 -2321 2421 -970 C
ATOM 2123 O ILE A1057 -2.308 27.908 0.718 1.00140.59 O
ANISOU 2123 O ILE A1057 20400 18299 14719 -2251 2378 -853 O
ATOM 2124 CB ILE A1057 -4.433 30.510 -0.013 1.00139.36 C
ANISOU 2124 CB ILE A1057 19374 18518 15059 -2379 2426 -1175 C
ATOM 2125 CG1 ILE A1057 -3.223 31.312 0.526 1.00138.49 C
ANISOU 2125 CG1 ILE A1057 19327 18407 14884 -2196 2225 -1014 C
ATOM 2126 CG2 ILE A1057 -5.768 31.193 0.297 1.00140.67 C
ANISOU 2126 CG2 ILE A1057 19337 18763 15350 -2538 2588 -1388 C
ATOM 2127 CD1 ILE A1057 -2.790 32.453 -0.341 1.00141.87 C
ANISOU 2127 CD1 ILE A1057 19437 18994 15472 -2029 2001 -965 C
ATOM 2128 N THR A1058 -3.140 28.008 -1.389 1.00135.54 N
ANISOU 2128 N THR A1058 19229 17882 14389 -2244 2319 -953 N
ATOM 2129 CA THR A1058 -2.022 27.296 -2.029 1.00134.41 C
ANISOU 2129 CA THR A1058 19200 17703 14165 -2074 2156 -796 C
ATOM 2130 C THR A1058 -0.958 28.266 -2.567 1.00135.40 C
ANISOU 2130 C THR A1058 19103 17962 14381 -1851 1890 -679 C
ATOM 2131 O THR A1058 -1.222 29.469 -2.652 1.00134.40 O
ANISOU 2131 O THR A1058 18710 17957 14398 -1838 1836 -726 O
ATOM 2132 CB THR A1058 -2.518 26.314 -3.109 1.00143.77 C
ANISOU 2132 CB THR A1058 20351 18883 15393 -2140 2227 -843 C
ATOM 2133 OG1 THR A1058 -3.313 27.009 -4.071 1.00142.41 O
ANISOU 2133 OG1 THR A1058 19792 18872 15446 -2173 2217 -956 O
ATOM 2134 CG2 THR A1058 -3.284 25.130 -2.530 1.00144.91 C
ANISOU 2134 CG2 THR A1058 20805 18863 15393 -2352 2482 -930 C
ATOM 2135 N LYS A1059 0.248 27.736 -2.913 1.00130.11 N
ANISOU 2135 N LYS A1059 18551 17267 13619 -1678 1728 -536 N
ATOM 2136 CA LYS A1059 1.390 28.488 -3.456 1.00127.77 C
ANISOU 2136 CA LYS A1059 18071 17093 13383 -1476 1485 -427 C
ATOM 2137 C LYS A1059 1.010 29.213 -4.755 1.00129.81 C
ANISOU 2137 C LYS A1059 17955 17509 13857 -1463 1417 -473 C
ATOM 2138 O LYS A1059 1.427 30.354 -4.967 1.00127.96 O
ANISOU 2138 O LYS A1059 17515 17388 13716 -1377 1279 -445 O
ATOM 2139 CB LYS A1059 2.583 27.551 -3.709 1.00129.90 C
ANISOU 2139 CB LYS A1059 18531 17309 13515 -1314 1357 -304 C
ATOM 2140 CG LYS A1059 3.730 27.680 -2.712 1.00139.98 C
ANISOU 2140 CG LYS A1059 20009 18540 14636 -1176 1233 -210 C
ATOM 2141 CD LYS A1059 5.012 27.066 -3.284 1.00147.77 C
ANISOU 2141 CD LYS A1059 21078 19534 15535 -979 1061 -109 C
ATOM 2142 CE LYS A1059 6.110 26.877 -2.266 1.00154.25 C
ANISOU 2142 CE LYS A1059 22101 20314 16192 -821 923 -35 C
ATOM 2143 NZ LYS A1059 7.376 26.422 -2.907 1.00158.35 N
ANISOU 2143 NZ LYS A1059 22633 20880 16653 -615 739 39 N
ATOM 2144 N ASP A1060 0.208 28.543 -5.611 1.00126.61 N
ANISOU 2144 N ASP A1060 17482 17103 13522 -1553 1517 -549 N
ATOM 2145 CA ASP A1060 -0.288 29.080 -6.880 1.00125.32 C
ANISOU 2145 CA ASP A1060 16993 17071 13552 -1546 1464 -609 C
ATOM 2146 C ASP A1060 -1.345 30.160 -6.639 1.00127.32 C
ANISOU 2146 C ASP A1060 17037 17397 13940 -1642 1531 -746 C
ATOM 2147 O ASP A1060 -1.341 31.160 -7.351 1.00125.69 O
ANISOU 2147 O ASP A1060 16578 17309 13871 -1569 1408 -758 O
ATOM 2148 CB ASP A1060 -0.824 27.961 -7.799 1.00128.04 C
ANISOU 2148 CB ASP A1060 17347 17386 13918 -1610 1548 -656 C
ATOM 2149 CG ASP A1060 -1.893 27.072 -7.178 1.00143.88 C
ANISOU 2149 CG ASP A1060 19522 19283 15862 -1815 1792 -779 C
ATOM 2150 OD1 ASP A1060 -1.539 26.218 -6.329 1.00145.71 O
ANISOU 2150 OD1 ASP A1060 20082 19371 15909 -1850 1874 -729 O
ATOM 2151 OD2 ASP A1060 -3.077 27.201 -7.571 1.00151.02 O
ANISOU 2151 OD2 ASP A1060 20238 20246 16897 -1942 1901 -933 O
ATOM 2152 N GLU A1061 -2.219 29.971 -5.615 1.00123.83 N
ANISOU 2152 N GLU A1061 16719 16882 13449 -1802 1723 -854 N
ATOM 2153 CA GLU A1061 -3.283 30.906 -5.217 1.00123.42 C
ANISOU 2153 CA GLU A1061 16491 16895 13509 -1903 1810 -1007 C
ATOM 2154 C GLU A1061 -2.719 32.226 -4.700 1.00125.22 C
ANISOU 2154 C GLU A1061 16647 17177 13754 -1799 1675 -948 C
ATOM 2155 O GLU A1061 -3.337 33.275 -4.893 1.00124.32 O
ANISOU 2155 O GLU A1061 16303 17159 13775 -1799 1646 -1044 O
ATOM 2156 CB GLU A1061 -4.199 30.276 -4.158 1.00126.57 C
ANISOU 2156 CB GLU A1061 17077 17191 13821 -2109 2064 -1130 C
ATOM 2157 CG GLU A1061 -5.407 29.569 -4.750 1.00138.46 C
ANISOU 2157 CG GLU A1061 18504 18706 15397 -2268 2233 -1292 C
ATOM 2158 CD GLU A1061 -6.308 28.809 -3.792 1.00160.59 C
ANISOU 2158 CD GLU A1061 21496 21411 18111 -2505 2509 -1433 C
ATOM 2159 OE1 GLU A1061 -6.246 29.060 -2.566 1.00156.67 O
ANISOU 2159 OE1 GLU A1061 21192 20835 17501 -2556 2585 -1418 O
ATOM 2160 OE2 GLU A1061 -7.105 27.976 -4.281 1.00155.02 O
ANISOU 2160 OE2 GLU A1061 20746 20708 17446 -2649 2658 -1568 O
ATOM 2161 N ALA A1062 -1.542 32.159 -4.042 1.00120.64 N
ANISOU 2161 N ALA A1062 16270 16534 13033 -1705 1586 -797 N
ATOM 2162 CA ALA A1062 -0.811 33.297 -3.487 1.00119.03 C
ANISOU 2162 CA ALA A1062 16036 16372 12819 -1606 1451 -724 C
ATOM 2163 C ALA A1062 -0.168 34.131 -4.593 1.00119.91 C
ANISOU 2163 C ALA A1062 15913 16606 13041 -1464 1244 -658 C
ATOM 2164 O ALA A1062 -0.162 35.357 -4.487 1.00119.29 O
ANISOU 2164 O ALA A1062 15701 16595 13028 -1424 1161 -668 O
ATOM 2165 CB ALA A1062 0.246 32.813 -2.507 1.00120.09 C
ANISOU 2165 CB ALA A1062 16464 16404 12762 -1547 1417 -599 C
ATOM 2166 N GLU A1063 0.358 33.469 -5.654 1.00114.33 N
ANISOU 2166 N GLU A1063 15172 15922 12348 -1393 1167 -596 N
ATOM 2167 CA GLU A1063 0.986 34.122 -6.809 1.00112.12 C
ANISOU 2167 CA GLU A1063 14692 15747 12160 -1273 987 -536 C
ATOM 2168 C GLU A1063 -0.047 34.900 -7.633 1.00113.96 C
ANISOU 2168 C GLU A1063 14674 16062 12563 -1305 985 -656 C
ATOM 2169 O GLU A1063 0.273 35.974 -8.145 1.00112.23 O
ANISOU 2169 O GLU A1063 14310 15919 12414 -1228 849 -633 O
ATOM 2170 CB GLU A1063 1.721 33.095 -7.692 1.00113.14 C
ANISOU 2170 CB GLU A1063 14868 15871 12250 -1200 927 -451 C
ATOM 2171 CG GLU A1063 2.744 33.724 -8.629 1.00122.87 C
ANISOU 2171 CG GLU A1063 15958 17201 13527 -1070 737 -361 C
ATOM 2172 CD GLU A1063 3.325 32.835 -9.711 1.00143.88 C
ANISOU 2172 CD GLU A1063 18611 19877 16181 -1003 681 -303 C
ATOM 2173 OE1 GLU A1063 3.845 31.743 -9.384 1.00135.03 O
ANISOU 2173 OE1 GLU A1063 17680 18686 14941 -977 710 -251 O
ATOM 2174 OE2 GLU A1063 3.303 33.259 -10.889 1.00139.01 O
ANISOU 2174 OE2 GLU A1063 17811 19336 15669 -967 600 -308 O
ATOM 2175 N LYS A1064 -1.278 34.357 -7.751 1.00110.81 N
ANISOU 2175 N LYS A1064 14236 15645 12223 -1418 1135 -793 N
ATOM 2176 CA LYS A1064 -2.383 34.968 -8.494 1.00110.52 C
ANISOU 2176 CA LYS A1064 13962 15686 12345 -1443 1140 -940 C
ATOM 2177 C LYS A1064 -2.785 36.304 -7.886 1.00114.88 C
ANISOU 2177 C LYS A1064 14420 16280 12948 -1437 1113 -1009 C
ATOM 2178 O LYS A1064 -2.991 37.258 -8.636 1.00113.90 O
ANISOU 2178 O LYS A1064 14117 16230 12929 -1362 994 -1047 O
ATOM 2179 CB LYS A1064 -3.609 34.033 -8.588 1.00114.13 C
ANISOU 2179 CB LYS A1064 14403 16121 12841 -1583 1326 -1096 C
ATOM 2180 CG LYS A1064 -3.345 32.622 -9.128 1.00128.58 C
ANISOU 2180 CG LYS A1064 16354 17891 14608 -1609 1378 -1042 C
ATOM 2181 CD LYS A1064 -2.957 32.562 -10.611 1.00137.98 C
ANISOU 2181 CD LYS A1064 17413 19142 15873 -1499 1232 -984 C
ATOM 2182 CE LYS A1064 -2.174 31.313 -10.955 1.00147.21 C
ANISOU 2182 CE LYS A1064 18756 20243 16934 -1470 1229 -860 C
ATOM 2183 NZ LYS A1064 -3.003 30.079 -10.871 1.00157.30 N
ANISOU 2183 NZ LYS A1064 20147 21447 18174 -1612 1416 -948 N
ATOM 2184 N LEU A1065 -2.881 36.385 -6.536 1.00112.76 N
ANISOU 2184 N LEU A1065 14291 15955 12596 -1510 1217 -1022 N
ATOM 2185 CA LEU A1065 -3.239 37.637 -5.859 1.00113.06 C
ANISOU 2185 CA LEU A1065 14261 16026 12671 -1506 1198 -1085 C
ATOM 2186 C LEU A1065 -2.079 38.625 -5.816 1.00115.00 C
ANISOU 2186 C LEU A1065 14521 16294 12880 -1383 1014 -941 C
ATOM 2187 O LEU A1065 -2.321 39.827 -5.911 1.00114.29 O
ANISOU 2187 O LEU A1065 14310 16255 12859 -1337 932 -986 O
ATOM 2188 CB LEU A1065 -3.881 37.454 -4.458 1.00114.76 C
ANISOU 2188 CB LEU A1065 14609 16177 12817 -1640 1386 -1171 C
ATOM 2189 CG LEU A1065 -3.177 36.611 -3.382 1.00120.36 C
ANISOU 2189 CG LEU A1065 15612 16770 13348 -1684 1464 -1058 C
ATOM 2190 CD1 LEU A1065 -2.154 37.433 -2.600 1.00120.38 C
ANISOU 2190 CD1 LEU A1065 15711 16758 13269 -1600 1349 -935 C
ATOM 2191 CD2 LEU A1065 -4.191 36.079 -2.383 1.00123.97 C
ANISOU 2191 CD2 LEU A1065 16191 17157 13756 -1862 1704 -1191 C
ATOM 2192 N PHE A1066 -0.830 38.127 -5.682 1.00110.72 N
ANISOU 2192 N PHE A1066 14126 15715 12226 -1329 949 -780 N
ATOM 2193 CA PHE A1066 0.373 38.966 -5.667 1.00109.67 C
ANISOU 2193 CA PHE A1066 14003 15615 12053 -1226 781 -652 C
ATOM 2194 C PHE A1066 0.511 39.720 -6.989 1.00111.39 C
ANISOU 2194 C PHE A1066 14036 15914 12374 -1146 635 -645 C
ATOM 2195 O PHE A1066 0.867 40.901 -6.982 1.00110.90 O
ANISOU 2195 O PHE A1066 13923 15887 12327 -1100 530 -624 O
ATOM 2196 CB PHE A1066 1.645 38.135 -5.388 1.00111.68 C
ANISOU 2196 CB PHE A1066 14429 15830 12173 -1176 738 -511 C
ATOM 2197 CG PHE A1066 2.935 38.836 -5.762 1.00112.61 C
ANISOU 2197 CG PHE A1066 14508 16012 12268 -1070 559 -397 C
ATOM 2198 CD1 PHE A1066 3.503 39.782 -4.916 1.00115.91 C
ANISOU 2198 CD1 PHE A1066 14966 16439 12636 -1051 498 -361 C
ATOM 2199 CD2 PHE A1066 3.563 38.574 -6.974 1.00114.19 C
ANISOU 2199 CD2 PHE A1066 14627 16265 12494 -1002 460 -337 C
ATOM 2200 CE1 PHE A1066 4.675 40.452 -5.277 1.00116.19 C
ANISOU 2200 CE1 PHE A1066 14956 16542 12650 -975 345 -274 C
ATOM 2201 CE2 PHE A1066 4.728 39.251 -7.336 1.00116.42 C
ANISOU 2201 CE2 PHE A1066 14866 16615 12755 -927 312 -252 C
ATOM 2202 CZ PHE A1066 5.293 40.164 -6.474 1.00114.65 C
ANISOU 2202 CZ PHE A1066 14679 16403 12479 -918 258 -223 C
ATOM 2203 N ASN A1067 0.249 39.022 -8.117 1.00106.01 N
ANISOU 2203 N ASN A1067 13276 15252 11752 -1132 630 -662 N
ATOM 2204 CA ASN A1067 0.310 39.584 -9.462 1.00104.19 C
ANISOU 2204 CA ASN A1067 12896 15083 11610 -1060 500 -660 C
ATOM 2205 C ASN A1067 -0.730 40.692 -9.643 1.00106.49 C
ANISOU 2205 C ASN A1067 13052 15405 12006 -1055 477 -792 C
ATOM 2206 O ASN A1067 -0.436 41.686 -10.305 1.00105.72 O
ANISOU 2206 O ASN A1067 12890 15339 11938 -984 342 -768 O
ATOM 2207 CB ASN A1067 0.172 38.484 -10.520 1.00104.83 C
ANISOU 2207 CB ASN A1067 12937 15168 11725 -1053 515 -661 C
ATOM 2208 CG ASN A1067 1.432 37.677 -10.756 1.00121.76 C
ANISOU 2208 CG ASN A1067 15186 17301 13775 -1011 474 -520 C
ATOM 2209 OD1 ASN A1067 2.556 38.197 -10.775 1.00112.65 O
ANISOU 2209 OD1 ASN A1067 14056 16178 12568 -950 364 -417 O
ATOM 2210 ND2 ASN A1067 1.267 36.386 -10.999 1.00113.82 N
ANISOU 2210 ND2 ASN A1067 14239 16258 12748 -1041 559 -525 N
ATOM 2211 N GLN A1068 -1.913 40.546 -9.001 1.00102.63 N
ANISOU 2211 N GLN A1068 12534 14903 11558 -1130 611 -937 N
ATOM 2212 CA GLN A1068 -3.003 41.530 -9.011 1.00102.60 C
ANISOU 2212 CA GLN A1068 12398 14935 11651 -1120 602 -1093 C
ATOM 2213 C GLN A1068 -2.589 42.795 -8.260 1.00105.89 C
ANISOU 2213 C GLN A1068 12860 15346 12027 -1085 528 -1053 C
ATOM 2214 O GLN A1068 -2.964 43.896 -8.669 1.00105.49 O
ANISOU 2214 O GLN A1068 12720 15324 12036 -1016 426 -1116 O
ATOM 2215 CB GLN A1068 -4.269 40.948 -8.370 1.00105.04 C
ANISOU 2215 CB GLN A1068 12672 15239 11999 -1230 788 -1265 C
ATOM 2216 CG GLN A1068 -5.007 39.940 -9.240 1.00114.20 C
ANISOU 2216 CG GLN A1068 13736 16421 13233 -1268 855 -1366 C
ATOM 2217 CD GLN A1068 -6.071 39.216 -8.458 1.00125.67 C
ANISOU 2217 CD GLN A1068 15195 17862 14693 -1414 1070 -1520 C
ATOM 2218 OE1 GLN A1068 -6.955 39.824 -7.843 1.00120.98 O
ANISOU 2218 OE1 GLN A1068 14528 17296 14143 -1456 1139 -1672 O
ATOM 2219 NE2 GLN A1068 -6.011 37.896 -8.467 1.00115.03 N
ANISOU 2219 NE2 GLN A1068 13943 16469 13295 -1502 1188 -1492 N
ATOM 2220 N ASP A1069 -1.820 42.626 -7.160 1.00102.06 N
ANISOU 2220 N ASP A1069 12528 14820 11432 -1126 574 -951 N
ATOM 2221 CA ASP A1069 -1.291 43.711 -6.327 1.00101.63 C
ANISOU 2221 CA ASP A1069 12538 14755 11320 -1104 512 -898 C
ATOM 2222 C ASP A1069 -0.182 44.454 -7.069 1.00103.72 C
ANISOU 2222 C ASP A1069 12803 15045 11560 -1022 338 -773 C
ATOM 2223 O ASP A1069 -0.082 45.673 -6.938 1.00102.98 O
ANISOU 2223 O ASP A1069 12702 14959 11468 -986 250 -775 O
ATOM 2224 CB ASP A1069 -0.761 43.175 -4.983 1.00103.89 C
ANISOU 2224 CB ASP A1069 12999 14987 11489 -1169 610 -831 C
ATOM 2225 CG ASP A1069 -1.783 42.474 -4.105 1.00115.92 C
ANISOU 2225 CG ASP A1069 14564 16470 13011 -1276 804 -952 C
ATOM 2226 OD1 ASP A1069 -2.903 43.018 -3.938 1.00117.38 O
ANISOU 2226 OD1 ASP A1069 14643 16679 13276 -1303 856 -1105 O
ATOM 2227 OD2 ASP A1069 -1.445 41.413 -3.533 1.00121.87 O
ANISOU 2227 OD2 ASP A1069 15469 17164 13671 -1334 903 -901 O
ATOM 2228 N VAL A1070 0.649 43.712 -7.841 1.00 99.32 N
ANISOU 2228 N VAL A1070 12262 14499 10975 -999 295 -671 N
ATOM 2229 CA VAL A1070 1.743 44.236 -8.666 1.00 98.25 C
ANISOU 2229 CA VAL A1070 12121 14395 10813 -940 150 -562 C
ATOM 2230 C VAL A1070 1.164 45.175 -9.718 1.00102.91 C
ANISOU 2230 C VAL A1070 12610 15003 11487 -889 54 -628 C
ATOM 2231 O VAL A1070 1.686 46.273 -9.897 1.00102.34 O
ANISOU 2231 O VAL A1070 12559 14936 11389 -861 -52 -588 O
ATOM 2232 CB VAL A1070 2.592 43.088 -9.272 1.00101.55 C
ANISOU 2232 CB VAL A1070 12564 14828 11194 -928 146 -469 C
ATOM 2233 CG1 VAL A1070 3.352 43.523 -10.520 1.00100.69 C
ANISOU 2233 CG1 VAL A1070 12405 14762 11090 -878 15 -400 C
ATOM 2234 CG2 VAL A1070 3.558 42.546 -8.239 1.00101.62 C
ANISOU 2234 CG2 VAL A1070 12702 14819 11089 -943 182 -384 C
ATOM 2235 N ASP A1071 0.054 44.763 -10.361 1.00100.31 N
ANISOU 2235 N ASP A1071 12185 14679 11251 -878 91 -741 N
ATOM 2236 CA ASP A1071 -0.659 45.553 -11.360 1.00100.61 C
ANISOU 2236 CA ASP A1071 12133 14725 11368 -810 -6 -829 C
ATOM 2237 C ASP A1071 -1.290 46.785 -10.725 1.00104.54 C
ANISOU 2237 C ASP A1071 12625 15213 11884 -785 -36 -922 C
ATOM 2238 O ASP A1071 -1.188 47.874 -11.288 1.00103.69 O
ANISOU 2238 O ASP A1071 12529 15093 11774 -719 -165 -922 O
ATOM 2239 CB ASP A1071 -1.706 44.693 -12.080 1.00103.52 C
ANISOU 2239 CB ASP A1071 12393 15110 11830 -804 46 -943 C
ATOM 2240 CG ASP A1071 -1.094 43.579 -12.915 1.00119.64 C
ANISOU 2240 CG ASP A1071 14444 17158 13856 -811 50 -851 C
ATOM 2241 OD1 ASP A1071 -0.115 43.855 -13.656 1.00120.04 O
ANISOU 2241 OD1 ASP A1071 14533 17213 13865 -773 -55 -739 O
ATOM 2242 OD2 ASP A1071 -1.606 42.436 -12.847 1.00128.13 O
ANISOU 2242 OD2 ASP A1071 15492 18234 14959 -859 162 -898 O
ATOM 2243 N ALA A1072 -1.886 46.620 -9.525 1.00102.11 N
ANISOU 2243 N ALA A1072 12319 14900 11578 -841 84 -998 N
ATOM 2244 CA ALA A1072 -2.500 47.700 -8.750 1.00102.55 C
ANISOU 2244 CA ALA A1072 12370 14949 11647 -822 74 -1094 C
ATOM 2245 C ALA A1072 -1.452 48.745 -8.365 1.00105.95 C
ANISOU 2245 C ALA A1072 12916 15353 11986 -809 -22 -972 C
ATOM 2246 O ALA A1072 -1.711 49.941 -8.505 1.00105.80 O
ANISOU 2246 O ALA A1072 12905 15321 11975 -748 -119 -1019 O
ATOM 2247 CB ALA A1072 -3.169 47.139 -7.505 1.00104.03 C
ANISOU 2247 CB ALA A1072 12554 15134 11837 -909 245 -1184 C
ATOM 2248 N ALA A1073 -0.258 48.288 -7.928 1.00102.07 N
ANISOU 2248 N ALA A1073 12519 14857 11405 -860 -2 -823 N
ATOM 2249 CA ALA A1073 0.866 49.143 -7.547 1.00101.82 C
ANISOU 2249 CA ALA A1073 12588 14816 11284 -865 -83 -709 C
ATOM 2250 C ALA A1073 1.380 49.895 -8.762 1.00107.04 C
ANISOU 2250 C ALA A1073 13252 15479 11939 -816 -225 -662 C
ATOM 2251 O ALA A1073 1.557 51.107 -8.675 1.00107.42 O
ANISOU 2251 O ALA A1073 13359 15505 11952 -799 -309 -655 O
ATOM 2252 CB ALA A1073 1.981 48.314 -6.930 1.00102.13 C
ANISOU 2252 CB ALA A1073 12703 14864 11237 -916 -36 -587 C
ATOM 2253 N VAL A1074 1.572 49.181 -9.907 1.00103.62 N
ANISOU 2253 N VAL A1074 12769 15065 11536 -798 -247 -634 N
ATOM 2254 CA VAL A1074 2.033 49.722 -11.195 1.00102.99 C
ANISOU 2254 CA VAL A1074 12703 14982 11448 -761 -366 -593 C
ATOM 2255 C VAL A1074 1.078 50.826 -11.650 1.00107.67 C
ANISOU 2255 C VAL A1074 13296 15533 12082 -686 -453 -701 C
ATOM 2256 O VAL A1074 1.542 51.904 -12.021 1.00107.62 O
ANISOU 2256 O VAL A1074 13379 15492 12018 -672 -555 -665 O
ATOM 2257 CB VAL A1074 2.234 48.602 -12.260 1.00106.30 C
ANISOU 2257 CB VAL A1074 13064 15427 11899 -754 -354 -560 C
ATOM 2258 CG1 VAL A1074 2.198 49.145 -13.683 1.00106.11 C
ANISOU 2258 CG1 VAL A1074 13045 15383 11889 -702 -466 -567 C
ATOM 2259 CG2 VAL A1074 3.531 47.842 -12.021 1.00105.52 C
ANISOU 2259 CG2 VAL A1074 12997 15367 11730 -806 -321 -436 C
ATOM 2260 N ARG A1075 -0.250 50.572 -11.557 1.00104.72 N
ANISOU 2260 N ARG A1075 12829 15162 11799 -641 -410 -845 N
ATOM 2261 CA ARG A1075 -1.299 51.537 -11.896 1.00105.35 C
ANISOU 2261 CA ARG A1075 12891 15213 11926 -545 -496 -982 C
ATOM 2262 C ARG A1075 -1.122 52.816 -11.074 1.00108.82 C
ANISOU 2262 C ARG A1075 13431 15614 12300 -539 -543 -977 C
ATOM 2263 O ARG A1075 -1.185 53.911 -11.630 1.00109.15 O
ANISOU 2263 O ARG A1075 13554 15606 12313 -468 -669 -1000 O
ATOM 2264 CB ARG A1075 -2.700 50.942 -11.660 1.00107.60 C
ANISOU 2264 CB ARG A1075 13031 15533 12319 -516 -415 -1158 C
ATOM 2265 CG ARG A1075 -3.222 50.082 -12.812 1.00120.33 C
ANISOU 2265 CG ARG A1075 14542 17171 14007 -479 -422 -1216 C
ATOM 2266 CD ARG A1075 -4.705 49.742 -12.677 1.00130.47 C
ANISOU 2266 CD ARG A1075 15671 18498 15403 -443 -364 -1429 C
ATOM 2267 NE ARG A1075 -4.980 48.790 -11.595 1.00137.94 N
ANISOU 2267 NE ARG A1075 16562 19480 16369 -556 -178 -1464 N
ATOM 2268 CZ ARG A1075 -4.969 47.466 -11.729 1.00151.45 C
ANISOU 2268 CZ ARG A1075 18226 21214 18103 -633 -62 -1449 C
ATOM 2269 NH1 ARG A1075 -4.689 46.912 -12.903 1.00138.30 N
ANISOU 2269 NH1 ARG A1075 16542 19550 16454 -607 -115 -1398 N
ATOM 2270 NH2 ARG A1075 -5.232 46.686 -10.690 1.00138.36 N
ANISOU 2270 NH2 ARG A1075 16558 19570 16443 -742 109 -1484 N
ATOM 2271 N GLY A1076 -0.847 52.651 -9.779 1.00104.31 N
ANISOU 2271 N GLY A1076 12877 15058 11697 -615 -444 -942 N
ATOM 2272 CA GLY A1076 -0.623 53.744 -8.842 1.00104.10 C
ANISOU 2272 CA GLY A1076 12947 15000 11606 -626 -470 -929 C
ATOM 2273 C GLY A1076 0.648 54.528 -9.107 1.00106.65 C
ANISOU 2273 C GLY A1076 13405 15293 11824 -660 -561 -793 C
ATOM 2274 O GLY A1076 0.623 55.761 -9.048 1.00107.15 O
ANISOU 2274 O GLY A1076 13567 15306 11841 -626 -649 -810 O
ATOM 2275 N ILE A1077 1.775 53.815 -9.389 1.00100.73 N
ANISOU 2275 N ILE A1077 12663 14577 11032 -730 -538 -666 N
ATOM 2276 CA ILE A1077 3.090 54.402 -9.696 1.00 99.21 C
ANISOU 2276 CA ILE A1077 12574 14379 10743 -786 -606 -548 C
ATOM 2277 C ILE A1077 2.948 55.321 -10.920 1.00102.57 C
ANISOU 2277 C ILE A1077 13076 14746 11150 -735 -727 -570 C
ATOM 2278 O ILE A1077 3.436 56.452 -10.899 1.00102.57 O
ANISOU 2278 O ILE A1077 13206 14699 11066 -761 -796 -538 O
ATOM 2279 CB ILE A1077 4.190 53.308 -9.888 1.00101.33 C
ANISOU 2279 CB ILE A1077 12800 14712 10987 -850 -558 -443 C
ATOM 2280 CG1 ILE A1077 4.452 52.526 -8.587 1.00101.16 C
ANISOU 2280 CG1 ILE A1077 12758 14729 10949 -894 -460 -412 C
ATOM 2281 CG2 ILE A1077 5.501 53.914 -10.400 1.00102.35 C
ANISOU 2281 CG2 ILE A1077 13008 14853 11028 -913 -627 -351 C
ATOM 2282 CD1 ILE A1077 4.997 51.105 -8.794 1.00104.54 C
ANISOU 2282 CD1 ILE A1077 13127 15211 11384 -910 -401 -355 C
ATOM 2283 N LEU A1078 2.224 54.847 -11.953 1.00 98.46 N
ANISOU 2283 N LEU A1078 12491 14219 10700 -662 -752 -631 N
ATOM 2284 CA LEU A1078 1.949 55.590 -13.184 1.00 98.14 C
ANISOU 2284 CA LEU A1078 12536 14111 10642 -592 -873 -665 C
ATOM 2285 C LEU A1078 0.970 56.748 -12.966 1.00103.20 C
ANISOU 2285 C LEU A1078 13250 14680 11281 -492 -957 -779 C
ATOM 2286 O LEU A1078 1.020 57.732 -13.704 1.00103.10 O
ANISOU 2286 O LEU A1078 13387 14586 11201 -448 -1073 -783 O
ATOM 2287 CB LEU A1078 1.492 54.653 -14.311 1.00 97.57 C
ANISOU 2287 CB LEU A1078 12369 14057 10646 -538 -877 -700 C
ATOM 2288 CG LEU A1078 2.552 53.666 -14.804 1.00100.77 C
ANISOU 2288 CG LEU A1078 12741 14516 11032 -621 -827 -584 C
ATOM 2289 CD1 LEU A1078 1.917 52.441 -15.392 1.00100.45 C
ANISOU 2289 CD1 LEU A1078 12565 14515 11088 -580 -780 -629 C
ATOM 2290 CD2 LEU A1078 3.509 54.315 -15.795 1.00102.93 C
ANISOU 2290 CD2 LEU A1078 13151 14744 11213 -658 -908 -510 C
ATOM 2291 N ARG A1079 0.110 56.648 -11.933 1.00100.71 N
ANISOU 2291 N ARG A1079 12845 14391 11028 -458 -899 -874 N
ATOM 2292 CA ARG A1079 -0.818 57.716 -11.544 1.00101.80 C
ANISOU 2292 CA ARG A1079 13035 14477 11166 -358 -970 -995 C
ATOM 2293 C ARG A1079 -0.062 58.770 -10.707 1.00105.09 C
ANISOU 2293 C ARG A1079 13605 14851 11474 -425 -986 -917 C
ATOM 2294 O ARG A1079 -0.503 59.919 -10.624 1.00105.35 O
ANISOU 2294 O ARG A1079 13754 14811 11463 -350 -1079 -980 O
ATOM 2295 CB ARG A1079 -2.013 57.157 -10.746 1.00103.79 C
ANISOU 2295 CB ARG A1079 13119 14788 11529 -311 -884 -1142 C
ATOM 2296 CG ARG A1079 -3.147 56.600 -11.610 1.00117.61 C
ANISOU 2296 CG ARG A1079 14734 16566 13387 -204 -911 -1287 C
ATOM 2297 CD ARG A1079 -4.433 56.391 -10.819 1.00132.53 C
ANISOU 2297 CD ARG A1079 16470 18511 15376 -153 -841 -1475 C
ATOM 2298 NE ARG A1079 -4.321 55.333 -9.809 1.00144.76 N
ANISOU 2298 NE ARG A1079 17915 20126 16960 -280 -657 -1451 N
ATOM 2299 CZ ARG A1079 -4.687 54.068 -9.995 1.00161.69 C
ANISOU 2299 CZ ARG A1079 19921 22330 19182 -325 -552 -1487 C
ATOM 2300 NH1 ARG A1079 -5.197 53.680 -11.159 1.00151.03 N
ANISOU 2300 NH1 ARG A1079 18497 20994 17893 -253 -614 -1553 N
ATOM 2301 NH2 ARG A1079 -4.546 53.179 -9.021 1.00147.99 N
ANISOU 2301 NH2 ARG A1079 18141 20633 17454 -442 -386 -1460 N
ATOM 2302 N ASN A1080 1.081 58.367 -10.098 1.00100.37 N
ANISOU 2302 N ASN A1080 13010 14297 10829 -560 -902 -787 N
ATOM 2303 CA ASN A1080 1.941 59.211 -9.267 1.00 99.93 C
ANISOU 2303 CA ASN A1080 13079 14219 10671 -645 -904 -708 C
ATOM 2304 C ASN A1080 2.943 59.984 -10.130 1.00103.54 C
ANISOU 2304 C ASN A1080 13701 14621 11018 -702 -990 -621 C
ATOM 2305 O ASN A1080 3.848 59.386 -10.715 1.00102.39 O
ANISOU 2305 O ASN A1080 13532 14518 10852 -782 -965 -534 O
ATOM 2306 CB ASN A1080 2.661 58.366 -8.207 1.00 98.82 C
ANISOU 2306 CB ASN A1080 12860 14157 10530 -749 -785 -630 C
ATOM 2307 CG ASN A1080 3.244 59.158 -7.064 1.00115.78 C
ANISOU 2307 CG ASN A1080 15102 16292 12597 -813 -775 -589 C
ATOM 2308 OD1 ASN A1080 4.083 60.043 -7.244 1.00107.90 O
ANISOU 2308 OD1 ASN A1080 14232 15262 11503 -875 -834 -525 O
ATOM 2309 ND2 ASN A1080 2.847 58.816 -5.849 1.00106.88 N
ANISOU 2309 ND2 ASN A1080 13917 15188 11503 -812 -691 -629 N
ATOM 2310 N ALA A1081 2.780 61.323 -10.182 1.00100.66 N
ANISOU 2310 N ALA A1081 13512 14159 10575 -666 -1086 -652 N
ATOM 2311 CA ALA A1081 3.602 62.272 -10.948 1.00100.42 C
ANISOU 2311 CA ALA A1081 13690 14048 10418 -728 -1166 -589 C
ATOM 2312 C ALA A1081 5.095 62.222 -10.617 1.00102.30 C
ANISOU 2312 C ALA A1081 13952 14341 10575 -908 -1104 -468 C
ATOM 2313 O ALA A1081 5.917 62.414 -11.514 1.00101.99 O
ANISOU 2313 O ALA A1081 14006 14282 10463 -990 -1126 -412 O
ATOM 2314 CB ALA A1081 3.076 63.686 -10.753 1.00102.26 C
ANISOU 2314 CB ALA A1081 14117 14163 10574 -657 -1265 -651 C
ATOM 2315 N LYS A1082 5.437 61.987 -9.331 1.00 97.00 N
ANISOU 2315 N LYS A1082 13202 13740 9914 -967 -1029 -441 N
ATOM 2316 CA LYS A1082 6.813 61.905 -8.833 1.00 95.63 C
ANISOU 2316 CA LYS A1082 13025 13637 9672 -1119 -977 -349 C
ATOM 2317 C LYS A1082 7.475 60.608 -9.305 1.00 96.77 C
ANISOU 2317 C LYS A1082 13015 13887 9865 -1162 -916 -298 C
ATOM 2318 O LYS A1082 8.583 60.651 -9.846 1.00 96.35 O
ANISOU 2318 O LYS A1082 12989 13873 9748 -1271 -914 -242 O
ATOM 2319 CB LYS A1082 6.854 61.966 -7.284 1.00 98.26 C
ANISOU 2319 CB LYS A1082 13323 14007 10005 -1141 -926 -348 C
ATOM 2320 CG LYS A1082 6.262 63.218 -6.630 1.00114.03 C
ANISOU 2320 CG LYS A1082 15463 15909 11953 -1101 -977 -399 C
ATOM 2321 CD LYS A1082 4.811 63.021 -6.167 1.00123.82 C
ANISOU 2321 CD LYS A1082 16623 17131 13291 -961 -961 -497 C
ATOM 2322 CE LYS A1082 4.194 64.280 -5.605 1.00135.28 C
ANISOU 2322 CE LYS A1082 18216 18488 14696 -898 -1024 -563 C
ATOM 2323 NZ LYS A1082 2.716 64.167 -5.482 1.00143.70 N
ANISOU 2323 NZ LYS A1082 19192 19543 15863 -750 -1021 -690 N
ATOM 2324 N LEU A1083 6.782 59.461 -9.106 1.00 91.48 N
ANISOU 2324 N LEU A1083 12188 13266 9304 -1080 -862 -326 N
ATOM 2325 CA LEU A1083 7.259 58.106 -9.410 1.00 90.11 C
ANISOU 2325 CA LEU A1083 11871 13187 9181 -1098 -801 -284 C
ATOM 2326 C LEU A1083 7.111 57.641 -10.874 1.00 93.47 C
ANISOU 2326 C LEU A1083 12271 13603 9641 -1066 -828 -286 C
ATOM 2327 O LEU A1083 7.754 56.654 -11.243 1.00 92.23 O
ANISOU 2327 O LEU A1083 12019 13523 9501 -1099 -787 -240 O
ATOM 2328 CB LEU A1083 6.591 57.079 -8.476 1.00 89.57 C
ANISOU 2328 CB LEU A1083 11678 13157 9196 -1039 -721 -314 C
ATOM 2329 CG LEU A1083 6.897 57.190 -6.987 1.00 93.82 C
ANISOU 2329 CG LEU A1083 12231 13717 9698 -1076 -676 -300 C
ATOM 2330 CD1 LEU A1083 5.927 56.367 -6.181 1.00 93.55 C
ANISOU 2330 CD1 LEU A1083 12119 13687 9740 -1017 -594 -353 C
ATOM 2331 CD2 LEU A1083 8.324 56.776 -6.678 1.00 96.06 C
ANISOU 2331 CD2 LEU A1083 12496 14086 9917 -1164 -661 -220 C
ATOM 2332 N LYS A1084 6.269 58.318 -11.691 1.00 90.53 N
ANISOU 2332 N LYS A1084 11987 13136 9274 -991 -902 -343 N
ATOM 2333 CA LYS A1084 6.053 57.960 -13.103 1.00 90.33 C
ANISOU 2333 CA LYS A1084 11961 13087 9273 -949 -941 -352 C
ATOM 2334 C LYS A1084 7.303 58.159 -14.015 1.00 94.64 C
ANISOU 2334 C LYS A1084 12587 13644 9727 -1067 -951 -277 C
ATOM 2335 O LYS A1084 7.591 57.223 -14.769 1.00 93.42 O
ANISOU 2335 O LYS A1084 12343 13543 9610 -1074 -923 -250 O
ATOM 2336 CB LYS A1084 4.824 58.673 -13.700 1.00 93.30 C
ANISOU 2336 CB LYS A1084 12429 13354 9667 -821 -1035 -445 C
ATOM 2337 CG LYS A1084 4.278 57.992 -14.947 1.00106.67 C
ANISOU 2337 CG LYS A1084 14070 15036 11422 -741 -1066 -480 C
ATOM 2338 CD LYS A1084 3.334 58.891 -15.729 1.00117.36 C
ANISOU 2338 CD LYS A1084 15562 16272 12756 -616 -1192 -568 C
ATOM 2339 CE LYS A1084 2.536 58.117 -16.755 1.00128.57 C
ANISOU 2339 CE LYS A1084 16894 17694 14263 -508 -1224 -631 C
ATOM 2340 NZ LYS A1084 3.383 57.627 -17.878 1.00138.35 N
ANISOU 2340 NZ LYS A1084 18163 18939 15463 -581 -1215 -547 N
ATOM 2341 N PRO A1085 8.042 59.317 -14.009 1.00 92.27 N
ANISOU 2341 N PRO A1085 12455 13297 9308 -1168 -984 -250 N
ATOM 2342 CA PRO A1085 9.207 59.444 -14.907 1.00 92.56 C
ANISOU 2342 CA PRO A1085 12557 13353 9258 -1301 -973 -198 C
ATOM 2343 C PRO A1085 10.367 58.539 -14.512 1.00 98.04 C
ANISOU 2343 C PRO A1085 13088 14199 9964 -1396 -891 -148 C
ATOM 2344 O PRO A1085 11.163 58.144 -15.365 1.00 98.18 O
ANISOU 2344 O PRO A1085 13080 14268 9956 -1471 -867 -122 O
ATOM 2345 CB PRO A1085 9.604 60.924 -14.786 1.00 95.02 C
ANISOU 2345 CB PRO A1085 13092 13575 9437 -1395 -1014 -197 C
ATOM 2346 CG PRO A1085 8.517 61.590 -14.021 1.00 99.46 C
ANISOU 2346 CG PRO A1085 13722 14050 10020 -1277 -1069 -251 C
ATOM 2347 CD PRO A1085 7.886 60.539 -13.190 1.00 94.32 C
ANISOU 2347 CD PRO A1085 12855 13484 9500 -1180 -1021 -272 C
ATOM 2348 N VAL A1086 10.456 58.221 -13.212 1.00 95.18 N
ANISOU 2348 N VAL A1086 12624 13905 9634 -1387 -853 -144 N
ATOM 2349 CA VAL A1086 11.488 57.374 -12.626 1.00 94.82 C
ANISOU 2349 CA VAL A1086 12435 14000 9594 -1445 -795 -110 C
ATOM 2350 C VAL A1086 11.252 55.915 -13.024 1.00 99.32 C
ANISOU 2350 C VAL A1086 12853 14629 10256 -1363 -759 -100 C
ATOM 2351 O VAL A1086 12.200 55.254 -13.438 1.00 98.64 O
ANISOU 2351 O VAL A1086 12686 14637 10157 -1414 -734 -76 O
ATOM 2352 CB VAL A1086 11.575 57.567 -11.093 1.00 98.45 C
ANISOU 2352 CB VAL A1086 12872 14491 10044 -1448 -778 -111 C
ATOM 2353 CG1 VAL A1086 12.804 56.866 -10.525 1.00 98.31 C
ANISOU 2353 CG1 VAL A1086 12734 14614 10004 -1507 -741 -86 C
ATOM 2354 CG2 VAL A1086 11.586 59.052 -10.724 1.00 98.83 C
ANISOU 2354 CG2 VAL A1086 13087 14458 10006 -1513 -817 -125 C
ATOM 2355 N TYR A1087 9.990 55.428 -12.924 1.00 96.67 N
ANISOU 2355 N TYR A1087 12479 14242 10010 -1240 -756 -131 N
ATOM 2356 CA TYR A1087 9.598 54.064 -13.287 1.00 96.40 C
ANISOU 2356 CA TYR A1087 12319 14246 10061 -1165 -717 -130 C
ATOM 2357 C TYR A1087 9.831 53.849 -14.777 1.00101.80 C
ANISOU 2357 C TYR A1087 13011 14926 10744 -1177 -739 -119 C
ATOM 2358 O TYR A1087 10.438 52.845 -15.151 1.00101.61 O
ANISOU 2358 O TYR A1087 12889 14980 10738 -1183 -705 -90 O
ATOM 2359 CB TYR A1087 8.123 53.796 -12.919 1.00 97.69 C
ANISOU 2359 CB TYR A1087 12455 14348 10314 -1054 -706 -190 C
ATOM 2360 CG TYR A1087 7.640 52.387 -13.215 1.00 99.51 C
ANISOU 2360 CG TYR A1087 12568 14613 10630 -991 -654 -199 C
ATOM 2361 CD1 TYR A1087 7.679 51.395 -12.240 1.00101.27 C
ANISOU 2361 CD1 TYR A1087 12718 14885 10876 -980 -580 -188 C
ATOM 2362 CD2 TYR A1087 7.112 52.056 -14.462 1.00100.28 C
ANISOU 2362 CD2 TYR A1087 12644 14682 10775 -943 -679 -222 C
ATOM 2363 CE1 TYR A1087 7.243 50.096 -12.510 1.00101.51 C
ANISOU 2363 CE1 TYR A1087 12665 14934 10970 -934 -526 -197 C
ATOM 2364 CE2 TYR A1087 6.682 50.759 -14.747 1.00100.76 C
ANISOU 2364 CE2 TYR A1087 12601 14772 10910 -895 -628 -232 C
ATOM 2365 CZ TYR A1087 6.745 49.782 -13.766 1.00107.59 C
ANISOU 2365 CZ TYR A1087 13403 15684 11793 -895 -548 -220 C
ATOM 2366 OH TYR A1087 6.311 48.506 -14.045 1.00108.00 O
ANISOU 2366 OH TYR A1087 13377 15752 11905 -857 -492 -232 O
ATOM 2367 N ASP A1088 9.363 54.800 -15.621 1.00 99.31 N
ANISOU 2367 N ASP A1088 12827 14510 10396 -1175 -801 -143 N
ATOM 2368 CA ASP A1088 9.493 54.766 -17.082 1.00 99.31 C
ANISOU 2368 CA ASP A1088 12878 14477 10377 -1186 -830 -137 C
ATOM 2369 C ASP A1088 10.948 54.714 -17.562 1.00103.88 C
ANISOU 2369 C ASP A1088 13454 15137 10880 -1320 -797 -91 C
ATOM 2370 O ASP A1088 11.224 54.090 -18.588 1.00103.92 O
ANISOU 2370 O ASP A1088 13428 15164 10894 -1327 -787 -78 O
ATOM 2371 CB ASP A1088 8.731 55.937 -17.728 1.00101.82 C
ANISOU 2371 CB ASP A1088 13381 14653 10653 -1148 -915 -178 C
ATOM 2372 CG ASP A1088 7.212 55.819 -17.680 1.00113.07 C
ANISOU 2372 CG ASP A1088 14782 16011 12169 -991 -960 -252 C
ATOM 2373 OD1 ASP A1088 6.695 54.686 -17.829 1.00113.24 O
ANISOU 2373 OD1 ASP A1088 14654 16082 12290 -921 -924 -270 O
ATOM 2374 OD2 ASP A1088 6.537 56.867 -17.558 1.00119.73 O
ANISOU 2374 OD2 ASP A1088 15759 16754 12979 -938 -1033 -302 O
ATOM 2375 N SER A1089 11.873 55.337 -16.803 1.00100.67 N
ANISOU 2375 N SER A1089 13067 14783 10401 -1428 -778 -78 N
ATOM 2376 CA SER A1089 13.318 55.377 -17.070 1.00100.69 C
ANISOU 2376 CA SER A1089 13041 14887 10329 -1570 -740 -61 C
ATOM 2377 C SER A1089 13.993 54.006 -16.879 1.00102.95 C
ANISOU 2377 C SER A1089 13129 15321 10667 -1543 -694 -47 C
ATOM 2378 O SER A1089 14.873 53.639 -17.663 1.00102.55 O
ANISOU 2378 O SER A1089 13024 15352 10588 -1614 -666 -46 O
ATOM 2379 CB SER A1089 13.985 56.416 -16.164 1.00105.15 C
ANISOU 2379 CB SER A1089 13678 15468 10808 -1685 -739 -70 C
ATOM 2380 OG SER A1089 15.387 56.244 -16.016 1.00114.95 O
ANISOU 2380 OG SER A1089 14828 16851 11998 -1810 -695 -76 O
ATOM 2381 N LEU A1090 13.590 53.275 -15.821 1.00 98.26 N
ANISOU 2381 N LEU A1090 12441 14754 10139 -1443 -684 -42 N
ATOM 2382 CA LEU A1090 14.163 51.995 -15.395 1.00 97.26 C
ANISOU 2382 CA LEU A1090 12163 14746 10046 -1395 -651 -30 C
ATOM 2383 C LEU A1090 13.817 50.794 -16.272 1.00100.11 C
ANISOU 2383 C LEU A1090 12450 15114 10473 -1314 -634 -18 C
ATOM 2384 O LEU A1090 12.760 50.753 -16.905 1.00 99.21 O
ANISOU 2384 O LEU A1090 12380 14905 10411 -1255 -645 -23 O
ATOM 2385 CB LEU A1090 13.790 51.683 -13.921 1.00 96.87 C
ANISOU 2385 CB LEU A1090 12087 14697 10022 -1325 -643 -29 C
ATOM 2386 CG LEU A1090 14.088 52.748 -12.854 1.00101.50 C
ANISOU 2386 CG LEU A1090 12739 15280 10548 -1389 -659 -40 C
ATOM 2387 CD1 LEU A1090 13.328 52.469 -11.581 1.00101.29 C
ANISOU 2387 CD1 LEU A1090 12718 15212 10556 -1306 -646 -41 C
ATOM 2388 CD2 LEU A1090 15.577 52.895 -12.585 1.00104.29 C
ANISOU 2388 CD2 LEU A1090 13033 15765 10829 -1481 -662 -51 C
ATOM 2389 N ASP A1091 14.721 49.794 -16.257 1.00 96.34 N
ANISOU 2389 N ASP A1091 11858 14756 9992 -1303 -613 -12 N
ATOM 2390 CA ASP A1091 14.601 48.504 -16.936 1.00 95.60 C
ANISOU 2390 CA ASP A1091 11686 14688 9949 -1225 -593 1 C
ATOM 2391 C ASP A1091 13.730 47.566 -16.086 1.00 98.96 C
ANISOU 2391 C ASP A1091 12092 15075 10434 -1110 -573 11 C
ATOM 2392 O ASP A1091 13.315 47.953 -14.994 1.00 99.20 O
ANISOU 2392 O ASP A1091 12162 15068 10460 -1099 -571 5 O
ATOM 2393 CB ASP A1091 15.997 47.893 -17.173 1.00 97.97 C
ANISOU 2393 CB ASP A1091 11880 15136 10207 -1253 -586 -9 C
ATOM 2394 CG ASP A1091 16.918 47.904 -15.964 1.00110.38 C
ANISOU 2394 CG ASP A1091 13397 16811 11730 -1259 -599 -29 C
ATOM 2395 OD1 ASP A1091 16.773 47.010 -15.098 1.00110.87 O
ANISOU 2395 OD1 ASP A1091 13432 16885 11809 -1155 -601 -19 O
ATOM 2396 OD2 ASP A1091 17.809 48.784 -15.904 1.00117.10 O
ANISOU 2396 OD2 ASP A1091 14241 17730 12520 -1371 -607 -62 O
ATOM 2397 N ALA A1092 13.465 46.338 -16.572 1.00 94.49 N
ANISOU 2397 N ALA A1092 11475 14514 9914 -1034 -550 22 N
ATOM 2398 CA ALA A1092 12.648 45.325 -15.887 1.00 93.61 C
ANISOU 2398 CA ALA A1092 11360 14359 9848 -944 -514 25 C
ATOM 2399 C ALA A1092 13.095 44.993 -14.444 1.00 96.93 C
ANISOU 2399 C ALA A1092 11789 14817 10222 -916 -505 30 C
ATOM 2400 O ALA A1092 12.248 44.854 -13.563 1.00 96.47 O
ANISOU 2400 O ALA A1092 11781 14689 10183 -887 -472 22 O
ATOM 2401 CB ALA A1092 12.586 44.055 -16.725 1.00 94.05 C
ANISOU 2401 CB ALA A1092 11368 14430 9938 -884 -492 37 C
ATOM 2402 N VAL A1093 14.415 44.882 -14.213 1.00 93.36 N
ANISOU 2402 N VAL A1093 11290 14477 9706 -923 -536 32 N
ATOM 2403 CA VAL A1093 15.022 44.541 -12.919 1.00 93.43 C
ANISOU 2403 CA VAL A1093 11311 14532 9656 -880 -550 30 C
ATOM 2404 C VAL A1093 14.921 45.705 -11.924 1.00 97.12 C
ANISOU 2404 C VAL A1093 11833 14972 10095 -938 -562 19 C
ATOM 2405 O VAL A1093 14.603 45.485 -10.750 1.00 96.53 O
ANISOU 2405 O VAL A1093 11822 14852 10003 -896 -547 23 O
ATOM 2406 CB VAL A1093 16.495 44.066 -13.080 1.00 97.86 C
ANISOU 2406 CB VAL A1093 11784 15239 10159 -857 -595 11 C
ATOM 2407 CG1 VAL A1093 16.958 43.281 -11.857 1.00 98.12 C
ANISOU 2407 CG1 VAL A1093 11847 15302 10132 -760 -621 5 C
ATOM 2408 CG2 VAL A1093 16.683 43.236 -14.350 1.00 97.55 C
ANISOU 2408 CG2 VAL A1093 11681 15235 10147 -825 -586 15 C
ATOM 2409 N ARG A1094 15.221 46.934 -12.397 1.00 93.13 N
ANISOU 2409 N ARG A1094 11322 14487 9578 -1038 -586 6 N
ATOM 2410 CA ARG A1094 15.205 48.153 -11.586 1.00 92.47 C
ANISOU 2410 CA ARG A1094 11297 14379 9460 -1105 -602 -6 C
ATOM 2411 C ARG A1094 13.789 48.650 -11.293 1.00 95.01 C
ANISOU 2411 C ARG A1094 11705 14566 9830 -1095 -576 -4 C
ATOM 2412 O ARG A1094 13.586 49.301 -10.270 1.00 94.98 O
ANISOU 2412 O ARG A1094 11759 14528 9801 -1112 -579 -11 O
ATOM 2413 CB ARG A1094 16.089 49.240 -12.200 1.00 91.85 C
ANISOU 2413 CB ARG A1094 11201 14362 9336 -1227 -630 -27 C
ATOM 2414 CG ARG A1094 17.571 48.882 -12.152 1.00101.08 C
ANISOU 2414 CG ARG A1094 12264 15691 10451 -1245 -654 -59 C
ATOM 2415 CD ARG A1094 18.446 50.045 -12.544 1.00107.22 C
ANISOU 2415 CD ARG A1094 13031 16535 11172 -1395 -664 -98 C
ATOM 2416 NE ARG A1094 19.502 49.653 -13.478 1.00114.03 N
ANISOU 2416 NE ARG A1094 13780 17530 12015 -1439 -660 -139 N
ATOM 2417 CZ ARG A1094 20.742 49.334 -13.120 1.00129.50 C
ANISOU 2417 CZ ARG A1094 15621 19649 13933 -1434 -687 -198 C
ATOM 2418 NH1 ARG A1094 21.092 49.338 -11.841 1.00120.16 N
ANISOU 2418 NH1 ARG A1094 14430 18504 12720 -1379 -728 -216 N
ATOM 2419 NH2 ARG A1094 21.636 48.993 -14.037 1.00115.72 N
ANISOU 2419 NH2 ARG A1094 13763 18029 12176 -1476 -676 -250 N
ATOM 2420 N ARG A1095 12.805 48.305 -12.149 1.00 90.30 N
ANISOU 2420 N ARG A1095 11109 13898 9302 -1061 -552 -5 N
ATOM 2421 CA ARG A1095 11.392 48.638 -11.925 1.00 89.68 C
ANISOU 2421 CA ARG A1095 11085 13708 9281 -1035 -528 -29 C
ATOM 2422 C ARG A1095 10.862 47.769 -10.771 1.00 92.08 C
ANISOU 2422 C ARG A1095 11404 13985 9598 -978 -472 -35 C
ATOM 2423 O ARG A1095 10.024 48.224 -9.991 1.00 91.63 O
ANISOU 2423 O ARG A1095 11396 13863 9557 -977 -448 -64 O
ATOM 2424 CB ARG A1095 10.554 48.404 -13.197 1.00 90.68 C
ANISOU 2424 CB ARG A1095 11193 13783 9477 -1006 -526 -45 C
ATOM 2425 CG ARG A1095 10.634 49.538 -14.216 1.00102.23 C
ANISOU 2425 CG ARG A1095 12704 15214 10923 -1059 -580 -54 C
ATOM 2426 CD ARG A1095 9.953 49.167 -15.521 1.00111.65 C
ANISOU 2426 CD ARG A1095 13883 16367 12173 -1019 -589 -67 C
ATOM 2427 NE ARG A1095 9.958 50.276 -16.479 1.00120.14 N
ANISOU 2427 NE ARG A1095 15045 17388 13216 -1061 -647 -78 N
ATOM 2428 CZ ARG A1095 9.123 50.387 -17.509 1.00133.61 C
ANISOU 2428 CZ ARG A1095 16784 19019 14962 -1014 -680 -108 C
ATOM 2429 NH1 ARG A1095 8.195 49.462 -17.724 1.00121.18 N
ANISOU 2429 NH1 ARG A1095 15140 17430 13474 -930 -658 -138 N
ATOM 2430 NH2 ARG A1095 9.202 51.429 -18.325 1.00119.59 N
ANISOU 2430 NH2 ARG A1095 15125 17179 13133 -1050 -739 -115 N
ATOM 2431 N ALA A1096 11.385 46.523 -10.660 1.00 87.40 N
ANISOU 2431 N ALA A1096 10782 13438 8987 -931 -450 -11 N
ATOM 2432 CA ALA A1096 11.055 45.547 -9.621 1.00 86.39 C
ANISOU 2432 CA ALA A1096 10704 13276 8845 -881 -393 -11 C
ATOM 2433 C ALA A1096 11.544 46.032 -8.264 1.00 89.96 C
ANISOU 2433 C ALA A1096 11218 13739 9224 -892 -410 -6 C
ATOM 2434 O ALA A1096 10.869 45.808 -7.259 1.00 90.62 O
ANISOU 2434 O ALA A1096 11377 13756 9298 -879 -355 -20 O
ATOM 2435 CB ALA A1096 11.685 44.208 -9.947 1.00 86.89 C
ANISOU 2435 CB ALA A1096 10746 13383 8885 -820 -388 15 C
ATOM 2436 N ALA A1097 12.707 46.714 -8.235 1.00 84.84 N
ANISOU 2436 N ALA A1097 10540 13175 8521 -925 -480 4 N
ATOM 2437 CA ALA A1097 13.272 47.270 -7.012 1.00 84.25 C
ANISOU 2437 CA ALA A1097 10514 13122 8374 -939 -510 2 C
ATOM 2438 C ALA A1097 12.357 48.372 -6.493 1.00 87.23 C
ANISOU 2438 C ALA A1097 10953 13417 8773 -990 -489 -17 C
ATOM 2439 O ALA A1097 12.123 48.451 -5.287 1.00 87.53 O
ANISOU 2439 O ALA A1097 11067 13416 8774 -980 -468 -22 O
ATOM 2440 CB ALA A1097 14.668 47.802 -7.276 1.00 85.20 C
ANISOU 2440 CB ALA A1097 10567 13364 8443 -981 -585 -3 C
ATOM 2441 N LEU A1098 11.776 49.163 -7.416 1.00 82.53 N
ANISOU 2441 N LEU A1098 10337 12787 8232 -1031 -494 -32 N
ATOM 2442 CA LEU A1098 10.834 50.239 -7.118 1.00 82.08 C
ANISOU 2442 CA LEU A1098 10336 12650 8200 -1060 -487 -63 C
ATOM 2443 C LEU A1098 9.508 49.670 -6.607 1.00 86.27 C
ANISOU 2443 C LEU A1098 10891 13101 8787 -1014 -408 -99 C
ATOM 2444 O LEU A1098 8.949 50.213 -5.654 1.00 86.31 O
ANISOU 2444 O LEU A1098 10954 13055 8783 -1024 -384 -127 O
ATOM 2445 CB LEU A1098 10.607 51.109 -8.369 1.00 81.80 C
ANISOU 2445 CB LEU A1098 10291 12594 8196 -1095 -529 -76 C
ATOM 2446 CG LEU A1098 10.033 52.508 -8.146 1.00 86.39 C
ANISOU 2446 CG LEU A1098 10952 13105 8769 -1126 -558 -107 C
ATOM 2447 CD1 LEU A1098 11.067 53.442 -7.517 1.00 87.17 C
ANISOU 2447 CD1 LEU A1098 11100 13241 8778 -1203 -599 -87 C
ATOM 2448 CD2 LEU A1098 9.525 53.093 -9.447 1.00 87.45 C
ANISOU 2448 CD2 LEU A1098 11102 13188 8937 -1124 -597 -129 C
ATOM 2449 N ILE A1099 9.017 48.574 -7.227 1.00 82.72 N
ANISOU 2449 N ILE A1099 10397 12643 8391 -974 -362 -106 N
ATOM 2450 CA ILE A1099 7.771 47.891 -6.846 1.00 82.50 C
ANISOU 2450 CA ILE A1099 10380 12549 8416 -951 -269 -156 C
ATOM 2451 C ILE A1099 7.907 47.277 -5.451 1.00 88.41 C
ANISOU 2451 C ILE A1099 11215 13276 9099 -948 -209 -144 C
ATOM 2452 O ILE A1099 6.982 47.389 -4.651 1.00 89.06 O
ANISOU 2452 O ILE A1099 11343 13299 9197 -963 -136 -195 O
ATOM 2453 CB ILE A1099 7.318 46.893 -7.951 1.00 84.60 C
ANISOU 2453 CB ILE A1099 10580 12817 8748 -921 -240 -167 C
ATOM 2454 CG1 ILE A1099 6.551 47.642 -9.054 1.00 83.98 C
ANISOU 2454 CG1 ILE A1099 10444 12718 8748 -915 -279 -217 C
ATOM 2455 CG2 ILE A1099 6.490 45.718 -7.398 1.00 85.19 C
ANISOU 2455 CG2 ILE A1099 10682 12845 8841 -913 -127 -202 C
ATOM 2456 CD1 ILE A1099 6.823 47.169 -10.397 1.00 87.06 C
ANISOU 2456 CD1 ILE A1099 10774 13135 9168 -895 -311 -196 C
ATOM 2457 N ASN A1100 9.082 46.695 -5.142 1.00 85.82 N
ANISOU 2457 N ASN A1100 10917 12998 8693 -925 -245 -87 N
ATOM 2458 CA ASN A1100 9.404 46.118 -3.832 1.00 86.73 C
ANISOU 2458 CA ASN A1100 11144 13089 8722 -905 -214 -70 C
ATOM 2459 C ASN A1100 9.284 47.206 -2.748 1.00 90.83 C
ANISOU 2459 C ASN A1100 11726 13580 9207 -941 -219 -86 C
ATOM 2460 O ASN A1100 8.775 46.934 -1.657 1.00 91.54 O
ANISOU 2460 O ASN A1100 11919 13602 9259 -946 -147 -105 O
ATOM 2461 CB ASN A1100 10.833 45.534 -3.852 1.00 89.93 C
ANISOU 2461 CB ASN A1100 11549 13574 9048 -854 -293 -21 C
ATOM 2462 CG ASN A1100 11.246 44.752 -2.619 1.00117.88 C
ANISOU 2462 CG ASN A1100 15223 17082 12483 -801 -282 -5 C
ATOM 2463 OD1 ASN A1100 11.338 45.277 -1.499 1.00113.47 O
ANISOU 2463 OD1 ASN A1100 14750 16499 11866 -812 -290 -8 O
ATOM 2464 ND2 ASN A1100 11.588 43.489 -2.818 1.00110.27 N
ANISOU 2464 ND2 ASN A1100 14297 16117 11485 -736 -275 13 N
ATOM 2465 N MET A1101 9.746 48.435 -3.068 1.00 85.98 N
ANISOU 2465 N MET A1101 11062 13010 8596 -974 -299 -81 N
ATOM 2466 CA MET A1101 9.723 49.597 -2.181 1.00 85.32 C
ANISOU 2466 CA MET A1101 11034 12906 8479 -1011 -320 -95 C
ATOM 2467 C MET A1101 8.311 50.106 -1.929 1.00 88.57 C
ANISOU 2467 C MET A1101 11465 13235 8953 -1029 -249 -157 C
ATOM 2468 O MET A1101 8.009 50.530 -0.815 1.00 88.33 O
ANISOU 2468 O MET A1101 11514 13160 8887 -1045 -217 -176 O
ATOM 2469 CB MET A1101 10.613 50.711 -2.734 1.00 87.23 C
ANISOU 2469 CB MET A1101 11229 13213 8702 -1053 -418 -77 C
ATOM 2470 CG MET A1101 12.071 50.479 -2.476 1.00 90.90 C
ANISOU 2470 CG MET A1101 11681 13770 9086 -1048 -486 -44 C
ATOM 2471 SD MET A1101 13.082 51.847 -3.052 1.00 95.05 S
ANISOU 2471 SD MET A1101 12157 14375 9582 -1135 -575 -45 S
ATOM 2472 CE MET A1101 12.761 53.053 -1.794 1.00 92.09 C
ANISOU 2472 CE MET A1101 11888 13935 9167 -1178 -577 -61 C
ATOM 2473 N VAL A1102 7.456 50.079 -2.964 1.00 84.80 N
ANISOU 2473 N VAL A1102 10911 12743 8566 -1021 -231 -197 N
ATOM 2474 CA VAL A1102 6.050 50.487 -2.879 1.00 84.71 C
ANISOU 2474 CA VAL A1102 10887 12672 8627 -1022 -172 -284 C
ATOM 2475 C VAL A1102 5.333 49.485 -1.973 1.00 89.22 C
ANISOU 2475 C VAL A1102 11506 13198 9196 -1031 -44 -323 C
ATOM 2476 O VAL A1102 4.557 49.901 -1.116 1.00 90.15 O
ANISOU 2476 O VAL A1102 11664 13271 9317 -1051 17 -384 O
ATOM 2477 CB VAL A1102 5.384 50.616 -4.281 1.00 88.00 C
ANISOU 2477 CB VAL A1102 11207 13092 9136 -996 -201 -328 C
ATOM 2478 CG1 VAL A1102 3.887 50.890 -4.172 1.00 88.17 C
ANISOU 2478 CG1 VAL A1102 11195 13068 9238 -979 -141 -445 C
ATOM 2479 CG2 VAL A1102 6.058 51.702 -5.111 1.00 87.47 C
ANISOU 2479 CG2 VAL A1102 11139 13045 9049 -1002 -318 -295 C
ATOM 2480 N PHE A1103 5.652 48.178 -2.116 1.00 84.88 N
ANISOU 2480 N PHE A1103 10969 12656 8626 -1020 -2 -288 N
ATOM 2481 CA PHE A1103 5.090 47.094 -1.306 1.00 85.12 C
ANISOU 2481 CA PHE A1103 11083 12629 8630 -1040 127 -316 C
ATOM 2482 C PHE A1103 5.409 47.236 0.200 1.00 89.74 C
ANISOU 2482 C PHE A1103 11815 13171 9112 -1059 157 -296 C
ATOM 2483 O PHE A1103 4.595 46.834 1.033 1.00 90.40 O
ANISOU 2483 O PHE A1103 11979 13188 9179 -1100 280 -351 O
ATOM 2484 CB PHE A1103 5.558 45.729 -1.834 1.00 86.77 C
ANISOU 2484 CB PHE A1103 11305 12849 8816 -1014 141 -269 C
ATOM 2485 CG PHE A1103 4.601 45.047 -2.787 1.00 88.40 C
ANISOU 2485 CG PHE A1103 11423 13048 9116 -1024 210 -329 C
ATOM 2486 CD1 PHE A1103 3.538 44.287 -2.310 1.00 92.59 C
ANISOU 2486 CD1 PHE A1103 11994 13519 9667 -1078 357 -411 C
ATOM 2487 CD2 PHE A1103 4.784 45.132 -4.161 1.00 89.76 C
ANISOU 2487 CD2 PHE A1103 11480 13273 9350 -990 133 -310 C
ATOM 2488 CE1 PHE A1103 2.662 43.647 -3.191 1.00 93.28 C
ANISOU 2488 CE1 PHE A1103 11991 13609 9841 -1095 421 -480 C
ATOM 2489 CE2 PHE A1103 3.905 44.495 -5.040 1.00 92.44 C
ANISOU 2489 CE2 PHE A1103 11740 13607 9775 -995 190 -369 C
ATOM 2490 CZ PHE A1103 2.854 43.754 -4.550 1.00 91.24 C
ANISOU 2490 CZ PHE A1103 11614 13404 9648 -1047 331 -457 C
ATOM 2491 N GLN A1104 6.572 47.843 0.529 1.00 85.66 N
ANISOU 2491 N GLN A1104 11330 12692 8524 -1036 47 -229 N
ATOM 2492 CA GLN A1104 7.094 48.066 1.879 1.00 85.86 C
ANISOU 2492 CA GLN A1104 11491 12688 8443 -1039 39 -202 C
ATOM 2493 C GLN A1104 6.615 49.374 2.544 1.00 91.23 C
ANISOU 2493 C GLN A1104 12184 13344 9134 -1077 41 -244 C
ATOM 2494 O GLN A1104 5.970 49.318 3.585 1.00 91.20 O
ANISOU 2494 O GLN A1104 12280 13272 9099 -1107 136 -285 O
ATOM 2495 CB GLN A1104 8.634 48.009 1.836 1.00 86.74 C
ANISOU 2495 CB GLN A1104 11610 12871 8477 -991 -89 -125 C
ATOM 2496 CG GLN A1104 9.344 48.169 3.181 1.00 90.39 C
ANISOU 2496 CG GLN A1104 12210 13314 8819 -974 -123 -99 C
ATOM 2497 CD GLN A1104 10.825 47.875 3.108 1.00105.67 C
ANISOU 2497 CD GLN A1104 14136 15335 10680 -911 -248 -50 C
ATOM 2498 OE1 GLN A1104 11.444 47.831 2.031 1.00102.88 O
ANISOU 2498 OE1 GLN A1104 13654 15069 10367 -896 -317 -35 O
ATOM 2499 NE2 GLN A1104 11.433 47.668 4.265 1.00 94.97 N
ANISOU 2499 NE2 GLN A1104 12915 13957 9211 -871 -282 -36 N
ATOM 2500 N MET A1105 6.970 50.534 1.959 1.00 89.32 N
ANISOU 2500 N MET A1105 11861 13152 8923 -1077 -61 -234 N
ATOM 2501 CA MET A1105 6.696 51.893 2.452 1.00 90.17 C
ANISOU 2501 CA MET A1105 11988 13241 9030 -1103 -89 -265 C
ATOM 2502 C MET A1105 5.399 52.539 1.963 1.00 93.93 C
ANISOU 2502 C MET A1105 12394 13689 9607 -1106 -49 -356 C
ATOM 2503 O MET A1105 4.861 53.414 2.644 1.00 93.76 O
ANISOU 2503 O MET A1105 12413 13628 9582 -1120 -26 -407 O
ATOM 2504 CB MET A1105 7.849 52.821 2.050 1.00 92.81 C
ANISOU 2504 CB MET A1105 12297 13638 9330 -1110 -222 -211 C
ATOM 2505 CG MET A1105 9.127 52.573 2.797 1.00 97.59 C
ANISOU 2505 CG MET A1105 12966 14283 9830 -1105 -279 -152 C
ATOM 2506 SD MET A1105 10.532 52.945 1.732 1.00102.24 S
ANISOU 2506 SD MET A1105 13457 14986 10405 -1119 -407 -107 S
ATOM 2507 CE MET A1105 10.788 51.364 1.003 1.00 98.96 C
ANISOU 2507 CE MET A1105 12984 14610 10008 -1061 -387 -83 C
ATOM 2508 N GLY A1106 4.961 52.168 0.763 1.00 90.33 N
ANISOU 2508 N GLY A1106 11832 13256 9234 -1084 -57 -380 N
ATOM 2509 CA GLY A1106 3.785 52.742 0.121 1.00 90.07 C
ANISOU 2509 CA GLY A1106 11718 13207 9297 -1064 -48 -477 C
ATOM 2510 C GLY A1106 4.216 53.723 -0.943 1.00 93.11 C
ANISOU 2510 C GLY A1106 12070 13615 9694 -1041 -179 -452 C
ATOM 2511 O GLY A1106 5.415 53.934 -1.125 1.00 92.84 O
ANISOU 2511 O GLY A1106 12070 13612 9593 -1062 -256 -365 O
ATOM 2512 N GLU A1107 3.258 54.336 -1.646 1.00 89.30 N
ANISOU 2512 N GLU A1107 11530 13114 9287 -998 -206 -537 N
ATOM 2513 CA GLU A1107 3.568 55.309 -2.690 1.00 88.94 C
ANISOU 2513 CA GLU A1107 11492 13065 9238 -973 -329 -520 C
ATOM 2514 C GLU A1107 4.119 56.600 -2.104 1.00 93.79 C
ANISOU 2514 C GLU A1107 12214 13651 9771 -999 -398 -490 C
ATOM 2515 O GLU A1107 5.113 57.118 -2.609 1.00 92.96 O
ANISOU 2515 O GLU A1107 12155 13558 9606 -1035 -479 -419 O
ATOM 2516 CB GLU A1107 2.357 55.564 -3.591 1.00 90.56 C
ANISOU 2516 CB GLU A1107 11627 13247 9534 -899 -353 -631 C
ATOM 2517 CG GLU A1107 2.601 55.127 -5.020 1.00 99.51 C
ANISOU 2517 CG GLU A1107 12700 14405 10705 -878 -398 -604 C
ATOM 2518 CD GLU A1107 1.355 54.716 -5.774 1.00116.83 C
ANISOU 2518 CD GLU A1107 14791 16595 13003 -805 -384 -724 C
ATOM 2519 OE1 GLU A1107 0.530 55.605 -6.086 1.00109.56 O
ANISOU 2519 OE1 GLU A1107 13878 15638 12110 -733 -454 -818 O
ATOM 2520 OE2 GLU A1107 1.216 53.507 -6.070 1.00108.40 O
ANISOU 2520 OE2 GLU A1107 13640 15561 11987 -816 -311 -730 O
ATOM 2521 N THR A1108 3.519 57.084 -1.007 1.00 92.35 N
ANISOU 2521 N THR A1108 12076 13432 9580 -995 -355 -548 N
ATOM 2522 CA THR A1108 3.978 58.292 -0.315 1.00 93.52 C
ANISOU 2522 CA THR A1108 12337 13548 9649 -1020 -411 -525 C
ATOM 2523 C THR A1108 5.378 58.087 0.318 1.00 97.59 C
ANISOU 2523 C THR A1108 12908 14102 10071 -1095 -420 -416 C
ATOM 2524 O THR A1108 6.115 59.058 0.526 1.00 97.54 O
ANISOU 2524 O THR A1108 12984 14087 9990 -1137 -490 -376 O
ATOM 2525 CB THR A1108 2.914 58.797 0.677 1.00108.23 C
ANISOU 2525 CB THR A1108 14223 15367 11531 -989 -356 -625 C
ATOM 2526 OG1 THR A1108 3.293 60.096 1.144 1.00111.69 O
ANISOU 2526 OG1 THR A1108 14779 15765 11893 -1004 -427 -606 O
ATOM 2527 CG2 THR A1108 2.671 57.833 1.863 1.00107.58 C
ANISOU 2527 CG2 THR A1108 14128 15295 11451 -1024 -220 -640 C
ATOM 2528 N GLY A1109 5.718 56.826 0.593 1.00 93.51 N
ANISOU 2528 N GLY A1109 12350 13626 9555 -1108 -353 -378 N
ATOM 2529 CA GLY A1109 7.001 56.432 1.155 1.00 92.97 C
ANISOU 2529 CA GLY A1109 12318 13604 9403 -1151 -370 -294 C
ATOM 2530 C GLY A1109 8.126 56.570 0.155 1.00 95.80 C
ANISOU 2530 C GLY A1109 12640 14024 9735 -1181 -457 -234 C
ATOM 2531 O GLY A1109 9.103 57.275 0.425 1.00 95.77 O
ANISOU 2531 O GLY A1109 12683 14048 9656 -1234 -519 -198 O
ATOM 2532 N VAL A1110 7.981 55.912 -1.020 1.00 91.14 N
ANISOU 2532 N VAL A1110 11965 13458 9205 -1156 -455 -233 N
ATOM 2533 CA VAL A1110 8.973 55.926 -2.105 1.00 90.56 C
ANISOU 2533 CA VAL A1110 11848 13446 9114 -1188 -520 -187 C
ATOM 2534 C VAL A1110 9.150 57.337 -2.678 1.00 95.67 C
ANISOU 2534 C VAL A1110 12556 14065 9729 -1235 -597 -192 C
ATOM 2535 O VAL A1110 10.280 57.727 -2.975 1.00 95.59 O
ANISOU 2535 O VAL A1110 12555 14109 9657 -1306 -645 -155 O
ATOM 2536 CB VAL A1110 8.722 54.868 -3.210 1.00 93.66 C
ANISOU 2536 CB VAL A1110 12147 13862 9578 -1148 -495 -186 C
ATOM 2537 CG1 VAL A1110 9.992 54.605 -4.014 1.00 93.35 C
ANISOU 2537 CG1 VAL A1110 12059 13905 9504 -1185 -546 -135 C
ATOM 2538 CG2 VAL A1110 8.212 53.566 -2.620 1.00 93.32 C
ANISOU 2538 CG2 VAL A1110 12078 13815 9563 -1104 -406 -195 C
ATOM 2539 N ALA A1111 8.045 58.114 -2.777 1.00 92.65 N
ANISOU 2539 N ALA A1111 12226 13599 9378 -1197 -606 -249 N
ATOM 2540 CA ALA A1111 8.040 59.502 -3.261 1.00 92.62 C
ANISOU 2540 CA ALA A1111 12326 13538 9329 -1225 -683 -262 C
ATOM 2541 C ALA A1111 8.960 60.413 -2.429 1.00 96.42 C
ANISOU 2541 C ALA A1111 12901 14026 9709 -1312 -713 -230 C
ATOM 2542 O ALA A1111 9.506 61.376 -2.966 1.00 96.96 O
ANISOU 2542 O ALA A1111 13058 14071 9711 -1380 -771 -218 O
ATOM 2543 CB ALA A1111 6.622 60.051 -3.269 1.00 93.64 C
ANISOU 2543 CB ALA A1111 12491 13579 9510 -1137 -692 -346 C
ATOM 2544 N GLY A1112 9.153 60.066 -1.155 1.00 92.07 N
ANISOU 2544 N GLY A1112 12341 13503 9139 -1316 -672 -220 N
ATOM 2545 CA GLY A1112 10.026 60.780 -0.229 1.00 92.13 C
ANISOU 2545 CA GLY A1112 12424 13527 9054 -1391 -698 -196 C
ATOM 2546 C GLY A1112 11.514 60.670 -0.524 1.00 95.74 C
ANISOU 2546 C GLY A1112 12844 14083 9449 -1484 -733 -154 C
ATOM 2547 O GLY A1112 12.308 61.400 0.075 1.00 95.50 O
ANISOU 2547 O GLY A1112 12875 14073 9338 -1565 -766 -147 O
ATOM 2548 N PHE A1113 11.913 59.770 -1.457 1.00 91.96 N
ANISOU 2548 N PHE A1113 12259 13674 9008 -1476 -724 -136 N
ATOM 2549 CA PHE A1113 13.312 59.552 -1.867 1.00 92.02 C
ANISOU 2549 CA PHE A1113 12200 13796 8968 -1556 -751 -116 C
ATOM 2550 C PHE A1113 13.691 60.461 -3.067 1.00 96.95 C
ANISOU 2550 C PHE A1113 12873 14407 9556 -1655 -784 -121 C
ATOM 2551 O PHE A1113 14.355 60.018 -4.008 1.00 96.49 O
ANISOU 2551 O PHE A1113 12739 14419 9502 -1693 -784 -116 O
ATOM 2552 CB PHE A1113 13.557 58.057 -2.179 1.00 93.14 C
ANISOU 2552 CB PHE A1113 12213 14016 9161 -1489 -724 -101 C
ATOM 2553 CG PHE A1113 13.461 57.122 -0.992 1.00 94.28 C
ANISOU 2553 CG PHE A1113 12342 14174 9308 -1409 -695 -94 C
ATOM 2554 CD1 PHE A1113 12.235 56.615 -0.582 1.00 96.42 C
ANISOU 2554 CD1 PHE A1113 12642 14359 9635 -1329 -635 -102 C
ATOM 2555 CD2 PHE A1113 14.601 56.728 -0.302 1.00 96.61 C
ANISOU 2555 CD2 PHE A1113 12600 14565 9542 -1415 -726 -90 C
ATOM 2556 CE1 PHE A1113 12.147 55.763 0.519 1.00 97.13 C
ANISOU 2556 CE1 PHE A1113 12753 14444 9709 -1271 -596 -97 C
ATOM 2557 CE2 PHE A1113 14.512 55.857 0.786 1.00 99.13 C
ANISOU 2557 CE2 PHE A1113 12943 14877 9845 -1332 -706 -83 C
ATOM 2558 CZ PHE A1113 13.286 55.376 1.184 1.00 96.66 C
ANISOU 2558 CZ PHE A1113 12686 14463 9577 -1268 -635 -81 C
ATOM 2559 N THR A1114 13.274 61.747 -2.987 1.00 93.98 N
ANISOU 2559 N THR A1114 12642 13933 9133 -1697 -810 -135 N
ATOM 2560 CA THR A1114 13.419 62.846 -3.950 1.00 94.14 C
ANISOU 2560 CA THR A1114 12786 13890 9093 -1789 -842 -144 C
ATOM 2561 C THR A1114 14.762 62.849 -4.724 1.00 98.70 C
ANISOU 2561 C THR A1114 13319 14569 9614 -1930 -839 -142 C
ATOM 2562 O THR A1114 14.740 62.749 -5.956 1.00 98.50 O
ANISOU 2562 O THR A1114 13303 14526 9595 -1950 -837 -140 O
ATOM 2563 CB THR A1114 13.155 64.185 -3.225 1.00101.40 C
ANISOU 2563 CB THR A1114 13875 14714 9939 -1827 -872 -159 C
ATOM 2564 OG1 THR A1114 11.841 64.157 -2.667 1.00 98.34 O
ANISOU 2564 OG1 THR A1114 13516 14238 9612 -1691 -870 -177 O
ATOM 2565 CG2 THR A1114 13.292 65.404 -4.136 1.00102.50 C
ANISOU 2565 CG2 THR A1114 14193 14763 9988 -1928 -907 -168 C
ATOM 2566 N ASN A1115 15.903 62.992 -4.012 1.00 95.48 N
ANISOU 2566 N ASN A1115 12864 14268 9147 -2028 -838 -155 N
ATOM 2567 CA ASN A1115 17.245 63.057 -4.607 1.00 95.67 C
ANISOU 2567 CA ASN A1115 12826 14410 9113 -2178 -828 -181 C
ATOM 2568 C ASN A1115 17.767 61.703 -5.092 1.00 97.84 C
ANISOU 2568 C ASN A1115 12906 14819 9451 -2128 -810 -183 C
ATOM 2569 O ASN A1115 18.547 61.669 -6.042 1.00 98.20 O
ANISOU 2569 O ASN A1115 12902 14939 9470 -2232 -792 -208 O
ATOM 2570 CB ASN A1115 18.250 63.734 -3.659 1.00 98.13 C
ANISOU 2570 CB ASN A1115 13148 14797 9339 -2302 -840 -217 C
ATOM 2571 CG ASN A1115 17.960 65.196 -3.375 1.00124.26 C
ANISOU 2571 CG ASN A1115 16672 17978 12564 -2392 -855 -220 C
ATOM 2572 OD1 ASN A1115 17.798 66.021 -4.285 1.00118.50 O
ANISOU 2572 OD1 ASN A1115 16095 17148 11783 -2471 -850 -219 O
ATOM 2573 ND2 ASN A1115 17.920 65.559 -2.098 1.00116.94 N
ANISOU 2573 ND2 ASN A1115 15779 17044 11608 -2381 -875 -225 N
ATOM 2574 N SER A1116 17.335 60.598 -4.455 1.00 92.14 N
ANISOU 2574 N SER A1116 12088 14117 8803 -1974 -810 -162 N
ATOM 2575 CA SER A1116 17.736 59.237 -4.819 1.00 90.88 C
ANISOU 2575 CA SER A1116 11767 14066 8698 -1901 -799 -161 C
ATOM 2576 C SER A1116 17.052 58.809 -6.123 1.00 92.49 C
ANISOU 2576 C SER A1116 11970 14211 8962 -1861 -776 -138 C
ATOM 2577 O SER A1116 17.705 58.207 -6.973 1.00 91.02 O
ANISOU 2577 O SER A1116 11685 14115 8783 -1890 -764 -149 O
ATOM 2578 CB SER A1116 17.405 58.258 -3.695 1.00 94.38 C
ANISOU 2578 CB SER A1116 12160 14519 9180 -1756 -803 -144 C
ATOM 2579 OG SER A1116 17.829 58.721 -2.422 1.00103.58 O
ANISOU 2579 OG SER A1116 13358 15710 10288 -1775 -830 -161 O
ATOM 2580 N LEU A1117 15.740 59.127 -6.277 1.00 89.31 N
ANISOU 2580 N LEU A1117 11672 13661 8599 -1790 -773 -116 N
ATOM 2581 CA LEU A1117 14.927 58.837 -7.471 1.00 88.95 C
ANISOU 2581 CA LEU A1117 11643 13542 8611 -1736 -764 -104 C
ATOM 2582 C LEU A1117 15.443 59.668 -8.649 1.00 94.19 C
ANISOU 2582 C LEU A1117 12387 14190 9210 -1868 -771 -114 C
ATOM 2583 O LEU A1117 15.469 59.181 -9.783 1.00 93.43 O
ANISOU 2583 O LEU A1117 12250 14109 9139 -1866 -759 -109 O
ATOM 2584 CB LEU A1117 13.435 59.158 -7.235 1.00 88.67 C
ANISOU 2584 CB LEU A1117 11704 13364 8622 -1635 -773 -107 C
ATOM 2585 CG LEU A1117 12.652 58.323 -6.208 1.00 92.89 C
ANISOU 2585 CG LEU A1117 12177 13889 9227 -1511 -744 -107 C
ATOM 2586 CD1 LEU A1117 11.470 59.105 -5.679 1.00 93.21 C
ANISOU 2586 CD1 LEU A1117 12324 13809 9281 -1457 -754 -135 C
ATOM 2587 CD2 LEU A1117 12.167 57.002 -6.795 1.00 93.89 C
ANISOU 2587 CD2 LEU A1117 12197 14036 9441 -1419 -711 -101 C
ATOM 2588 N ARG A1118 15.868 60.920 -8.360 1.00 92.13 N
ANISOU 2588 N ARG A1118 12255 13894 8855 -1990 -786 -131 N
ATOM 2589 CA ARG A1118 16.448 61.867 -9.310 1.00 93.18 C
ANISOU 2589 CA ARG A1118 12512 13998 8896 -2150 -781 -148 C
ATOM 2590 C ARG A1118 17.695 61.238 -9.933 1.00100.34 C
ANISOU 2590 C ARG A1118 13273 15062 9789 -2251 -742 -171 C
ATOM 2591 O ARG A1118 17.828 61.238 -11.155 1.00100.54 O
ANISOU 2591 O ARG A1118 13336 15069 9797 -2308 -722 -174 O
ATOM 2592 CB ARG A1118 16.803 63.181 -8.590 1.00 92.24 C
ANISOU 2592 CB ARG A1118 12538 13835 8673 -2271 -794 -167 C
ATOM 2593 CG ARG A1118 17.034 64.369 -9.512 1.00 96.90 C
ANISOU 2593 CG ARG A1118 13344 14323 9150 -2422 -791 -181 C
ATOM 2594 CD ARG A1118 16.862 65.680 -8.773 1.00102.78 C
ANISOU 2594 CD ARG A1118 14281 14968 9803 -2489 -817 -190 C
ATOM 2595 NE ARG A1118 18.112 66.128 -8.158 1.00112.00 N
ANISOU 2595 NE ARG A1118 15405 16253 10895 -2668 -784 -228 N
ATOM 2596 CZ ARG A1118 18.745 67.252 -8.480 1.00127.87 C
ANISOU 2596 CZ ARG A1118 17587 18223 12775 -2869 -761 -259 C
ATOM 2597 NH1 ARG A1118 18.243 68.066 -9.400 1.00121.72 N
ANISOU 2597 NH1 ARG A1118 17064 17269 11914 -2910 -773 -248 N
ATOM 2598 NH2 ARG A1118 19.880 67.577 -7.877 1.00110.82 N
ANISOU 2598 NH2 ARG A1118 15356 16193 10559 -3032 -729 -310 N
ATOM 2599 N MET A1119 18.573 60.658 -9.087 1.00 99.02 N
ANISOU 2599 N MET A1119 12940 15050 9632 -2257 -736 -196 N
ATOM 2600 CA MET A1119 19.810 59.983 -9.487 1.00100.15 C
ANISOU 2600 CA MET A1119 12911 15372 9768 -2329 -709 -241 C
ATOM 2601 C MET A1119 19.517 58.704 -10.289 1.00104.04 C
ANISOU 2601 C MET A1119 13287 15897 10346 -2209 -698 -217 C
ATOM 2602 O MET A1119 20.193 58.453 -11.289 1.00103.93 O
ANISOU 2602 O MET A1119 13207 15963 10317 -2289 -666 -248 O
ATOM 2603 CB MET A1119 20.695 59.691 -8.261 1.00103.25 C
ANISOU 2603 CB MET A1119 13168 15914 10147 -2327 -730 -285 C
ATOM 2604 CG MET A1119 21.287 60.946 -7.626 1.00108.54 C
ANISOU 2604 CG MET A1119 13928 16589 10722 -2489 -732 -329 C
ATOM 2605 SD MET A1119 21.797 60.695 -5.901 1.00113.65 S
ANISOU 2605 SD MET A1119 14478 17340 11362 -2423 -783 -359 S
ATOM 2606 CE MET A1119 21.822 62.396 -5.308 1.00111.18 C
ANISOU 2606 CE MET A1119 14362 16934 10946 -2591 -783 -375 C
ATOM 2607 N LEU A1120 18.488 57.922 -9.875 1.00100.12 N
ANISOU 2607 N LEU A1120 12772 15335 9934 -2028 -717 -170 N
ATOM 2608 CA LEU A1120 18.066 56.689 -10.560 1.00 99.21 C
ANISOU 2608 CA LEU A1120 12564 15232 9900 -1908 -705 -145 C
ATOM 2609 C LEU A1120 17.496 56.996 -11.942 1.00104.75 C
ANISOU 2609 C LEU A1120 13361 15832 10607 -1938 -692 -129 C
ATOM 2610 O LEU A1120 17.724 56.233 -12.887 1.00104.61 O
ANISOU 2610 O LEU A1120 13264 15865 10617 -1926 -673 -129 O
ATOM 2611 CB LEU A1120 17.031 55.904 -9.734 1.00 97.94 C
ANISOU 2611 CB LEU A1120 12388 15009 9815 -1736 -715 -109 C
ATOM 2612 CG LEU A1120 17.533 55.125 -8.524 1.00101.49 C
ANISOU 2612 CG LEU A1120 12742 15553 10266 -1662 -727 -116 C
ATOM 2613 CD1 LEU A1120 16.376 54.669 -7.688 1.00100.60 C
ANISOU 2613 CD1 LEU A1120 12676 15342 10206 -1534 -718 -85 C
ATOM 2614 CD2 LEU A1120 18.378 53.928 -8.935 1.00102.75 C
ANISOU 2614 CD2 LEU A1120 12751 15849 10439 -1618 -727 -133 C
ATOM 2615 N GLN A1121 16.758 58.121 -12.053 1.00102.12 N
ANISOU 2615 N GLN A1121 13211 15350 10239 -1967 -711 -119 N
ATOM 2616 CA GLN A1121 16.169 58.618 -13.300 1.00102.31 C
ANISOU 2616 CA GLN A1121 13378 15251 10246 -1987 -719 -111 C
ATOM 2617 C GLN A1121 17.294 58.952 -14.288 1.00107.22 C
ANISOU 2617 C GLN A1121 14023 15933 10783 -2164 -681 -137 C
ATOM 2618 O GLN A1121 17.196 58.608 -15.467 1.00106.31 O
ANISOU 2618 O GLN A1121 13924 15793 10676 -2165 -668 -131 O
ATOM 2619 CB GLN A1121 15.328 59.872 -13.001 1.00104.04 C
ANISOU 2619 CB GLN A1121 13802 15308 10420 -1981 -761 -110 C
ATOM 2620 CG GLN A1121 14.552 60.434 -14.182 1.00118.71 C
ANISOU 2620 CG GLN A1121 15838 17012 12253 -1957 -795 -108 C
ATOM 2621 CD GLN A1121 13.841 61.703 -13.792 1.00137.63 C
ANISOU 2621 CD GLN A1121 18443 19258 14592 -1940 -849 -120 C
ATOM 2622 OE1 GLN A1121 12.638 61.705 -13.516 1.00132.37 O
ANISOU 2622 OE1 GLN A1121 17794 18511 13991 -1787 -893 -129 O
ATOM 2623 NE2 GLN A1121 14.575 62.808 -13.738 1.00131.12 N
ANISOU 2623 NE2 GLN A1121 17778 18399 13642 -2102 -842 -130 N
ATOM 2624 N GLN A1122 18.381 59.581 -13.768 1.00105.11 N
ANISOU 2624 N GLN A1122 13748 15754 10436 -2319 -657 -176 N
ATOM 2625 CA GLN A1122 19.583 60.025 -14.482 1.00105.92 C
ANISOU 2625 CA GLN A1122 13860 15937 10446 -2527 -603 -227 C
ATOM 2626 C GLN A1122 20.645 58.918 -14.681 1.00110.10 C
ANISOU 2626 C GLN A1122 14143 16675 11015 -2539 -566 -270 C
ATOM 2627 O GLN A1122 21.751 59.205 -15.142 1.00110.90 O
ANISOU 2627 O GLN A1122 14205 16884 11048 -2717 -512 -337 O
ATOM 2628 CB GLN A1122 20.181 61.260 -13.781 1.00108.23 C
ANISOU 2628 CB GLN A1122 14260 16227 10634 -2693 -593 -266 C
ATOM 2629 CG GLN A1122 19.295 62.502 -13.876 1.00125.12 C
ANISOU 2629 CG GLN A1122 16683 18151 12704 -2707 -626 -235 C
ATOM 2630 CD GLN A1122 19.774 63.639 -13.008 1.00148.96 C
ANISOU 2630 CD GLN A1122 19807 21162 15628 -2846 -623 -266 C
ATOM 2631 OE1 GLN A1122 19.976 63.496 -11.796 1.00144.33 O
ANISOU 2631 OE1 GLN A1122 19098 20668 15073 -2811 -640 -278 O
ATOM 2632 NE2 GLN A1122 19.915 64.813 -13.604 1.00144.58 N
ANISOU 2632 NE2 GLN A1122 19508 20479 14947 -3001 -605 -278 N
ATOM 2633 N LYS A1123 20.294 57.659 -14.340 1.00105.94 N
ANISOU 2633 N LYS A1123 13458 16201 10592 -2352 -593 -242 N
ATOM 2634 CA LYS A1123 21.095 56.429 -14.470 1.00105.71 C
ANISOU 2634 CA LYS A1123 13206 16349 10610 -2302 -579 -275 C
ATOM 2635 C LYS A1123 22.440 56.437 -13.674 1.00111.58 C
ANISOU 2635 C LYS A1123 13794 17288 11313 -2383 -577 -360 C
ATOM 2636 O LYS A1123 23.380 55.730 -14.051 1.00111.61 O
ANISOU 2636 O LYS A1123 13628 17455 11322 -2402 -558 -423 O
ATOM 2637 CB LYS A1123 21.313 56.058 -15.951 1.00107.74 C
ANISOU 2637 CB LYS A1123 13452 16619 10867 -2353 -535 -284 C
ATOM 2638 CG LYS A1123 20.007 55.911 -16.723 1.00121.69 C
ANISOU 2638 CG LYS A1123 15349 18208 12680 -2247 -552 -211 C
ATOM 2639 CD LYS A1123 20.090 54.880 -17.838 1.00129.98 C
ANISOU 2639 CD LYS A1123 16321 19297 13768 -2211 -525 -207 C
ATOM 2640 CE LYS A1123 18.737 54.618 -18.461 1.00136.42 C
ANISOU 2640 CE LYS A1123 17243 19950 14642 -2082 -555 -145 C
ATOM 2641 NZ LYS A1123 17.833 53.852 -17.558 1.00142.04 N
ANISOU 2641 NZ LYS A1123 17876 20641 15451 -1891 -593 -107 N
ATOM 2642 N ARG A1124 22.493 57.168 -12.534 1.00108.94 N
ANISOU 2642 N ARG A1124 13508 16941 10943 -2410 -605 -370 N
ATOM 2643 CA ARG A1124 23.662 57.231 -11.643 1.00109.87 C
ANISOU 2643 CA ARG A1124 13488 17234 11023 -2469 -621 -457 C
ATOM 2644 C ARG A1124 23.525 56.115 -10.587 1.00113.91 C
ANISOU 2644 C ARG A1124 13879 17805 11598 -2255 -684 -439 C
ATOM 2645 O ARG A1124 23.361 56.398 -9.396 1.00112.74 O
ANISOU 2645 O ARG A1124 13768 17630 11437 -2207 -725 -428 O
ATOM 2646 CB ARG A1124 23.755 58.602 -10.940 1.00110.55 C
ANISOU 2646 CB ARG A1124 13711 17263 11031 -2607 -622 -473 C
ATOM 2647 CG ARG A1124 23.898 59.821 -11.834 1.00120.93 C
ANISOU 2647 CG ARG A1124 15189 18504 12255 -2835 -558 -497 C
ATOM 2648 CD ARG A1124 23.693 61.067 -10.996 1.00130.06 C
ANISOU 2648 CD ARG A1124 16518 19556 13341 -2919 -574 -487 C
ATOM 2649 NE ARG A1124 23.668 62.288 -11.799 1.00139.53 N
ANISOU 2649 NE ARG A1124 17938 20640 14438 -3123 -520 -496 N
ATOM 2650 CZ ARG A1124 23.387 63.495 -11.316 1.00155.36 C
ANISOU 2650 CZ ARG A1124 20147 22519 16362 -3213 -527 -484 C
ATOM 2651 NH1 ARG A1124 23.104 63.655 -10.027 1.00139.67 N
ANISOU 2651 NH1 ARG A1124 18157 20517 14394 -3121 -583 -464 N
ATOM 2652 NH2 ARG A1124 23.384 64.551 -12.118 1.00146.13 N
ANISOU 2652 NH2 ARG A1124 19207 21232 15084 -3396 -478 -494 N
ATOM 2653 N TRP A1125 23.585 54.846 -11.037 1.00111.67 N
ANISOU 2653 N TRP A1125 13470 17588 11370 -2128 -691 -436 N
ATOM 2654 CA TRP A1125 23.424 53.651 -10.198 1.00111.87 C
ANISOU 2654 CA TRP A1125 13415 17649 11443 -1919 -746 -415 C
ATOM 2655 C TRP A1125 24.343 53.602 -8.972 1.00117.15 C
ANISOU 2655 C TRP A1125 13988 18454 12069 -1888 -808 -490 C
ATOM 2656 O TRP A1125 23.900 53.182 -7.901 1.00116.48 O
ANISOU 2656 O TRP A1125 13944 18320 11994 -1744 -855 -452 O
ATOM 2657 CB TRP A1125 23.560 52.355 -11.020 1.00110.76 C
ANISOU 2657 CB TRP A1125 13162 17573 11350 -1813 -741 -417 C
ATOM 2658 CG TRP A1125 22.918 52.356 -12.383 1.00111.44 C
ANISOU 2658 CG TRP A1125 13313 17559 11470 -1855 -685 -366 C
ATOM 2659 CD1 TRP A1125 23.499 51.967 -13.554 1.00114.72 C
ANISOU 2659 CD1 TRP A1125 13641 18060 11889 -1908 -649 -405 C
ATOM 2660 CD2 TRP A1125 21.563 52.719 -12.708 1.00110.50 C
ANISOU 2660 CD2 TRP A1125 13359 17240 11386 -1836 -666 -276 C
ATOM 2661 NE1 TRP A1125 22.601 52.080 -14.592 1.00113.64 N
ANISOU 2661 NE1 TRP A1125 13617 17780 11780 -1925 -611 -338 N
ATOM 2662 CE2 TRP A1125 21.409 52.552 -14.104 1.00114.35 C
ANISOU 2662 CE2 TRP A1125 13859 17697 11891 -1876 -626 -263 C
ATOM 2663 CE3 TRP A1125 20.466 53.186 -11.958 1.00111.22 C
ANISOU 2663 CE3 TRP A1125 13585 17181 11494 -1784 -681 -217 C
ATOM 2664 CZ2 TRP A1125 20.199 52.817 -14.762 1.00112.88 C
ANISOU 2664 CZ2 TRP A1125 13816 17336 11739 -1855 -613 -197 C
ATOM 2665 CZ3 TRP A1125 19.280 53.479 -12.617 1.00112.05 C
ANISOU 2665 CZ3 TRP A1125 13816 17123 11634 -1768 -664 -162 C
ATOM 2666 CH2 TRP A1125 19.155 53.298 -14.003 1.00112.52 C
ANISOU 2666 CH2 TRP A1125 13886 17155 11710 -1798 -636 -153 C
ATOM 2667 N ASP A1126 25.606 54.031 -9.119 1.00115.16 N
ANISOU 2667 N ASP A1126 13616 18374 11766 -2025 -805 -606 N
ATOM 2668 CA ASP A1126 26.558 54.037 -8.008 1.00116.02 C
ANISOU 2668 CA ASP A1126 13618 18631 11832 -1999 -874 -701 C
ATOM 2669 C ASP A1126 26.314 55.186 -7.031 1.00118.77 C
ANISOU 2669 C ASP A1126 14095 18897 12135 -2085 -884 -684 C
ATOM 2670 O ASP A1126 26.484 54.995 -5.826 1.00118.34 O
ANISOU 2670 O ASP A1126 14033 18868 12061 -1980 -955 -698 O
ATOM 2671 CB ASP A1126 28.005 54.005 -8.512 1.00119.65 C
ANISOU 2671 CB ASP A1126 13871 19330 12262 -2107 -869 -857 C
ATOM 2672 CG ASP A1126 28.482 52.603 -8.828 1.00131.76 C
ANISOU 2672 CG ASP A1126 15240 20992 13830 -1937 -912 -905 C
ATOM 2673 OD1 ASP A1126 28.324 52.170 -9.991 1.00131.79 O
ANISOU 2673 OD1 ASP A1126 15229 20975 13871 -1945 -857 -875 O
ATOM 2674 OD2 ASP A1126 28.989 51.928 -7.905 1.00139.60 O
ANISOU 2674 OD2 ASP A1126 16134 22099 14809 -1784 -1007 -972 O
ATOM 2675 N GLU A1127 25.898 56.365 -7.544 1.00114.52 N
ANISOU 2675 N GLU A1127 13694 18249 11570 -2266 -817 -652 N
ATOM 2676 CA GLU A1127 25.595 57.545 -6.727 1.00114.16 C
ANISOU 2676 CA GLU A1127 13795 18106 11475 -2357 -821 -631 C
ATOM 2677 C GLU A1127 24.301 57.340 -5.956 1.00115.78 C
ANISOU 2677 C GLU A1127 14144 18129 11718 -2195 -849 -516 C
ATOM 2678 O GLU A1127 24.219 57.730 -4.790 1.00115.32 O
ANISOU 2678 O GLU A1127 14139 18046 11631 -2168 -889 -514 O
ATOM 2679 CB GLU A1127 25.499 58.810 -7.588 1.00115.91 C
ANISOU 2679 CB GLU A1127 14153 18242 11644 -2583 -745 -630 C
ATOM 2680 CG GLU A1127 26.846 59.415 -7.925 1.00129.25 C
ANISOU 2680 CG GLU A1127 15737 20106 13266 -2804 -704 -767 C
ATOM 2681 CD GLU A1127 26.760 60.663 -8.778 1.00154.62 C
ANISOU 2681 CD GLU A1127 19130 23214 16406 -3042 -621 -765 C
ATOM 2682 OE1 GLU A1127 26.640 61.769 -8.202 1.00151.69 O
ANISOU 2682 OE1 GLU A1127 18903 22763 15969 -3149 -620 -763 O
ATOM 2683 OE2 GLU A1127 26.816 60.537 -10.023 1.00149.09 O
ANISOU 2683 OE2 GLU A1127 18443 22502 15702 -3120 -557 -769 O
ATOM 2684 N ALA A1128 23.295 56.719 -6.608 1.00110.59 N
ANISOU 2684 N ALA A1128 13542 17351 11125 -2093 -824 -430 N
ATOM 2685 CA ALA A1128 21.993 56.419 -6.013 1.00109.07 C
ANISOU 2685 CA ALA A1128 13468 16996 10978 -1947 -833 -338 C
ATOM 2686 C ALA A1128 22.110 55.351 -4.921 1.00111.98 C
ANISOU 2686 C ALA A1128 13773 17415 11359 -1772 -884 -338 C
ATOM 2687 O ALA A1128 21.385 55.424 -3.930 1.00111.51 O
ANISOU 2687 O ALA A1128 13817 17251 11301 -1695 -895 -293 O
ATOM 2688 CB ALA A1128 21.012 55.979 -7.083 1.00108.86 C
ANISOU 2688 CB ALA A1128 13489 16855 11016 -1894 -792 -273 C
ATOM 2689 N ALA A1129 23.046 54.390 -5.084 1.00107.92 N
ANISOU 2689 N ALA A1129 13103 17060 10843 -1710 -918 -397 N
ATOM 2690 CA ALA A1129 23.311 53.325 -4.109 1.00107.44 C
ANISOU 2690 CA ALA A1129 13000 17051 10772 -1533 -983 -410 C
ATOM 2691 C ALA A1129 23.892 53.884 -2.799 1.00109.99 C
ANISOU 2691 C ALA A1129 13341 17424 11028 -1544 -1045 -461 C
ATOM 2692 O ALA A1129 23.713 53.282 -1.739 1.00109.44 O
ANISOU 2692 O ALA A1129 13328 17317 10936 -1401 -1092 -442 O
ATOM 2693 CB ALA A1129 24.260 52.298 -4.703 1.00108.89 C
ANISOU 2693 CB ALA A1129 13015 17399 10960 -1466 -1016 -480 C
ATOM 2694 N VAL A1130 24.583 55.035 -2.887 1.00105.99 N
ANISOU 2694 N VAL A1130 12798 16994 10480 -1720 -1041 -527 N
ATOM 2695 CA VAL A1130 25.186 55.744 -1.755 1.00106.16 C
ANISOU 2695 CA VAL A1130 12830 17070 10436 -1764 -1095 -586 C
ATOM 2696 C VAL A1130 24.078 56.470 -0.978 1.00108.17 C
ANISOU 2696 C VAL A1130 13283 17132 10683 -1771 -1071 -496 C
ATOM 2697 O VAL A1130 24.012 56.351 0.247 1.00108.08 O
ANISOU 2697 O VAL A1130 13333 17093 10638 -1681 -1121 -491 O
ATOM 2698 CB VAL A1130 26.308 56.716 -2.235 1.00111.11 C
ANISOU 2698 CB VAL A1130 13348 17850 11020 -1976 -1082 -701 C
ATOM 2699 CG1 VAL A1130 26.728 57.692 -1.137 1.00111.76 C
ANISOU 2699 CG1 VAL A1130 13473 17957 11035 -2059 -1121 -751 C
ATOM 2700 CG2 VAL A1130 27.519 55.952 -2.765 1.00111.88 C
ANISOU 2700 CG2 VAL A1130 13220 18170 11119 -1952 -1116 -822 C
ATOM 2701 N ASN A1131 23.214 57.211 -1.705 1.00102.85 N
ANISOU 2701 N ASN A1131 12717 16324 10038 -1870 -998 -433 N
ATOM 2702 CA ASN A1131 22.114 58.011 -1.165 1.00101.49 C
ANISOU 2702 CA ASN A1131 12725 15972 9863 -1883 -972 -362 C
ATOM 2703 C ASN A1131 20.976 57.177 -0.555 1.00101.96 C
ANISOU 2703 C ASN A1131 12867 15905 9969 -1709 -962 -287 C
ATOM 2704 O ASN A1131 20.434 57.566 0.487 1.00101.39 O
ANISOU 2704 O ASN A1131 12909 15739 9875 -1680 -966 -261 O
ATOM 2705 CB ASN A1131 21.586 58.976 -2.229 1.00103.78 C
ANISOU 2705 CB ASN A1131 13105 16165 10160 -2019 -914 -336 C
ATOM 2706 CG ASN A1131 21.012 60.252 -1.662 1.00136.76 C
ANISOU 2706 CG ASN A1131 17455 20211 14298 -2090 -908 -310 C
ATOM 2707 OD1 ASN A1131 19.789 60.425 -1.573 1.00133.89 O
ANISOU 2707 OD1 ASN A1131 17209 19693 13970 -2018 -887 -249 O
ATOM 2708 ND2 ASN A1131 21.884 61.180 -1.274 1.00130.48 N
ANISOU 2708 ND2 ASN A1131 16672 19478 13425 -2233 -925 -368 N
ATOM 2709 N LEU A1132 20.621 56.036 -1.190 1.00 95.53 N
ANISOU 2709 N LEU A1132 11998 15086 9212 -1604 -941 -258 N
ATOM 2710 CA LEU A1132 19.566 55.149 -0.692 1.00 93.55 C
ANISOU 2710 CA LEU A1132 11823 14721 9001 -1459 -915 -199 C
ATOM 2711 C LEU A1132 19.966 54.447 0.614 1.00 98.23 C
ANISOU 2711 C LEU A1132 12439 15343 9540 -1343 -966 -213 C
ATOM 2712 O LEU A1132 19.090 53.986 1.348 1.00 97.98 O
ANISOU 2712 O LEU A1132 12518 15196 9513 -1256 -935 -171 O
ATOM 2713 CB LEU A1132 19.135 54.127 -1.755 1.00 92.37 C
ANISOU 2713 CB LEU A1132 11617 14559 8920 -1393 -877 -171 C
ATOM 2714 CG LEU A1132 18.250 54.636 -2.890 1.00 95.45 C
ANISOU 2714 CG LEU A1132 12039 14857 9370 -1457 -822 -140 C
ATOM 2715 CD1 LEU A1132 18.307 53.705 -4.064 1.00 95.03 C
ANISOU 2715 CD1 LEU A1132 11893 14848 9367 -1421 -804 -134 C
ATOM 2716 CD2 LEU A1132 16.817 54.774 -2.456 1.00 96.60 C
ANISOU 2716 CD2 LEU A1132 12301 14845 9557 -1404 -775 -101 C
ATOM 2717 N ALA A1133 21.282 54.394 0.912 1.00 95.25 N
ANISOU 2717 N ALA A1133 11965 15120 9106 -1343 -1044 -284 N
ATOM 2718 CA ALA A1133 21.857 53.807 2.126 1.00 95.55 C
ANISOU 2718 CA ALA A1133 12027 15201 9075 -1224 -1120 -315 C
ATOM 2719 C ALA A1133 21.938 54.847 3.262 1.00 99.90 C
ANISOU 2719 C ALA A1133 12668 15723 9567 -1284 -1148 -330 C
ATOM 2720 O ALA A1133 22.072 54.479 4.436 1.00100.18 O
ANISOU 2720 O ALA A1133 12785 15738 9542 -1182 -1199 -336 O
ATOM 2721 CB ALA A1133 23.239 53.249 1.823 1.00 97.24 C
ANISOU 2721 CB ALA A1133 12075 15611 9261 -1181 -1204 -406 C
ATOM 2722 N LYS A1134 21.836 56.146 2.907 1.00 95.89 N
ANISOU 2722 N LYS A1134 12167 15200 9067 -1447 -1115 -334 N
ATOM 2723 CA LYS A1134 21.868 57.270 3.852 1.00 95.82 C
ANISOU 2723 CA LYS A1134 12250 15155 9003 -1526 -1133 -346 C
ATOM 2724 C LYS A1134 20.466 57.576 4.433 1.00 98.42 C
ANISOU 2724 C LYS A1134 12755 15289 9351 -1501 -1069 -268 C
ATOM 2725 O LYS A1134 20.275 58.633 5.042 1.00 98.53 O
ANISOU 2725 O LYS A1134 12859 15245 9332 -1583 -1066 -267 O
ATOM 2726 CB LYS A1134 22.447 58.525 3.166 1.00 98.48 C
ANISOU 2726 CB LYS A1134 12532 15560 9326 -1722 -1124 -394 C
ATOM 2727 CG LYS A1134 23.945 58.471 2.900 1.00114.79 C
ANISOU 2727 CG LYS A1134 14422 17838 11354 -1781 -1186 -505 C
ATOM 2728 CD LYS A1134 24.426 59.749 2.223 1.00126.85 C
ANISOU 2728 CD LYS A1134 15926 19412 12858 -2006 -1150 -554 C
ATOM 2729 CE LYS A1134 25.919 59.759 2.008 1.00139.74 C
ANISOU 2729 CE LYS A1134 17372 21270 14453 -2090 -1197 -689 C
ATOM 2730 NZ LYS A1134 26.359 60.976 1.277 1.00149.70 N
ANISOU 2730 NZ LYS A1134 18634 22565 15679 -2337 -1140 -741 N
ATOM 2731 N SER A1135 19.496 56.648 4.251 1.00 93.10 N
ANISOU 2731 N SER A1135 12127 14519 8728 -1393 -1015 -214 N
ATOM 2732 CA SER A1135 18.107 56.806 4.687 1.00 91.72 C
ANISOU 2732 CA SER A1135 12090 14177 8584 -1369 -940 -162 C
ATOM 2733 C SER A1135 17.771 56.165 6.039 1.00 95.82 C
ANISOU 2733 C SER A1135 12732 14620 9054 -1262 -934 -147 C
ATOM 2734 O SER A1135 18.550 55.368 6.573 1.00 96.27 O
ANISOU 2734 O SER A1135 12783 14741 9056 -1173 -995 -166 O
ATOM 2735 CB SER A1135 17.156 56.288 3.612 1.00 93.50 C
ANISOU 2735 CB SER A1135 12287 14339 8899 -1349 -867 -129 C
ATOM 2736 OG SER A1135 17.170 54.871 3.544 1.00 99.93 O
ANISOU 2736 OG SER A1135 13073 15169 9728 -1236 -857 -117 O
ATOM 2737 N ARG A1136 16.580 56.527 6.576 1.00 90.98 N
ANISOU 2737 N ARG A1136 12242 13868 8459 -1268 -861 -121 N
ATOM 2738 CA ARG A1136 15.985 56.020 7.815 1.00 90.05 C
ANISOU 2738 CA ARG A1136 12268 13648 8298 -1193 -820 -106 C
ATOM 2739 C ARG A1136 15.404 54.624 7.530 1.00 93.85 C
ANISOU 2739 C ARG A1136 12760 14086 8812 -1104 -757 -86 C
ATOM 2740 O ARG A1136 15.253 53.823 8.449 1.00 94.14 O
ANISOU 2740 O ARG A1136 12917 14065 8788 -1028 -739 -79 O
ATOM 2741 CB ARG A1136 14.886 56.986 8.287 1.00 87.25 C
ANISOU 2741 CB ARG A1136 12012 13175 7964 -1246 -750 -103 C
ATOM 2742 CG ARG A1136 14.439 56.791 9.720 1.00 92.81 C
ANISOU 2742 CG ARG A1136 12878 13783 8604 -1201 -710 -101 C
ATOM 2743 CD ARG A1136 13.504 57.895 10.159 1.00 99.37 C
ANISOU 2743 CD ARG A1136 13787 14520 9449 -1259 -656 -112 C
ATOM 2744 NE ARG A1136 14.233 59.025 10.739 1.00106.29 N
ANISOU 2744 NE ARG A1136 14697 15430 10259 -1316 -736 -122 N
ATOM 2745 CZ ARG A1136 13.710 60.228 10.960 1.00116.36 C
ANISOU 2745 CZ ARG A1136 16027 16646 11537 -1378 -722 -134 C
ATOM 2746 NH1 ARG A1136 12.449 60.481 10.637 1.00102.58 N
ANISOU 2746 NH1 ARG A1136 14299 14815 9863 -1378 -638 -147 N
ATOM 2747 NH2 ARG A1136 14.449 61.191 11.494 1.00 99.91 N
ANISOU 2747 NH2 ARG A1136 13982 14594 9385 -1436 -795 -142 N
ATOM 2748 N TRP A1137 15.093 54.343 6.242 1.00 89.58 N
ANISOU 2748 N TRP A1137 12110 13568 8360 -1119 -723 -79 N
ATOM 2749 CA TRP A1137 14.583 53.068 5.732 1.00 88.74 C
ANISOU 2749 CA TRP A1137 11991 13432 8293 -1052 -664 -64 C
ATOM 2750 C TRP A1137 15.680 52.003 5.810 1.00 92.80 C
ANISOU 2750 C TRP A1137 12487 14030 8744 -960 -740 -65 C
ATOM 2751 O TRP A1137 15.397 50.870 6.203 1.00 92.58 O
ANISOU 2751 O TRP A1137 12553 13941 8683 -878 -704 -52 O
ATOM 2752 CB TRP A1137 14.086 53.250 4.281 1.00 86.55 C
ANISOU 2752 CB TRP A1137 11593 13171 8122 -1097 -631 -63 C
ATOM 2753 CG TRP A1137 14.101 52.012 3.430 1.00 87.18 C
ANISOU 2753 CG TRP A1137 11608 13277 8239 -1038 -611 -51 C
ATOM 2754 CD1 TRP A1137 13.344 50.890 3.598 1.00 90.02 C
ANISOU 2754 CD1 TRP A1137 12035 13559 8610 -980 -530 -42 C
ATOM 2755 CD2 TRP A1137 14.869 51.804 2.234 1.00 86.80 C
ANISOU 2755 CD2 TRP A1137 11422 13335 8222 -1042 -663 -50 C
ATOM 2756 NE1 TRP A1137 13.625 49.977 2.608 1.00 89.31 N
ANISOU 2756 NE1 TRP A1137 11862 13520 8553 -939 -539 -31 N
ATOM 2757 CE2 TRP A1137 14.545 50.519 1.746 1.00 90.58 C
ANISOU 2757 CE2 TRP A1137 11891 13795 8730 -972 -620 -36 C
ATOM 2758 CE3 TRP A1137 15.799 52.581 1.522 1.00 88.05 C
ANISOU 2758 CE3 TRP A1137 11473 13601 8380 -1111 -732 -67 C
ATOM 2759 CZ2 TRP A1137 15.106 49.998 0.570 1.00 89.62 C
ANISOU 2759 CZ2 TRP A1137 11649 13761 8643 -956 -651 -34 C
ATOM 2760 CZ3 TRP A1137 16.364 52.059 0.367 1.00 89.31 C
ANISOU 2760 CZ3 TRP A1137 11512 13849 8572 -1104 -754 -70 C
ATOM 2761 CH2 TRP A1137 16.024 50.780 -0.094 1.00 89.62 C
ANISOU 2761 CH2 TRP A1137 11538 13870 8644 -1020 -718 -53 C
ATOM 2762 N TYR A1138 16.922 52.375 5.427 1.00 89.46 N
ANISOU 2762 N TYR A1138 11946 13745 8298 -977 -844 -91 N
ATOM 2763 CA TYR A1138 18.103 51.515 5.442 1.00 89.84 C
ANISOU 2763 CA TYR A1138 11942 13904 8289 -883 -939 -118 C
ATOM 2764 C TYR A1138 18.490 51.134 6.859 1.00 94.02 C
ANISOU 2764 C TYR A1138 12617 14403 8704 -787 -998 -131 C
ATOM 2765 O TYR A1138 18.783 49.968 7.096 1.00 94.52 O
ANISOU 2765 O TYR A1138 12733 14469 8711 -662 -1038 -135 O
ATOM 2766 CB TYR A1138 19.280 52.200 4.734 1.00 91.77 C
ANISOU 2766 CB TYR A1138 12010 14316 8542 -951 -1022 -168 C
ATOM 2767 CG TYR A1138 20.575 51.413 4.748 1.00 95.35 C
ANISOU 2767 CG TYR A1138 12377 14913 8940 -850 -1131 -225 C
ATOM 2768 CD1 TYR A1138 20.875 50.508 3.734 1.00 97.45 C
ANISOU 2768 CD1 TYR A1138 12540 15245 9243 -794 -1136 -232 C
ATOM 2769 CD2 TYR A1138 21.530 51.620 5.741 1.00 97.38 C
ANISOU 2769 CD2 TYR A1138 12646 15247 9107 -806 -1238 -283 C
ATOM 2770 CE1 TYR A1138 22.083 49.810 3.720 1.00 99.71 C
ANISOU 2770 CE1 TYR A1138 12735 15674 9478 -688 -1245 -300 C
ATOM 2771 CE2 TYR A1138 22.738 50.923 5.741 1.00 99.44 C
ANISOU 2771 CE2 TYR A1138 12812 15653 9317 -696 -1354 -358 C
ATOM 2772 CZ TYR A1138 23.010 50.017 4.729 1.00107.83 C
ANISOU 2772 CZ TYR A1138 13769 16783 10418 -634 -1357 -369 C
ATOM 2773 OH TYR A1138 24.204 49.335 4.717 1.00110.79 O
ANISOU 2773 OH TYR A1138 14042 17310 10743 -512 -1477 -457 O
ATOM 2774 N ASN A1139 18.534 52.110 7.788 1.00 89.93 N
ANISOU 2774 N ASN A1139 12175 13853 8143 -839 -1012 -139 N
ATOM 2775 CA ASN A1139 18.906 51.857 9.183 1.00 90.49 C
ANISOU 2775 CA ASN A1139 12400 13886 8097 -751 -1074 -153 C
ATOM 2776 C ASN A1139 17.932 50.899 9.872 1.00 94.07 C
ANISOU 2776 C ASN A1139 13063 14171 8508 -679 -985 -111 C
ATOM 2777 O ASN A1139 18.372 49.983 10.564 1.00 94.92 O
ANISOU 2777 O ASN A1139 13297 14255 8515 -553 -1044 -119 O
ATOM 2778 CB ASN A1139 19.036 53.168 9.978 1.00 89.93 C
ANISOU 2778 CB ASN A1139 12364 13812 7994 -836 -1099 -170 C
ATOM 2779 CG ASN A1139 20.165 54.085 9.553 1.00108.34 C
ANISOU 2779 CG ASN A1139 14521 16309 10334 -915 -1192 -227 C
ATOM 2780 OD1 ASN A1139 21.021 53.751 8.719 1.00104.67 O
ANISOU 2780 OD1 ASN A1139 13897 15985 9886 -896 -1256 -271 O
ATOM 2781 ND2 ASN A1139 20.198 55.273 10.137 1.00 97.30 N
ANISOU 2781 ND2 ASN A1139 13154 14896 8919 -1014 -1196 -237 N
ATOM 2782 N GLN A1140 16.622 51.080 9.634 1.00 88.74 N
ANISOU 2782 N GLN A1140 12428 13383 7905 -758 -844 -77 N
ATOM 2783 CA GLN A1140 15.561 50.276 10.238 1.00 88.06 C
ANISOU 2783 CA GLN A1140 12532 13137 7789 -732 -725 -52 C
ATOM 2784 C GLN A1140 15.509 48.846 9.689 1.00 91.27 C
ANISOU 2784 C GLN A1140 12964 13524 8189 -650 -700 -38 C
ATOM 2785 O GLN A1140 15.610 47.904 10.477 1.00 91.31 O
ANISOU 2785 O GLN A1140 13163 13446 8084 -559 -704 -32 O
ATOM 2786 CB GLN A1140 14.207 50.993 10.136 1.00 88.29 C
ANISOU 2786 CB GLN A1140 12562 13079 7906 -845 -587 -48 C
ATOM 2787 CG GLN A1140 14.097 52.171 11.107 1.00 89.93 C
ANISOU 2787 CG GLN A1140 12832 13257 8080 -903 -597 -60 C
ATOM 2788 CD GLN A1140 12.925 53.080 10.845 1.00 98.94 C
ANISOU 2788 CD GLN A1140 13935 14342 9316 -1001 -492 -73 C
ATOM 2789 OE1 GLN A1140 11.955 52.724 10.177 1.00 94.19 O
ANISOU 2789 OE1 GLN A1140 13288 13702 8799 -1024 -392 -81 O
ATOM 2790 NE2 GLN A1140 12.969 54.271 11.410 1.00 89.21 N
ANISOU 2790 NE2 GLN A1140 12726 13103 8065 -1053 -518 -84 N
ATOM 2791 N THR A1141 15.384 48.679 8.355 1.00 86.85 N
ANISOU 2791 N THR A1141 12230 13032 7736 -677 -681 -34 N
ATOM 2792 CA THR A1141 15.380 47.356 7.720 1.00 86.63 C
ANISOU 2792 CA THR A1141 12210 12996 7709 -601 -664 -21 C
ATOM 2793 C THR A1141 16.645 47.210 6.846 1.00 90.41 C
ANISOU 2793 C THR A1141 12509 13643 8201 -541 -797 -41 C
ATOM 2794 O THR A1141 16.543 47.353 5.629 1.00 88.08 O
ANISOU 2794 O THR A1141 12045 13414 8008 -592 -776 -39 O
ATOM 2795 CB THR A1141 14.068 47.088 6.961 1.00 93.80 C
ANISOU 2795 CB THR A1141 13088 13830 8723 -677 -514 -9 C
ATOM 2796 OG1 THR A1141 13.939 48.014 5.887 1.00 90.28 O
ANISOU 2796 OG1 THR A1141 12437 13468 8398 -758 -519 -17 O
ATOM 2797 CG2 THR A1141 12.840 47.137 7.861 1.00 95.02 C
ANISOU 2797 CG2 THR A1141 13409 13835 8861 -738 -373 -15 C
ATOM 2798 N PRO A1142 17.852 46.965 7.431 1.00 89.09 N
ANISOU 2798 N PRO A1142 12368 13551 7930 -432 -937 -73 N
ATOM 2799 CA PRO A1142 19.061 46.884 6.598 1.00 89.69 C
ANISOU 2799 CA PRO A1142 12246 13807 8025 -384 -1057 -116 C
ATOM 2800 C PRO A1142 19.125 45.693 5.650 1.00 95.76 C
ANISOU 2800 C PRO A1142 12973 14595 8815 -303 -1051 -109 C
ATOM 2801 O PRO A1142 19.487 45.881 4.489 1.00 94.66 O
ANISOU 2801 O PRO A1142 12630 14578 8757 -342 -1070 -127 O
ATOM 2802 CB PRO A1142 20.204 46.869 7.620 1.00 92.47 C
ANISOU 2802 CB PRO A1142 12653 14227 8256 -274 -1207 -171 C
ATOM 2803 CG PRO A1142 19.591 47.262 8.920 1.00 96.79 C
ANISOU 2803 CG PRO A1142 13411 14633 8733 -296 -1164 -146 C
ATOM 2804 CD PRO A1142 18.195 46.779 8.853 1.00 91.53 C
ANISOU 2804 CD PRO A1142 12881 13796 8101 -346 -998 -84 C
ATOM 2805 N ASN A1143 18.771 44.482 6.136 1.00 93.96 N
ANISOU 2805 N ASN A1143 12952 14241 8508 -199 -1022 -83 N
ATOM 2806 CA ASN A1143 18.814 43.235 5.364 1.00 93.68 C
ANISOU 2806 CA ASN A1143 12921 14202 8472 -110 -1017 -74 C
ATOM 2807 C ASN A1143 18.047 43.329 4.044 1.00 94.67 C
ANISOU 2807 C ASN A1143 12892 14338 8740 -221 -908 -45 C
ATOM 2808 O ASN A1143 18.601 42.956 3.007 1.00 94.11 O
ANISOU 2808 O ASN A1143 12667 14376 8713 -186 -955 -62 O
ATOM 2809 CB ASN A1143 18.368 42.037 6.211 1.00 96.15 C
ANISOU 2809 CB ASN A1143 13532 14339 8660 -10 -979 -46 C
ATOM 2810 CG ASN A1143 19.272 41.773 7.397 1.00119.54 C
ANISOU 2810 CG ASN A1143 16663 17293 11462 141 -1119 -82 C
ATOM 2811 OD1 ASN A1143 19.272 42.508 8.395 1.00114.61 O
ANISOU 2811 OD1 ASN A1143 16116 16639 10791 111 -1137 -90 O
ATOM 2812 ND2 ASN A1143 20.070 40.719 7.310 1.00111.77 N
ANISOU 2812 ND2 ASN A1143 15750 16332 10387 318 -1229 -109 N
ATOM 2813 N ARG A1144 16.817 43.887 4.074 1.00 89.15 N
ANISOU 2813 N ARG A1144 12223 13536 8113 -351 -772 -13 N
ATOM 2814 CA ARG A1144 15.989 44.083 2.877 1.00 87.14 C
ANISOU 2814 CA ARG A1144 11833 13282 7993 -452 -675 3 C
ATOM 2815 C ARG A1144 16.548 45.236 2.030 1.00 90.57 C
ANISOU 2815 C ARG A1144 12043 13858 8510 -530 -733 -17 C
ATOM 2816 O ARG A1144 16.738 45.050 0.830 1.00 89.35 O
ANISOU 2816 O ARG A1144 11747 13779 8424 -541 -739 -18 O
ATOM 2817 CB ARG A1144 14.516 44.322 3.258 1.00 84.85 C
ANISOU 2817 CB ARG A1144 11646 12849 7746 -550 -526 18 C
ATOM 2818 CG ARG A1144 13.551 44.314 2.085 1.00 88.37 C
ANISOU 2818 CG ARG A1144 11976 13279 8320 -627 -429 20 C
ATOM 2819 CD ARG A1144 12.113 44.493 2.534 1.00 94.11 C
ANISOU 2819 CD ARG A1144 12795 13879 9085 -710 -284 7 C
ATOM 2820 NE ARG A1144 11.199 44.600 1.395 1.00100.46 N
ANISOU 2820 NE ARG A1144 13468 14684 10018 -774 -211 -10 N
ATOM 2821 CZ ARG A1144 9.876 44.686 1.496 1.00113.78 C
ANISOU 2821 CZ ARG A1144 15181 16287 11765 -845 -84 -47 C
ATOM 2822 NH1 ARG A1144 9.293 44.687 2.688 1.00101.48 N
ANISOU 2822 NH1 ARG A1144 13776 14634 10149 -877 -2 -68 N
ATOM 2823 NH2 ARG A1144 9.126 44.783 0.406 1.00 99.02 N
ANISOU 2823 NH2 ARG A1144 13181 14431 10011 -884 -41 -74 N
ATOM 2824 N ALA A1145 16.849 46.401 2.661 1.00 88.08 N
ANISOU 2824 N ALA A1145 11713 13576 8177 -589 -774 -35 N
ATOM 2825 CA ALA A1145 17.405 47.592 2.004 1.00 87.87 C
ANISOU 2825 CA ALA A1145 11515 13668 8205 -684 -822 -59 C
ATOM 2826 C ALA A1145 18.682 47.299 1.222 1.00 92.71 C
ANISOU 2826 C ALA A1145 11971 14446 8810 -642 -919 -99 C
ATOM 2827 O ALA A1145 18.732 47.626 0.037 1.00 92.34 O
ANISOU 2827 O ALA A1145 11785 14463 8838 -715 -902 -103 O
ATOM 2828 CB ALA A1145 17.651 48.698 3.014 1.00 89.13 C
ANISOU 2828 CB ALA A1145 11721 13827 8316 -736 -858 -76 C
ATOM 2829 N LYS A1146 19.685 46.641 1.861 1.00 89.68 N
ANISOU 2829 N LYS A1146 11613 14130 8332 -518 -1021 -138 N
ATOM 2830 CA LYS A1146 20.954 46.236 1.244 1.00 89.54 C
ANISOU 2830 CA LYS A1146 11439 14284 8297 -453 -1123 -201 C
ATOM 2831 C LYS A1146 20.714 45.465 -0.055 1.00 92.85 C
ANISOU 2831 C LYS A1146 11777 14716 8784 -439 -1076 -180 C
ATOM 2832 O LYS A1146 21.413 45.717 -1.033 1.00 93.65 O
ANISOU 2832 O LYS A1146 11699 14956 8926 -482 -1106 -224 O
ATOM 2833 CB LYS A1146 21.804 45.400 2.212 1.00 92.68 C
ANISOU 2833 CB LYS A1146 11924 14715 8576 -276 -1241 -247 C
ATOM 2834 CG LYS A1146 22.717 46.224 3.115 1.00102.50 C
ANISOU 2834 CG LYS A1146 13132 16059 9755 -279 -1347 -318 C
ATOM 2835 CD LYS A1146 23.491 45.327 4.081 1.00112.63 C
ANISOU 2835 CD LYS A1146 14527 17357 10912 -76 -1477 -368 C
ATOM 2836 CE LYS A1146 24.542 46.066 4.875 1.00123.22 C
ANISOU 2836 CE LYS A1146 15799 18830 12190 -60 -1604 -464 C
ATOM 2837 NZ LYS A1146 25.261 45.169 5.821 1.00131.68 N
ANISOU 2837 NZ LYS A1146 16993 19908 13130 163 -1749 -521 N
ATOM 2838 N ARG A1147 19.689 44.580 -0.083 1.00 87.53 N
ANISOU 2838 N ARG A1147 11238 13897 8124 -395 -993 -119 N
ATOM 2839 CA ARG A1147 19.321 43.797 -1.264 1.00 86.34 C
ANISOU 2839 CA ARG A1147 11032 13738 8037 -382 -941 -95 C
ATOM 2840 C ARG A1147 18.705 44.683 -2.354 1.00 90.66 C
ANISOU 2840 C ARG A1147 11462 14286 8699 -532 -864 -75 C
ATOM 2841 O ARG A1147 19.193 44.667 -3.484 1.00 90.61 O
ANISOU 2841 O ARG A1147 11314 14376 8739 -553 -878 -93 O
ATOM 2842 CB ARG A1147 18.389 42.632 -0.898 1.00 84.28 C
ANISOU 2842 CB ARG A1147 10960 13317 7744 -304 -871 -48 C
ATOM 2843 CG ARG A1147 19.044 41.612 0.021 1.00 91.50 C
ANISOU 2843 CG ARG A1147 12021 14218 8528 -135 -958 -68 C
ATOM 2844 CD ARG A1147 18.259 40.320 0.138 1.00 96.16 C
ANISOU 2844 CD ARG A1147 12808 14654 9075 -67 -883 -25 C
ATOM 2845 NE ARG A1147 16.983 40.486 0.833 1.00101.61 N
ANISOU 2845 NE ARG A1147 13661 15176 9771 -157 -752 14 N
ATOM 2846 CZ ARG A1147 16.818 40.363 2.145 1.00117.88 C
ANISOU 2846 CZ ARG A1147 15935 17129 11725 -124 -746 18 C
ATOM 2847 NH1 ARG A1147 17.855 40.094 2.930 1.00107.73 N
ANISOU 2847 NH1 ARG A1147 14735 15881 10317 10 -877 -11 N
ATOM 2848 NH2 ARG A1147 15.617 40.520 2.686 1.00106.36 N
ANISOU 2848 NH2 ARG A1147 14605 15528 10279 -222 -609 41 N
ATOM 2849 N VAL A1148 17.662 45.477 -2.005 1.00 87.07 N
ANISOU 2849 N VAL A1148 11076 13723 8284 -627 -788 -45 N
ATOM 2850 CA VAL A1148 16.946 46.411 -2.897 1.00 85.87 C
ANISOU 2850 CA VAL A1148 10853 13547 8227 -752 -728 -32 C
ATOM 2851 C VAL A1148 17.934 47.413 -3.543 1.00 90.87 C
ANISOU 2851 C VAL A1148 11345 14316 8866 -839 -788 -69 C
ATOM 2852 O VAL A1148 17.860 47.653 -4.753 1.00 89.58 O
ANISOU 2852 O VAL A1148 11094 14180 8761 -901 -767 -68 O
ATOM 2853 CB VAL A1148 15.753 47.111 -2.165 1.00 88.89 C
ANISOU 2853 CB VAL A1148 11344 13799 8632 -813 -657 -15 C
ATOM 2854 CG1 VAL A1148 15.115 48.204 -3.022 1.00 88.01 C
ANISOU 2854 CG1 VAL A1148 11170 13667 8601 -919 -624 -16 C
ATOM 2855 CG2 VAL A1148 14.697 46.098 -1.727 1.00 88.34 C
ANISOU 2855 CG2 VAL A1148 11400 13601 8565 -759 -569 5 C
ATOM 2856 N ILE A1149 18.879 47.950 -2.733 1.00 89.42 N
ANISOU 2856 N ILE A1149 11148 14216 8613 -847 -861 -110 N
ATOM 2857 CA ILE A1149 19.913 48.900 -3.162 1.00 90.24 C
ANISOU 2857 CA ILE A1149 11125 14458 8704 -946 -911 -164 C
ATOM 2858 C ILE A1149 20.861 48.248 -4.179 1.00 96.98 C
ANISOU 2858 C ILE A1149 11831 15452 9566 -914 -945 -208 C
ATOM 2859 O ILE A1149 21.096 48.833 -5.239 1.00 96.75 O
ANISOU 2859 O ILE A1149 11708 15482 9572 -1025 -923 -227 O
ATOM 2860 CB ILE A1149 20.642 49.554 -1.950 1.00 93.81 C
ANISOU 2860 CB ILE A1149 11599 14965 9078 -956 -980 -209 C
ATOM 2861 CG1 ILE A1149 19.696 50.525 -1.215 1.00 93.16 C
ANISOU 2861 CG1 ILE A1149 11646 14750 8999 -1028 -934 -170 C
ATOM 2862 CG2 ILE A1149 21.923 50.278 -2.385 1.00 95.67 C
ANISOU 2862 CG2 ILE A1149 11681 15378 9290 -1052 -1034 -293 C
ATOM 2863 CD1 ILE A1149 20.013 50.779 0.212 1.00 96.54 C
ANISOU 2863 CD1 ILE A1149 12161 15171 9350 -990 -985 -188 C
ATOM 2864 N THR A1150 21.348 47.017 -3.884 1.00 95.39 N
ANISOU 2864 N THR A1150 11629 15290 9326 -759 -995 -224 N
ATOM 2865 CA THR A1150 22.240 46.252 -4.770 1.00 96.01 C
ANISOU 2865 CA THR A1150 11574 15498 9408 -696 -1033 -271 C
ATOM 2866 C THR A1150 21.567 45.992 -6.131 1.00 99.36 C
ANISOU 2866 C THR A1150 11961 15877 9913 -754 -954 -227 C
ATOM 2867 O THR A1150 22.247 46.038 -7.153 1.00 99.11 O
ANISOU 2867 O THR A1150 11793 15963 9903 -817 -956 -272 O
ATOM 2868 CB THR A1150 22.767 44.989 -4.061 1.00104.91 C
ANISOU 2868 CB THR A1150 12763 16631 10466 -497 -1105 -287 C
ATOM 2869 OG1 THR A1150 23.403 45.389 -2.848 1.00105.08 O
ANISOU 2869 OG1 THR A1150 12800 16718 10408 -448 -1197 -347 O
ATOM 2870 CG2 THR A1150 23.776 44.205 -4.901 1.00104.55 C
ANISOU 2870 CG2 THR A1150 12590 16712 10422 -406 -1149 -339 C
ATOM 2871 N THR A1151 20.237 45.789 -6.143 1.00 96.02 N
ANISOU 2871 N THR A1151 11659 15289 9535 -743 -880 -149 N
ATOM 2872 CA THR A1151 19.461 45.579 -7.368 1.00 95.60 C
ANISOU 2872 CA THR A1151 11588 15174 9561 -786 -810 -108 C
ATOM 2873 C THR A1151 19.332 46.906 -8.152 1.00101.58 C
ANISOU 2873 C THR A1151 12303 15936 10357 -948 -781 -113 C
ATOM 2874 O THR A1151 19.395 46.896 -9.382 1.00101.27 O
ANISOU 2874 O THR A1151 12196 15926 10356 -998 -758 -115 O
ATOM 2875 CB THR A1151 18.135 44.877 -7.042 1.00 99.85 C
ANISOU 2875 CB THR A1151 12260 15549 10130 -725 -744 -49 C
ATOM 2876 OG1 THR A1151 18.434 43.643 -6.386 1.00 98.02 O
ANISOU 2876 OG1 THR A1151 12094 15312 9836 -584 -775 -50 O
ATOM 2877 CG2 THR A1151 17.291 44.591 -8.282 1.00 97.00 C
ANISOU 2877 CG2 THR A1151 11875 15128 9851 -753 -680 -19 C
ATOM 2878 N PHE A1152 19.209 48.042 -7.440 1.00 99.37 N
ANISOU 2878 N PHE A1152 12077 15624 10054 -1028 -785 -117 N
ATOM 2879 CA PHE A1152 19.131 49.366 -8.063 1.00 99.29 C
ANISOU 2879 CA PHE A1152 12066 15603 10057 -1179 -765 -125 C
ATOM 2880 C PHE A1152 20.485 49.811 -8.626 1.00103.96 C
ANISOU 2880 C PHE A1152 12537 16354 10609 -1277 -794 -192 C
ATOM 2881 O PHE A1152 20.523 50.706 -9.469 1.00103.53 O
ANISOU 2881 O PHE A1152 12488 16292 10557 -1410 -766 -201 O
ATOM 2882 CB PHE A1152 18.613 50.417 -7.062 1.00101.28 C
ANISOU 2882 CB PHE A1152 12425 15769 10287 -1228 -764 -114 C
ATOM 2883 CG PHE A1152 17.131 50.721 -7.098 1.00102.20 C
ANISOU 2883 CG PHE A1152 12649 15723 10458 -1225 -713 -69 C
ATOM 2884 CD1 PHE A1152 16.484 50.981 -8.303 1.00104.66 C
ANISOU 2884 CD1 PHE A1152 12967 15977 10823 -1268 -684 -55 C
ATOM 2885 CD2 PHE A1152 16.401 50.836 -5.923 1.00104.38 C
ANISOU 2885 CD2 PHE A1152 13023 15909 10729 -1183 -698 -54 C
ATOM 2886 CE1 PHE A1152 15.125 51.302 -8.332 1.00105.00 C
ANISOU 2886 CE1 PHE A1152 13094 15883 10918 -1251 -651 -37 C
ATOM 2887 CE2 PHE A1152 15.041 51.160 -5.954 1.00106.67 C
ANISOU 2887 CE2 PHE A1152 13390 16066 11073 -1180 -650 -37 C
ATOM 2888 CZ PHE A1152 14.411 51.388 -7.159 1.00104.18 C
ANISOU 2888 CZ PHE A1152 13064 15705 10815 -1208 -633 -34 C
ATOM 2889 N ARG A1153 21.589 49.198 -8.153 1.00101.96 N
ANISOU 2889 N ARG A1153 12184 16244 10313 -1211 -850 -252 N
ATOM 2890 CA ARG A1153 22.957 49.520 -8.572 1.00103.28 C
ANISOU 2890 CA ARG A1153 12206 16594 10443 -1298 -876 -347 C
ATOM 2891 C ARG A1153 23.465 48.614 -9.702 1.00108.61 C
ANISOU 2891 C ARG A1153 12760 17363 11142 -1257 -868 -376 C
ATOM 2892 O ARG A1153 23.993 49.129 -10.684 1.00108.47 O
ANISOU 2892 O ARG A1153 12672 17415 11125 -1391 -830 -418 O
ATOM 2893 CB ARG A1153 23.923 49.511 -7.365 1.00103.82 C
ANISOU 2893 CB ARG A1153 12218 16782 10446 -1250 -955 -423 C
ATOM 2894 CG ARG A1153 25.363 49.924 -7.693 1.00112.19 C
ANISOU 2894 CG ARG A1153 13108 18051 11467 -1357 -981 -551 C
ATOM 2895 CD ARG A1153 26.345 49.693 -6.551 1.00117.94 C
ANISOU 2895 CD ARG A1153 13759 18916 12137 -1268 -1080 -645 C
ATOM 2896 NE ARG A1153 26.268 48.341 -5.984 1.00121.74 N
ANISOU 2896 NE ARG A1153 14261 19388 12608 -1034 -1150 -630 N
ATOM 2897 CZ ARG A1153 26.915 47.279 -6.458 1.00129.71 C
ANISOU 2897 CZ ARG A1153 15149 20520 13615 -917 -1194 -694 C
ATOM 2898 NH1 ARG A1153 27.697 47.389 -7.525 1.00110.53 N
ANISOU 2898 NH1 ARG A1153 12548 18247 11203 -1016 -1169 -784 N
ATOM 2899 NH2 ARG A1153 26.782 46.098 -5.869 1.00115.20 N
ANISOU 2899 NH2 ARG A1153 13376 18645 11751 -702 -1262 -674 N
ATOM 2900 N THR A1154 23.324 47.282 -9.559 1.00106.17 N
ANISOU 2900 N THR A1154 12445 17052 10844 -1079 -899 -358 N
ATOM 2901 CA THR A1154 23.795 46.315 -10.559 1.00106.58 C
ANISOU 2901 CA THR A1154 12391 17188 10915 -1014 -899 -385 C
ATOM 2902 C THR A1154 22.843 46.153 -11.751 1.00111.71 C
ANISOU 2902 C THR A1154 13097 17717 11631 -1048 -824 -307 C
ATOM 2903 O THR A1154 23.304 46.022 -12.886 1.00111.89 O
ANISOU 2903 O THR A1154 13031 17814 11669 -1098 -798 -337 O
ATOM 2904 CB THR A1154 24.122 44.953 -9.921 1.00111.42 C
ANISOU 2904 CB THR A1154 12996 17843 11497 -802 -973 -404 C
ATOM 2905 OG1 THR A1154 22.933 44.383 -9.375 1.00109.21 O
ANISOU 2905 OG1 THR A1154 12884 17382 11229 -705 -953 -307 O
ATOM 2906 CG2 THR A1154 25.218 45.033 -8.863 1.00110.14 C
ANISOU 2906 CG2 THR A1154 12759 17825 11264 -746 -1069 -505 C
ATOM 2907 N GLY A1155 21.539 46.141 -11.473 1.00108.53 N
ANISOU 2907 N GLY A1155 12836 17137 11263 -1020 -791 -219 N
ATOM 2908 CA GLY A1155 20.489 45.949 -12.466 1.00107.93 C
ANISOU 2908 CA GLY A1155 12817 16939 11253 -1032 -732 -155 C
ATOM 2909 C GLY A1155 20.259 44.486 -12.765 1.00113.81 C
ANISOU 2909 C GLY A1155 13547 17674 12020 -892 -731 -133 C
ATOM 2910 O GLY A1155 19.777 44.145 -13.844 1.00113.33 O
ANISOU 2910 O GLY A1155 13478 17576 12006 -903 -694 -108 O
ATOM 2911 N THR A1156 20.623 43.615 -11.812 1.00112.78 N
ANISOU 2911 N THR A1156 13432 17573 11846 -757 -778 -146 N
ATOM 2912 CA THR A1156 20.515 42.160 -11.911 1.00113.86 C
ANISOU 2912 CA THR A1156 13590 17694 11979 -608 -788 -130 C
ATOM 2913 C THR A1156 20.101 41.526 -10.585 1.00120.73 C
ANISOU 2913 C THR A1156 14601 18466 12806 -498 -801 -100 C
ATOM 2914 O THR A1156 20.217 42.158 -9.531 1.00120.92 O
ANISOU 2914 O THR A1156 14674 18475 12794 -522 -822 -108 O
ATOM 2915 CB THR A1156 21.805 41.553 -12.492 1.00126.17 C
ANISOU 2915 CB THR A1156 15012 19430 13495 -537 -852 -208 C
ATOM 2916 OG1 THR A1156 22.936 42.332 -12.086 1.00127.39 O
ANISOU 2916 OG1 THR A1156 15100 19710 13593 -549 -919 -285 O
ATOM 2917 CG2 THR A1156 21.761 41.430 -14.015 1.00125.80 C
ANISOU 2917 CG2 THR A1156 14846 19460 13491 -623 -817 -231 C
ATOM 2918 N TRP A1157 19.637 40.267 -10.636 1.00119.40 N
ANISOU 2918 N TRP A1157 14512 18229 12627 -382 -789 -70 N
ATOM 2919 CA TRP A1157 19.171 39.512 -9.469 1.00120.75 C
ANISOU 2919 CA TRP A1157 14852 18285 12742 -293 -785 -42 C
ATOM 2920 C TRP A1157 20.301 38.896 -8.629 1.00128.69 C
ANISOU 2920 C TRP A1157 15874 19377 13645 -153 -890 -93 C
ATOM 2921 O TRP A1157 20.047 37.974 -7.848 1.00128.20 O
ANISOU 2921 O TRP A1157 15974 19228 13510 -39 -905 -77 O
ATOM 2922 CB TRP A1157 18.149 38.443 -9.902 1.00119.08 C
ANISOU 2922 CB TRP A1157 14746 17943 12556 -250 -713 7 C
ATOM 2923 CG TRP A1157 17.019 39.010 -10.710 1.00119.07 C
ANISOU 2923 CG TRP A1157 14710 17875 12658 -370 -629 37 C
ATOM 2924 CD1 TRP A1157 16.883 38.980 -12.068 1.00121.48 C
ANISOU 2924 CD1 TRP A1157 14920 18209 13027 -402 -609 42 C
ATOM 2925 CD2 TRP A1157 15.926 39.788 -10.214 1.00118.43 C
ANISOU 2925 CD2 TRP A1157 14687 17688 12623 -462 -563 55 C
ATOM 2926 NE1 TRP A1157 15.751 39.664 -12.446 1.00120.10 N
ANISOU 2926 NE1 TRP A1157 14750 17950 12934 -501 -543 61 N
ATOM 2927 CE2 TRP A1157 15.145 40.174 -11.327 1.00121.58 C
ANISOU 2927 CE2 TRP A1157 15022 18058 13114 -536 -516 65 C
ATOM 2928 CE3 TRP A1157 15.520 40.189 -8.929 1.00119.85 C
ANISOU 2928 CE3 TRP A1157 14969 17796 12773 -483 -543 57 C
ATOM 2929 CZ2 TRP A1157 13.983 40.946 -11.196 1.00120.40 C
ANISOU 2929 CZ2 TRP A1157 14900 17818 13028 -616 -460 66 C
ATOM 2930 CZ3 TRP A1157 14.375 40.956 -8.801 1.00120.81 C
ANISOU 2930 CZ3 TRP A1157 15111 17831 12961 -574 -475 62 C
ATOM 2931 CH2 TRP A1157 13.613 41.315 -9.923 1.00120.78 C
ANISOU 2931 CH2 TRP A1157 15034 17806 13049 -633 -439 62 C
ATOM 2932 N ASP A1158 21.536 39.429 -8.758 1.00128.88 N
ANISOU 2932 N ASP A1158 15735 19574 13658 -166 -962 -166 N
ATOM 2933 CA ASP A1158 22.712 38.959 -8.004 1.00131.26 C
ANISOU 2933 CA ASP A1158 16009 19996 13869 -27 -1081 -245 C
ATOM 2934 C ASP A1158 22.575 39.230 -6.504 1.00137.79 C
ANISOU 2934 C ASP A1158 16990 20739 14626 9 -1110 -232 C
ATOM 2935 O ASP A1158 23.198 38.536 -5.698 1.00138.63 O
ANISOU 2935 O ASP A1158 17199 20839 14635 170 -1194 -260 O
ATOM 2936 CB ASP A1158 24.040 39.536 -8.541 1.00133.88 C
ANISOU 2936 CB ASP A1158 16116 20542 14212 -94 -1136 -346 C
ATOM 2937 CG ASP A1158 23.915 40.503 -9.700 1.00144.55 C
ANISOU 2937 CG ASP A1158 17341 21930 15653 -258 -1053 -335 C
ATOM 2938 OD1 ASP A1158 24.299 40.131 -10.827 1.00145.64 O
ANISOU 2938 OD1 ASP A1158 17310 22229 15796 -268 -1079 -415 O
ATOM 2939 OD2 ASP A1158 23.462 41.645 -9.474 1.00150.40 O
ANISOU 2939 OD2 ASP A1158 18157 22536 16454 -372 -963 -254 O
ATOM 2940 N ALA A1159 21.743 40.226 -6.133 1.00135.00 N
ANISOU 2940 N ALA A1159 16667 20313 14315 -134 -1044 -193 N
ATOM 2941 CA ALA A1159 21.464 40.569 -4.738 1.00135.86 C
ANISOU 2941 CA ALA A1159 16922 20339 14358 -112 -1063 -181 C
ATOM 2942 C ALA A1159 20.627 39.456 -4.098 1.00141.11 C
ANISOU 2942 C ALA A1159 17811 20841 14965 2 -1033 -129 C
ATOM 2943 O ALA A1159 20.819 39.131 -2.925 1.00141.37 O
ANISOU 2943 O ALA A1159 17988 20834 14893 115 -1097 -143 O
ATOM 2944 CB ALA A1159 20.714 41.887 -4.669 1.00135.79 C
ANISOU 2944 CB ALA A1159 16923 20258 14412 -282 -981 -141 C
ATOM 2945 N TYR A1160 19.719 38.861 -4.894 1.00138.15 N
ANISOU 2945 N TYR A1160 17476 20365 14648 -33 -935 -73 N
ATOM 2946 CA TYR A1160 18.835 37.770 -4.502 1.00138.67 C
ANISOU 2946 CA TYR A1160 17762 20271 14656 48 -885 -30 C
ATOM 2947 C TYR A1160 19.414 36.485 -5.094 1.00145.65 C
ANISOU 2947 C TYR A1160 18658 21199 15483 205 -955 -52 C
ATOM 2948 O TYR A1160 18.854 35.915 -6.039 1.00144.82 O
ANISOU 2948 O TYR A1160 18516 21078 15431 196 -903 -29 O
ATOM 2949 CB TYR A1160 17.395 38.051 -4.992 1.00138.21 C
ANISOU 2949 CB TYR A1160 17740 20084 14690 -77 -739 25 C
ATOM 2950 CG TYR A1160 16.809 39.323 -4.421 1.00138.67 C
ANISOU 2950 CG TYR A1160 17794 20101 14793 -208 -686 32 C
ATOM 2951 CD1 TYR A1160 17.046 40.556 -5.024 1.00140.16 C
ANISOU 2951 CD1 TYR A1160 17820 20405 15031 -289 -731 7 C
ATOM 2952 CD2 TYR A1160 16.033 39.299 -3.267 1.00139.14 C
ANISOU 2952 CD2 TYR A1160 18024 20008 14836 -250 -591 56 C
ATOM 2953 CE1 TYR A1160 16.549 41.735 -4.476 1.00140.16 C
ANISOU 2953 CE1 TYR A1160 17832 20361 15061 -397 -691 13 C
ATOM 2954 CE2 TYR A1160 15.518 40.471 -2.719 1.00139.56 C
ANISOU 2954 CE2 TYR A1160 18069 20029 14927 -356 -548 54 C
ATOM 2955 CZ TYR A1160 15.777 41.686 -3.329 1.00146.19 C
ANISOU 2955 CZ TYR A1160 18754 20979 15814 -421 -605 36 C
ATOM 2956 OH TYR A1160 15.276 42.848 -2.801 1.00147.19 O
ANISOU 2956 OH TYR A1160 18891 21065 15970 -517 -568 34 O
ATOM 2957 N ASP A 250 20.581 36.066 -4.553 1.00145.18 N
ANISOU 2957 N ASP A 250 18656 21197 15309 360 -1082 -103 N
ATOM 2958 CA ASP A 250 21.314 34.881 -5.000 1.00146.74 C
ANISOU 2958 CA ASP A 250 18872 21450 15434 544 -1178 -144 C
ATOM 2959 C ASP A 250 20.572 33.574 -4.726 1.00152.54 C
ANISOU 2959 C ASP A 250 19839 22003 16117 603 -1107 -83 C
ATOM 2960 O ASP A 250 20.845 32.587 -5.408 1.00152.58 O
ANISOU 2960 O ASP A 250 19823 22031 16118 687 -1126 -89 O
ATOM 2961 CB ASP A 250 22.735 34.842 -4.427 1.00150.09 C
ANISOU 2961 CB ASP A 250 19346 21950 15732 716 -1340 -222 C
ATOM 2962 N ASN A 251 19.608 33.572 -3.774 1.00149.85 N
ANISOU 2962 N ASN A 251 19725 21481 15732 550 -1019 -31 N
ATOM 2963 CA ASN A 251 18.779 32.404 -3.452 1.00150.21 C
ANISOU 2963 CA ASN A 251 20025 21338 15709 581 -933 18 C
ATOM 2964 C ASN A 251 17.968 31.962 -4.690 1.00153.79 C
ANISOU 2964 C ASN A 251 20396 21766 16271 489 -822 53 C
ATOM 2965 O ASN A 251 17.696 30.769 -4.853 1.00153.90 O
ANISOU 2965 O ASN A 251 20553 21697 16226 568 -805 69 O
ATOM 2966 CB ASN A 251 17.850 32.709 -2.276 1.00150.92 C
ANISOU 2966 CB ASN A 251 20348 21248 15745 494 -829 54 C
ATOM 2967 N LYS A 252 17.637 32.927 -5.582 1.00149.43 N
ANISOU 2967 N LYS A 252 19629 21280 15869 330 -752 62 N
ATOM 2968 CA LYS A 252 16.903 32.700 -6.825 1.00148.45 C
ANISOU 2968 CA LYS A 252 19430 21127 15848 245 -653 90 C
ATOM 2969 C LYS A 252 17.829 32.268 -7.969 1.00152.29 C
ANISOU 2969 C LYS A 252 19751 21749 16362 328 -732 67 C
ATOM 2970 O LYS A 252 18.054 33.028 -8.920 1.00150.87 O
ANISOU 2970 O LYS A 252 19350 21679 16295 243 -726 59 O
ATOM 2971 CB LYS A 252 16.071 33.936 -7.210 1.00149.93 C
ANISOU 2971 CB LYS A 252 19467 21324 16174 62 -562 101 C
ATOM 2972 N TYR A 253 18.371 31.037 -7.862 1.00149.91 N
ANISOU 2972 N TYR A 253 19579 21434 15947 500 -809 53 N
ATOM 2973 CA TYR A 253 19.226 30.437 -8.890 1.00149.81 C
ANISOU 2973 CA TYR A 253 19431 21544 15945 602 -886 22 C
ATOM 2974 C TYR A 253 18.411 29.572 -9.846 1.00151.33 C
ANISOU 2974 C TYR A 253 19669 21642 16187 557 -783 67 C
ATOM 2975 O TYR A 253 18.885 29.242 -10.935 1.00150.38 O
ANISOU 2975 O TYR A 253 19405 21615 16118 583 -806 53 O
ATOM 2976 CB TYR A 253 20.407 29.658 -8.286 1.00153.06 C
ANISOU 2976 CB TYR A 253 19959 21989 16206 830 -1032 -29 C
ATOM 2977 CG TYR A 253 21.627 30.516 -8.028 1.00156.26 C
ANISOU 2977 CG TYR A 253 20173 22594 16605 893 -1168 -113 C
ATOM 2978 CD1 TYR A 253 22.046 31.468 -8.956 1.00158.03 C
ANISOU 2978 CD1 TYR A 253 20105 23013 16927 847 -1197 -164 C
ATOM 2979 CD2 TYR A 253 22.383 30.357 -6.871 1.00158.38 C
ANISOU 2979 CD2 TYR A 253 20555 22855 16766 987 -1262 -149 C
ATOM 2980 CE1 TYR A 253 23.166 32.266 -8.721 1.00160.02 C
ANISOU 2980 CE1 TYR A 253 20171 23457 17173 882 -1307 -258 C
ATOM 2981 CE2 TYR A 253 23.499 31.156 -6.620 1.00160.11 C
ANISOU 2981 CE2 TYR A 253 20584 23268 16982 1037 -1386 -241 C
ATOM 2982 CZ TYR A 253 23.892 32.103 -7.552 1.00167.65 C
ANISOU 2982 CZ TYR A 253 21236 24424 18039 978 -1403 -300 C
ATOM 2983 OH TYR A 253 24.999 32.881 -7.315 1.00169.56 O
ANISOU 2983 OH TYR A 253 21277 24870 18279 1006 -1513 -409 O
ATOM 2984 N ARG A 254 17.167 29.238 -9.442 1.00146.57 N
ANISOU 2984 N ARG A 254 19269 20857 15565 481 -664 111 N
ATOM 2985 CA ARG A 254 16.211 28.460 -10.226 1.00145.26 C
ANISOU 2985 CA ARG A 254 19165 20586 15442 420 -552 144 C
ATOM 2986 C ARG A 254 15.672 29.305 -11.381 1.00146.44 C
ANISOU 2986 C ARG A 254 19068 20812 15759 280 -494 149 C
ATOM 2987 O ARG A 254 15.349 28.763 -12.440 1.00145.50 O
ANISOU 2987 O ARG A 254 18888 20705 15689 280 -471 158 O
ATOM 2988 CB ARG A 254 15.058 27.987 -9.332 1.00145.73 C
ANISOU 2988 CB ARG A 254 19468 20449 15452 330 -420 168 C
ATOM 2989 N SER A 255 15.575 30.633 -11.170 1.00141.27 N
ANISOU 2989 N SER A 255 18291 20202 15184 165 -475 142 N
ATOM 2990 CA SER A 255 15.113 31.594 -12.173 1.00139.21 C
ANISOU 2990 CA SER A 255 17825 20002 15067 40 -434 142 C
ATOM 2991 C SER A 255 16.212 31.848 -13.214 1.00140.66 C
ANISOU 2991 C SER A 255 17825 20343 15276 96 -524 124 C
ATOM 2992 O SER A 255 15.901 32.127 -14.373 1.00139.25 O
ANISOU 2992 O SER A 255 17532 20193 15184 41 -494 130 O
ATOM 2993 CB SER A 255 14.725 32.914 -11.508 1.00142.66 C
ANISOU 2993 CB SER A 255 18195 20451 15559 -73 -414 134 C
ATOM 2994 OG SER A 255 13.728 32.771 -10.508 1.00152.24 O
ANISOU 2994 OG SER A 255 19587 21536 16723 -105 -344 138 O
ATOM 2995 N SER A 256 17.495 31.759 -12.787 1.00136.30 N
ANISOU 2995 N SER A 256 17242 19900 14647 201 -634 90 N
ATOM 2996 CA SER A 256 18.701 31.983 -13.597 1.00135.20 C
ANISOU 2996 CA SER A 256 16917 19933 14521 251 -718 47 C
ATOM 2997 C SER A 256 18.977 30.832 -14.571 1.00136.87 C
ANISOU 2997 C SER A 256 17134 20153 14719 348 -728 48 C
ATOM 2998 O SER A 256 19.501 31.071 -15.663 1.00135.80 O
ANISOU 2998 O SER A 256 16835 20116 14648 313 -732 32 O
ATOM 2999 CB SER A 256 19.917 32.185 -12.694 1.00139.25 C
ANISOU 2999 CB SER A 256 17398 20562 14947 354 -836 -13 C
ATOM 3000 OG SER A 256 19.613 32.957 -11.547 1.00147.43 O
ANISOU 3000 OG SER A 256 18632 21485 15898 398 -840 4 O
ATOM 3001 N GLU A 257 18.648 29.589 -14.161 1.00132.41 N
ANISOU 3001 N GLU A 257 16772 19477 14060 465 -732 65 N
ATOM 3002 CA GLU A 257 18.868 28.378 -14.948 1.00131.78 C
ANISOU 3002 CA GLU A 257 16727 19391 13951 570 -746 66 C
ATOM 3003 C GLU A 257 17.934 28.269 -16.160 1.00133.30 C
ANISOU 3003 C GLU A 257 16875 19526 14246 461 -645 107 C
ATOM 3004 O GLU A 257 18.421 28.070 -17.274 1.00132.84 O
ANISOU 3004 O GLU A 257 16709 19546 14219 495 -666 94 O
ATOM 3005 CB GLU A 257 18.802 27.127 -14.054 1.00134.19 C
ANISOU 3005 CB GLU A 257 17311 19559 14115 711 -766 80 C
ATOM 3006 CG GLU A 257 18.983 25.800 -14.783 1.00146.14 C
ANISOU 3006 CG GLU A 257 18922 21016 15587 806 -760 93 C
ATOM 3007 CD GLU A 257 20.382 25.369 -15.196 1.00170.26 C
ANISOU 3007 CD GLU A 257 21840 24239 18613 964 -885 32 C
ATOM 3008 OE1 GLU A 257 20.648 24.146 -15.145 1.00168.07 O
ANISOU 3008 OE1 GLU A 257 21715 23917 18227 1134 -944 20 O
ATOM 3009 OE2 GLU A 257 21.203 26.229 -15.592 1.00163.90 O
ANISOU 3009 OE2 GLU A 257 20780 23608 17887 915 -920 -13 O
ATOM 3010 N THR A 258 16.604 28.393 -15.952 1.00127.69 N
ANISOU 3010 N THR A 258 16242 18684 13590 332 -536 145 N
ATOM 3011 CA THR A 258 15.610 28.311 -17.035 1.00125.67 C
ANISOU 3011 CA THR A 258 15942 18372 13434 232 -446 168 C
ATOM 3012 C THR A 258 15.719 29.495 -18.011 1.00125.96 C
ANISOU 3012 C THR A 258 15752 18520 13588 130 -453 157 C
ATOM 3013 O THR A 258 15.258 29.388 -19.150 1.00125.30 O
ANISOU 3013 O THR A 258 15602 18431 13574 88 -419 167 O
ATOM 3014 CB THR A 258 14.192 28.113 -16.489 1.00134.55 C
ANISOU 3014 CB THR A 258 17216 19330 14577 133 -326 187 C
ATOM 3015 OG1 THR A 258 13.934 29.077 -15.467 1.00135.80 O
ANISOU 3015 OG1 THR A 258 17387 19472 14739 64 -311 179 O
ATOM 3016 CG2 THR A 258 13.959 26.698 -15.966 1.00133.66 C
ANISOU 3016 CG2 THR A 258 17350 19085 14350 210 -291 201 C
ATOM 3017 N LYS A 259 16.356 30.603 -17.570 1.00119.87 N
ANISOU 3017 N LYS A 259 14879 17841 12824 92 -500 135 N
ATOM 3018 CA LYS A 259 16.630 31.798 -18.372 1.00117.88 C
ANISOU 3018 CA LYS A 259 14446 17691 12653 -9 -512 119 C
ATOM 3019 C LYS A 259 17.692 31.428 -19.419 1.00118.44 C
ANISOU 3019 C LYS A 259 14397 17891 12715 50 -564 92 C
ATOM 3020 O LYS A 259 17.565 31.812 -20.579 1.00116.98 O
ANISOU 3020 O LYS A 259 14115 17733 12598 -26 -540 94 O
ATOM 3021 CB LYS A 259 17.128 32.932 -17.457 1.00121.06 C
ANISOU 3021 CB LYS A 259 14802 18158 13037 -52 -552 95 C
ATOM 3022 CG LYS A 259 17.268 34.315 -18.112 1.00137.02 C
ANISOU 3022 CG LYS A 259 16685 20249 15129 -184 -549 81 C
ATOM 3023 CD LYS A 259 17.169 35.468 -17.080 1.00148.73 C
ANISOU 3023 CD LYS A 259 18178 21730 16604 -254 -558 72 C
ATOM 3024 CE LYS A 259 18.385 35.650 -16.186 1.00158.83 C
ANISOU 3024 CE LYS A 259 19418 23129 17803 -196 -636 28 C
ATOM 3025 NZ LYS A 259 18.108 36.576 -15.053 1.00164.25 N
ANISOU 3025 NZ LYS A 259 20153 23780 18473 -249 -638 28 N
ATOM 3026 N ARG A 260 18.707 30.640 -19.004 1.00113.68 N
ANISOU 3026 N ARG A 260 13812 17361 12021 195 -638 59 N
ATOM 3027 CA ARG A 260 19.800 30.139 -19.843 1.00112.77 C
ANISOU 3027 CA ARG A 260 13584 17381 11883 279 -693 13 C
ATOM 3028 C ARG A 260 19.293 29.065 -20.840 1.00113.04 C
ANISOU 3028 C ARG A 260 13674 17340 11937 317 -652 48 C
ATOM 3029 O ARG A 260 19.713 29.075 -22.000 1.00112.60 O
ANISOU 3029 O ARG A 260 13497 17367 11918 297 -651 29 O
ATOM 3030 CB ARG A 260 20.937 29.588 -18.951 1.00114.12 C
ANISOU 3030 CB ARG A 260 13773 17642 11944 448 -798 -48 C
ATOM 3031 CG ARG A 260 22.258 29.294 -19.669 1.00125.09 C
ANISOU 3031 CG ARG A 260 15004 19216 13309 541 -870 -131 C
ATOM 3032 CD ARG A 260 22.509 27.801 -19.857 1.00135.36 C
ANISOU 3032 CD ARG A 260 16412 20483 14537 728 -913 -135 C
ATOM 3033 NE ARG A 260 22.856 27.122 -18.604 1.00141.54 N
ANISOU 3033 NE ARG A 260 17358 21220 15201 899 -998 -154 N
ATOM 3034 CZ ARG A 260 22.927 25.801 -18.458 1.00154.70 C
ANISOU 3034 CZ ARG A 260 19195 22810 16775 1074 -1042 -149 C
ATOM 3035 NH1 ARG A 260 22.665 24.996 -19.481 1.00139.46 N
ANISOU 3035 NH1 ARG A 260 17280 20844 14863 1098 -1006 -124 N
ATOM 3036 NH2 ARG A 260 23.245 25.275 -17.283 1.00144.09 N
ANISOU 3036 NH2 ARG A 260 18027 21413 15309 1229 -1126 -169 N
ATOM 3037 N ILE A 261 18.403 28.149 -20.383 1.00106.36 N
ANISOU 3037 N ILE A 261 13017 16335 11059 362 -611 94 N
ATOM 3038 CA ILE A 261 17.836 27.061 -21.193 1.00104.30 C
ANISOU 3038 CA ILE A 261 12838 15986 10807 394 -567 125 C
ATOM 3039 C ILE A 261 16.972 27.617 -22.339 1.00104.38 C
ANISOU 3039 C ILE A 261 12760 15965 10936 251 -495 150 C
ATOM 3040 O ILE A 261 17.179 27.230 -23.490 1.00103.62 O
ANISOU 3040 O ILE A 261 12601 15904 10864 266 -495 148 O
ATOM 3041 CB ILE A 261 17.097 25.991 -20.322 1.00107.57 C
ANISOU 3041 CB ILE A 261 13497 16230 11143 453 -529 158 C
ATOM 3042 CG1 ILE A 261 18.035 25.390 -19.248 1.00109.15 C
ANISOU 3042 CG1 ILE A 261 13816 16450 11205 621 -621 130 C
ATOM 3043 CG2 ILE A 261 16.504 24.870 -21.188 1.00107.94 C
ANISOU 3043 CG2 ILE A 261 13633 16184 11195 472 -477 185 C
ATOM 3044 CD1 ILE A 261 17.333 24.862 -17.985 1.00116.13 C
ANISOU 3044 CD1 ILE A 261 14957 17167 12001 634 -580 157 C
ATOM 3045 N ASN A 262 16.035 28.541 -22.029 1.00 98.42 N
ANISOU 3045 N ASN A 262 12001 15145 10248 122 -442 165 N
ATOM 3046 CA ASN A 262 15.145 29.161 -23.021 1.00 96.22 C
ANISOU 3046 CA ASN A 262 11653 14829 10076 1 -391 175 C
ATOM 3047 C ASN A 262 15.887 30.042 -24.038 1.00 98.37 C
ANISOU 3047 C ASN A 262 11768 15222 10385 -49 -426 157 C
ATOM 3048 O ASN A 262 15.435 30.133 -25.179 1.00 97.69 O
ANISOU 3048 O ASN A 262 11646 15114 10359 -99 -403 165 O
ATOM 3049 CB ASN A 262 13.994 29.928 -22.352 1.00 93.92 C
ANISOU 3049 CB ASN A 262 11401 14446 9839 -102 -338 178 C
ATOM 3050 CG ASN A 262 13.020 29.051 -21.601 1.00107.95 C
ANISOU 3050 CG ASN A 262 13331 16089 11596 -94 -269 185 C
ATOM 3051 OD1 ASN A 262 12.512 28.049 -22.112 1.00100.64 O
ANISOU 3051 OD1 ASN A 262 12460 15091 10686 -89 -222 190 O
ATOM 3052 ND2 ASN A 262 12.714 29.422 -20.371 1.00 99.39 N
ANISOU 3052 ND2 ASN A 262 12328 14964 10473 -107 -252 181 N
ATOM 3053 N ILE A 263 17.021 30.673 -23.634 1.00 93.86 N
ANISOU 3053 N ILE A 263 11114 14778 9772 -42 -480 123 N
ATOM 3054 CA ILE A 263 17.860 31.511 -24.503 1.00 92.99 C
ANISOU 3054 CA ILE A 263 10864 14792 9677 -110 -500 91 C
ATOM 3055 C ILE A 263 18.602 30.620 -25.517 1.00 96.36 C
ANISOU 3055 C ILE A 263 11235 15296 10082 -35 -515 70 C
ATOM 3056 O ILE A 263 18.718 30.980 -26.693 1.00 95.66 O
ANISOU 3056 O ILE A 263 11076 15243 10026 -107 -496 62 O
ATOM 3057 CB ILE A 263 18.775 32.458 -23.665 1.00 96.64 C
ANISOU 3057 CB ILE A 263 11252 15366 10099 -142 -541 46 C
ATOM 3058 CG1 ILE A 263 18.013 33.754 -23.301 1.00 96.54 C
ANISOU 3058 CG1 ILE A 263 11267 15281 10131 -269 -515 66 C
ATOM 3059 CG2 ILE A 263 20.110 32.783 -24.363 1.00 98.19 C
ANISOU 3059 CG2 ILE A 263 11300 15734 10273 -172 -565 -19 C
ATOM 3060 CD1 ILE A 263 18.613 34.603 -22.139 1.00104.24 C
ANISOU 3060 CD1 ILE A 263 12215 16327 11064 -295 -550 34 C
ATOM 3061 N MET A 264 19.055 29.437 -25.055 1.00 92.88 N
ANISOU 3061 N MET A 264 10847 14867 9577 113 -549 62 N
ATOM 3062 CA MET A 264 19.732 28.424 -25.862 1.00 92.83 C
ANISOU 3062 CA MET A 264 10808 14925 9538 216 -571 38 C
ATOM 3063 C MET A 264 18.740 27.844 -26.870 1.00 93.87 C
ANISOU 3063 C MET A 264 11006 14936 9723 190 -515 91 C
ATOM 3064 O MET A 264 19.052 27.792 -28.061 1.00 93.60 O
ANISOU 3064 O MET A 264 10897 14954 9711 167 -505 79 O
ATOM 3065 CB MET A 264 20.292 27.319 -24.951 1.00 96.58 C
ANISOU 3065 CB MET A 264 11366 15412 9917 398 -634 16 C
ATOM 3066 CG MET A 264 20.955 26.171 -25.692 1.00101.63 C
ANISOU 3066 CG MET A 264 11991 16111 10513 533 -669 -14 C
ATOM 3067 SD MET A 264 21.448 24.814 -24.595 1.00107.94 S
ANISOU 3067 SD MET A 264 12956 16875 11181 768 -753 -33 S
ATOM 3068 CE MET A 264 19.846 24.108 -24.207 1.00103.96 C
ANISOU 3068 CE MET A 264 12702 16116 10682 727 -668 68 C
ATOM 3069 N LEU A 265 17.540 27.436 -26.391 1.00 87.93 N
ANISOU 3069 N LEU A 265 10393 14028 8989 182 -474 139 N
ATOM 3070 CA LEU A 265 16.477 26.860 -27.221 1.00 85.90 C
ANISOU 3070 CA LEU A 265 10202 13652 8785 152 -420 176 C
ATOM 3071 C LEU A 265 15.972 27.831 -28.280 1.00 87.93 C
ANISOU 3071 C LEU A 265 10377 13902 9129 25 -394 180 C
ATOM 3072 O LEU A 265 15.658 27.393 -29.389 1.00 87.46 O
ANISOU 3072 O LEU A 265 10317 13812 9102 21 -377 191 O
ATOM 3073 CB LEU A 265 15.323 26.293 -26.378 1.00 85.43 C
ANISOU 3073 CB LEU A 265 10296 13441 8724 149 -370 203 C
ATOM 3074 CG LEU A 265 15.639 25.075 -25.500 1.00 90.10 C
ANISOU 3074 CG LEU A 265 11036 13989 9208 279 -385 207 C
ATOM 3075 CD1 LEU A 265 14.591 24.893 -24.467 1.00 89.99 C
ANISOU 3075 CD1 LEU A 265 11171 13837 9185 233 -323 222 C
ATOM 3076 CD2 LEU A 265 15.763 23.800 -26.310 1.00 92.01 C
ANISOU 3076 CD2 LEU A 265 11340 14205 9415 369 -386 217 C
ATOM 3077 N LEU A 266 15.937 29.145 -27.964 1.00 83.47 N
ANISOU 3077 N LEU A 266 9758 13363 8593 -72 -399 169 N
ATOM 3078 CA LEU A 266 15.545 30.171 -28.929 1.00 82.95 C
ANISOU 3078 CA LEU A 266 9644 13283 8589 -184 -389 168 C
ATOM 3079 C LEU A 266 16.647 30.317 -29.982 1.00 88.83 C
ANISOU 3079 C LEU A 266 10300 14143 9307 -197 -404 145 C
ATOM 3080 O LEU A 266 16.343 30.425 -31.172 1.00 88.59 O
ANISOU 3080 O LEU A 266 10271 14079 9310 -243 -390 152 O
ATOM 3081 CB LEU A 266 15.252 31.521 -28.248 1.00 82.66 C
ANISOU 3081 CB LEU A 266 9598 13236 8572 -276 -394 159 C
ATOM 3082 CG LEU A 266 14.883 32.708 -29.166 1.00 86.89 C
ANISOU 3082 CG LEU A 266 10119 13746 9150 -385 -397 154 C
ATOM 3083 CD1 LEU A 266 13.512 32.534 -29.810 1.00 86.09 C
ANISOU 3083 CD1 LEU A 266 10074 13517 9120 -393 -383 163 C
ATOM 3084 CD2 LEU A 266 14.926 34.009 -28.410 1.00 90.14 C
ANISOU 3084 CD2 LEU A 266 10525 14169 9554 -462 -410 141 C
ATOM 3085 N SER A 267 17.926 30.277 -29.547 1.00 86.39 N
ANISOU 3085 N SER A 267 9917 13972 8937 -155 -432 106 N
ATOM 3086 CA SER A 267 19.089 30.380 -30.433 1.00 86.49 C
ANISOU 3086 CA SER A 267 9825 14119 8918 -174 -435 59 C
ATOM 3087 C SER A 267 19.176 29.206 -31.416 1.00 89.92 C
ANISOU 3087 C SER A 267 10268 14550 9348 -91 -428 65 C
ATOM 3088 O SER A 267 19.654 29.404 -32.529 1.00 90.18 O
ANISOU 3088 O SER A 267 10244 14642 9380 -143 -408 41 O
ATOM 3089 CB SER A 267 20.375 30.528 -29.627 1.00 90.60 C
ANISOU 3089 CB SER A 267 10246 14800 9378 -136 -472 -8 C
ATOM 3090 OG SER A 267 20.355 31.715 -28.851 1.00 98.05 O
ANISOU 3090 OG SER A 267 11176 15753 10324 -233 -474 -18 O
ATOM 3091 N ILE A 268 18.678 28.004 -31.022 1.00 85.31 N
ANISOU 3091 N ILE A 268 9772 13886 8756 28 -436 97 N
ATOM 3092 CA ILE A 268 18.626 26.804 -31.872 1.00 84.39 C
ANISOU 3092 CA ILE A 268 9691 13742 8631 113 -429 110 C
ATOM 3093 C ILE A 268 17.646 27.052 -33.029 1.00 86.66 C
ANISOU 3093 C ILE A 268 10014 13926 8986 22 -391 146 C
ATOM 3094 O ILE A 268 17.983 26.750 -34.175 1.00 86.40 O
ANISOU 3094 O ILE A 268 9952 13925 8951 23 -381 138 O
ATOM 3095 CB ILE A 268 18.299 25.511 -31.055 1.00 87.35 C
ANISOU 3095 CB ILE A 268 10186 14040 8963 250 -444 133 C
ATOM 3096 CG1 ILE A 268 19.484 25.117 -30.137 1.00 88.16 C
ANISOU 3096 CG1 ILE A 268 10257 14260 8978 380 -506 83 C
ATOM 3097 CG2 ILE A 268 17.890 24.335 -31.972 1.00 87.88 C
ANISOU 3097 CG2 ILE A 268 10325 14033 9032 310 -424 160 C
ATOM 3098 CD1 ILE A 268 19.176 24.063 -29.044 1.00 92.49 C
ANISOU 3098 CD1 ILE A 268 10967 14715 9459 510 -530 104 C
ATOM 3099 N VAL A 269 16.460 27.639 -32.723 1.00 82.18 N
ANISOU 3099 N VAL A 269 9506 13241 8476 -52 -374 175 N
ATOM 3100 CA VAL A 269 15.389 27.995 -33.681 1.00 81.05 C
ANISOU 3100 CA VAL A 269 9402 12993 8400 -127 -356 194 C
ATOM 3101 C VAL A 269 15.897 29.020 -34.710 1.00 84.38 C
ANISOU 3101 C VAL A 269 9775 13467 8819 -221 -359 177 C
ATOM 3102 O VAL A 269 15.693 28.825 -35.905 1.00 84.08 O
ANISOU 3102 O VAL A 269 9758 13394 8795 -235 -352 184 O
ATOM 3103 CB VAL A 269 14.107 28.512 -32.960 1.00 84.40 C
ANISOU 3103 CB VAL A 269 9880 13307 8882 -174 -347 202 C
ATOM 3104 CG1 VAL A 269 13.046 28.970 -33.956 1.00 83.67 C
ANISOU 3104 CG1 VAL A 269 9815 13121 8856 -234 -350 199 C
ATOM 3105 CG2 VAL A 269 13.536 27.467 -32.009 1.00 84.29 C
ANISOU 3105 CG2 VAL A 269 9937 13227 8861 -107 -323 212 C
ATOM 3106 N VAL A 270 16.553 30.104 -34.235 1.00 80.95 N
ANISOU 3106 N VAL A 270 9291 13108 8359 -294 -365 153 N
ATOM 3107 CA VAL A 270 17.113 31.181 -35.065 1.00 80.62 C
ANISOU 3107 CA VAL A 270 9226 13111 8294 -410 -355 129 C
ATOM 3108 C VAL A 270 18.196 30.610 -35.988 1.00 84.51 C
ANISOU 3108 C VAL A 270 9656 13713 8742 -395 -333 98 C
ATOM 3109 O VAL A 270 18.171 30.895 -37.184 1.00 84.27 O
ANISOU 3109 O VAL A 270 9659 13653 8705 -462 -313 98 O
ATOM 3110 CB VAL A 270 17.620 32.404 -34.236 1.00 84.54 C
ANISOU 3110 CB VAL A 270 9689 13669 8763 -497 -359 102 C
ATOM 3111 CG1 VAL A 270 18.087 33.538 -35.146 1.00 84.63 C
ANISOU 3111 CG1 VAL A 270 9715 13701 8738 -639 -335 77 C
ATOM 3112 CG2 VAL A 270 16.551 32.913 -33.270 1.00 83.72 C
ANISOU 3112 CG2 VAL A 270 9646 13461 8703 -500 -379 128 C
ATOM 3113 N ALA A 271 19.106 29.770 -35.441 1.00 81.16 N
ANISOU 3113 N ALA A 271 9150 13407 8282 -298 -342 67 N
ATOM 3114 CA ALA A 271 20.176 29.120 -36.205 1.00 81.60 C
ANISOU 3114 CA ALA A 271 9126 13584 8295 -259 -326 19 C
ATOM 3115 C ALA A 271 19.604 28.190 -37.272 1.00 84.50 C
ANISOU 3115 C ALA A 271 9560 13863 8684 -205 -317 58 C
ATOM 3116 O ALA A 271 20.155 28.124 -38.369 1.00 84.51 O
ANISOU 3116 O ALA A 271 9534 13913 8663 -243 -287 31 O
ATOM 3117 CB ALA A 271 21.106 28.352 -35.280 1.00 83.07 C
ANISOU 3117 CB ALA A 271 9226 13900 8438 -130 -361 -30 C
ATOM 3118 N PHE A 272 18.483 27.505 -36.963 1.00 79.29 N
ANISOU 3118 N PHE A 272 8991 13070 8064 -130 -334 114 N
ATOM 3119 CA PHE A 272 17.801 26.623 -37.900 1.00 78.54 C
ANISOU 3119 CA PHE A 272 8968 12879 7994 -84 -327 149 C
ATOM 3120 C PHE A 272 17.208 27.465 -39.036 1.00 82.49 C
ANISOU 3120 C PHE A 272 9518 13298 8525 -197 -313 162 C
ATOM 3121 O PHE A 272 17.455 27.176 -40.211 1.00 82.41 O
ANISOU 3121 O PHE A 272 9518 13295 8500 -206 -296 157 O
ATOM 3122 CB PHE A 272 16.709 25.807 -37.177 1.00 79.83 C
ANISOU 3122 CB PHE A 272 9218 12922 8192 -9 -337 189 C
ATOM 3123 CG PHE A 272 15.821 25.003 -38.094 1.00 81.03 C
ANISOU 3123 CG PHE A 272 9446 12966 8377 19 -326 217 C
ATOM 3124 CD1 PHE A 272 16.255 23.794 -38.627 1.00 84.56 C
ANISOU 3124 CD1 PHE A 272 9905 13437 8786 116 -323 218 C
ATOM 3125 CD2 PHE A 272 14.559 25.462 -38.443 1.00 82.70 C
ANISOU 3125 CD2 PHE A 272 9712 13055 8654 -45 -326 232 C
ATOM 3126 CE1 PHE A 272 15.450 23.069 -39.509 1.00 85.05 C
ANISOU 3126 CE1 PHE A 272 10040 13400 8877 135 -312 242 C
ATOM 3127 CE2 PHE A 272 13.750 24.730 -39.317 1.00 85.44 C
ANISOU 3127 CE2 PHE A 272 10119 13311 9033 -21 -321 245 C
ATOM 3128 CZ PHE A 272 14.197 23.535 -39.838 1.00 83.71 C
ANISOU 3128 CZ PHE A 272 9917 13114 8776 62 -310 254 C
ATOM 3129 N ALA A 273 16.449 28.521 -38.668 1.00 78.36 N
ANISOU 3129 N ALA A 273 9039 12697 8038 -275 -326 174 N
ATOM 3130 CA ALA A 273 15.796 29.449 -39.589 1.00 77.65 C
ANISOU 3130 CA ALA A 273 9026 12511 7967 -366 -334 181 C
ATOM 3131 C ALA A 273 16.788 30.143 -40.520 1.00 82.22 C
ANISOU 3131 C ALA A 273 9599 13157 8483 -465 -304 153 C
ATOM 3132 O ALA A 273 16.565 30.161 -41.728 1.00 82.08 O
ANISOU 3132 O ALA A 273 9653 13076 8457 -493 -300 160 O
ATOM 3133 CB ALA A 273 14.986 30.478 -38.812 1.00 77.92 C
ANISOU 3133 CB ALA A 273 9096 12474 8035 -414 -361 183 C
ATOM 3134 N VAL A 274 17.892 30.675 -39.970 1.00 79.32 N
ANISOU 3134 N VAL A 274 9150 12920 8068 -523 -279 114 N
ATOM 3135 CA VAL A 274 18.914 31.382 -40.743 1.00 80.21 C
ANISOU 3135 CA VAL A 274 9249 13113 8114 -646 -229 68 C
ATOM 3136 C VAL A 274 19.661 30.416 -41.682 1.00 86.88 C
ANISOU 3136 C VAL A 274 10043 14037 8930 -607 -193 43 C
ATOM 3137 O VAL A 274 19.811 30.742 -42.858 1.00 87.23 O
ANISOU 3137 O VAL A 274 10157 14046 8939 -691 -158 35 O
ATOM 3138 CB VAL A 274 19.851 32.232 -39.840 1.00 84.39 C
ANISOU 3138 CB VAL A 274 9690 13770 8603 -730 -208 16 C
ATOM 3139 CG1 VAL A 274 21.071 32.748 -40.599 1.00 85.15 C
ANISOU 3139 CG1 VAL A 274 9740 13987 8625 -862 -136 -57 C
ATOM 3140 CG2 VAL A 274 19.090 33.398 -39.214 1.00 83.87 C
ANISOU 3140 CG2 VAL A 274 9712 13603 8551 -800 -236 42 C
ATOM 3141 N CYS A 275 20.076 29.224 -41.189 1.00 84.38 N
ANISOU 3141 N CYS A 275 9627 13812 8621 -473 -205 29 N
ATOM 3142 CA CYS A 275 20.792 28.210 -41.983 1.00 84.59 C
ANISOU 3142 CA CYS A 275 9599 13922 8621 -408 -179 -3 C
ATOM 3143 C CYS A 275 20.061 27.830 -43.278 1.00 87.81 C
ANISOU 3143 C CYS A 275 10120 14200 9042 -407 -173 43 C
ATOM 3144 O CYS A 275 20.679 27.823 -44.344 1.00 88.08 O
ANISOU 3144 O CYS A 275 10153 14280 9034 -465 -125 9 O
ATOM 3145 CB CYS A 275 21.100 26.972 -41.144 1.00 84.98 C
ANISOU 3145 CB CYS A 275 9571 14044 8672 -235 -217 -13 C
ATOM 3146 SG CYS A 275 22.623 27.082 -40.170 1.00 89.99 S
ANISOU 3146 SG CYS A 275 10026 14910 9257 -208 -220 -119 S
ATOM 3147 N TRP A 276 18.754 27.512 -43.175 1.00 83.22 N
ANISOU 3147 N TRP A 276 9636 13465 8519 -347 -219 109 N
ATOM 3148 CA TRP A 276 17.920 27.088 -44.298 1.00 82.60 C
ANISOU 3148 CA TRP A 276 9664 13257 8462 -329 -229 147 C
ATOM 3149 C TRP A 276 17.445 28.221 -45.178 1.00 86.68 C
ANISOU 3149 C TRP A 276 10298 13669 8966 -450 -230 154 C
ATOM 3150 O TRP A 276 17.106 27.966 -46.335 1.00 87.17 O
ANISOU 3150 O TRP A 276 10446 13655 9020 -451 -230 167 O
ATOM 3151 CB TRP A 276 16.729 26.253 -43.818 1.00 80.62 C
ANISOU 3151 CB TRP A 276 9457 12898 8278 -223 -273 191 C
ATOM 3152 CG TRP A 276 17.107 24.871 -43.384 1.00 81.80 C
ANISOU 3152 CG TRP A 276 9558 13105 8418 -92 -270 192 C
ATOM 3153 CD1 TRP A 276 17.328 24.443 -42.108 1.00 84.72 C
ANISOU 3153 CD1 TRP A 276 9882 13525 8783 -16 -283 188 C
ATOM 3154 CD2 TRP A 276 17.330 23.736 -44.233 1.00 81.90 C
ANISOU 3154 CD2 TRP A 276 9588 13120 8412 -16 -260 196 C
ATOM 3155 NE1 TRP A 276 17.675 23.111 -42.106 1.00 84.37 N
ANISOU 3155 NE1 TRP A 276 9838 13508 8711 109 -286 188 N
ATOM 3156 CE2 TRP A 276 17.681 22.650 -43.398 1.00 85.89 C
ANISOU 3156 CE2 TRP A 276 10063 13674 8897 111 -270 193 C
ATOM 3157 CE3 TRP A 276 17.277 23.532 -45.625 1.00 83.23 C
ANISOU 3157 CE3 TRP A 276 9808 13247 8570 -38 -245 200 C
ATOM 3158 CZ2 TRP A 276 17.972 21.375 -43.907 1.00 85.44 C
ANISOU 3158 CZ2 TRP A 276 10027 13626 8811 219 -268 194 C
ATOM 3159 CZ3 TRP A 276 17.577 22.273 -46.128 1.00 84.93 C
ANISOU 3159 CZ3 TRP A 276 10027 13479 8762 62 -237 202 C
ATOM 3160 CH2 TRP A 276 17.913 21.210 -45.274 1.00 85.72 C
ANISOU 3160 CH2 TRP A 276 10096 13628 8844 190 -249 199 C
ATOM 3161 N LEU A 277 17.426 29.464 -44.651 1.00 82.23 N
ANISOU 3161 N LEU A 277 9758 13095 8392 -545 -235 144 N
ATOM 3162 CA LEU A 277 16.959 30.645 -45.379 1.00 81.79 C
ANISOU 3162 CA LEU A 277 9847 12922 8306 -652 -248 149 C
ATOM 3163 C LEU A 277 17.657 30.866 -46.761 1.00 85.77 C
ANISOU 3163 C LEU A 277 10429 13430 8729 -748 -192 127 C
ATOM 3164 O LEU A 277 16.908 31.058 -47.723 1.00 85.68 O
ANISOU 3164 O LEU A 277 10567 13277 8710 -752 -227 149 O
ATOM 3165 CB LEU A 277 17.011 31.914 -44.506 1.00 81.88 C
ANISOU 3165 CB LEU A 277 9869 12939 8301 -741 -254 135 C
ATOM 3166 CG LEU A 277 16.319 33.186 -45.044 1.00 86.59 C
ANISOU 3166 CG LEU A 277 10648 13386 8866 -824 -292 142 C
ATOM 3167 CD1 LEU A 277 14.852 32.942 -45.428 1.00 85.70 C
ANISOU 3167 CD1 LEU A 277 10628 13115 8819 -722 -379 169 C
ATOM 3168 CD2 LEU A 277 16.424 34.321 -44.046 1.00 89.08 C
ANISOU 3168 CD2 LEU A 277 10964 13717 9164 -901 -296 129 C
ATOM 3169 N PRO A 278 19.009 30.797 -46.940 1.00 81.80 N
ANISOU 3169 N PRO A 278 9835 13081 8166 -819 -110 75 N
ATOM 3170 CA PRO A 278 19.576 31.007 -48.287 1.00 82.24 C
ANISOU 3170 CA PRO A 278 9980 13126 8140 -924 -44 48 C
ATOM 3171 C PRO A 278 19.153 29.974 -49.342 1.00 85.11 C
ANISOU 3171 C PRO A 278 10399 13420 8520 -832 -60 78 C
ATOM 3172 O PRO A 278 18.955 30.340 -50.506 1.00 85.00 O
ANISOU 3172 O PRO A 278 10546 13298 8452 -900 -49 85 O
ATOM 3173 CB PRO A 278 21.087 30.997 -48.037 1.00 84.90 C
ANISOU 3173 CB PRO A 278 10158 13674 8427 -1005 49 -36 C
ATOM 3174 CG PRO A 278 21.257 30.200 -46.806 1.00 88.81 C
ANISOU 3174 CG PRO A 278 10472 14286 8987 -866 10 -42 C
ATOM 3175 CD PRO A 278 20.088 30.585 -45.959 1.00 83.60 C
ANISOU 3175 CD PRO A 278 9877 13499 8388 -814 -72 22 C
ATOM 3176 N LEU A 279 18.996 28.696 -48.938 1.00 79.96 N
ANISOU 3176 N LEU A 279 9632 12816 7932 -679 -89 95 N
ATOM 3177 CA LEU A 279 18.573 27.636 -49.853 1.00 78.44 C
ANISOU 3177 CA LEU A 279 9486 12559 7757 -585 -106 123 C
ATOM 3178 C LEU A 279 17.093 27.764 -50.168 1.00 80.88 C
ANISOU 3178 C LEU A 279 9936 12677 8117 -538 -191 175 C
ATOM 3179 O LEU A 279 16.699 27.500 -51.303 1.00 80.73 O
ANISOU 3179 O LEU A 279 10027 12562 8084 -524 -205 190 O
ATOM 3180 CB LEU A 279 18.896 26.244 -49.292 1.00 77.92 C
ANISOU 3180 CB LEU A 279 9278 12599 7730 -440 -109 119 C
ATOM 3181 CG LEU A 279 18.891 25.094 -50.305 1.00 81.96 C
ANISOU 3181 CG LEU A 279 9817 13088 8237 -357 -102 131 C
ATOM 3182 CD1 LEU A 279 19.877 25.342 -51.450 1.00 83.11 C
ANISOU 3182 CD1 LEU A 279 9979 13297 8301 -455 -22 82 C
ATOM 3183 CD2 LEU A 279 19.170 23.766 -49.627 1.00 82.82 C
ANISOU 3183 CD2 LEU A 279 9815 13281 8370 -204 -117 129 C
ATOM 3184 N THR A 280 16.279 28.199 -49.177 1.00 75.89 N
ANISOU 3184 N THR A 280 9297 11994 7542 -512 -249 191 N
ATOM 3185 CA THR A 280 14.834 28.417 -49.337 1.00 74.72 C
ANISOU 3185 CA THR A 280 9255 11685 7451 -464 -335 214 C
ATOM 3186 C THR A 280 14.575 29.533 -50.364 1.00 78.08 C
ANISOU 3186 C THR A 280 9867 11986 7813 -550 -362 208 C
ATOM 3187 O THR A 280 13.660 29.403 -51.180 1.00 77.33 O
ANISOU 3187 O THR A 280 9885 11762 7736 -499 -428 214 O
ATOM 3188 CB THR A 280 14.165 28.646 -47.974 1.00 81.85 C
ANISOU 3188 CB THR A 280 10089 12588 8424 -426 -374 216 C
ATOM 3189 OG1 THR A 280 14.541 27.586 -47.101 1.00 85.85 O
ANISOU 3189 OG1 THR A 280 10459 13198 8961 -351 -343 222 O
ATOM 3190 CG2 THR A 280 12.663 28.674 -48.056 1.00 76.69 C
ANISOU 3190 CG2 THR A 280 9502 11796 7841 -364 -458 215 C
ATOM 3191 N ILE A 281 15.416 30.597 -50.351 1.00 74.56 N
ANISOU 3191 N ILE A 281 9466 11579 7285 -683 -310 188 N
ATOM 3192 CA ILE A 281 15.333 31.707 -51.305 1.00 74.44 C
ANISOU 3192 CA ILE A 281 9665 11440 7177 -784 -321 181 C
ATOM 3193 C ILE A 281 15.789 31.207 -52.675 1.00 77.71 C
ANISOU 3193 C ILE A 281 10164 11835 7528 -810 -274 179 C
ATOM 3194 O ILE A 281 15.075 31.408 -53.655 1.00 77.60 O
ANISOU 3194 O ILE A 281 10332 11667 7486 -787 -336 190 O
ATOM 3195 CB ILE A 281 16.097 32.989 -50.851 1.00 77.98 C
ANISOU 3195 CB ILE A 281 10153 11931 7545 -939 -265 155 C
ATOM 3196 CG1 ILE A 281 15.559 33.524 -49.507 1.00 76.95 C
ANISOU 3196 CG1 ILE A 281 9961 11801 7476 -906 -321 159 C
ATOM 3197 CG2 ILE A 281 16.033 34.090 -51.941 1.00 80.09 C
ANISOU 3197 CG2 ILE A 281 10689 12051 7689 -1055 -263 147 C
ATOM 3198 CD1 ILE A 281 16.542 34.305 -48.718 1.00 78.45 C
ANISOU 3198 CD1 ILE A 281 10082 12107 7619 -1031 -249 131 C
ATOM 3199 N PHE A 282 16.945 30.522 -52.736 1.00 73.81 N
ANISOU 3199 N PHE A 282 9536 11497 7012 -844 -173 158 N
ATOM 3200 CA PHE A 282 17.470 29.976 -53.991 1.00 73.95 C
ANISOU 3200 CA PHE A 282 9611 11518 6969 -871 -114 149 C
ATOM 3201 C PHE A 282 16.436 29.087 -54.686 1.00 77.30 C
ANISOU 3201 C PHE A 282 10104 11820 7446 -735 -197 186 C
ATOM 3202 O PHE A 282 16.193 29.271 -55.876 1.00 77.63 O
ANISOU 3202 O PHE A 282 10333 11737 7425 -763 -213 191 O
ATOM 3203 CB PHE A 282 18.783 29.210 -53.758 1.00 75.89 C
ANISOU 3203 CB PHE A 282 9653 11972 7208 -882 -12 106 C
ATOM 3204 CG PHE A 282 19.521 28.864 -55.027 1.00 78.05 C
ANISOU 3204 CG PHE A 282 9983 12271 7402 -947 74 76 C
ATOM 3205 CD1 PHE A 282 19.301 27.655 -55.672 1.00 80.47 C
ANISOU 3205 CD1 PHE A 282 10270 12565 7739 -830 57 96 C
ATOM 3206 CD2 PHE A 282 20.442 29.746 -55.576 1.00 81.52 C
ANISOU 3206 CD2 PHE A 282 10504 12741 7729 -1138 179 21 C
ATOM 3207 CE1 PHE A 282 19.973 27.344 -56.855 1.00 82.00 C
ANISOU 3207 CE1 PHE A 282 10523 12778 7857 -890 138 66 C
ATOM 3208 CE2 PHE A 282 21.130 29.422 -56.750 1.00 84.89 C
ANISOU 3208 CE2 PHE A 282 10987 13190 8076 -1211 271 -16 C
ATOM 3209 CZ PHE A 282 20.881 28.229 -57.387 1.00 82.26 C
ANISOU 3209 CZ PHE A 282 10630 12845 7779 -1081 247 9 C
ATOM 3210 N ASN A 283 15.794 28.172 -53.931 1.00 72.69 N
ANISOU 3210 N ASN A 283 9386 11264 6970 -595 -251 207 N
ATOM 3211 CA ASN A 283 14.791 27.243 -54.444 1.00 71.90 C
ANISOU 3211 CA ASN A 283 9322 11067 6931 -471 -323 231 C
ATOM 3212 C ASN A 283 13.525 27.934 -54.954 1.00 76.48 C
ANISOU 3212 C ASN A 283 10075 11464 7520 -447 -433 232 C
ATOM 3213 O ASN A 283 13.066 27.563 -56.028 1.00 76.55 O
ANISOU 3213 O ASN A 283 10198 11374 7512 -407 -472 236 O
ATOM 3214 CB ASN A 283 14.461 26.145 -53.420 1.00 72.25 C
ANISOU 3214 CB ASN A 283 9196 11183 7074 -354 -339 243 C
ATOM 3215 CG ASN A 283 15.532 25.079 -53.239 1.00 91.94 C
ANISOU 3215 CG ASN A 283 11552 13829 9553 -322 -260 238 C
ATOM 3216 OD1 ASN A 283 16.641 25.162 -53.768 1.00 89.81 O
ANISOU 3216 OD1 ASN A 283 11270 13644 9209 -390 -184 213 O
ATOM 3217 ND2 ASN A 283 15.227 24.042 -52.475 1.00 81.01 N
ANISOU 3217 ND2 ASN A 283 10066 12481 8232 -214 -275 251 N
ATOM 3218 N THR A 284 12.968 28.933 -54.224 1.00 73.84 N
ANISOU 3218 N THR A 284 9765 11083 7206 -462 -490 221 N
ATOM 3219 CA THR A 284 11.751 29.638 -54.679 1.00 74.06 C
ANISOU 3219 CA THR A 284 9956 10943 7240 -417 -612 204 C
ATOM 3220 C THR A 284 12.031 30.539 -55.857 1.00 79.56 C
ANISOU 3220 C THR A 284 10897 11523 7808 -499 -619 200 C
ATOM 3221 O THR A 284 11.250 30.542 -56.802 1.00 79.49 O
ANISOU 3221 O THR A 284 11043 11377 7784 -436 -709 189 O
ATOM 3222 CB THR A 284 11.033 30.417 -53.573 1.00 81.84 C
ANISOU 3222 CB THR A 284 10901 11911 8283 -396 -676 183 C
ATOM 3223 OG1 THR A 284 11.892 31.434 -53.067 1.00 84.61 O
ANISOU 3223 OG1 THR A 284 11262 12321 8566 -514 -612 188 O
ATOM 3224 CG2 THR A 284 10.507 29.536 -52.465 1.00 77.93 C
ANISOU 3224 CG2 THR A 284 10206 11490 7913 -309 -683 177 C
ATOM 3225 N VAL A 285 13.149 31.291 -55.816 1.00 78.14 N
ANISOU 3225 N VAL A 285 10763 11397 7528 -646 -521 202 N
ATOM 3226 CA VAL A 285 13.562 32.189 -56.903 1.00 79.97 C
ANISOU 3226 CA VAL A 285 11254 11518 7613 -760 -497 195 C
ATOM 3227 C VAL A 285 13.625 31.417 -58.229 1.00 86.27 C
ANISOU 3227 C VAL A 285 12146 12262 8371 -734 -485 204 C
ATOM 3228 O VAL A 285 13.070 31.880 -59.224 1.00 86.29 O
ANISOU 3228 O VAL A 285 12396 12093 8299 -720 -560 199 O
ATOM 3229 CB VAL A 285 14.869 32.970 -56.568 1.00 84.55 C
ANISOU 3229 CB VAL A 285 11831 12198 8098 -947 -362 181 C
ATOM 3230 CG1 VAL A 285 15.513 33.575 -57.812 1.00 85.78 C
ANISOU 3230 CG1 VAL A 285 12239 12264 8091 -1094 -289 168 C
ATOM 3231 CG2 VAL A 285 14.603 34.059 -55.533 1.00 84.27 C
ANISOU 3231 CG2 VAL A 285 11807 12144 8067 -980 -403 172 C
ATOM 3232 N PHE A 286 14.211 30.202 -58.204 1.00 84.78 N
ANISOU 3232 N PHE A 286 11767 12212 8234 -708 -406 213 N
ATOM 3233 CA PHE A 286 14.341 29.335 -59.376 1.00 85.91 C
ANISOU 3233 CA PHE A 286 11969 12325 8349 -677 -385 221 C
ATOM 3234 C PHE A 286 13.100 28.449 -59.636 1.00 91.24 C
ANISOU 3234 C PHE A 286 12629 12916 9121 -507 -508 232 C
ATOM 3235 O PHE A 286 13.078 27.710 -60.621 1.00 90.84 O
ANISOU 3235 O PHE A 286 12647 12820 9049 -470 -509 239 O
ATOM 3236 CB PHE A 286 15.646 28.524 -59.312 1.00 87.93 C
ANISOU 3236 CB PHE A 286 12048 12766 8594 -732 -242 213 C
ATOM 3237 CG PHE A 286 16.829 29.423 -59.596 1.00 90.71 C
ANISOU 3237 CG PHE A 286 12480 13167 8818 -925 -116 179 C
ATOM 3238 CD1 PHE A 286 17.068 29.903 -60.880 1.00 94.60 C
ANISOU 3238 CD1 PHE A 286 13220 13545 9180 -1028 -75 169 C
ATOM 3239 CD2 PHE A 286 17.657 29.857 -58.567 1.00 92.84 C
ANISOU 3239 CD2 PHE A 286 12596 13588 9092 -1014 -39 149 C
ATOM 3240 CE1 PHE A 286 18.128 30.775 -61.131 1.00 96.60 C
ANISOU 3240 CE1 PHE A 286 13563 13835 9304 -1232 57 126 C
ATOM 3241 CE2 PHE A 286 18.714 30.735 -58.821 1.00 96.61 C
ANISOU 3241 CE2 PHE A 286 13147 14112 9449 -1212 84 102 C
ATOM 3242 CZ PHE A 286 18.943 31.186 -60.099 1.00 95.66 C
ANISOU 3242 CZ PHE A 286 13273 13877 9197 -1328 138 89 C
ATOM 3243 N ASP A 287 12.051 28.576 -58.802 1.00 89.09 N
ANISOU 3243 N ASP A 287 12278 12621 8952 -413 -609 222 N
ATOM 3244 CA ASP A 287 10.785 27.875 -59.008 1.00 89.29 C
ANISOU 3244 CA ASP A 287 12287 12569 9071 -269 -724 208 C
ATOM 3245 C ASP A 287 9.871 28.780 -59.802 1.00 97.15 C
ANISOU 3245 C ASP A 287 13522 13378 10014 -232 -857 177 C
ATOM 3246 O ASP A 287 9.075 28.296 -60.606 1.00 97.05 O
ANISOU 3246 O ASP A 287 13584 13273 10018 -140 -943 158 O
ATOM 3247 CB ASP A 287 10.140 27.454 -57.686 1.00 89.91 C
ANISOU 3247 CB ASP A 287 12156 12722 9282 -197 -754 194 C
ATOM 3248 CG ASP A 287 10.494 26.046 -57.262 1.00 98.87 C
ANISOU 3248 CG ASP A 287 13101 13980 10486 -156 -679 216 C
ATOM 3249 OD1 ASP A 287 11.250 25.372 -57.999 1.00100.30 O
ANISOU 3249 OD1 ASP A 287 13295 14198 10617 -173 -610 239 O
ATOM 3250 OD2 ASP A 287 10.015 25.613 -56.201 1.00103.31 O
ANISOU 3250 OD2 ASP A 287 13515 14595 11142 -108 -688 206 O
ATOM 3251 N TRP A 288 10.011 30.101 -59.594 1.00 96.90 N
ANISOU 3251 N TRP A 288 13625 13287 9906 -300 -877 167 N
ATOM 3252 CA TRP A 288 9.275 31.134 -60.317 1.00 99.13 C
ANISOU 3252 CA TRP A 288 14179 13380 10106 -265 -1008 135 C
ATOM 3253 C TRP A 288 9.976 31.423 -61.662 1.00106.72 C
ANISOU 3253 C TRP A 288 15401 14242 10907 -353 -959 156 C
ATOM 3254 O TRP A 288 9.312 31.708 -62.662 1.00106.99 O
ANISOU 3254 O TRP A 288 15662 14110 10880 -281 -1074 134 O
ATOM 3255 CB TRP A 288 9.160 32.403 -59.462 1.00 98.32 C
ANISOU 3255 CB TRP A 288 14130 13250 9977 -303 -1043 117 C
ATOM 3256 CG TRP A 288 8.219 32.269 -58.299 1.00 98.59 C
ANISOU 3256 CG TRP A 288 13961 13340 10157 -199 -1121 80 C
ATOM 3257 CD1 TRP A 288 8.545 31.962 -57.013 1.00100.61 C
ANISOU 3257 CD1 TRP A 288 13974 13751 10503 -232 -1039 95 C
ATOM 3258 CD2 TRP A 288 6.799 32.470 -58.316 1.00 98.76 C
ANISOU 3258 CD2 TRP A 288 14010 13267 10248 -46 -1293 8 C
ATOM 3259 NE1 TRP A 288 7.415 31.937 -56.229 1.00 99.69 N
ANISOU 3259 NE1 TRP A 288 13738 13636 10504 -124 -1136 43 N
ATOM 3260 CE2 TRP A 288 6.331 32.262 -56.999 1.00101.89 C
ANISOU 3260 CE2 TRP A 288 14166 13771 10776 -10 -1292 -18 C
ATOM 3261 CE3 TRP A 288 5.870 32.793 -59.322 1.00100.98 C
ANISOU 3261 CE3 TRP A 288 14494 13384 10489 69 -1454 -49 C
ATOM 3262 CZ2 TRP A 288 4.975 32.360 -56.662 1.00101.43 C
ANISOU 3262 CZ2 TRP A 288 14047 13675 10817 124 -1431 -107 C
ATOM 3263 CZ3 TRP A 288 4.528 32.902 -58.985 1.00102.61 C
ANISOU 3263 CZ3 TRP A 288 14634 13559 10796 219 -1608 -142 C
ATOM 3264 CH2 TRP A 288 4.092 32.687 -57.670 1.00102.51 C
ANISOU 3264 CH2 TRP A 288 14363 13666 10920 239 -1590 -175 C
ATOM 3265 N ASN A 289 11.320 31.315 -61.678 1.00105.41 N
ANISOU 3265 N ASN A 289 15197 14182 10672 -507 -788 188 N
ATOM 3266 CA ASN A 289 12.168 31.511 -62.855 1.00107.12 C
ANISOU 3266 CA ASN A 289 15630 14335 10735 -627 -698 200 C
ATOM 3267 C ASN A 289 12.754 30.156 -63.300 1.00112.98 C
ANISOU 3267 C ASN A 289 16215 15193 11518 -618 -601 219 C
ATOM 3268 O ASN A 289 13.974 29.965 -63.387 1.00112.26 O
ANISOU 3268 O ASN A 289 16051 15226 11377 -746 -443 222 O
ATOM 3269 CB ASN A 289 13.240 32.567 -62.571 1.00108.40 C
ANISOU 3269 CB ASN A 289 15882 14530 10776 -825 -571 198 C
ATOM 3270 CG ASN A 289 12.656 33.929 -62.289 1.00132.61 C
ANISOU 3270 CG ASN A 289 19162 17449 13774 -832 -671 182 C
ATOM 3271 OD1 ASN A 289 12.362 34.282 -61.139 1.00126.85 O
ANISOU 3271 OD1 ASN A 289 18291 16778 13129 -795 -714 174 O
ATOM 3272 ND2 ASN A 289 12.438 34.712 -63.340 1.00125.09 N
ANISOU 3272 ND2 ASN A 289 18573 16293 12663 -869 -719 174 N
ATOM 3273 N HIS A 290 11.834 29.211 -63.568 1.00111.47 N
ANISOU 3273 N HIS A 290 15966 14965 11421 -461 -704 218 N
ATOM 3274 CA HIS A 290 12.085 27.828 -63.986 1.00111.93 C
ANISOU 3274 CA HIS A 290 15892 15106 11531 -414 -649 235 C
ATOM 3275 C HIS A 290 12.676 27.716 -65.393 1.00118.39 C
ANISOU 3275 C HIS A 290 16917 15849 12217 -484 -585 243 C
ATOM 3276 O HIS A 290 13.250 26.676 -65.730 1.00118.28 O
ANISOU 3276 O HIS A 290 16794 15928 12219 -482 -499 255 O
ATOM 3277 CB HIS A 290 10.790 26.997 -63.878 1.00112.18 C
ANISOU 3277 CB HIS A 290 15826 15103 11696 -239 -782 222 C
ATOM 3278 CG HIS A 290 9.597 27.655 -64.503 1.00116.36 C
ANISOU 3278 CG HIS A 290 16563 15443 12205 -146 -957 184 C
ATOM 3279 ND1 HIS A 290 8.784 28.512 -63.778 1.00118.19 N
ANISOU 3279 ND1 HIS A 290 16785 15633 12488 -90 -1069 146 N
ATOM 3280 CD2 HIS A 290 9.131 27.581 -65.772 1.00118.90 C
ANISOU 3280 CD2 HIS A 290 17107 15613 12457 -93 -1042 171 C
ATOM 3281 CE1 HIS A 290 7.848 28.920 -64.621 1.00118.32 C
ANISOU 3281 CE1 HIS A 290 17009 15480 12466 6 -1225 103 C
ATOM 3282 NE2 HIS A 290 8.016 28.388 -65.833 1.00119.13 N
ANISOU 3282 NE2 HIS A 290 17262 15507 12494 9 -1218 118 N
ATOM 3283 N GLN A 291 12.524 28.776 -66.211 1.00116.55 N
ANISOU 3283 N GLN A 291 16997 15440 11846 -542 -629 233 N
ATOM 3284 CA GLN A 291 13.007 28.859 -67.594 1.00117.57 C
ANISOU 3284 CA GLN A 291 17387 15462 11823 -623 -573 236 C
ATOM 3285 C GLN A 291 14.541 28.957 -67.645 1.00122.13 C
ANISOU 3285 C GLN A 291 17921 16173 12311 -823 -356 231 C
ATOM 3286 O GLN A 291 15.159 28.379 -68.538 1.00122.20 O
ANISOU 3286 O GLN A 291 17986 16192 12251 -877 -261 230 O
ATOM 3287 CB GLN A 291 12.382 30.066 -68.332 1.00120.22 C
ANISOU 3287 CB GLN A 291 18103 15555 12020 -626 -690 222 C
ATOM 3288 CG GLN A 291 10.910 30.380 -68.000 1.00138.35 C
ANISOU 3288 CG GLN A 291 20431 17737 14397 -442 -913 197 C
ATOM 3289 CD GLN A 291 10.722 31.342 -66.834 1.00158.78 C
ANISOU 3289 CD GLN A 291 22954 20357 17019 -463 -943 183 C
ATOM 3290 OE1 GLN A 291 11.584 32.172 -66.510 1.00154.11 O
ANISOU 3290 OE1 GLN A 291 22440 19785 16329 -626 -831 190 O
ATOM 3291 NE2 GLN A 291 9.566 31.267 -66.190 1.00150.78 N
ANISOU 3291 NE2 GLN A 291 21797 19349 16142 -304 -1090 153 N
ATOM 3292 N ILE A 292 15.135 29.691 -66.679 1.00119.10 N
ANISOU 3292 N ILE A 292 17429 15895 11927 -932 -280 217 N
ATOM 3293 CA ILE A 292 16.568 29.982 -66.512 1.00119.69 C
ANISOU 3293 CA ILE A 292 17433 16118 11925 -1133 -80 187 C
ATOM 3294 C ILE A 292 17.438 28.709 -66.463 1.00123.58 C
ANISOU 3294 C ILE A 292 17652 16818 12484 -1122 39 173 C
ATOM 3295 O ILE A 292 17.142 27.772 -65.719 1.00121.60 O
ANISOU 3295 O ILE A 292 17145 16678 12378 -977 -12 190 O
ATOM 3296 CB ILE A 292 16.783 30.918 -65.271 1.00122.53 C
ANISOU 3296 CB ILE A 292 17693 16556 12306 -1210 -60 172 C
ATOM 3297 CG1 ILE A 292 15.959 32.246 -65.375 1.00123.35 C
ANISOU 3297 CG1 ILE A 292 18096 16442 12330 -1213 -184 180 C
ATOM 3298 CG2 ILE A 292 18.265 31.197 -64.962 1.00123.86 C
ANISOU 3298 CG2 ILE A 292 17754 16902 12406 -1422 145 120 C
ATOM 3299 CD1 ILE A 292 16.088 33.114 -66.717 1.00131.44 C
ANISOU 3299 CD1 ILE A 292 19558 17244 13140 -1338 -164 171 C
ATOM 3300 N ILE A 293 18.518 28.709 -67.270 1.00122.04 N
ANISOU 3300 N ILE A 293 17530 16669 12170 -1278 200 134 N
ATOM 3301 CA ILE A 293 19.493 27.622 -67.420 1.00122.06 C
ANISOU 3301 CA ILE A 293 17312 16866 12201 -1287 328 99 C
ATOM 3302 C ILE A 293 20.605 27.721 -66.349 1.00127.00 C
ANISOU 3302 C ILE A 293 17656 17737 12861 -1382 452 38 C
ATOM 3303 O ILE A 293 21.173 28.799 -66.154 1.00127.72 O
ANISOU 3303 O ILE A 293 17822 17840 12865 -1563 537 -5 O
ATOM 3304 CB ILE A 293 20.057 27.612 -68.874 1.00126.30 C
ANISOU 3304 CB ILE A 293 18080 17325 12585 -1414 440 71 C
ATOM 3305 CG1 ILE A 293 18.930 27.494 -69.928 1.00126.57 C
ANISOU 3305 CG1 ILE A 293 18390 17114 12586 -1298 299 129 C
ATOM 3306 CG2 ILE A 293 21.102 26.517 -69.077 1.00127.10 C
ANISOU 3306 CG2 ILE A 293 17952 17637 12702 -1435 584 15 C
ATOM 3307 CD1 ILE A 293 18.621 28.789 -70.697 1.00134.46 C
ANISOU 3307 CD1 ILE A 293 19800 17869 13420 -1408 266 136 C
ATOM 3308 N ALA A 294 20.911 26.587 -65.673 1.00122.84 N
ANISOU 3308 N ALA A 294 16819 17400 12453 -1256 456 27 N
ATOM 3309 CA ALA A 294 21.937 26.479 -64.631 1.00122.82 C
ANISOU 3309 CA ALA A 294 16528 17644 12495 -1299 548 -41 C
ATOM 3310 C ALA A 294 23.358 26.670 -65.184 1.00129.54 C
ANISOU 3310 C ALA A 294 17345 18640 13236 -1496 744 -149 C
ATOM 3311 O ALA A 294 23.813 25.876 -66.013 1.00129.67 O
ANISOU 3311 O ALA A 294 17350 18700 13219 -1485 813 -180 O
ATOM 3312 CB ALA A 294 21.821 25.137 -63.920 1.00122.30 C
ANISOU 3312 CB ALA A 294 16196 17709 12563 -1090 486 -25 C
ATOM 3313 N THR A 295 24.045 27.742 -64.731 1.00127.88 N
ANISOU 3313 N THR A 295 17122 18502 12964 -1684 839 -214 N
ATOM 3314 CA THR A 295 25.420 28.091 -65.129 1.00129.69 C
ANISOU 3314 CA THR A 295 17305 18885 13087 -1910 1042 -342 C
ATOM 3315 C THR A 295 26.418 27.701 -64.025 1.00134.80 C
ANISOU 3315 C THR A 295 17575 19830 13813 -1888 1099 -443 C
ATOM 3316 O THR A 295 26.007 27.157 -62.997 1.00133.14 O
ANISOU 3316 O THR A 295 17179 19680 13727 -1698 978 -398 O
ATOM 3317 CB THR A 295 25.540 29.594 -65.511 1.00137.16 C
ANISOU 3317 CB THR A 295 18536 19694 13884 -2166 1125 -362 C
ATOM 3318 OG1 THR A 295 25.436 30.419 -64.347 1.00134.80 O
ANISOU 3318 OG1 THR A 295 18172 19420 13625 -2193 1077 -355 O
ATOM 3319 CG2 THR A 295 24.539 30.027 -66.583 1.00135.56 C
ANISOU 3319 CG2 THR A 295 18736 19184 13586 -2170 1052 -272 C
ATOM 3320 N CYS A 296 27.722 27.987 -64.236 1.00134.11 N
ANISOU 3320 N CYS A 296 17381 19928 13646 -2085 1283 -589 N
ATOM 3321 CA CYS A 296 28.796 27.715 -63.266 1.00135.00 C
ANISOU 3321 CA CYS A 296 17135 20342 13817 -2081 1345 -719 C
ATOM 3322 C CYS A 296 28.623 28.627 -62.051 1.00134.43 C
ANISOU 3322 C CYS A 296 17011 20287 13781 -2125 1295 -707 C
ATOM 3323 O CYS A 296 28.895 28.205 -60.924 1.00133.42 O
ANISOU 3323 O CYS A 296 16606 20337 13749 -2000 1240 -744 O
ATOM 3324 CB CYS A 296 30.178 27.881 -63.895 1.00138.81 C
ANISOU 3324 CB CYS A 296 17528 21014 14200 -2301 1561 -899 C
ATOM 3325 SG CYS A 296 30.195 27.812 -65.707 1.00144.73 S
ANISOU 3325 SG CYS A 296 18572 21604 14815 -2427 1677 -896 S
ATOM 3326 N ASN A 297 28.151 29.873 -62.292 1.00128.06 N
ANISOU 3326 N ASN A 297 16490 19280 12886 -2294 1306 -654 N
ATOM 3327 CA ASN A 297 27.873 30.880 -61.267 1.00125.88 C
ANISOU 3327 CA ASN A 297 16227 18976 12626 -2351 1256 -630 C
ATOM 3328 C ASN A 297 26.696 30.439 -60.396 1.00122.91 C
ANISOU 3328 C ASN A 297 15810 18505 12384 -2090 1048 -495 C
ATOM 3329 O ASN A 297 26.723 30.663 -59.183 1.00122.18 O
ANISOU 3329 O ASN A 297 15555 18505 12362 -2046 996 -501 O
ATOM 3330 CB ASN A 297 27.594 32.246 -61.904 1.00128.37 C
ANISOU 3330 CB ASN A 297 16906 19076 12794 -2586 1317 -607 C
ATOM 3331 CG ASN A 297 28.830 32.964 -62.392 1.00153.37 C
ANISOU 3331 CG ASN A 297 20090 22360 15823 -2900 1543 -761 C
ATOM 3332 OD1 ASN A 297 29.673 33.422 -61.609 1.00148.48 O
ANISOU 3332 OD1 ASN A 297 19269 21935 15211 -3019 1622 -869 O
ATOM 3333 ND2 ASN A 297 28.940 33.120 -63.701 1.00146.07 N
ANISOU 3333 ND2 ASN A 297 19424 21313 14762 -3053 1654 -779 N
ATOM 3334 N HIS A 298 25.680 29.789 -61.014 1.00113.98 N
ANISOU 3334 N HIS A 298 14825 17196 11287 -1925 937 -385 N
ATOM 3335 CA HIS A 298 24.504 29.262 -60.323 1.00109.71 C
ANISOU 3335 CA HIS A 298 14253 16561 10871 -1688 753 -270 C
ATOM 3336 C HIS A 298 24.892 28.097 -59.434 1.00109.13 C
ANISOU 3336 C HIS A 298 13857 16694 10914 -1505 717 -298 C
ATOM 3337 O HIS A 298 24.489 28.073 -58.276 1.00107.92 O
ANISOU 3337 O HIS A 298 13589 16567 10847 -1399 624 -262 O
ATOM 3338 CB HIS A 298 23.420 28.825 -61.314 1.00109.44 C
ANISOU 3338 CB HIS A 298 14446 16302 10835 -1577 657 -173 C
ATOM 3339 CG HIS A 298 22.666 29.954 -61.938 1.00112.93 C
ANISOU 3339 CG HIS A 298 15231 16497 11181 -1681 621 -123 C
ATOM 3340 ND1 HIS A 298 22.380 29.965 -63.288 1.00115.14 N
ANISOU 3340 ND1 HIS A 298 15774 16608 11366 -1719 633 -100 N
ATOM 3341 CD2 HIS A 298 22.156 31.074 -61.374 1.00114.42 C
ANISOU 3341 CD2 HIS A 298 15546 16579 11350 -1738 565 -95 C
ATOM 3342 CE1 HIS A 298 21.711 31.084 -63.504 1.00114.80 C
ANISOU 3342 CE1 HIS A 298 16017 16358 11242 -1791 577 -63 C
ATOM 3343 NE2 HIS A 298 21.554 31.785 -62.383 1.00114.72 N
ANISOU 3343 NE2 HIS A 298 15936 16379 11275 -1804 535 -59 N
ATOM 3344 N ASN A 299 25.695 27.151 -59.966 1.00103.46 N
ANISOU 3344 N ASN A 299 13005 16118 10187 -1467 790 -367 N
ATOM 3345 CA ASN A 299 26.179 25.973 -59.242 1.00101.69 C
ANISOU 3345 CA ASN A 299 12498 16090 10050 -1281 757 -409 C
ATOM 3346 C ASN A 299 27.039 26.343 -58.024 1.00103.42 C
ANISOU 3346 C ASN A 299 12479 16524 10292 -1319 787 -506 C
ATOM 3347 O ASN A 299 26.941 25.674 -56.995 1.00102.44 O
ANISOU 3347 O ASN A 299 12187 16481 10253 -1138 695 -492 O
ATOM 3348 CB ASN A 299 26.921 25.017 -60.180 1.00102.65 C
ANISOU 3348 CB ASN A 299 12550 16315 10138 -1247 835 -480 C
ATOM 3349 CG ASN A 299 26.041 24.362 -61.221 1.00123.67 C
ANISOU 3349 CG ASN A 299 15407 18784 12799 -1153 779 -380 C
ATOM 3350 OD1 ASN A 299 25.004 23.764 -60.915 1.00115.53 O
ANISOU 3350 OD1 ASN A 299 14414 17636 11847 -975 645 -275 O
ATOM 3351 ND2 ASN A 299 26.457 24.425 -62.477 1.00117.34 N
ANISOU 3351 ND2 ASN A 299 14731 17949 11903 -1276 885 -421 N
ATOM 3352 N LEU A 300 27.847 27.422 -58.127 1.00 98.75 N
ANISOU 3352 N LEU A 300 11890 16013 9618 -1558 916 -606 N
ATOM 3353 CA LEU A 300 28.674 27.903 -57.018 1.00 98.11 C
ANISOU 3353 CA LEU A 300 11591 16135 9551 -1621 950 -711 C
ATOM 3354 C LEU A 300 27.777 28.513 -55.942 1.00 97.94 C
ANISOU 3354 C LEU A 300 11628 15999 9587 -1574 833 -609 C
ATOM 3355 O LEU A 300 27.959 28.208 -54.766 1.00 96.90 O
ANISOU 3355 O LEU A 300 11297 15997 9525 -1458 770 -633 O
ATOM 3356 CB LEU A 300 29.717 28.923 -57.502 1.00100.15 C
ANISOU 3356 CB LEU A 300 11860 16496 9698 -1917 1132 -851 C
ATOM 3357 CG LEU A 300 30.750 29.377 -56.461 1.00105.90 C
ANISOU 3357 CG LEU A 300 12325 17477 10436 -1998 1187 -999 C
ATOM 3358 CD1 LEU A 300 32.144 29.323 -57.027 1.00108.30 C
ANISOU 3358 CD1 LEU A 300 12456 18019 10674 -2149 1359 -1202 C
ATOM 3359 CD2 LEU A 300 30.451 30.778 -55.966 1.00108.29 C
ANISOU 3359 CD2 LEU A 300 12767 17682 10696 -2185 1204 -971 C
ATOM 3360 N LEU A 301 26.810 29.366 -56.354 1.00 92.18 N
ANISOU 3360 N LEU A 301 11177 15024 8822 -1655 800 -503 N
ATOM 3361 CA LEU A 301 25.839 30.018 -55.474 1.00 89.86 C
ANISOU 3361 CA LEU A 301 10970 14596 8577 -1613 687 -407 C
ATOM 3362 C LEU A 301 24.996 28.964 -54.761 1.00 91.81 C
ANISOU 3362 C LEU A 301 11126 14813 8946 -1349 541 -318 C
ATOM 3363 O LEU A 301 24.769 29.094 -53.556 1.00 90.49 O
ANISOU 3363 O LEU A 301 10856 14684 8841 -1278 473 -300 O
ATOM 3364 CB LEU A 301 24.947 31.000 -56.271 1.00 89.39 C
ANISOU 3364 CB LEU A 301 11246 14273 8444 -1726 671 -326 C
ATOM 3365 CG LEU A 301 23.824 31.743 -55.520 1.00 92.11 C
ANISOU 3365 CG LEU A 301 11711 14454 8832 -1674 545 -232 C
ATOM 3366 CD1 LEU A 301 24.366 32.592 -54.380 1.00 92.52 C
ANISOU 3366 CD1 LEU A 301 11642 14624 8886 -1768 572 -284 C
ATOM 3367 CD2 LEU A 301 23.040 32.616 -56.457 1.00 93.47 C
ANISOU 3367 CD2 LEU A 301 12224 14375 8916 -1764 522 -174 C
ATOM 3368 N PHE A 302 24.574 27.906 -55.498 1.00 87.59 N
ANISOU 3368 N PHE A 302 10633 14212 8436 -1214 503 -270 N
ATOM 3369 CA PHE A 302 23.792 26.789 -54.964 1.00 86.01 C
ANISOU 3369 CA PHE A 302 10370 13974 8337 -980 383 -194 C
ATOM 3370 C PHE A 302 24.570 26.017 -53.900 1.00 90.87 C
ANISOU 3370 C PHE A 302 10725 14802 8998 -856 374 -258 C
ATOM 3371 O PHE A 302 23.986 25.674 -52.874 1.00 89.41 O
ANISOU 3371 O PHE A 302 10492 14596 8885 -719 280 -205 O
ATOM 3372 CB PHE A 302 23.306 25.844 -56.080 1.00 87.21 C
ANISOU 3372 CB PHE A 302 10630 14018 8489 -887 362 -144 C
ATOM 3373 CG PHE A 302 22.582 24.608 -55.595 1.00 87.30 C
ANISOU 3373 CG PHE A 302 10585 13994 8590 -665 257 -78 C
ATOM 3374 CD1 PHE A 302 21.308 24.698 -55.045 1.00 88.81 C
ANISOU 3374 CD1 PHE A 302 10855 14038 8852 -591 151 8 C
ATOM 3375 CD2 PHE A 302 23.174 23.356 -55.684 1.00 89.56 C
ANISOU 3375 CD2 PHE A 302 10749 14394 8885 -535 269 -112 C
ATOM 3376 CE1 PHE A 302 20.644 23.558 -54.585 1.00 88.63 C
ANISOU 3376 CE1 PHE A 302 10792 13980 8903 -412 73 58 C
ATOM 3377 CE2 PHE A 302 22.508 22.216 -55.225 1.00 91.27 C
ANISOU 3377 CE2 PHE A 302 10947 14562 9169 -343 179 -52 C
ATOM 3378 CZ PHE A 302 21.247 22.325 -54.679 1.00 87.93 C
ANISOU 3378 CZ PHE A 302 10607 13991 8812 -293 89 33 C
ATOM 3379 N LEU A 303 25.876 25.748 -54.138 1.00 89.08 N
ANISOU 3379 N LEU A 303 10341 14781 8725 -900 468 -382 N
ATOM 3380 CA LEU A 303 26.725 25.033 -53.181 1.00 89.30 C
ANISOU 3380 CA LEU A 303 10121 15026 8784 -768 449 -468 C
ATOM 3381 C LEU A 303 26.981 25.870 -51.936 1.00 93.70 C
ANISOU 3381 C LEU A 303 10577 15666 9358 -820 431 -502 C
ATOM 3382 O LEU A 303 27.058 25.304 -50.845 1.00 93.65 O
ANISOU 3382 O LEU A 303 10443 15740 9399 -658 351 -508 O
ATOM 3383 CB LEU A 303 28.042 24.536 -53.809 1.00 90.86 C
ANISOU 3383 CB LEU A 303 10161 15433 8928 -794 549 -616 C
ATOM 3384 CG LEU A 303 27.933 23.423 -54.869 1.00 95.33 C
ANISOU 3384 CG LEU A 303 10778 15959 9485 -682 551 -596 C
ATOM 3385 CD1 LEU A 303 29.250 23.197 -55.558 1.00 96.95 C
ANISOU 3385 CD1 LEU A 303 10833 16374 9630 -746 668 -759 C
ATOM 3386 CD2 LEU A 303 27.420 22.112 -54.280 1.00 97.25 C
ANISOU 3386 CD2 LEU A 303 10987 16175 9790 -413 426 -531 C
ATOM 3387 N LEU A 304 27.051 27.213 -52.082 1.00 90.22 N
ANISOU 3387 N LEU A 304 10220 15188 8871 -1041 499 -519 N
ATOM 3388 CA LEU A 304 27.223 28.120 -50.947 1.00 90.17 C
ANISOU 3388 CA LEU A 304 10145 15240 8875 -1111 485 -544 C
ATOM 3389 C LEU A 304 25.940 28.221 -50.117 1.00 94.54 C
ANISOU 3389 C LEU A 304 10803 15618 9498 -1001 362 -409 C
ATOM 3390 O LEU A 304 26.018 28.477 -48.920 1.00 93.75 O
ANISOU 3390 O LEU A 304 10600 15586 9434 -949 311 -419 O
ATOM 3391 CB LEU A 304 27.719 29.509 -51.375 1.00 91.09 C
ANISOU 3391 CB LEU A 304 10344 15357 8908 -1389 601 -606 C
ATOM 3392 CG LEU A 304 29.167 29.603 -51.890 1.00 97.82 C
ANISOU 3392 CG LEU A 304 11044 16434 9691 -1541 746 -782 C
ATOM 3393 CD1 LEU A 304 29.506 31.021 -52.280 1.00 99.03 C
ANISOU 3393 CD1 LEU A 304 11343 16538 9747 -1838 869 -825 C
ATOM 3394 CD2 LEU A 304 30.183 29.111 -50.859 1.00100.77 C
ANISOU 3394 CD2 LEU A 304 11115 17075 10098 -1457 730 -915 C
ATOM 3395 N CYS A 305 24.768 27.995 -50.752 1.00 91.59 N
ANISOU 3395 N CYS A 305 10630 15026 9144 -962 313 -293 N
ATOM 3396 CA CYS A 305 23.450 27.989 -50.107 1.00 90.43 C
ANISOU 3396 CA CYS A 305 10580 14711 9067 -858 202 -179 C
ATOM 3397 C CYS A 305 23.216 26.624 -49.451 1.00 91.56 C
ANISOU 3397 C CYS A 305 10621 14891 9277 -635 126 -150 C
ATOM 3398 O CYS A 305 22.728 26.557 -48.316 1.00 90.66 O
ANISOU 3398 O CYS A 305 10474 14758 9215 -552 58 -113 O
ATOM 3399 CB CYS A 305 22.348 28.304 -51.118 1.00 91.09 C
ANISOU 3399 CB CYS A 305 10899 14569 9143 -895 175 -96 C
ATOM 3400 SG CYS A 305 22.311 30.027 -51.680 1.00 96.25 S
ANISOU 3400 SG CYS A 305 11751 15115 9704 -1136 232 -107 S
ATOM 3401 N HIS A 306 23.538 25.537 -50.193 1.00 86.30 N
ANISOU 3401 N HIS A 306 9924 14265 8600 -543 142 -168 N
ATOM 3402 CA HIS A 306 23.389 24.145 -49.773 1.00 84.57 C
ANISOU 3402 CA HIS A 306 9645 14068 8421 -333 79 -145 C
ATOM 3403 C HIS A 306 24.214 23.863 -48.529 1.00 88.71 C
ANISOU 3403 C HIS A 306 9992 14766 8947 -242 54 -214 C
ATOM 3404 O HIS A 306 23.701 23.233 -47.610 1.00 87.39 O
ANISOU 3404 O HIS A 306 9830 14556 8818 -101 -21 -166 O
ATOM 3405 CB HIS A 306 23.751 23.178 -50.913 1.00 85.08 C
ANISOU 3405 CB HIS A 306 9715 14156 8455 -274 112 -168 C
ATOM 3406 CG HIS A 306 23.502 21.743 -50.583 1.00 87.64 C
ANISOU 3406 CG HIS A 306 10025 14468 8808 -62 46 -136 C
ATOM 3407 ND1 HIS A 306 22.227 21.217 -50.586 1.00 88.24 N
ANISOU 3407 ND1 HIS A 306 10237 14360 8932 12 -15 -32 N
ATOM 3408 CD2 HIS A 306 24.376 20.771 -50.238 1.00 89.94 C
ANISOU 3408 CD2 HIS A 306 10191 14906 9076 85 32 -204 C
ATOM 3409 CE1 HIS A 306 22.362 19.949 -50.234 1.00 87.75 C
ANISOU 3409 CE1 HIS A 306 10146 14327 8869 186 -55 -32 C
ATOM 3410 NE2 HIS A 306 23.640 19.632 -50.028 1.00 89.12 N
ANISOU 3410 NE2 HIS A 306 10173 14693 8997 247 -35 -130 N
ATOM 3411 N LEU A 307 25.470 24.364 -48.486 1.00 86.67 N
ANISOU 3411 N LEU A 307 9587 14701 8643 -330 118 -335 N
ATOM 3412 CA LEU A 307 26.382 24.199 -47.349 1.00 87.16 C
ANISOU 3412 CA LEU A 307 9464 14953 8699 -248 90 -428 C
ATOM 3413 C LEU A 307 25.846 24.924 -46.106 1.00 90.66 C
ANISOU 3413 C LEU A 307 9928 15342 9176 -269 38 -379 C
ATOM 3414 O LEU A 307 25.790 24.309 -45.043 1.00 90.10 O
ANISOU 3414 O LEU A 307 9815 15293 9124 -111 -40 -369 O
ATOM 3415 CB LEU A 307 27.813 24.658 -47.717 1.00 88.52 C
ANISOU 3415 CB LEU A 307 9464 15351 8817 -367 183 -590 C
ATOM 3416 CG LEU A 307 28.951 24.449 -46.701 1.00 93.41 C
ANISOU 3416 CG LEU A 307 9857 16209 9424 -273 152 -730 C
ATOM 3417 CD1 LEU A 307 29.197 22.969 -46.406 1.00 93.48 C
ANISOU 3417 CD1 LEU A 307 9806 16280 9434 -4 66 -753 C
ATOM 3418 CD2 LEU A 307 30.225 25.055 -47.219 1.00 96.34 C
ANISOU 3418 CD2 LEU A 307 10066 16792 9747 -440 264 -901 C
ATOM 3419 N THR A 308 25.398 26.196 -46.256 1.00 87.08 N
ANISOU 3419 N THR A 308 9564 14800 8723 -457 77 -345 N
ATOM 3420 CA THR A 308 24.815 27.002 -45.174 1.00 86.53 C
ANISOU 3420 CA THR A 308 9530 14664 8683 -494 33 -297 C
ATOM 3421 C THR A 308 23.615 26.265 -44.562 1.00 90.38 C
ANISOU 3421 C THR A 308 10113 14997 9230 -338 -55 -187 C
ATOM 3422 O THR A 308 23.494 26.210 -43.338 1.00 90.67 O
ANISOU 3422 O THR A 308 10111 15051 9288 -264 -109 -178 O
ATOM 3423 CB THR A 308 24.460 28.414 -45.666 1.00 94.35 C
ANISOU 3423 CB THR A 308 10644 15553 9652 -709 86 -274 C
ATOM 3424 OG1 THR A 308 25.560 28.945 -46.404 1.00 94.75 O
ANISOU 3424 OG1 THR A 308 10632 15733 9634 -869 189 -380 O
ATOM 3425 CG2 THR A 308 24.118 29.367 -44.520 1.00 92.53 C
ANISOU 3425 CG2 THR A 308 10425 15291 9441 -762 51 -251 C
ATOM 3426 N ALA A 309 22.760 25.669 -45.416 1.00 85.71 N
ANISOU 3426 N ALA A 309 9646 14260 8661 -295 -66 -114 N
ATOM 3427 CA ALA A 309 21.615 24.864 -45.008 1.00 83.82 C
ANISOU 3427 CA ALA A 309 9498 13876 8474 -166 -131 -25 C
ATOM 3428 C ALA A 309 22.107 23.596 -44.292 1.00 87.84 C
ANISOU 3428 C ALA A 309 9933 14472 8971 21 -171 -49 C
ATOM 3429 O ALA A 309 21.609 23.284 -43.215 1.00 87.20 O
ANISOU 3429 O ALA A 309 9879 14342 8912 104 -220 -13 O
ATOM 3430 CB ALA A 309 20.780 24.506 -46.223 1.00 83.92 C
ANISOU 3430 CB ALA A 309 9641 13741 8502 -173 -127 32 C
ATOM 3431 N MET A 310 23.138 22.922 -44.843 1.00 85.43 N
ANISOU 3431 N MET A 310 9540 14299 8621 84 -150 -121 N
ATOM 3432 CA MET A 310 23.731 21.711 -44.266 1.00 85.98 C
ANISOU 3432 CA MET A 310 9550 14457 8660 280 -199 -160 C
ATOM 3433 C MET A 310 24.365 21.940 -42.893 1.00 92.57 C
ANISOU 3433 C MET A 310 10282 15413 9477 338 -244 -219 C
ATOM 3434 O MET A 310 24.401 21.014 -42.083 1.00 92.70 O
ANISOU 3434 O MET A 310 10321 15428 9471 512 -309 -216 O
ATOM 3435 CB MET A 310 24.731 21.054 -45.235 1.00 88.94 C
ANISOU 3435 CB MET A 310 9843 14961 8990 334 -168 -243 C
ATOM 3436 CG MET A 310 24.080 20.370 -46.424 1.00 91.41 C
ANISOU 3436 CG MET A 310 10279 15143 9311 348 -148 -178 C
ATOM 3437 SD MET A 310 22.679 19.314 -46.002 1.00 93.83 S
ANISOU 3437 SD MET A 310 10766 15234 9651 477 -212 -56 S
ATOM 3438 CE MET A 310 21.372 20.207 -46.807 1.00 89.36 C
ANISOU 3438 CE MET A 310 10325 14483 9146 302 -180 31 C
ATOM 3439 N ILE A 311 24.826 23.181 -42.622 1.00 90.30 N
ANISOU 3439 N ILE A 311 9905 15215 9191 191 -210 -270 N
ATOM 3440 CA ILE A 311 25.414 23.601 -41.347 1.00 90.77 C
ANISOU 3440 CA ILE A 311 9862 15390 9237 218 -250 -331 C
ATOM 3441 C ILE A 311 24.393 23.451 -40.196 1.00 95.25 C
ANISOU 3441 C ILE A 311 10549 15809 9831 287 -310 -235 C
ATOM 3442 O ILE A 311 24.815 23.182 -39.077 1.00 95.51 O
ANISOU 3442 O ILE A 311 10540 15911 9837 401 -370 -272 O
ATOM 3443 CB ILE A 311 26.048 25.023 -41.472 1.00 94.04 C
ANISOU 3443 CB ILE A 311 10172 15915 9644 12 -185 -405 C
ATOM 3444 CG1 ILE A 311 27.409 24.933 -42.189 1.00 95.82 C
ANISOU 3444 CG1 ILE A 311 10228 16355 9824 -15 -132 -551 C
ATOM 3445 CG2 ILE A 311 26.185 25.762 -40.125 1.00 94.35 C
ANISOU 3445 CG2 ILE A 311 10159 16003 9686 -7 -224 -426 C
ATOM 3446 CD1 ILE A 311 27.823 26.176 -42.976 1.00104.42 C
ANISOU 3446 CD1 ILE A 311 11283 17495 10896 -268 -23 -607 C
ATOM 3447 N SER A 312 23.063 23.532 -40.481 1.00 91.88 N
ANISOU 3447 N SER A 312 10273 15183 9453 230 -297 -124 N
ATOM 3448 CA SER A 312 22.001 23.362 -39.472 1.00 91.69 C
ANISOU 3448 CA SER A 312 10363 15015 9459 275 -335 -44 C
ATOM 3449 C SER A 312 22.096 22.026 -38.726 1.00 97.08 C
ANISOU 3449 C SER A 312 11100 15687 10100 475 -392 -40 C
ATOM 3450 O SER A 312 21.633 21.923 -37.585 1.00 96.18 O
ANISOU 3450 O SER A 312 11057 15504 9984 520 -423 -7 O
ATOM 3451 CB SER A 312 20.612 23.520 -40.087 1.00 94.53 C
ANISOU 3451 CB SER A 312 10854 15186 9878 195 -311 45 C
ATOM 3452 OG SER A 312 20.258 22.418 -40.905 1.00103.84 O
ANISOU 3452 OG SER A 312 12106 16293 11056 272 -308 75 O
ATOM 3453 N THR A 313 22.718 21.013 -39.368 1.00 95.53 N
ANISOU 3453 N THR A 313 10884 15553 9861 594 -403 -79 N
ATOM 3454 CA THR A 313 22.924 19.687 -38.785 1.00 96.71 C
ANISOU 3454 CA THR A 313 11107 15689 9949 799 -464 -85 C
ATOM 3455 C THR A 313 23.922 19.767 -37.624 1.00104.42 C
ANISOU 3455 C THR A 313 11998 16807 10871 903 -530 -168 C
ATOM 3456 O THR A 313 23.833 18.971 -36.692 1.00105.08 O
ANISOU 3456 O THR A 313 12192 16833 10902 1050 -590 -154 O
ATOM 3457 CB THR A 313 23.308 18.645 -39.860 1.00103.45 C
ANISOU 3457 CB THR A 313 11968 16569 10770 900 -463 -109 C
ATOM 3458 OG1 THR A 313 24.600 18.937 -40.385 1.00105.35 O
ANISOU 3458 OG1 THR A 313 12025 17016 10987 901 -457 -223 O
ATOM 3459 CG2 THR A 313 22.299 18.563 -40.998 1.00 98.49 C
ANISOU 3459 CG2 THR A 313 11432 15795 10193 801 -405 -29 C
ATOM 3460 N CYS A 314 24.834 20.765 -37.665 1.00102.88 N
ANISOU 3460 N CYS A 314 11618 16788 10682 818 -518 -259 N
ATOM 3461 CA CYS A 314 25.874 21.027 -36.666 1.00104.22 C
ANISOU 3461 CA CYS A 314 11665 17125 10808 895 -579 -364 C
ATOM 3462 C CYS A 314 25.451 21.978 -35.556 1.00109.32 C
ANISOU 3462 C CYS A 314 12333 17726 11478 805 -586 -328 C
ATOM 3463 O CYS A 314 26.021 21.892 -34.474 1.00109.62 O
ANISOU 3463 O CYS A 314 12344 17838 11468 917 -659 -384 O
ATOM 3464 CB CYS A 314 27.151 21.516 -37.340 1.00105.57 C
ANISOU 3464 CB CYS A 314 11614 17527 10972 841 -553 -503 C
ATOM 3465 SG CYS A 314 27.911 20.306 -38.444 1.00110.52 S
ANISOU 3465 SG CYS A 314 12186 18249 11556 989 -560 -582 S
ATOM 3466 N VAL A 315 24.496 22.901 -35.811 1.00106.72 N
ANISOU 3466 N VAL A 315 12052 17280 11215 614 -519 -246 N
ATOM 3467 CA VAL A 315 24.059 23.876 -34.795 1.00107.15 C
ANISOU 3467 CA VAL A 315 12128 17290 11294 521 -521 -214 C
ATOM 3468 C VAL A 315 23.327 23.200 -33.615 1.00112.68 C
ANISOU 3468 C VAL A 315 12989 17853 11970 640 -569 -148 C
ATOM 3469 O VAL A 315 23.363 23.739 -32.509 1.00112.23 O
ANISOU 3469 O VAL A 315 12933 17804 11905 628 -596 -154 O
ATOM 3470 CB VAL A 315 23.274 25.109 -35.328 1.00110.27 C
ANISOU 3470 CB VAL A 315 12542 17600 11757 303 -449 -157 C
ATOM 3471 CG1 VAL A 315 24.126 25.944 -36.280 1.00110.74 C
ANISOU 3471 CG1 VAL A 315 12465 17797 11815 164 -396 -234 C
ATOM 3472 CG2 VAL A 315 21.937 24.724 -35.962 1.00108.98 C
ANISOU 3472 CG2 VAL A 315 12527 17240 11641 277 -418 -54 C
ATOM 3473 N ASN A 316 22.692 22.027 -33.839 1.00110.39 N
ANISOU 3473 N ASN A 316 12844 17436 11662 745 -574 -92 N
ATOM 3474 CA ASN A 316 22.007 21.290 -32.773 1.00110.35 C
ANISOU 3474 CA ASN A 316 13021 17290 11618 844 -603 -37 C
ATOM 3475 C ASN A 316 23.009 20.794 -31.685 1.00115.22 C
ANISOU 3475 C ASN A 316 13639 18002 12137 1030 -699 -109 C
ATOM 3476 O ASN A 316 22.836 21.224 -30.547 1.00114.52 O
ANISOU 3476 O ASN A 316 13595 17884 12033 1021 -720 -100 O
ATOM 3477 CB ASN A 316 21.101 20.174 -33.326 1.00111.39 C
ANISOU 3477 CB ASN A 316 13317 17259 11749 885 -572 33 C
ATOM 3478 CG ASN A 316 19.872 19.886 -32.489 1.00132.14 C
ANISOU 3478 CG ASN A 316 16133 19698 14375 861 -544 106 C
ATOM 3479 OD1 ASN A 316 19.470 20.665 -31.615 1.00125.83 O
ANISOU 3479 OD1 ASN A 316 15335 18863 13613 763 -524 125 O
ATOM 3480 ND2 ASN A 316 19.221 18.767 -32.764 1.00123.12 N
ANISOU 3480 ND2 ASN A 316 15158 18429 13192 937 -532 144 N
ATOM 3481 N PRO A 317 24.110 20.037 -31.978 1.00113.21 N
ANISOU 3481 N PRO A 317 13323 17876 11817 1198 -764 -194 N
ATOM 3482 CA PRO A 317 25.032 19.652 -30.891 1.00114.82 C
ANISOU 3482 CA PRO A 317 13531 18172 11925 1389 -874 -277 C
ATOM 3483 C PRO A 317 25.966 20.754 -30.343 1.00120.60 C
ANISOU 3483 C PRO A 317 14056 19100 12668 1346 -910 -380 C
ATOM 3484 O PRO A 317 26.349 20.657 -29.177 1.00120.49 O
ANISOU 3484 O PRO A 317 14080 19115 12585 1472 -998 -425 O
ATOM 3485 CB PRO A 317 25.827 18.496 -31.497 1.00117.53 C
ANISOU 3485 CB PRO A 317 13873 18584 12199 1588 -935 -344 C
ATOM 3486 CG PRO A 317 25.833 18.768 -32.943 1.00121.06 C
ANISOU 3486 CG PRO A 317 14190 19087 12721 1461 -853 -345 C
ATOM 3487 CD PRO A 317 24.513 19.406 -33.254 1.00114.86 C
ANISOU 3487 CD PRO A 317 13475 18141 12026 1243 -750 -224 C
ATOM 3488 N ILE A 318 26.347 21.778 -31.155 1.00118.48 N
ANISOU 3488 N ILE A 318 13585 18958 12474 1168 -845 -423 N
ATOM 3489 CA ILE A 318 27.248 22.867 -30.712 1.00119.56 C
ANISOU 3489 CA ILE A 318 13523 19284 12619 1096 -863 -531 C
ATOM 3490 C ILE A 318 26.562 23.826 -29.721 1.00125.03 C
ANISOU 3490 C ILE A 318 14281 19886 13340 976 -846 -464 C
ATOM 3491 O ILE A 318 27.220 24.295 -28.794 1.00125.28 O
ANISOU 3491 O ILE A 318 14232 20029 13341 1008 -906 -542 O
ATOM 3492 CB ILE A 318 27.969 23.649 -31.859 1.00122.66 C
ANISOU 3492 CB ILE A 318 13695 19850 13060 936 -789 -618 C
ATOM 3493 CG1 ILE A 318 27.007 24.513 -32.706 1.00121.30 C
ANISOU 3493 CG1 ILE A 318 13569 19552 12968 693 -672 -512 C
ATOM 3494 CG2 ILE A 318 28.804 22.723 -32.738 1.00124.30 C
ANISOU 3494 CG2 ILE A 318 13812 20181 13234 1067 -810 -712 C
ATOM 3495 CD1 ILE A 318 27.477 25.923 -32.950 1.00126.87 C
ANISOU 3495 CD1 ILE A 318 14118 20381 13706 478 -606 -578 C
ATOM 3496 N PHE A 319 25.264 24.133 -29.932 1.00122.34 N
ANISOU 3496 N PHE A 319 14074 19352 13057 840 -768 -333 N
ATOM 3497 CA PHE A 319 24.477 25.000 -29.051 1.00122.26 C
ANISOU 3497 CA PHE A 319 14137 19240 13078 727 -746 -267 C
ATOM 3498 C PHE A 319 24.035 24.215 -27.821 1.00128.92 C
ANISOU 3498 C PHE A 319 15170 19957 13856 873 -802 -223 C
ATOM 3499 O PHE A 319 23.882 24.796 -26.751 1.00128.36 O
ANISOU 3499 O PHE A 319 15133 19861 13776 844 -819 -214 O
ATOM 3500 CB PHE A 319 23.257 25.581 -29.782 1.00122.53 C
ANISOU 3500 CB PHE A 319 14231 19128 13198 541 -650 -167 C
ATOM 3501 CG PHE A 319 23.527 26.826 -30.596 1.00123.97 C
ANISOU 3501 CG PHE A 319 14273 19399 13431 352 -593 -200 C
ATOM 3502 CD1 PHE A 319 23.984 26.736 -31.906 1.00127.50 C
ANISOU 3502 CD1 PHE A 319 14629 19928 13888 311 -557 -241 C
ATOM 3503 CD2 PHE A 319 23.291 28.087 -30.066 1.00125.89 C
ANISOU 3503 CD2 PHE A 319 14499 19630 13704 209 -572 -189 C
ATOM 3504 CE1 PHE A 319 24.220 27.887 -32.665 1.00128.48 C
ANISOU 3504 CE1 PHE A 319 14661 20115 14041 122 -495 -271 C
ATOM 3505 CE2 PHE A 319 23.528 29.239 -30.826 1.00128.77 C
ANISOU 3505 CE2 PHE A 319 14773 20056 14097 27 -517 -218 C
ATOM 3506 CZ PHE A 319 23.985 29.131 -32.121 1.00127.20 C
ANISOU 3506 CZ PHE A 319 14500 19931 13899 -20 -476 -259 C
ATOM 3507 N TYR A 320 23.850 22.890 -27.971 1.00127.99 N
ANISOU 3507 N TYR A 320 15192 19754 13685 1026 -828 -197 N
ATOM 3508 CA TYR A 320 23.448 21.994 -26.886 1.00129.26 C
ANISOU 3508 CA TYR A 320 15579 19775 13760 1168 -874 -158 C
ATOM 3509 C TYR A 320 24.660 21.378 -26.175 1.00136.33 C
ANISOU 3509 C TYR A 320 16467 20790 14543 1398 -1004 -260 C
ATOM 3510 O TYR A 320 24.489 20.552 -25.279 1.00136.35 O
ANISOU 3510 O TYR A 320 16681 20679 14446 1544 -1060 -240 O
ATOM 3511 CB TYR A 320 22.521 20.898 -27.426 1.00130.41 C
ANISOU 3511 CB TYR A 320 15912 19743 13896 1196 -824 -77 C
ATOM 3512 CG TYR A 320 21.369 20.559 -26.509 1.00132.33 C
ANISOU 3512 CG TYR A 320 16393 19775 14110 1168 -782 6 C
ATOM 3513 CD1 TYR A 320 20.166 21.253 -26.584 1.00133.01 C
ANISOU 3513 CD1 TYR A 320 16494 19754 14291 973 -682 74 C
ATOM 3514 CD2 TYR A 320 21.464 19.512 -25.596 1.00134.38 C
ANISOU 3514 CD2 TYR A 320 16877 19939 14242 1337 -839 7 C
ATOM 3515 CE1 TYR A 320 19.093 20.930 -25.758 1.00133.67 C
ANISOU 3515 CE1 TYR A 320 16781 19655 14351 933 -628 131 C
ATOM 3516 CE2 TYR A 320 20.400 19.183 -24.760 1.00135.27 C
ANISOU 3516 CE2 TYR A 320 17225 19853 14319 1289 -781 75 C
ATOM 3517 CZ TYR A 320 19.215 19.896 -24.844 1.00142.14 C
ANISOU 3517 CZ TYR A 320 18079 20635 15294 1080 -669 133 C
ATOM 3518 OH TYR A 320 18.163 19.583 -24.021 1.00144.28 O
ANISOU 3518 OH TYR A 320 18564 20724 15533 1018 -598 181 O
ATOM 3519 N GLY A 321 25.861 21.793 -26.576 1.00135.38 N
ANISOU 3519 N GLY A 321 16111 20895 14432 1426 -1052 -379 N
ATOM 3520 CA GLY A 321 27.119 21.322 -26.007 1.00137.68 C
ANISOU 3520 CA GLY A 321 16340 21344 14630 1647 -1187 -512 C
ATOM 3521 C GLY A 321 27.965 22.420 -25.398 1.00143.85 C
ANISOU 3521 C GLY A 321 16916 22313 15427 1595 -1229 -618 C
ATOM 3522 O GLY A 321 28.300 22.357 -24.215 1.00144.28 O
ANISOU 3522 O GLY A 321 17033 22381 15407 1722 -1327 -662 O
ATOM 3523 N PHE A 322 28.297 23.443 -26.199 1.00141.47 N
ANISOU 3523 N PHE A 322 16387 22150 15216 1399 -1151 -662 N
ATOM 3524 CA PHE A 322 29.139 24.561 -25.772 1.00142.74 C
ANISOU 3524 CA PHE A 322 16335 22503 15396 1310 -1170 -774 C
ATOM 3525 C PHE A 322 28.382 25.654 -24.989 1.00147.50 C
ANISOU 3525 C PHE A 322 16999 23002 16041 1129 -1117 -687 C
ATOM 3526 O PHE A 322 29.025 26.517 -24.391 1.00147.54 O
ANISOU 3526 O PHE A 322 16861 23146 16052 1060 -1138 -773 O
ATOM 3527 CB PHE A 322 29.913 25.142 -26.970 1.00144.96 C
ANISOU 3527 CB PHE A 322 16359 22985 15733 1179 -1105 -881 C
ATOM 3528 CG PHE A 322 30.638 24.099 -27.798 1.00147.60 C
ANISOU 3528 CG PHE A 322 16622 23427 16034 1344 -1145 -971 C
ATOM 3529 CD1 PHE A 322 31.517 23.197 -27.202 1.00152.48 C
ANISOU 3529 CD1 PHE A 322 17226 24148 16561 1621 -1290 -1091 C
ATOM 3530 CD2 PHE A 322 30.454 24.027 -29.172 1.00149.11 C
ANISOU 3530 CD2 PHE A 322 16766 23614 16276 1232 -1044 -945 C
ATOM 3531 CE1 PHE A 322 32.175 22.228 -27.966 1.00154.44 C
ANISOU 3531 CE1 PHE A 322 17411 24494 16774 1787 -1333 -1182 C
ATOM 3532 CE2 PHE A 322 31.122 23.064 -29.936 1.00152.94 C
ANISOU 3532 CE2 PHE A 322 17184 24197 16728 1386 -1079 -1031 C
ATOM 3533 CZ PHE A 322 31.976 22.170 -29.328 1.00152.76 C
ANISOU 3533 CZ PHE A 322 17143 24279 16619 1663 -1222 -1150 C
ATOM 3534 N LEU A 323 27.034 25.589 -24.953 1.00144.61 N
ANISOU 3534 N LEU A 323 16844 22401 15702 1061 -1051 -531 N
ATOM 3535 CA LEU A 323 26.177 26.526 -24.209 1.00144.45 C
ANISOU 3535 CA LEU A 323 16902 22262 15720 908 -1001 -446 C
ATOM 3536 C LEU A 323 25.434 25.836 -23.047 1.00149.99 C
ANISOU 3536 C LEU A 323 17856 22775 16357 1023 -1037 -366 C
ATOM 3537 O LEU A 323 25.048 26.506 -22.085 1.00149.24 O
ANISOU 3537 O LEU A 323 17824 22614 16268 950 -1026 -328 O
ATOM 3538 CB LEU A 323 25.185 27.256 -25.138 1.00143.13 C
ANISOU 3538 CB LEU A 323 16735 21995 15652 684 -875 -353 C
ATOM 3539 CG LEU A 323 25.687 28.531 -25.827 1.00148.01 C
ANISOU 3539 CG LEU A 323 17160 22751 16326 489 -820 -410 C
ATOM 3540 CD1 LEU A 323 26.391 28.217 -27.153 1.00148.76 C
ANISOU 3540 CD1 LEU A 323 17119 22972 16432 482 -794 -479 C
ATOM 3541 CD2 LEU A 323 24.538 29.494 -26.077 1.00148.82 C
ANISOU 3541 CD2 LEU A 323 17335 22709 16502 289 -731 -309 C
ATOM 3542 N ASN A 324 25.241 24.504 -23.139 1.00148.20 N
ANISOU 3542 N ASN A 324 17786 22459 16063 1198 -1074 -343 N
ATOM 3543 CA ASN A 324 24.592 23.692 -22.110 1.00148.81 C
ANISOU 3543 CA ASN A 324 18139 22348 16055 1310 -1100 -277 C
ATOM 3544 C ASN A 324 25.677 23.149 -21.167 1.00157.43 C
ANISOU 3544 C ASN A 324 19269 23526 17021 1550 -1251 -376 C
ATOM 3545 O ASN A 324 26.583 22.441 -21.619 1.00158.35 O
ANISOU 3545 O ASN A 324 19321 23756 17087 1720 -1334 -464 O
ATOM 3546 CB ASN A 324 23.788 22.555 -22.756 1.00146.52 C
ANISOU 3546 CB ASN A 324 18024 21893 15754 1344 -1044 -196 C
ATOM 3547 CG ASN A 324 22.881 21.791 -21.820 1.00159.22 C
ANISOU 3547 CG ASN A 324 19940 23278 17280 1398 -1028 -118 C
ATOM 3548 OD1 ASN A 324 23.035 20.581 -21.624 1.00151.34 O
ANISOU 3548 OD1 ASN A 324 19128 22204 16171 1578 -1084 -123 O
ATOM 3549 ND2 ASN A 324 21.879 22.463 -21.266 1.00148.35 N
ANISOU 3549 ND2 ASN A 324 18635 21782 15951 1238 -943 -49 N
ATOM 3550 N LYS A 325 25.605 23.524 -19.867 1.00156.18 N
ANISOU 3550 N LYS A 325 19212 23320 16810 1570 -1294 -373 N
ATOM 3551 CA LYS A 325 26.569 23.143 -18.824 1.00158.46 C
ANISOU 3551 CA LYS A 325 19558 23676 16973 1796 -1450 -469 C
ATOM 3552 C LYS A 325 26.641 21.635 -18.541 1.00165.40 C
ANISOU 3552 C LYS A 325 20700 24434 17710 2046 -1535 -467 C
ATOM 3553 O LYS A 325 27.740 21.112 -18.342 1.00166.69 O
ANISOU 3553 O LYS A 325 20826 24724 17784 2277 -1683 -587 O
ATOM 3554 CB LYS A 325 26.308 23.922 -17.527 1.00160.84 C
ANISOU 3554 CB LYS A 325 19942 23917 17251 1736 -1458 -446 C
ATOM 3555 N ASN A 326 25.479 20.949 -18.514 1.00162.63 N
ANISOU 3555 N ASN A 326 20618 23841 17333 2000 -1443 -342 N
ATOM 3556 CA ASN A 326 25.361 19.507 -18.249 1.00164.17 C
ANISOU 3556 CA ASN A 326 21123 23874 17382 2200 -1496 -319 C
ATOM 3557 C ASN A 326 26.079 18.636 -19.288 1.00169.52 C
ANISOU 3557 C ASN A 326 21723 24650 18038 2361 -1561 -385 C
ATOM 3558 O ASN A 326 26.721 17.652 -18.918 1.00170.62 O
ANISOU 3558 O ASN A 326 22026 24770 18032 2621 -1694 -445 O
ATOM 3559 CB ASN A 326 23.875 19.101 -18.119 1.00165.48 C
ANISOU 3559 CB ASN A 326 21556 23771 17546 2050 -1346 -179 C
ATOM 3560 CG ASN A 326 23.595 17.609 -18.139 1.00192.49 C
ANISOU 3560 CG ASN A 326 25297 27008 20832 2196 -1357 -142 C
ATOM 3561 OD1 ASN A 326 24.145 16.829 -17.349 1.00187.66 O
ANISOU 3561 OD1 ASN A 326 24917 26334 20050 2424 -1481 -183 O
ATOM 3562 ND2 ASN A 326 22.721 17.183 -19.044 1.00184.63 N
ANISOU 3562 ND2 ASN A 326 24338 25912 19901 2068 -1231 -68 N
ATOM 3563 N PHE A 327 25.964 19.006 -20.574 1.00165.60 N
ANISOU 3563 N PHE A 327 20991 24252 17677 2213 -1470 -376 N
ATOM 3564 CA PHE A 327 26.512 18.276 -21.714 1.00166.10 C
ANISOU 3564 CA PHE A 327 20961 24406 17742 2320 -1499 -428 C
ATOM 3565 C PHE A 327 28.026 18.440 -21.934 1.00170.94 C
ANISOU 3565 C PHE A 327 21307 25299 18345 2480 -1633 -601 C
ATOM 3566 O PHE A 327 28.677 17.451 -22.278 1.00171.59 O
ANISOU 3566 O PHE A 327 21423 25427 18348 2698 -1727 -674 O
ATOM 3567 CB PHE A 327 25.736 18.654 -22.983 1.00166.42 C
ANISOU 3567 CB PHE A 327 20876 24427 17928 2084 -1343 -348 C
ATOM 3568 CG PHE A 327 25.838 17.679 -24.130 1.00168.50 C
ANISOU 3568 CG PHE A 327 21155 24683 18183 2164 -1334 -349 C
ATOM 3569 CD1 PHE A 327 24.938 16.628 -24.253 1.00171.75 C
ANISOU 3569 CD1 PHE A 327 21850 24870 18536 2189 -1284 -252 C
ATOM 3570 CD2 PHE A 327 26.804 17.839 -25.116 1.00171.33 C
ANISOU 3570 CD2 PHE A 327 21244 25260 18595 2193 -1361 -449 C
ATOM 3571 CE1 PHE A 327 25.021 15.740 -25.330 1.00172.94 C
ANISOU 3571 CE1 PHE A 327 22019 25011 18680 2258 -1274 -251 C
ATOM 3572 CE2 PHE A 327 26.893 16.945 -26.186 1.00174.43 C
ANISOU 3572 CE2 PHE A 327 21652 25645 18979 2266 -1350 -450 C
ATOM 3573 CZ PHE A 327 26.003 15.901 -26.285 1.00172.34 C
ANISOU 3573 CZ PHE A 327 21675 25153 18655 2304 -1312 -347 C
ATOM 3574 N GLN A 328 28.581 19.667 -21.773 1.00167.31 N
ANISOU 3574 N GLN A 328 20580 25027 17962 2370 -1638 -678 N
ATOM 3575 CA GLN A 328 30.012 19.934 -22.000 1.00168.60 C
ANISOU 3575 CA GLN A 328 20453 25481 18128 2483 -1745 -867 C
ATOM 3576 C GLN A 328 30.938 19.099 -21.107 1.00175.35 C
ANISOU 3576 C GLN A 328 21409 26388 18829 2817 -1948 -992 C
ATOM 3577 O GLN A 328 31.935 18.569 -21.603 1.00176.35 O
ANISOU 3577 O GLN A 328 21392 26691 18922 3001 -2047 -1137 O
ATOM 3578 CB GLN A 328 30.366 21.434 -21.924 1.00169.41 C
ANISOU 3578 CB GLN A 328 20274 25759 18336 2270 -1696 -925 C
ATOM 3579 CG GLN A 328 29.904 22.183 -20.672 1.00183.69 C
ANISOU 3579 CG GLN A 328 22189 27473 20133 2188 -1695 -866 C
ATOM 3580 CD GLN A 328 30.213 23.667 -20.705 1.00201.94 C
ANISOU 3580 CD GLN A 328 24236 29947 22545 1965 -1638 -918 C
ATOM 3581 OE1 GLN A 328 30.843 24.195 -21.633 1.00197.48 O
ANISOU 3581 OE1 GLN A 328 23402 29577 22055 1860 -1595 -1010 O
ATOM 3582 NE2 GLN A 328 29.773 24.379 -19.677 1.00193.00 N
ANISOU 3582 NE2 GLN A 328 23191 28732 21410 1880 -1629 -864 N
ATOM 3583 N ARG A 329 30.597 18.952 -19.817 1.00172.85 N
ANISOU 3583 N ARG A 329 21350 25914 18410 2903 -2012 -943 N
ATOM 3584 CA ARG A 329 31.381 18.147 -18.883 1.00175.13 C
ANISOU 3584 CA ARG A 329 21793 26215 18532 3233 -2216 -1052 C
ATOM 3585 C ARG A 329 31.143 16.656 -19.131 1.00180.17 C
ANISOU 3585 C ARG A 329 22736 26677 19045 3444 -2265 -1008 C
ATOM 3586 O ARG A 329 32.063 15.857 -18.955 1.00181.79 O
ANISOU 3586 O ARG A 329 22984 26960 19129 3750 -2443 -1140 O
ATOM 3587 CB ARG A 329 31.048 18.515 -17.432 1.00175.81 C
ANISOU 3587 CB ARG A 329 22080 26175 18543 3239 -2261 -1009 C
ATOM 3588 N ASP A 330 29.914 16.293 -19.558 1.00175.52 N
ANISOU 3588 N ASP A 330 22354 25854 18482 3283 -2109 -832 N
ATOM 3589 CA ASP A 330 29.513 14.913 -19.837 1.00175.98 C
ANISOU 3589 CA ASP A 330 22727 25714 18424 3433 -2122 -769 C
ATOM 3590 C ASP A 330 30.132 14.345 -21.113 1.00180.93 C
ANISOU 3590 C ASP A 330 23179 26481 19084 3527 -2143 -846 C
ATOM 3591 O ASP A 330 30.442 13.153 -21.139 1.00181.86 O
ANISOU 3591 O ASP A 330 23508 26527 19065 3782 -2250 -880 O
ATOM 3592 CB ASP A 330 27.983 14.771 -19.858 1.00176.03 C
ANISOU 3592 CB ASP A 330 22999 25436 18450 3209 -1941 -575 C
ATOM 3593 CG ASP A 330 27.461 13.363 -19.621 1.00185.74 C
ANISOU 3593 CG ASP A 330 24652 26407 19514 3358 -1958 -505 C
ATOM 3594 OD1 ASP A 330 28.169 12.565 -18.965 1.00188.05 O
ANISOU 3594 OD1 ASP A 330 25156 26666 19628 3651 -2130 -582 O
ATOM 3595 OD2 ASP A 330 26.321 13.077 -20.041 1.00189.99 O
ANISOU 3595 OD2 ASP A 330 25328 26767 20092 3179 -1800 -379 O
ATOM 3596 N LEU A 331 30.308 15.178 -22.167 1.00177.02 N
ANISOU 3596 N LEU A 331 22323 26176 18760 3326 -2040 -873 N
ATOM 3597 CA LEU A 331 30.918 14.731 -23.427 1.00177.58 C
ANISOU 3597 CA LEU A 331 22205 26396 18871 3391 -2044 -953 C
ATOM 3598 C LEU A 331 32.438 14.524 -23.275 1.00184.80 C
ANISOU 3598 C LEU A 331 22925 27571 19720 3672 -2235 -1179 C
ATOM 3599 O LEU A 331 33.018 13.696 -23.980 1.00185.45 O
ANISOU 3599 O LEU A 331 22980 27725 19759 3856 -2301 -1262 O
ATOM 3600 CB LEU A 331 30.549 15.640 -24.630 1.00175.75 C
ANISOU 3600 CB LEU A 331 21693 26257 18826 3079 -1865 -906 C
ATOM 3601 CG LEU A 331 31.278 16.982 -24.809 1.00180.30 C
ANISOU 3601 CG LEU A 331 21892 27093 19519 2920 -1839 -1015 C
ATOM 3602 CD1 LEU A 331 32.419 16.857 -25.810 1.00181.75 C
ANISOU 3602 CD1 LEU A 331 21772 27554 19729 3013 -1889 -1198 C
ATOM 3603 CD2 LEU A 331 30.337 18.039 -25.328 1.00180.26 C
ANISOU 3603 CD2 LEU A 331 21801 27028 19661 2575 -1650 -888 C
ATOM 3604 N GLN A 332 33.066 15.275 -22.343 1.00182.87 N
ANISOU 3604 N GLN A 332 22541 27471 19469 3708 -2327 -1288 N
ATOM 3605 CA GLN A 332 34.493 15.198 -22.029 1.00185.26 C
ANISOU 3605 CA GLN A 332 22639 28038 19712 3970 -2520 -1527 C
ATOM 3606 C GLN A 332 34.773 13.968 -21.158 1.00192.35 C
ANISOU 3606 C GLN A 332 23878 28803 20402 4346 -2724 -1568 C
ATOM 3607 O GLN A 332 35.805 13.322 -21.340 1.00193.94 O
ANISOU 3607 O GLN A 332 23990 29169 20530 4633 -2888 -1751 O
ATOM 3608 CB GLN A 332 34.953 16.482 -21.326 1.00186.55 C
ANISOU 3608 CB GLN A 332 22556 28382 19942 3849 -2535 -1618 C
ATOM 3609 CG GLN A 332 36.462 16.704 -21.370 1.00199.11 C
ANISOU 3609 CG GLN A 332 23786 30327 21538 4012 -2675 -1895 C
ATOM 3610 CD GLN A 332 36.868 18.128 -21.067 1.00213.63 C
ANISOU 3610 CD GLN A 332 25319 32369 23481 3800 -2631 -1982 C
ATOM 3611 OE1 GLN A 332 36.143 18.900 -20.427 1.00206.69 O
ANISOU 3611 OE1 GLN A 332 24541 31358 22635 3607 -2553 -1850 O
ATOM 3612 NE2 GLN A 332 38.056 18.503 -21.512 1.00206.19 N
ANISOU 3612 NE2 GLN A 332 23996 31759 22589 3830 -2678 -2219 N
ATOM 3613 N PHE A 333 33.841 13.638 -20.231 1.00189.45 N
ANISOU 3613 N PHE A 333 23914 28133 19934 4343 -2711 -1404 N
ATOM 3614 CA PHE A 333 33.917 12.480 -19.330 1.00191.54 C
ANISOU 3614 CA PHE A 333 24593 28205 19977 4667 -2882 -1410 C
ATOM 3615 C PHE A 333 33.478 11.168 -20.024 1.00196.64 C
ANISOU 3615 C PHE A 333 25522 28655 20536 4772 -2858 -1324 C
ATOM 3616 O PHE A 333 33.367 10.128 -19.369 1.00197.50 O
ANISOU 3616 O PHE A 333 26044 28547 20449 5005 -2969 -1296 O
ATOM 3617 CB PHE A 333 33.103 12.738 -18.049 1.00192.85 C
ANISOU 3617 CB PHE A 333 25074 28132 20067 4587 -2858 -1280 C
ATOM 3618 N PHE A 334 33.240 11.233 -21.352 1.00192.73 N
ANISOU 3618 N PHE A 334 24818 28231 20179 4595 -2713 -1286 N
ATOM 3619 CA PHE A 334 32.853 10.115 -22.214 1.00192.80 C
ANISOU 3619 CA PHE A 334 25022 28095 20140 4655 -2669 -1214 C
ATOM 3620 C PHE A 334 33.922 9.888 -23.291 1.00198.76 C
ANISOU 3620 C PHE A 334 25450 29125 20945 4796 -2737 -1387 C
ATOM 3621 O PHE A 334 34.257 8.739 -23.575 1.00199.77 O
ANISOU 3621 O PHE A 334 25750 29204 20951 5056 -2842 -1436 O
ATOM 3622 CB PHE A 334 31.480 10.369 -22.856 1.00191.95 C
ANISOU 3622 CB PHE A 334 24977 27803 20152 4299 -2422 -1003 C
ATOM 3623 N PHE A 335 34.464 10.985 -23.874 1.00195.41 N
ANISOU 3623 N PHE A 335 24566 28987 20692 4622 -2674 -1488 N
ATOM 3624 CA PHE A 335 35.512 10.950 -24.899 1.00196.53 C
ANISOU 3624 CA PHE A 335 24349 29425 20899 4706 -2711 -1674 C
ATOM 3625 C PHE A 335 36.855 10.510 -24.305 1.00204.24 C
ANISOU 3625 C PHE A 335 25247 30602 21754 5092 -2966 -1924 C
ATOM 3626 O PHE A 335 37.528 9.660 -24.893 1.00205.12 O
ANISOU 3626 O PHE A 335 25327 30805 21803 5336 -3068 -2048 O
ATOM 3627 CB PHE A 335 35.645 12.312 -25.596 1.00196.93 C
ANISOU 3627 CB PHE A 335 23974 29698 21152 4374 -2551 -1706 C
ATOM 3628 N ASN A 336 37.234 11.080 -23.136 1.00202.47 N
ANISOU 3628 N ASN A 336 24993 30445 21492 5156 -3077 -2003 N
ATOM 3629 CA ASN A 336 38.468 10.749 -22.410 1.00205.59 C
ANISOU 3629 CA ASN A 336 25321 31027 21768 5530 -3339 -2250 C
ATOM 3630 C ASN A 336 38.356 9.401 -21.684 1.00211.67 C
ANISOU 3630 C ASN A 336 26578 31544 22302 5895 -3526 -2220 C
ATOM 3631 O ASN A 336 39.380 8.770 -21.407 1.00213.41 O
ANISOU 3631 O ASN A 336 26786 31834 22466 6164 -3720 -2380 O
ATOM 3632 CB ASN A 336 38.852 11.864 -21.428 1.00206.76 C
ANISOU 3632 CB ASN A 336 25283 31321 21957 5457 -3388 -2338 C
ATOM 3633 CG ASN A 336 39.850 12.857 -21.976 1.00226.36 C
ANISOU 3633 CG ASN A 336 27378 33605 25024 4645 -3123 -2166 C
ATOM 3634 OD1 ASN A 336 39.609 13.537 -22.981 1.00223.32 O
ANISOU 3634 OD1 ASN A 336 26634 33758 24459 4875 -3098 -2416 O
ATOM 3635 ND2 ASN A 336 40.984 12.988 -21.303 1.00219.95 N
ANISOU 3635 ND2 ASN A 336 26348 33133 24090 4968 -3343 -2460 N
ATOM 3636 N PHE A 337 37.111 8.968 -21.376 1.00206.83 N
ANISOU 3636 N PHE A 337 26404 30565 21618 5783 -3425 -1969 N
ATOM 3637 CA PHE A 337 36.819 7.692 -20.718 1.00208.03 C
ANISOU 3637 CA PHE A 337 27087 30421 21533 6072 -3562 -1907 C
ATOM 3638 C PHE A 337 37.041 6.516 -21.680 1.00212.75 C
ANISOU 3638 C PHE A 337 27790 30984 22061 6265 -3600 -1934 C
ATOM 3639 O PHE A 337 37.452 5.441 -21.235 1.00213.47 O
ANISOU 3639 O PHE A 337 28171 30851 22086 6383 -3715 -1904 O
ATOM 3640 CB PHE A 337 35.386 7.674 -20.171 1.00208.01 C
ANISOU 3640 CB PHE A 337 27490 30054 21489 5839 -3405 -1642 C
ATOM 3641 N CYS A 338 36.787 6.733 -22.998 1.00207.03 N
ANISOU 3641 N CYS A 338 26801 30356 21506 6028 -3416 -1888 N
ATOM 3642 CA CYS A 338 36.959 5.748 -24.077 1.00206.82 C
ANISOU 3642 CA CYS A 338 26817 30319 21445 6161 -3421 -1909 C
ATOM 3643 C CYS A 338 38.418 5.306 -24.267 1.00212.21 C
ANISOU 3643 C CYS A 338 27266 31259 22105 6477 -3628 -2172 C
ATOM 3644 O CYS A 338 38.663 4.235 -24.827 1.00211.57 O
ANISOU 3644 O CYS A 338 27312 31012 22062 6473 -3626 -2115 O
ATOM 3645 CB CYS A 338 36.356 6.262 -25.381 1.00204.44 C
ANISOU 3645 CB CYS A 338 26277 30055 21347 5791 -3164 -1789 C
ATOM 3646 SG CYS A 338 34.555 6.098 -25.481 1.00205.68 S
ANISOU 3646 SG CYS A 338 26843 29799 21506 5482 -2934 -1463 S
ATOM 3647 N ASP A 339 39.375 6.133 -23.800 1.00209.56 N
ANISOU 3647 N ASP A 339 26572 31251 21799 6589 -3751 -2401 N
ATOM 3648 CA ASP A 339 40.815 5.888 -23.863 1.00221.92 C
ANISOU 3648 CA ASP A 339 27889 32133 24298 5268 -3380 -1911 C
ATOM 3649 C ASP A 339 41.283 5.119 -22.622 1.00232.48 C
ANISOU 3649 C ASP A 339 29459 32797 26076 4492 -3210 -1454 C
ATOM 3650 O ASP A 339 40.943 5.481 -21.495 1.00201.40 O
ANISOU 3650 O ASP A 339 25754 29992 20776 6747 -4090 -2475 O
ATOM 3651 CB ASP A 339 41.571 7.223 -24.000 1.00223.13 C
ANISOU 3651 CB ASP A 339 27595 32521 24663 5058 -3319 -2019 C
ATOM 3652 CG ASP A 339 43.078 7.094 -24.080 1.00229.45 C
ANISOU 3652 CG ASP A 339 28193 33073 25916 4561 -3208 -1871 C
ATOM 3653 OD1 ASP A 339 43.574 6.545 -25.088 1.00229.61 O
ANISOU 3653 OD1 ASP A 339 28109 33104 26029 4545 -3164 -1894 O
ATOM 3654 OD2 ASP A 339 43.763 7.571 -23.152 1.00233.59 O
ANISOU 3654 OD2 ASP A 339 28667 33422 26665 4240 -3174 -1745 O
TER 3655 ASP A 339
HETATM 3656 C1 9AF A1201 10.259 23.314 -46.898 1.00 76.68 C
HETATM 3657 C10 9AF A1201 11.775 23.295 -48.961 1.00 75.79 C
HETATM 3658 C11 9AF A1201 11.335 24.217 -50.115 1.00 76.31 C
HETATM 3659 C12 9AF A1201 10.881 25.538 -49.883 1.00 75.92 C
HETATM 3660 C13 9AF A1201 10.652 26.401 -50.954 1.00 76.97 C
HETATM 3661 C2 9AF A1201 11.403 23.942 -47.643 1.00 76.26 C
HETATM 3662 C3 9AF A1201 12.240 24.897 -47.081 1.00 75.92 C
HETATM 3663 C4 9AF A1201 11.962 25.730 -45.887 1.00 76.12 C
HETATM 3664 C5 9AF A1201 14.085 24.200 -48.585 1.00 74.56 C
HETATM 3665 C6 9AF A1201 15.547 24.402 -48.783 1.00 74.78 C
HETATM 3666 C7 9AF A1201 13.277 23.218 -49.129 1.00 73.93 C
HETATM 3667 C8 9AF A1201 13.804 21.957 -49.718 1.00 71.76 C
HETATM 3668 C9 9AF A1201 13.070 19.846 -50.736 1.00 69.67 C
HETATM 3669 N1 9AF A1201 11.306 24.298 -53.903 1.00 78.38 N
HETATM 3670 N2 9AF A1201 11.550 23.179 -55.934 1.00 79.94 N
HETATM 3671 O1 9AF A1201 9.698 22.272 -47.246 1.00 75.63 O
HETATM 3672 O2 9AF A1201 14.981 21.623 -49.814 1.00 71.93 O
HETATM 3673 O3 9AF A1201 12.789 21.098 -50.141 1.00 70.26 O
HETATM 3674 O4 9AF A1201 12.275 22.150 -53.989 1.00 79.98 O
HETATM 3675 C16 9AF A1201 11.727 23.114 -54.547 1.00 79.38 C
HETATM 3676 C15 9AF A1201 11.267 24.639 -52.533 1.00 77.75 C
HETATM 3677 C14 9AF A1201 10.849 25.967 -52.271 1.00 77.48 C
HETATM 3678 C32 9AF A1201 11.508 23.762 -51.452 1.00 77.24 C
HETATM 3679 N 9AF A1201 13.583 24.967 -47.511 1.00 75.32 N
HETATM 3680 O 9AF A1201 9.775 23.867 -45.717 1.00 78.12 O
HETATM 3681 C 9AF A1201 8.730 23.286 -44.967 1.00 78.69 C
HETATM 3682 C17 9AF A1201 11.923 22.106 -56.859 1.00 81.97 C
HETATM 3683 C18 9AF A1201 13.178 22.544 -57.646 1.00 84.51 C
HETATM 3684 C19 9AF A1201 14.442 22.502 -56.768 1.00 86.83 C
HETATM 3685 N3 9AF A1201 15.583 23.047 -57.555 1.00 89.58 N
HETATM 3686 C31 9AF A1201 16.634 21.982 -57.796 1.00 90.81 C
HETATM 3687 C30 9AF A1201 17.754 22.563 -58.705 1.00 90.39 C
HETATM 3688 C22 9AF A1201 18.386 23.791 -58.010 1.00 89.82 C
HETATM 3689 C21 9AF A1201 17.307 24.885 -57.734 1.00 89.69 C
HETATM 3690 C20 9AF A1201 16.150 24.284 -56.886 1.00 90.00 C
HETATM 3691 C23 9AF A1201 19.573 24.297 -58.791 1.00 89.80 C
HETATM 3692 C29 9AF A1201 19.456 25.403 -59.663 1.00 89.57 C
HETATM 3693 C27 9AF A1201 20.609 25.892 -60.324 1.00 88.99 C
HETATM 3694 O5 9AF A1201 20.597 27.054 -61.093 1.00 88.43 O
HETATM 3695 C28 9AF A1201 19.431 27.326 -61.860 1.00 88.53 C
HETATM 3696 C26 9AF A1201 21.869 25.262 -60.157 1.00 89.10 C
HETATM 3697 C25 9AF A1201 21.975 24.147 -59.300 1.00 88.77 C
HETATM 3698 C24 9AF A1201 20.842 23.671 -58.617 1.00 89.34 C
CONECT 16 3325
CONECT 629 1304
CONECT 1304 629
CONECT 3325 16
CONECT 3656 3661 3671 3680
CONECT 3657 3658 3661 3666
CONECT 3658 3657 3659 3678
CONECT 3659 3658 3660
CONECT 3660 3659 3677
CONECT 3661 3656 3657 3662
CONECT 3662 3661 3663 3679
CONECT 3663 3662
CONECT 3664 3665 3666 3679
CONECT 3665 3664
CONECT 3666 3657 3664 3667
CONECT 3667 3666 3672 3673
CONECT 3668 3673
CONECT 3669 3675 3676
CONECT 3670 3675 3682
CONECT 3671 3656
CONECT 3672 3667
CONECT 3673 3667 3668
CONECT 3674 3675
CONECT 3675 3669 3670 3674
CONECT 3676 3669 3677 3678
CONECT 3677 3660 3676
CONECT 3678 3658 3676
CONECT 3679 3662 3664
CONECT 3680 3656 3681
CONECT 3681 3680
CONECT 3682 3670 3683
CONECT 3683 3682 3684
CONECT 3684 3683 3685
CONECT 3685 3684 3686 3690
CONECT 3686 3685 3687
CONECT 3687 3686 3688
CONECT 3688 3687 3689 3691
CONECT 3689 3688 3690
CONECT 3690 3685 3689
CONECT 3691 3688 3692 3698
CONECT 3692 3691 3693
CONECT 3693 3692 3694 3696
CONECT 3694 3693 3695
CONECT 3695 3694
CONECT 3696 3693 3697
CONECT 3697 3696 3698
CONECT 3698 3691 3697
MASTER 372 0 1 21 5 0 5 6 3697 1 47 41
END