HEADER TRANSPORT PROTEIN/INHIBITOR 30-MAR-15 4Z35
TITLE CRYSTAL STRUCTURE OF HUMAN LYSOPHOSPHATIDIC ACID RECEPTOR 1 IN COMPLEX
TITLE 2 WITH ONO-9910539
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOPHOSPHATIDIC ACID RECEPTOR 1,SOLUBLE CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LPA-1,LYSOPHOSPHATIDIC ACID RECEPTOR EDG-2,CYTOCHROME B-562,
COMPND 5 CYTOCHROME B-562,LPA-1,LYSOPHOSPHATIDIC ACID RECEPTOR EDG-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: LPAR1, EDG2, LPA1, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1711;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS HUMAN LYSOPHOSPHATIDIC ACID RECEPTOR 1 (LPA1), G-PROTEIN COUPLED
KEYWDS 2 RECEPTOR (GPCR), MEMBRANE PROTEIN, ANTAGONIST, ENDOGENOUS LIGAND,
KEYWDS 3 PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR NETWORK, LIPIDIC CUBIC PHASE
KEYWDS 4 (LCP), COMPOUND DESIGN, POLYPHARMACOLOGY, LIPID RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.CHRENCIK,C.B.ROTH,M.TERAKADO,H.KURATA,R.OMI,Y.KIHARA,
AUTHOR 2 D.WARSHAVIAK,S.NAKADE,G.ASMAR-ROVIRA,M.MILENI,H.MIZUNO,M.T.GRIFFITH,
AUTHOR 3 C.RODGERS,G.W.HAN,J.VELASQUEZ,J.CHUN,R.C.STEVENS,M.A.HANSON,GPCR
AUTHOR 4 NETWORK (GPCR)
REVDAT 2 01-JUL-15 4Z35 1 JRNL
REVDAT 1 03-JUN-15 4Z35 0
JRNL AUTH J.E.CHRENCIK,C.B.ROTH,M.TERAKADO,H.KURATA,R.OMI,Y.KIHARA,
JRNL AUTH 2 D.WARSHAVIAK,S.NAKADE,G.ASMAR-ROVIRA,M.MILENI,H.MIZUNO,
JRNL AUTH 3 M.T.GRIFFITH,C.RODGERS,G.W.HAN,J.VELASQUEZ,J.CHUN,
JRNL AUTH 4 R.C.STEVENS,M.A.HANSON
JRNL TITL CRYSTAL STRUCTURE OF ANTAGONIST BOUND HUMAN LYSOPHOSPHATIDIC
JRNL TITL 2 ACID RECEPTOR 1.
JRNL REF CELL V. 161 1633 2015
JRNL REFN ISSN 1097-4172
JRNL PMID 26091040
JRNL DOI 10.1016/J.CELL.2015.06.002
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.9
REMARK 3 NUMBER OF REFLECTIONS : 11627
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) : 0.266
REMARK 3 R VALUE (WORKING SET) : 0.265
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 584
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2334
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2687
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2228
REMARK 3 BIN R VALUE (WORKING SET) : 0.2685
REMARK 3 BIN FREE R VALUE : 0.2732
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.54
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 106
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2977
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 3
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 99.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.32290
REMARK 3 B22 (A**2) : -4.03480
REMARK 3 B33 (A**2) : -0.28810
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) : 0.708
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.438
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.890
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.863
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3103 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4220 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1416 ; 4.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 62 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 475 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3103 ; 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 : 417 ; 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 : 3553 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.92
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.63
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.64
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): -0.3927 -18.8700 31.1438
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: 0.3040
REMARK 3 T33: 0.1997 T12: -0.0999
REMARK 3 T13: -0.0203 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.7326 L22: 1.5606
REMARK 3 L33: 1.0154 L12: -0.6175
REMARK 3 L13: 0.3548 L23: -1.2685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: 0.0053 S13: -0.1374
REMARK 3 S21: -0.0997 S22: 0.0812 S23: 0.0111
REMARK 3 S31: -0.0519 S32: -0.1653 S33: -0.0322
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Z35 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-12; 20-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 23-ID-D; 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033; 1.033
REMARK 200 MONOCHROMATOR : MIRRORS; MIRRORS
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC
REMARK 200 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11627
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.0
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB IDS 3V2Y AND 4EIY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE (PH 5.5), 34 -
REMARK 280 38% (V/V) PEG400 AND 200 MM AMMONIUM ACETATE, LIPIDIC CUBIC
REMARK 280 PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.30500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.83500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.83500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.30500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: AUTHORS HAVE INDICATED 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A -17
REMARK 465 LYS A -16
REMARK 465 THR A -15
REMARK 465 ILE A -14
REMARK 465 ILE A -13
REMARK 465 ALA A -12
REMARK 465 LEU A -11
REMARK 465 SER A -10
REMARK 465 TYR A -9
REMARK 465 ILE A -8
REMARK 465 PHE A -7
REMARK 465 CYS A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PHE A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 PRO A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ILE A 4
REMARK 465 SER A 5
REMARK 465 THR A 6
REMARK 465 SER A 7
REMARK 465 ILE A 8
REMARK 465 PRO A 9
REMARK 465 VAL A 10
REMARK 465 ILE A 11
REMARK 465 SER A 12
REMARK 465 GLN A 13
REMARK 465 PRO A 14
REMARK 465 GLN A 15
REMARK 465 PHE A 16
REMARK 465 THR A 17
REMARK 465 ALA A 18
REMARK 465 MET A 19
REMARK 465 ASN A 20
REMARK 465 GLU A 21
REMARK 465 PRO A 22
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 ARG A 328
REMARK 465 PRO A 329
REMARK 465 LEU A 330
REMARK 465 GLU A 331
REMARK 465 VAL A 332
REMARK 465 LEU A 333
REMARK 465 PHE A 334
REMARK 465 GLN A 335
REMARK 465 GLY A 336
REMARK 465 PRO A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 ASP A 348
REMARK 465 TYR A 349
REMARK 465 LYS A 350
REMARK 465 ASP A 351
REMARK 465 ASP A 352
REMARK 465 ASP A 353
REMARK 465 ASP A 354
REMARK 465 LYS A 355
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 GLN A 23 CG CD OE1 NE2
REMARK 470 ILE A 30 CG1 CG2 CD1
REMARK 470 LEU A 41 CG CD1 CD2
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1092 CG CD OE1 OE2
REMARK 470 LYS A1104 CG CD CE NZ
REMARK 470 LEU A1106 CG CD1 CD2
REMARK 470 GLN A 324 CG CD OE1 NE2
REMARK 470 ILE A 325 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 24 95.94 -68.38
REMARK 500 MET A 153 -56.76 63.31
REMARK 500 ASP A 191 51.87 -143.38
REMARK 500 ASN A 194 39.05 -98.59
REMARK 500 ALA A1020 96.20 -63.08
REMARK 500 GLN A 286 0.33 82.12
REMARK 500 LEU A 290 59.84 -95.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1WV A 2002
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ON9 A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1WV A 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GPCR-235 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4Z36 RELATED DB: PDB
REMARK 900 RELATED ID: 4Z34 RELATED DB: PDB
DBREF 4Z35 A 2 232 UNP Q92633 LPAR1_HUMAN 2 232
DBREF 4Z35 A 1001 1042 UNP P0ABE7 C562_ECOLX 23 64
DBREF 4Z35 A 1051 1105 UNP P0ABE7 C562_ECOLX 73 127
DBREF 4Z35 A 248 326 UNP Q92633 LPAR1_HUMAN 248 326
SEQADV 4Z35 MET A -17 UNP Q92633 INITIATING METHIONINE
SEQADV 4Z35 LYS A -16 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 THR A -15 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ILE A -14 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ILE A -13 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ALA A -12 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LEU A -11 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 SER A -10 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 TYR A -9 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ILE A -8 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PHE A -7 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 CYS A -6 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LEU A -5 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 VAL A -4 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PHE A -3 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ALA A -2 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 GLY A -1 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ALA A 0 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PRO A 1 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 4Z35 ALA A 1043 UNP P0ABE7 LINKER
SEQADV 4Z35 THR A 1044 UNP P0ABE7 LINKER
SEQADV 4Z35 PRO A 1045 UNP P0ABE7 LINKER
SEQADV 4Z35 PRO A 1046 UNP P0ABE7 LINKER
SEQADV 4Z35 LYS A 1047 UNP P0ABE7 LINKER
SEQADV 4Z35 LEU A 1048 UNP P0ABE7 LINKER
SEQADV 4Z35 GLU A 1049 UNP P0ABE7 LINKER
SEQADV 4Z35 ASP A 1050 UNP P0ABE7 LINKER
SEQADV 4Z35 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 4Z35 LEU A 1106 UNP P0ABE7 LINKER
SEQADV 4Z35 GLY A 327 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ARG A 328 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PRO A 329 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LEU A 330 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 GLU A 331 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 VAL A 332 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LEU A 333 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PHE A 334 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 GLN A 335 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 GLY A 336 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 PRO A 337 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 338 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 339 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 340 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 341 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 342 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 343 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 344 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 345 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 346 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 HIS A 347 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ASP A 348 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 TYR A 349 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LYS A 350 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ASP A 351 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ASP A 352 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ASP A 353 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 ASP A 354 UNP Q92633 EXPRESSION TAG
SEQADV 4Z35 LYS A 355 UNP Q92633 EXPRESSION TAG
SEQRES 1 A 464 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 464 VAL PHE ALA GLY ALA PRO ALA ALA ILE SER THR SER ILE
SEQRES 3 A 464 PRO VAL ILE SER GLN PRO GLN PHE THR ALA MET ASN GLU
SEQRES 4 A 464 PRO GLN CYS PHE TYR ASN GLU SER ILE ALA PHE PHE TYR
SEQRES 5 A 464 ASN ARG SER GLY LYS HIS LEU ALA THR GLU TRP ASN THR
SEQRES 6 A 464 VAL SER LYS LEU VAL MET GLY LEU GLY ILE THR VAL CYS
SEQRES 7 A 464 ILE PHE ILE MET LEU ALA ASN LEU LEU VAL MET VAL ALA
SEQRES 8 A 464 ILE TYR VAL ASN ARG ARG PHE HIS PHE PRO ILE TYR TYR
SEQRES 9 A 464 LEU MET ALA ASN LEU ALA ALA ALA ASP PHE PHE ALA GLY
SEQRES 10 A 464 LEU ALA TYR PHE TYR LEU MET PHE ASN THR GLY PRO ASN
SEQRES 11 A 464 THR ARG ARG LEU THR VAL SER THR TRP LEU LEU ARG GLN
SEQRES 12 A 464 GLY LEU ILE ASP THR SER LEU THR ALA SER VAL ALA ASN
SEQRES 13 A 464 LEU LEU ALA ILE ALA ILE GLU ARG HIS ILE THR VAL PHE
SEQRES 14 A 464 ARG MET GLN LEU HIS THR ARG MET SER ASN ARG ARG VAL
SEQRES 15 A 464 VAL VAL VAL ILE VAL VAL ILE TRP THR MET ALA ILE VAL
SEQRES 16 A 464 MET GLY ALA ILE PRO SER VAL GLY TRP ASN CYS ILE CYS
SEQRES 17 A 464 ASP ILE GLU ASN CYS SER ASN MET ALA PRO LEU TYR SER
SEQRES 18 A 464 ASP SER TYR LEU VAL PHE TRP ALA ILE PHE ASN LEU VAL
SEQRES 19 A 464 THR PHE VAL VAL MET VAL VAL LEU TYR ALA HIS ILE PHE
SEQRES 20 A 464 GLY TYR VAL ALA ASP LEU GLU ASP ASN TRP GLU THR LEU
SEQRES 21 A 464 ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA
SEQRES 22 A 464 ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA
SEQRES 23 A 464 ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU
SEQRES 24 A 464 ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG
SEQRES 25 A 464 HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA
SEQRES 26 A 464 LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN
SEQRES 27 A 464 ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR
SEQRES 28 A 464 ILE GLN LYS TYR LEU ARG ASN ARG ASP THR MET MET SER
SEQRES 29 A 464 LEU LEU LYS THR VAL VAL ILE VAL LEU GLY ALA PHE ILE
SEQRES 30 A 464 ILE CYS TRP THR PRO GLY LEU VAL LEU LEU LEU LEU ASP
SEQRES 31 A 464 VAL CYS CYS PRO GLN CYS ASP VAL LEU ALA TYR GLU LYS
SEQRES 32 A 464 PHE PHE LEU LEU LEU ALA GLU PHE ASN SER ALA MET ASN
SEQRES 33 A 464 PRO ILE ILE TYR SER TYR ARG ASP LYS GLU MET SER ALA
SEQRES 34 A 464 THR PHE ARG GLN ILE LEU GLY ARG PRO LEU GLU VAL LEU
SEQRES 35 A 464 PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 36 A 464 HIS ASP TYR LYS ASP ASP ASP ASP LYS
HET ON9 A2001 41
HET 1WV A2002 18
HETNAM ON9 3-{1-[(2S,3S)-3-(4-ACETYL-3,5-DIMETHOXYPHENYL)-2-(2,3-
HETNAM 2 ON9 DIHYDRO-1H-INDEN-2-YLMETHYL)-3-HYDROXYPROPYL]-4-
HETNAM 3 ON9 (METHOXYCARBONYL)-1H-PYRROL-3-YL}PROPANOIC ACID
HETNAM 1WV (2S)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE
HETSYN ON9 ONO-9910539
FORMUL 2 ON9 C32 H37 N O8
FORMUL 3 1WV C17 H32 O4
FORMUL 4 HOH *3(H2 O)
HELIX 1 AA1 SER A 29 SER A 37 1 9
HELIX 2 AA2 ASN A 46 ASN A 77 1 32
HELIX 3 AA3 ARG A 78 HIS A 81 5 4
HELIX 4 AA4 PHE A 82 PHE A 107 1 26
HELIX 5 AA5 ASN A 108 ARG A 114 5 7
HELIX 6 AA6 THR A 117 ARG A 152 1 36
HELIX 7 AA7 THR A 157 GLY A 179 1 23
HELIX 8 AA8 ALA A 180 VAL A 184 5 5
HELIX 9 AA9 ASP A 191 CYS A 195 5 5
HELIX 10 AB1 SER A 203 LYS A 1019 1 49
HELIX 11 AB2 ASN A 1022 LYS A 1042 1 21
HELIX 12 AB3 LYS A 1059 HIS A 1063 1 5
HELIX 13 AB4 GLY A 1064 GLY A 1082 1 19
HELIX 14 AB5 LYS A 1083 ASN A 1099 1 17
HELIX 15 AB6 TYR A 1105 CYS A 284 1 39
HELIX 16 AB7 GLU A 293 ASP A 315 1 23
HELIX 17 AB8 ASP A 315 GLY A 327 1 13
SSBOND 1 CYS A 24 CYS A 190 1555 1555 2.04
SSBOND 2 CYS A 188 CYS A 195 1555 1555 2.04
SSBOND 3 CYS A 284 CYS A 287 1555 1555 2.04
SITE 1 AC1 16 TYR A 34 LYS A 39 THR A 113 ARG A 124
SITE 2 AC1 16 GLN A 125 ILE A 128 ASP A 129 MET A 198
SITE 3 AC1 16 TRP A 210 TRP A 271 GLY A 274 LEU A 278
SITE 4 AC1 16 GLU A 293 LYS A 294 PHE A 296 LEU A 297
SITE 1 AC2 4 LEU A 51 THR A 130 GLY A 179 SER A 183
CRYST1 34.610 112.400 155.670 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.028893 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006424 0.00000
ATOM 1 N GLN A 23 12.204 -30.959 69.428 1.00 98.97 N1+
ANISOU 1 N GLN A 23 9327 15105 13173 283 -820 1781 N1+
ATOM 2 CA GLN A 23 11.455 -30.385 68.319 1.00 97.71 C
ANISOU 2 CA GLN A 23 9161 14938 13028 274 -758 1714 C
ATOM 3 C GLN A 23 12.242 -30.494 67.005 1.00100.00 C
ANISOU 3 C GLN A 23 9299 15161 13536 48 -795 1678 C
ATOM 4 O GLN A 23 11.665 -30.900 65.993 1.00 97.92 O
ANISOU 4 O GLN A 23 8876 14933 13394 -2 -669 1676 O
ATOM 5 CB GLN A 23 11.102 -28.925 68.614 1.00100.00 C
ANISOU 5 CB GLN A 23 9746 15164 13087 398 -868 1624 C
ATOM 6 N CYS A 24 13.555 -30.146 67.029 1.00 97.00 N
ANISOU 6 N CYS A 24 8972 14680 13203 -84 -972 1659 N
ATOM 7 CA CYS A 24 14.450 -30.179 65.869 1.00 95.88 C
ANISOU 7 CA CYS A 24 8704 14470 13258 -285 -1019 1643 C
ATOM 8 C CYS A 24 14.702 -31.639 65.439 1.00101.83 C
ANISOU 8 C CYS A 24 9185 15281 14226 -380 -881 1724 C
ATOM 9 O CYS A 24 15.567 -32.318 66.004 1.00101.71 O
ANISOU 9 O CYS A 24 9097 15262 14288 -436 -920 1796 O
ATOM 10 CB CYS A 24 15.754 -29.436 66.164 1.00 96.17 C
ANISOU 10 CB CYS A 24 8867 14389 13284 -383 -1250 1633 C
ATOM 11 SG CYS A 24 16.945 -29.417 64.794 1.00 98.73 S
ANISOU 11 SG CYS A 24 9032 14629 13852 -618 -1311 1646 S
ATOM 12 N PHE A 25 13.912 -32.099 64.440 1.00 99.65 N
ANISOU 12 N PHE A 25 8769 15052 14041 -392 -724 1712 N
ATOM 13 CA PHE A 25 13.900 -33.432 63.815 1.00 99.41 C
ANISOU 13 CA PHE A 25 8500 15065 14207 -471 -582 1768 C
ATOM 14 C PHE A 25 13.768 -34.574 64.845 1.00105.32 C
ANISOU 14 C PHE A 25 9155 15891 14972 -405 -502 1865 C
ATOM 15 O PHE A 25 14.512 -35.556 64.805 1.00104.78 O
ANISOU 15 O PHE A 25 8937 15817 15058 -498 -475 1928 O
ATOM 16 CB PHE A 25 15.140 -33.659 62.927 1.00100.74 C
ANISOU 16 CB PHE A 25 8563 15158 14555 -647 -628 1777 C
ATOM 17 CG PHE A 25 15.114 -32.915 61.617 1.00101.75 C
ANISOU 17 CG PHE A 25 8712 15231 14717 -718 -644 1702 C
ATOM 18 CD1 PHE A 25 14.255 -33.303 60.596 1.00103.82 C
ANISOU 18 CD1 PHE A 25 8880 15524 15043 -724 -510 1670 C
ATOM 19 CD2 PHE A 25 15.980 -31.855 61.386 1.00104.46 C
ANISOU 19 CD2 PHE A 25 9160 15485 15045 -791 -801 1673 C
ATOM 20 CE1 PHE A 25 14.236 -32.619 59.377 1.00104.26 C
ANISOU 20 CE1 PHE A 25 8958 15530 15125 -787 -524 1602 C
ATOM 21 CE2 PHE A 25 15.973 -31.178 60.162 1.00106.71 C
ANISOU 21 CE2 PHE A 25 9454 15721 15369 -855 -809 1614 C
ATOM 22 CZ PHE A 25 15.102 -31.565 59.162 1.00103.78 C
ANISOU 22 CZ PHE A 25 8997 15390 15045 -847 -666 1577 C
ATOM 23 N TYR A 26 12.793 -34.436 65.761 1.00103.37 N
ANISOU 23 N TYR A 26 8991 15715 14571 -239 -457 1886 N
ATOM 24 CA TYR A 26 12.493 -35.444 66.781 1.00103.97 C
ANISOU 24 CA TYR A 26 8986 15873 14645 -154 -375 1987 C
ATOM 25 C TYR A 26 11.568 -36.490 66.174 1.00108.05 C
ANISOU 25 C TYR A 26 9300 16457 15296 -156 -200 2039 C
ATOM 26 O TYR A 26 10.953 -36.213 65.139 1.00106.91 O
ANISOU 26 O TYR A 26 9125 16304 15193 -188 -152 1989 O
ATOM 27 CB TYR A 26 11.845 -34.770 68.006 1.00106.31 C
ANISOU 27 CB TYR A 26 9475 16215 14701 45 -401 1998 C
ATOM 28 CG TYR A 26 12.549 -35.026 69.318 1.00108.99 C
ANISOU 28 CG TYR A 26 9879 16559 14971 88 -482 2057 C
ATOM 29 CD1 TYR A 26 12.232 -36.136 70.099 1.00111.22 C
ANISOU 29 CD1 TYR A 26 10036 16931 15293 155 -375 2170 C
ATOM 30 CD2 TYR A 26 13.480 -34.122 69.816 1.00110.65 C
ANISOU 30 CD2 TYR A 26 10284 16683 15076 62 -677 2005 C
ATOM 31 CE1 TYR A 26 12.845 -36.354 71.332 1.00113.34 C
ANISOU 31 CE1 TYR A 26 10368 17206 15489 198 -452 2227 C
ATOM 32 CE2 TYR A 26 14.101 -34.329 71.046 1.00112.72 C
ANISOU 32 CE2 TYR A 26 10616 16944 15268 98 -769 2061 C
ATOM 33 CZ TYR A 26 13.782 -35.449 71.800 1.00121.06 C
ANISOU 33 CZ TYR A 26 11546 18096 16357 169 -652 2169 C
ATOM 34 OH TYR A 26 14.402 -35.657 73.009 1.00123.84 O
ANISOU 34 OH TYR A 26 11968 18450 16635 208 -741 2226 O
ATOM 35 N ASN A 27 11.429 -37.673 66.808 1.00105.60 N
ANISOU 35 N ASN A 27 8855 16213 15055 -121 -111 2146 N
ATOM 36 CA ASN A 27 10.514 -38.698 66.285 1.00105.24 C
ANISOU 36 CA ASN A 27 8619 16222 15143 -124 37 2210 C
ATOM 37 C ASN A 27 9.088 -38.383 66.795 1.00109.73 C
ANISOU 37 C ASN A 27 9237 16880 15577 54 116 2255 C
ATOM 38 O ASN A 27 8.433 -39.218 67.429 1.00110.02 O
ANISOU 38 O ASN A 27 9167 16999 15638 141 216 2371 O
ATOM 39 CB ASN A 27 10.977 -40.120 66.649 1.00107.41 C
ANISOU 39 CB ASN A 27 8727 16520 15564 -169 90 2313 C
ATOM 40 CG ASN A 27 10.309 -41.231 65.848 1.00133.93 C
ANISOU 40 CG ASN A 27 11885 19905 19096 -209 216 2376 C
ATOM 41 OD1 ASN A 27 9.960 -41.084 64.667 1.00127.83 O
ANISOU 41 OD1 ASN A 27 11067 19099 18405 -280 246 2323 O
ATOM 42 ND2 ASN A 27 10.163 -42.393 66.466 1.00127.59 N
ANISOU 42 ND2 ASN A 27 10963 19158 18359 -170 284 2494 N
ATOM 43 N GLU A 28 8.630 -37.147 66.507 1.00106.06 N
ANISOU 43 N GLU A 28 8929 16397 14971 112 73 2172 N
ATOM 44 CA GLU A 28 7.318 -36.618 66.875 1.00106.41 C
ANISOU 44 CA GLU A 28 9045 16517 14869 291 145 2209 C
ATOM 45 C GLU A 28 6.317 -36.871 65.769 1.00108.57 C
ANISOU 45 C GLU A 28 9188 16811 15254 250 234 2218 C
ATOM 46 O GLU A 28 6.650 -36.739 64.589 1.00107.28 O
ANISOU 46 O GLU A 28 8992 16578 15193 106 198 2132 O
ATOM 47 CB GLU A 28 7.389 -35.108 67.183 1.00108.50 C
ANISOU 47 CB GLU A 28 9571 16743 14911 386 43 2115 C
ATOM 48 CG GLU A 28 8.117 -34.745 68.468 1.00121.27 C
ANISOU 48 CG GLU A 28 11363 18347 16368 473 -55 2116 C
ATOM 49 CD GLU A 28 7.468 -35.145 69.783 1.00146.97 C
ANISOU 49 CD GLU A 28 14638 21704 19501 675 32 2237 C
ATOM 50 OE1 GLU A 28 8.216 -35.376 70.759 1.00145.29 O
ANISOU 50 OE1 GLU A 28 14486 21485 19232 699 -33 2264 O
ATOM 51 OE2 GLU A 28 6.220 -35.226 69.845 1.00142.73 O1-
ANISOU 51 OE2 GLU A 28 14053 21252 18924 812 164 2314 O1-
ATOM 52 N SER A 29 5.082 -37.211 66.157 1.00104.71 N
ANISOU 52 N SER A 29 8629 16417 14739 386 348 2333 N
ATOM 53 CA SER A 29 3.987 -37.457 65.231 1.00103.71 C
ANISOU 53 CA SER A 29 8377 16321 14709 369 428 2373 C
ATOM 54 C SER A 29 3.482 -36.126 64.650 1.00106.15 C
ANISOU 54 C SER A 29 8836 16608 14888 415 395 2280 C
ATOM 55 O SER A 29 3.899 -35.057 65.106 1.00105.83 O
ANISOU 55 O SER A 29 9002 16536 14672 486 320 2200 O
ATOM 56 CB SER A 29 2.865 -38.210 65.939 1.00108.51 C
ANISOU 56 CB SER A 29 8858 17041 15328 512 553 2554 C
ATOM 57 OG SER A 29 1.839 -38.568 65.030 1.00118.06 O
ANISOU 57 OG SER A 29 9923 18277 16659 479 618 2616 O
ATOM 58 N ILE A 30 2.586 -36.190 63.647 1.00101.57 N
ANISOU 58 N ILE A 30 8158 16039 14397 373 442 2293 N
ATOM 59 CA ILE A 30 2.007 -35.009 63.006 1.00100.91 C
ANISOU 59 CA ILE A 30 8189 15940 14211 411 423 2219 C
ATOM 60 C ILE A 30 1.128 -34.236 64.009 1.00105.27 C
ANISOU 60 C ILE A 30 8864 16575 14559 651 484 2295 C
ATOM 61 O ILE A 30 0.996 -33.018 63.889 1.00104.97 O
ANISOU 61 O ILE A 30 9002 16512 14371 721 446 2214 O
ATOM 62 CB ILE A 30 1.217 -35.410 61.744 1.00103.35 C
ANISOU 62 CB ILE A 30 8344 16247 14678 305 459 2236 C
ATOM 63 N ALA A 31 0.593 -34.940 65.033 1.00102.38 N
ANISOU 63 N ALA A 31 8416 16303 14182 785 580 2454 N
ATOM 64 CA ALA A 31 -0.246 -34.391 66.102 1.00103.54 C
ANISOU 64 CA ALA A 31 8666 16540 14136 1041 664 2557 C
ATOM 65 C ALA A 31 0.482 -33.314 66.911 1.00107.49 C
ANISOU 65 C ALA A 31 9448 16993 14399 1150 579 2450 C
ATOM 66 O ALA A 31 -0.164 -32.375 67.369 1.00108.00 O
ANISOU 66 O ALA A 31 9678 17090 14268 1345 614 2464 O
ATOM 67 CB ALA A 31 -0.706 -35.505 67.029 1.00105.21 C
ANISOU 67 CB ALA A 31 8715 16851 14407 1137 775 2751 C
ATOM 68 N PHE A 32 1.812 -33.451 67.077 1.00103.32 N
ANISOU 68 N PHE A 32 8981 16385 13892 1024 461 2348 N
ATOM 69 CA PHE A 32 2.666 -32.514 67.810 1.00103.57 C
ANISOU 69 CA PHE A 32 9275 16350 13726 1086 341 2243 C
ATOM 70 C PHE A 32 2.715 -31.142 67.111 1.00106.84 C
ANISOU 70 C PHE A 32 9878 16680 14035 1070 249 2099 C
ATOM 71 O PHE A 32 2.595 -30.117 67.782 1.00107.30 O
ANISOU 71 O PHE A 32 10179 16721 13869 1234 210 2060 O
ATOM 72 CB PHE A 32 4.087 -33.099 67.957 1.00104.74 C
ANISOU 72 CB PHE A 32 9388 16430 13977 916 232 2191 C
ATOM 73 CG PHE A 32 5.108 -32.198 68.612 1.00106.88 C
ANISOU 73 CG PHE A 32 9913 16617 14080 939 75 2088 C
ATOM 74 CD1 PHE A 32 5.166 -32.075 69.995 1.00111.42 C
ANISOU 74 CD1 PHE A 32 10643 17226 14466 1123 67 2138 C
ATOM 75 CD2 PHE A 32 6.041 -31.508 67.848 1.00108.18 C
ANISOU 75 CD2 PHE A 32 10163 16662 14277 777 -73 1949 C
ATOM 76 CE1 PHE A 32 6.117 -31.249 70.599 1.00113.02 C
ANISOU 76 CE1 PHE A 32 11096 17337 14511 1137 -103 2042 C
ATOM 77 CE2 PHE A 32 6.984 -30.675 68.452 1.00111.69 C
ANISOU 77 CE2 PHE A 32 10841 17019 14577 788 -239 1866 C
ATOM 78 CZ PHE A 32 7.024 -30.560 69.822 1.00111.26 C
ANISOU 78 CZ PHE A 32 10950 16990 14333 963 -262 1909 C
ATOM 79 N PHE A 33 2.894 -31.134 65.776 1.00102.06 N
ANISOU 79 N PHE A 33 9169 16021 13588 880 217 2023 N
ATOM 80 CA PHE A 33 2.988 -29.919 64.962 1.00101.47 C
ANISOU 80 CA PHE A 33 9238 15867 13451 837 133 1893 C
ATOM 81 C PHE A 33 1.617 -29.272 64.765 1.00105.12 C
ANISOU 81 C PHE A 33 9736 16391 13815 996 234 1939 C
ATOM 82 O PHE A 33 1.510 -28.049 64.843 1.00105.12 O
ANISOU 82 O PHE A 33 9951 16345 13643 1091 181 1863 O
ATOM 83 CB PHE A 33 3.622 -30.228 63.589 1.00101.92 C
ANISOU 83 CB PHE A 33 9156 15854 13713 590 81 1814 C
ATOM 84 CG PHE A 33 5.006 -30.824 63.641 1.00103.16 C
ANISOU 84 CG PHE A 33 9268 15946 13980 430 -11 1777 C
ATOM 85 CD1 PHE A 33 6.126 -30.010 63.726 1.00106.49 C
ANISOU 85 CD1 PHE A 33 9856 16267 14338 367 -165 1675 C
ATOM 86 CD2 PHE A 33 5.191 -32.199 63.584 1.00105.10 C
ANISOU 86 CD2 PHE A 33 9301 16227 14403 341 52 1855 C
ATOM 87 CE1 PHE A 33 7.408 -30.563 63.776 1.00107.16 C
ANISOU 87 CE1 PHE A 33 9884 16297 14536 221 -247 1664 C
ATOM 88 CE2 PHE A 33 6.474 -32.752 63.636 1.00107.72 C
ANISOU 88 CE2 PHE A 33 9588 16502 14838 203 -22 1833 C
ATOM 89 CZ PHE A 33 7.573 -31.930 63.732 1.00105.90 C
ANISOU 89 CZ PHE A 33 9513 16180 14545 145 -168 1743 C
ATOM 90 N TYR A 34 0.582 -30.092 64.498 1.00101.25 N
ANISOU 90 N TYR A 34 9034 15999 13439 1022 373 2072 N
ATOM 91 CA TYR A 34 -0.792 -29.658 64.248 1.00101.52 C
ANISOU 91 CA TYR A 34 9048 16106 13420 1161 483 2155 C
ATOM 92 C TYR A 34 -1.482 -29.092 65.494 1.00107.83 C
ANISOU 92 C TYR A 34 10010 16973 13986 1450 562 2243 C
ATOM 93 O TYR A 34 -2.357 -28.239 65.350 1.00108.21 O
ANISOU 93 O TYR A 34 10144 17047 13922 1588 618 2264 O
ATOM 94 CB TYR A 34 -1.617 -30.826 63.700 1.00102.00 C
ANISOU 94 CB TYR A 34 8818 16245 13691 1092 589 2296 C
ATOM 95 CG TYR A 34 -1.583 -30.937 62.193 1.00101.87 C
ANISOU 95 CG TYR A 34 8684 16174 13848 881 544 2220 C
ATOM 96 CD1 TYR A 34 -0.519 -31.554 61.542 1.00102.35 C
ANISOU 96 CD1 TYR A 34 8675 16154 14059 662 458 2124 C
ATOM 97 CD2 TYR A 34 -2.636 -30.466 61.419 1.00102.57 C
ANISOU 97 CD2 TYR A 34 8727 16293 13950 906 592 2254 C
ATOM 98 CE1 TYR A 34 -0.486 -31.665 60.154 1.00101.28 C
ANISOU 98 CE1 TYR A 34 8450 15966 14065 485 421 2054 C
ATOM 99 CE2 TYR A 34 -2.612 -30.564 60.030 1.00102.19 C
ANISOU 99 CE2 TYR A 34 8586 16193 14049 717 544 2182 C
ATOM 100 CZ TYR A 34 -1.534 -31.164 59.401 1.00106.84 C
ANISOU 100 CZ TYR A 34 9123 16699 14771 511 460 2079 C
ATOM 101 OH TYR A 34 -1.511 -31.271 58.035 1.00105.36 O
ANISOU 101 OH TYR A 34 8860 16458 14713 341 418 2009 O
ATOM 102 N ASN A 35 -1.115 -29.563 66.700 1.00105.73 N
ANISOU 102 N ASN A 35 9790 16738 13644 1549 573 2301 N
ATOM 103 CA ASN A 35 -1.727 -29.089 67.946 1.00107.54 C
ANISOU 103 CA ASN A 35 10192 17032 13636 1842 653 2389 C
ATOM 104 C ASN A 35 -1.142 -27.736 68.376 1.00112.69 C
ANISOU 104 C ASN A 35 11190 17584 14045 1934 530 2235 C
ATOM 105 O ASN A 35 -1.886 -26.905 68.905 1.00113.49 O
ANISOU 105 O ASN A 35 11469 17715 13938 2174 596 2271 O
ATOM 106 CB ASN A 35 -1.563 -30.121 69.069 1.00109.25 C
ANISOU 106 CB ASN A 35 10344 17311 13855 1909 698 2500 C
ATOM 107 CG ASN A 35 -2.266 -29.777 70.361 1.00137.35 C
ANISOU 107 CG ASN A 35 13999 20973 17214 2222 833 2651 C
ATOM 108 OD1 ASN A 35 -1.626 -29.484 71.377 1.00133.18 O
ANISOU 108 OD1 ASN A 35 13758 20413 16430 2407 793 2597 O
ATOM 109 ND2 ASN A 35 -3.598 -29.804 70.357 1.00131.35 N
ANISOU 109 ND2 ASN A 35 12993 20336 16578 2282 989 2855 N
ATOM 110 N ARG A 36 0.179 -27.519 68.160 1.00109.17 N
ANISOU 110 N ARG A 36 10841 17014 13626 1750 348 2075 N
ATOM 111 CA ARG A 36 0.881 -26.284 68.536 1.00109.89 C
ANISOU 111 CA ARG A 36 11256 16985 13512 1797 190 1924 C
ATOM 112 C ARG A 36 0.349 -25.076 67.760 1.00114.34 C
ANISOU 112 C ARG A 36 11936 17505 14002 1836 185 1850 C
ATOM 113 O ARG A 36 0.150 -24.017 68.357 1.00115.34 O
ANISOU 113 O ARG A 36 12339 17595 13890 2033 161 1810 O
ATOM 114 CB ARG A 36 2.404 -26.407 68.352 1.00109.09 C
ANISOU 114 CB ARG A 36 11177 16763 13508 1558 -4 1798 C
ATOM 115 CG ARG A 36 3.042 -27.319 69.387 1.00120.08 C
ANISOU 115 CG ARG A 36 12519 18178 14927 1541 -29 1855 C
ATOM 116 CD ARG A 36 4.521 -27.118 69.609 1.00132.07 C
ANISOU 116 CD ARG A 36 14244 19575 16362 1471 -239 1748 C
ATOM 117 NE ARG A 36 4.734 -26.015 70.550 1.00146.31 N
ANISOU 117 NE ARG A 36 16379 21346 17868 1710 -292 1719 N
ATOM 118 CZ ARG A 36 4.660 -26.109 71.881 1.00166.09 C
ANISOU 118 CZ ARG A 36 18976 23922 20210 1926 -222 1810 C
ATOM 119 NH1 ARG A 36 4.862 -25.039 72.638 1.00157.73 N
ANISOU 119 NH1 ARG A 36 18247 22820 18864 2154 -272 1771 N
ATOM 120 NH2 ARG A 36 4.368 -27.271 72.461 1.00153.55 N1+
ANISOU 120 NH2 ARG A 36 17156 22446 18741 1926 -96 1944 N1+
ATOM 121 N SER A 37 0.088 -25.246 66.450 1.00109.83 N
ANISOU 121 N SER A 37 11162 16939 13628 1661 211 1837 N
ATOM 122 CA SER A 37 -0.478 -24.211 65.583 1.00109.57 C
ANISOU 122 CA SER A 37 11199 16876 13558 1677 215 1779 C
ATOM 123 C SER A 37 -2.007 -24.292 65.604 1.00114.56 C
ANISOU 123 C SER A 37 11731 17637 14160 1867 412 1936 C
ATOM 124 O SER A 37 -2.556 -25.339 65.952 1.00114.57 O
ANISOU 124 O SER A 37 11536 17749 14247 1914 537 2090 O
ATOM 125 CB SER A 37 0.047 -24.355 64.156 1.00111.33 C
ANISOU 125 CB SER A 37 11261 17040 13999 1400 143 1692 C
ATOM 126 OG SER A 37 1.456 -24.206 64.089 1.00119.10 O
ANISOU 126 OG SER A 37 12329 17906 15016 1231 -33 1567 O
ATOM 127 N GLY A 38 -2.677 -23.203 65.228 1.00111.78 N
ANISOU 127 N GLY A 38 11505 17269 13697 1973 436 1907 N
ATOM 128 CA GLY A 38 -4.135 -23.138 65.180 1.00112.47 C
ANISOU 128 CA GLY A 38 11505 17474 13754 2158 618 2064 C
ATOM 129 C GLY A 38 -4.707 -23.886 63.992 1.00115.20 C
ANISOU 129 C GLY A 38 11531 17883 14357 1983 684 2142 C
ATOM 130 O GLY A 38 -5.281 -23.270 63.088 1.00114.43 O
ANISOU 130 O GLY A 38 11408 17781 14289 1955 699 2125 O
ATOM 131 N LYS A 39 -4.542 -25.224 63.986 1.00111.09 N
ANISOU 131 N LYS A 39 10771 17416 14022 1862 714 2226 N
ATOM 132 CA LYS A 39 -4.989 -26.117 62.918 1.00109.76 C
ANISOU 132 CA LYS A 39 10302 17294 14108 1681 755 2302 C
ATOM 133 C LYS A 39 -5.697 -27.349 63.507 1.00114.63 C
ANISOU 133 C LYS A 39 10699 18032 14825 1753 884 2514 C
ATOM 134 O LYS A 39 -5.281 -27.860 64.548 1.00114.49 O
ANISOU 134 O LYS A 39 10722 18032 14747 1830 895 2549 O
ATOM 135 CB LYS A 39 -3.784 -26.532 62.051 1.00110.17 C
ANISOU 135 CB LYS A 39 10291 17245 14325 1389 614 2147 C
ATOM 136 CG LYS A 39 -4.155 -27.305 60.806 1.00117.94 C
ANISOU 136 CG LYS A 39 11022 18249 15540 1206 634 2189 C
ATOM 137 CD LYS A 39 -3.795 -26.667 59.560 1.00123.67 C
ANISOU 137 CD LYS A 39 11756 18874 16359 987 517 2027 C
ATOM 138 CE LYS A 39 -4.538 -27.231 58.387 1.00129.74 C
ANISOU 138 CE LYS A 39 12315 19675 17304 870 554 2088 C
ATOM 139 NZ LYS A 39 -3.635 -27.607 57.264 1.00135.57 N1+
ANISOU 139 NZ LYS A 39 13004 20323 18185 628 453 1954 N1+
ATOM 140 N HIS A 40 -6.768 -27.809 62.829 1.00111.82 N
ANISOU 140 N HIS A 40 10107 17753 14628 1722 973 2661 N
ATOM 141 CA HIS A 40 -7.594 -28.961 63.205 1.00112.64 C
ANISOU 141 CA HIS A 40 9966 17969 14861 1773 1092 2891 C
ATOM 142 C HIS A 40 -6.934 -30.295 62.838 1.00115.53 C
ANISOU 142 C HIS A 40 10143 18305 15448 1544 1029 2877 C
ATOM 143 O HIS A 40 -6.293 -30.394 61.788 1.00113.66 O
ANISOU 143 O HIS A 40 9872 17979 15336 1312 918 2734 O
ATOM 144 CB HIS A 40 -8.975 -28.881 62.509 1.00113.98 C
ANISOU 144 CB HIS A 40 9954 18215 15139 1796 1178 3051 C
ATOM 145 CG HIS A 40 -8.912 -28.682 61.016 1.00116.10 C
ANISOU 145 CG HIS A 40 10121 18411 15578 1540 1076 2945 C
ATOM 146 ND1 HIS A 40 -8.195 -29.542 60.195 1.00116.84 N
ANISOU 146 ND1 HIS A 40 10034 18464 15896 1300 1004 2922 N
ATOM 147 CD2 HIS A 40 -9.514 -27.750 60.240 1.00117.51 C
ANISOU 147 CD2 HIS A 40 10370 18553 15726 1503 1039 2860 C
ATOM 148 CE1 HIS A 40 -8.351 -29.082 58.965 1.00115.31 C
ANISOU 148 CE1 HIS A 40 9817 18208 15786 1133 925 2819 C
ATOM 149 NE2 HIS A 40 -9.135 -28.007 58.942 1.00115.98 N
ANISOU 149 NE2 HIS A 40 10040 18297 15730 1243 943 2783 N
ATOM 150 N LEU A 41 -7.139 -31.326 63.674 1.00112.97 N
ANISOU 150 N LEU A 41 9691 18057 15175 1620 1108 3040 N
ATOM 151 CA LEU A 41 -6.647 -32.686 63.435 1.00112.16 C
ANISOU 151 CA LEU A 41 9396 17938 15283 1435 1071 3065 C
ATOM 152 C LEU A 41 -7.707 -33.681 63.895 1.00117.34 C
ANISOU 152 C LEU A 41 9796 18708 16080 1508 1193 3335 C
ATOM 153 O LEU A 41 -8.007 -33.760 65.089 1.00118.08 O
ANISOU 153 O LEU A 41 9905 18896 16065 1732 1306 3490 O
ATOM 154 CB LEU A 41 -5.299 -32.940 64.118 1.00112.05 C
ANISOU 154 CB LEU A 41 9515 17879 15180 1438 1015 2965 C
ATOM 155 N ALA A 42 -8.315 -34.389 62.929 1.00113.98 N
ANISOU 155 N ALA A 42 9145 18271 15891 1328 1166 3401 N
ATOM 156 CA ALA A 42 -9.385 -35.350 63.168 1.00115.15 C
ANISOU 156 CA ALA A 42 9030 18513 16208 1365 1256 3668 C
ATOM 157 C ALA A 42 -8.836 -36.751 63.405 1.00119.44 C
ANISOU 157 C ALA A 42 9417 19035 16932 1230 1226 3711 C
ATOM 158 O ALA A 42 -7.771 -37.100 62.891 1.00117.66 O
ANISOU 158 O ALA A 42 9236 18705 16766 1040 1117 3526 O
ATOM 159 CB ALA A 42 -10.348 -35.361 61.991 1.00115.82 C
ANISOU 159 CB ALA A 42 8964 18593 16448 1252 1229 3734 C
ATOM 160 N THR A 43 -9.573 -37.548 64.198 1.00118.02 N
ANISOU 160 N THR A 43 9047 18956 16839 1339 1331 3970 N
ATOM 161 CA THR A 43 -9.231 -38.932 64.545 1.00118.22 C
ANISOU 161 CA THR A 43 8897 18977 17045 1242 1323 4062 C
ATOM 162 C THR A 43 -10.355 -39.873 64.054 1.00122.68 C
ANISOU 162 C THR A 43 9171 19570 17871 1149 1329 4287 C
ATOM 163 O THR A 43 -10.097 -41.047 63.782 1.00121.90 O
ANISOU 163 O THR A 43 8922 19414 17982 970 1264 4308 O
ATOM 164 CB THR A 43 -8.983 -39.070 66.068 1.00129.82 C
ANISOU 164 CB THR A 43 10413 20541 18374 1469 1437 4179 C
ATOM 165 OG1 THR A 43 -8.382 -37.878 66.586 1.00130.41 O
ANISOU 165 OG1 THR A 43 10778 20589 18181 1581 1421 3988 O
ATOM 166 CG2 THR A 43 -8.098 -40.268 66.419 1.00128.71 C
ANISOU 166 CG2 THR A 43 10126 20386 18391 1371 1423 4239 C
ATOM 167 N GLU A 44 -11.588 -39.342 63.927 1.00120.18 N
ANISOU 167 N GLU A 44 8781 19338 17546 1273 1404 4462 N
ATOM 168 CA GLU A 44 -12.775 -40.070 63.475 1.00120.91 C
ANISOU 168 CA GLU A 44 8596 19465 17879 1204 1406 4709 C
ATOM 169 C GLU A 44 -13.096 -39.741 62.002 1.00123.99 C
ANISOU 169 C GLU A 44 8979 19769 18364 1010 1282 4599 C
ATOM 170 O GLU A 44 -12.685 -38.690 61.497 1.00122.57 O
ANISOU 170 O GLU A 44 9004 19544 18022 1010 1247 4387 O
ATOM 171 CB GLU A 44 -13.986 -39.746 64.386 1.00124.27 C
ANISOU 171 CB GLU A 44 8919 20051 18246 1479 1579 5018 C
ATOM 172 CG GLU A 44 -14.616 -38.360 64.229 1.00135.05 C
ANISOU 172 CG GLU A 44 10421 21469 19424 1648 1645 5010 C
ATOM 173 CD GLU A 44 -13.782 -37.139 64.580 1.00152.37 C
ANISOU 173 CD GLU A 44 12946 23638 21310 1780 1662 4762 C
ATOM 174 OE1 GLU A 44 -13.097 -37.160 65.628 1.00148.10 O
ANISOU 174 OE1 GLU A 44 12532 23119 20621 1909 1715 4721 O
ATOM 175 OE2 GLU A 44 -13.850 -36.142 63.824 1.00142.81 O1-
ANISOU 175 OE2 GLU A 44 11871 22384 20007 1756 1617 4618 O1-
ATOM 176 N TRP A 45 -13.838 -40.638 61.325 1.00121.18 N
ANISOU 176 N TRP A 45 8388 19385 18271 847 1209 4750 N
ATOM 177 CA TRP A 45 -14.246 -40.431 59.935 1.00120.61 C
ANISOU 177 CA TRP A 45 8292 19232 18302 663 1084 4675 C
ATOM 178 C TRP A 45 -15.463 -39.501 59.898 1.00125.65 C
ANISOU 178 C TRP A 45 8883 19974 18886 818 1165 4854 C
ATOM 179 O TRP A 45 -16.589 -39.907 60.207 1.00126.86 O
ANISOU 179 O TRP A 45 8809 20215 19178 886 1224 5161 O
ATOM 180 CB TRP A 45 -14.521 -41.762 59.212 1.00119.64 C
ANISOU 180 CB TRP A 45 7964 19021 18474 422 951 4756 C
ATOM 181 CG TRP A 45 -13.336 -42.279 58.450 1.00118.86 C
ANISOU 181 CG TRP A 45 7983 18767 18411 203 815 4477 C
ATOM 182 CD1 TRP A 45 -12.510 -43.304 58.809 1.00121.57 C
ANISOU 182 CD1 TRP A 45 8308 19050 18834 121 788 4424 C
ATOM 183 CD2 TRP A 45 -12.811 -41.752 57.225 1.00117.50 C
ANISOU 183 CD2 TRP A 45 7972 18483 18189 54 700 4216 C
ATOM 184 NE1 TRP A 45 -11.515 -43.461 57.872 1.00119.50 N
ANISOU 184 NE1 TRP A 45 8182 18646 18577 -65 668 4155 N
ATOM 185 CE2 TRP A 45 -11.674 -42.520 56.889 1.00120.31 C
ANISOU 185 CE2 TRP A 45 8398 18716 18597 -106 614 4024 C
ATOM 186 CE3 TRP A 45 -13.188 -40.696 56.381 1.00118.29 C
ANISOU 186 CE3 TRP A 45 8163 18580 18202 51 669 4135 C
ATOM 187 CZ2 TRP A 45 -10.917 -42.273 55.738 1.00118.35 C
ANISOU 187 CZ2 TRP A 45 8306 18345 18318 -263 504 3763 C
ATOM 188 CZ3 TRP A 45 -12.442 -40.458 55.238 1.00118.46 C
ANISOU 188 CZ3 TRP A 45 8337 18478 18194 -113 553 3870 C
ATOM 189 CH2 TRP A 45 -11.321 -41.240 54.927 1.00118.13 C
ANISOU 189 CH2 TRP A 45 8362 18318 18204 -262 475 3690 C
ATOM 190 N ASN A 46 -15.209 -38.231 59.552 1.00121.27 N
ANISOU 190 N ASN A 46 8543 19411 18124 885 1176 4669 N
ATOM 191 CA ASN A 46 -16.211 -37.162 59.483 1.00121.66 C
ANISOU 191 CA ASN A 46 8598 19548 18078 1047 1259 4792 C
ATOM 192 C ASN A 46 -17.082 -37.292 58.215 1.00123.85 C
ANISOU 192 C ASN A 46 8720 19785 18551 867 1145 4869 C
ATOM 193 O ASN A 46 -16.699 -37.998 57.280 1.00122.49 O
ANISOU 193 O ASN A 46 8519 19494 18529 615 987 4742 O
ATOM 194 CB ASN A 46 -15.500 -35.805 59.512 1.00122.77 C
ANISOU 194 CB ASN A 46 9041 19668 17940 1153 1284 4539 C
ATOM 195 CG ASN A 46 -16.350 -34.680 60.033 1.00145.22 C
ANISOU 195 CG ASN A 46 11941 22626 20611 1424 1431 4680 C
ATOM 196 OD1 ASN A 46 -17.227 -34.164 59.334 1.00138.64 O
ANISOU 196 OD1 ASN A 46 11037 21818 19822 1423 1429 4774 O
ATOM 197 ND2 ASN A 46 -16.120 -34.293 61.285 1.00137.42 N
ANISOU 197 ND2 ASN A 46 11089 21706 19417 1670 1561 4701 N
ATOM 198 N THR A 47 -18.247 -36.614 58.191 1.00120.51 N
ANISOU 198 N THR A 47 8206 19461 18120 1004 1226 5083 N
ATOM 199 CA THR A 47 -19.189 -36.647 57.063 1.00120.40 C
ANISOU 199 CA THR A 47 8036 19426 18284 858 1124 5195 C
ATOM 200 C THR A 47 -18.637 -35.825 55.871 1.00121.55 C
ANISOU 200 C THR A 47 8384 19469 18332 723 1008 4893 C
ATOM 201 O THR A 47 -18.709 -36.299 54.732 1.00120.92 O
ANISOU 201 O THR A 47 8241 19292 18413 485 844 4832 O
ATOM 202 CB THR A 47 -20.588 -36.150 57.493 1.00129.46 C
ANISOU 202 CB THR A 47 9023 20724 19443 1074 1266 5537 C
ATOM 203 OG1 THR A 47 -20.982 -36.804 58.702 1.00129.65 O
ANISOU 203 OG1 THR A 47 8890 20852 19518 1237 1399 5804 O
ATOM 204 CG2 THR A 47 -21.655 -36.389 56.424 1.00128.70 C
ANISOU 204 CG2 THR A 47 8712 20614 19575 915 1152 5716 C
ATOM 205 N VAL A 48 -18.095 -34.614 56.129 1.00116.08 N
ANISOU 205 N VAL A 48 7936 18791 17377 875 1087 4711 N
ATOM 206 CA VAL A 48 -17.545 -33.744 55.077 1.00113.88 C
ANISOU 206 CA VAL A 48 7853 18423 16994 769 993 4435 C
ATOM 207 C VAL A 48 -16.196 -34.299 54.570 1.00114.82 C
ANISOU 207 C VAL A 48 8098 18402 17128 558 861 4142 C
ATOM 208 O VAL A 48 -15.855 -34.064 53.406 1.00113.52 O
ANISOU 208 O VAL A 48 8014 18142 16976 390 740 3955 O
ATOM 209 CB VAL A 48 -17.411 -32.248 55.488 1.00117.64 C
ANISOU 209 CB VAL A 48 8554 18949 17197 993 1107 4342 C
ATOM 210 CG1 VAL A 48 -18.779 -31.593 55.645 1.00119.09 C
ANISOU 210 CG1 VAL A 48 8625 19252 17371 1175 1221 4609 C
ATOM 211 CG2 VAL A 48 -16.560 -32.057 56.746 1.00117.31 C
ANISOU 211 CG2 VAL A 48 8685 18929 16960 1170 1207 4256 C
ATOM 212 N SER A 49 -15.448 -35.033 55.429 1.00110.01 N
ANISOU 212 N SER A 49 7501 17782 16515 575 890 4113 N
ATOM 213 CA SER A 49 -14.151 -35.626 55.081 1.00107.76 C
ANISOU 213 CA SER A 49 7319 17373 16251 397 785 3866 C
ATOM 214 C SER A 49 -14.311 -36.731 54.025 1.00110.63 C
ANISOU 214 C SER A 49 7539 17640 16854 143 634 3873 C
ATOM 215 O SER A 49 -13.436 -36.889 53.170 1.00108.92 O
ANISOU 215 O SER A 49 7434 17306 16645 -26 525 3643 O
ATOM 216 CB SER A 49 -13.457 -36.183 56.320 1.00110.83 C
ANISOU 216 CB SER A 49 7728 17788 16593 490 859 3878 C
ATOM 217 OG SER A 49 -14.106 -37.340 56.820 1.00119.15 O
ANISOU 217 OG SER A 49 8549 18889 17834 483 884 4124 O
ATOM 218 N LYS A 50 -15.431 -37.485 54.094 1.00107.95 N
ANISOU 218 N LYS A 50 6959 17348 16709 122 627 4144 N
ATOM 219 CA LYS A 50 -15.769 -38.565 53.162 1.00107.58 C
ANISOU 219 CA LYS A 50 6768 17204 16901 -111 469 4189 C
ATOM 220 C LYS A 50 -16.137 -37.999 51.793 1.00110.34 C
ANISOU 220 C LYS A 50 7164 17497 17264 -233 354 4102 C
ATOM 221 O LYS A 50 -15.780 -38.592 50.772 1.00109.40 O
ANISOU 221 O LYS A 50 7070 17250 17247 -442 201 3971 O
ATOM 222 CB LYS A 50 -16.927 -39.423 53.714 1.00111.68 C
ANISOU 222 CB LYS A 50 7010 17796 17628 -86 490 4535 C
ATOM 223 CG LYS A 50 -16.529 -40.332 54.872 1.00124.82 C
ANISOU 223 CG LYS A 50 8597 19495 19335 -15 571 4632 C
ATOM 224 CD LYS A 50 -17.730 -41.048 55.485 1.00135.88 C
ANISOU 224 CD LYS A 50 9707 20969 20953 12 592 4998 C
ATOM 225 CE LYS A 50 -17.335 -42.028 56.566 1.00147.45 C
ANISOU 225 CE LYS A 50 11082 22606 22338 288 795 5250 C
ATOM 226 NZ LYS A 50 -18.545 -42.572 57.260 1.00157.52 N1+
ANISOU 226 NZ LYS A 50 12058 23939 23855 289 806 5609 N1+
ATOM 227 N LEU A 51 -16.846 -36.851 51.775 1.00106.74 N
ANISOU 227 N LEU A 51 6725 17132 16699 -95 430 4178 N
ATOM 228 CA LEU A 51 -17.299 -36.204 50.548 1.00106.22 C
ANISOU 228 CA LEU A 51 6695 17029 16636 -188 336 4119 C
ATOM 229 C LEU A 51 -16.170 -35.419 49.865 1.00107.65 C
ANISOU 229 C LEU A 51 7135 17127 16641 -238 299 3784 C
ATOM 230 O LEU A 51 -16.124 -35.406 48.633 1.00107.23 O
ANISOU 230 O LEU A 51 7126 16983 16633 -403 166 3664 O
ATOM 231 CB LEU A 51 -18.486 -35.274 50.822 1.00107.60 C
ANISOU 231 CB LEU A 51 6782 17335 16764 -13 440 4341 C
ATOM 232 CG LEU A 51 -19.379 -34.993 49.615 1.00113.21 C
ANISOU 232 CG LEU A 51 7414 18024 17578 -133 323 4410 C
ATOM 233 CD1 LEU A 51 -20.580 -35.938 49.583 1.00115.34 C
ANISOU 233 CD1 LEU A 51 7395 18327 18102 -197 265 4741 C
ATOM 234 CD2 LEU A 51 -19.857 -33.571 49.629 1.00116.19 C
ANISOU 234 CD2 LEU A 51 7873 18488 17786 34 426 4423 C
ATOM 235 N VAL A 52 -15.265 -34.772 50.642 1.00102.15 N
ANISOU 235 N VAL A 52 6609 16455 15748 -99 406 3641 N
ATOM 236 CA VAL A 52 -14.144 -34.003 50.081 1.00 99.84 C
ANISOU 236 CA VAL A 52 6552 16085 15298 -141 373 3344 C
ATOM 237 C VAL A 52 -13.123 -34.998 49.457 1.00101.50 C
ANISOU 237 C VAL A 52 6804 16160 15600 -346 255 3165 C
ATOM 238 O VAL A 52 -12.482 -34.665 48.455 1.00100.20 O
ANISOU 238 O VAL A 52 6774 15907 15390 -456 175 2958 O
ATOM 239 CB VAL A 52 -13.497 -33.018 51.103 1.00103.32 C
ANISOU 239 CB VAL A 52 7165 16580 15512 59 499 3256 C
ATOM 240 CG1 VAL A 52 -12.663 -33.732 52.168 1.00102.88 C
ANISOU 240 CG1 VAL A 52 7125 16522 15445 99 546 3238 C
ATOM 241 CG2 VAL A 52 -12.678 -31.943 50.396 1.00101.95 C
ANISOU 241 CG2 VAL A 52 7212 16341 15186 27 459 3001 C
ATOM 242 N MET A 53 -13.033 -36.225 50.018 1.00 97.42 N
ANISOU 242 N MET A 53 6167 15631 15219 -389 248 3262 N
ATOM 243 CA MET A 53 -12.182 -37.295 49.498 1.00 96.24 C
ANISOU 243 CA MET A 53 6038 15355 15173 -567 145 3130 C
ATOM 244 C MET A 53 -12.842 -37.898 48.254 1.00100.50 C
ANISOU 244 C MET A 53 6498 15811 15878 -750 -7 3163 C
ATOM 245 O MET A 53 -12.166 -38.129 47.247 1.00 99.55 O
ANISOU 245 O MET A 53 6489 15571 15763 -892 -108 2973 O
ATOM 246 CB MET A 53 -11.931 -38.368 50.573 1.00 98.84 C
ANISOU 246 CB MET A 53 6262 15703 15591 -537 194 3240 C
ATOM 247 CG MET A 53 -10.993 -39.471 50.123 1.00101.69 C
ANISOU 247 CG MET A 53 6653 15933 16051 -702 104 3107 C
ATOM 248 SD MET A 53 -10.776 -40.764 51.360 1.00106.27 S
ANISOU 248 SD MET A 53 7091 16536 16749 -670 160 3256 S
ATOM 249 CE MET A 53 -9.692 -41.863 50.474 1.00102.30 C
ANISOU 249 CE MET A 53 6663 15858 16347 -874 40 3065 C
ATOM 250 N GLY A 54 -14.157 -38.127 48.346 1.00 97.98 N
ANISOU 250 N GLY A 54 5990 15554 15685 -738 -23 3412 N
ATOM 251 CA GLY A 54 -14.982 -38.679 47.277 1.00 98.52 C
ANISOU 251 CA GLY A 54 5962 15551 15922 -904 -182 3491 C
ATOM 252 C GLY A 54 -14.969 -37.824 46.029 1.00101.44 C
ANISOU 252 C GLY A 54 6469 15872 16202 -971 -259 3329 C
ATOM 253 O GLY A 54 -14.757 -38.343 44.931 1.00101.03 O
ANISOU 253 O GLY A 54 6477 15693 16215 -1142 -407 3211 O
ATOM 254 N LEU A 55 -15.169 -36.499 46.198 1.00 97.25 N
ANISOU 254 N LEU A 55 6002 15437 15511 -828 -157 3317 N
ATOM 255 CA LEU A 55 -15.149 -35.526 45.105 1.00 96.21 C
ANISOU 255 CA LEU A 55 6004 15276 15275 -865 -207 3169 C
ATOM 256 C LEU A 55 -13.715 -35.332 44.607 1.00 98.23 C
ANISOU 256 C LEU A 55 6477 15434 15412 -923 -225 2870 C
ATOM 257 O LEU A 55 -13.505 -35.217 43.401 1.00 97.41 O
ANISOU 257 O LEU A 55 6470 15242 15298 -1042 -330 2728 O
ATOM 258 CB LEU A 55 -15.764 -34.181 45.546 1.00 96.36 C
ANISOU 258 CB LEU A 55 6033 15424 15157 -679 -80 3250 C
ATOM 259 CG LEU A 55 -15.934 -33.082 44.475 1.00100.72 C
ANISOU 259 CG LEU A 55 6673 15962 15633 -714 -134 3161 C
ATOM 260 CD1 LEU A 55 -17.123 -33.350 43.561 1.00102.29 C
ANISOU 260 CD1 LEU A 55 6704 16246 15915 -676 -139 3412 C
ATOM 261 CD2 LEU A 55 -16.122 -31.732 45.120 1.00102.03 C
ANISOU 261 CD2 LEU A 55 7033 16156 15580 -588 -32 2985 C
ATOM 262 N GLY A 56 -12.756 -35.325 45.537 1.00 93.90 N
ANISOU 262 N GLY A 56 5998 14901 14776 -834 -123 2791 N
ATOM 263 CA GLY A 56 -11.333 -35.157 45.256 1.00 92.27 C
ANISOU 263 CA GLY A 56 5978 14615 14467 -871 -122 2540 C
ATOM 264 C GLY A 56 -10.758 -36.184 44.301 1.00 95.81 C
ANISOU 264 C GLY A 56 6466 14925 15014 -1048 -243 2421 C
ATOM 265 O GLY A 56 -10.068 -35.821 43.345 1.00 94.75 O
ANISOU 265 O GLY A 56 6478 14714 14807 -1112 -288 2233 O
ATOM 266 N ILE A 57 -11.058 -37.474 44.545 1.00 93.02 N
ANISOU 266 N ILE A 57 5984 14533 14825 -1121 -295 2537 N
ATOM 267 CA ILE A 57 -10.607 -38.601 43.720 1.00 92.84 C
ANISOU 267 CA ILE A 57 6000 14367 14907 -1282 -416 2443 C
ATOM 268 C ILE A 57 -11.318 -38.547 42.346 1.00 97.55 C
ANISOU 268 C ILE A 57 6624 14893 15548 -1402 -561 2423 C
ATOM 269 O ILE A 57 -10.649 -38.694 41.323 1.00 96.94 O
ANISOU 269 O ILE A 57 6695 14705 15434 -1490 -633 2241 O
ATOM 270 CB ILE A 57 -10.835 -39.957 44.456 1.00 96.74 C
ANISOU 270 CB ILE A 57 6342 14842 15573 -1319 -435 2596 C
ATOM 271 CG1 ILE A 57 -9.923 -40.063 45.706 1.00 96.52 C
ANISOU 271 CG1 ILE A 57 6319 14866 15490 -1212 -301 2580 C
ATOM 272 CG2 ILE A 57 -10.628 -41.163 43.516 1.00 97.73 C
ANISOU 272 CG2 ILE A 57 6504 14805 15823 -1490 -585 2526 C
ATOM 273 CD1 ILE A 57 -10.317 -41.145 46.731 1.00105.83 C
ANISOU 273 CD1 ILE A 57 7317 16075 16820 -1198 -279 2781 C
ATOM 274 N THR A 58 -12.649 -38.297 42.329 1.00 94.96 N
ANISOU 274 N THR A 58 6158 14633 15289 -1395 -600 2614 N
ATOM 275 CA THR A 58 -13.480 -38.206 41.115 1.00 95.49 C
ANISOU 275 CA THR A 58 6227 14646 15407 -1507 -748 2632 C
ATOM 276 C THR A 58 -12.908 -37.144 40.145 1.00 98.28 C
ANISOU 276 C THR A 58 6775 14976 15591 -1502 -745 2418 C
ATOM 277 O THR A 58 -12.853 -37.396 38.938 1.00 97.97 O
ANISOU 277 O THR A 58 6835 14827 15560 -1620 -875 2311 O
ATOM 278 CB THR A 58 -14.945 -37.904 41.494 1.00103.19 C
ANISOU 278 CB THR A 58 7004 15733 16470 -1461 -749 2900 C
ATOM 279 OG1 THR A 58 -15.390 -38.892 42.424 1.00103.40 O
ANISOU 279 OG1 THR A 58 6848 15785 16656 -1457 -740 3106 O
ATOM 280 CG2 THR A 58 -15.883 -37.892 40.287 1.00102.09 C
ANISOU 280 CG2 THR A 58 6844 15538 16408 -1589 -923 2951 C
ATOM 281 N VAL A 59 -12.461 -35.989 40.680 1.00 93.91 N
ANISOU 281 N VAL A 59 6283 14517 14881 -1362 -601 2358 N
ATOM 282 CA VAL A 59 -11.867 -34.907 39.891 1.00 92.91 C
ANISOU 282 CA VAL A 59 6329 14377 14595 -1344 -582 2171 C
ATOM 283 C VAL A 59 -10.470 -35.362 39.407 1.00 97.02 C
ANISOU 283 C VAL A 59 7011 14784 15069 -1402 -593 1953 C
ATOM 284 O VAL A 59 -10.157 -35.175 38.232 1.00 96.88 O
ANISOU 284 O VAL A 59 7121 14689 15001 -1472 -663 1815 O
ATOM 285 CB VAL A 59 -11.826 -33.560 40.673 1.00 96.02 C
ANISOU 285 CB VAL A 59 6742 14895 14847 -1177 -437 2186 C
ATOM 286 CG1 VAL A 59 -11.052 -32.485 39.914 1.00 94.67 C
ANISOU 286 CG1 VAL A 59 6751 14699 14521 -1163 -419 1987 C
ATOM 287 CG2 VAL A 59 -13.232 -33.059 40.967 1.00 96.88 C
ANISOU 287 CG2 VAL A 59 6706 15112 14993 -1109 -421 2401 C
ATOM 288 N CYS A 60 -9.667 -35.999 40.296 1.00 93.31 N
ANISOU 288 N CYS A 60 6527 14305 14620 -1372 -524 1939 N
ATOM 289 CA CYS A 60 -8.316 -36.497 40.007 1.00 92.28 C
ANISOU 289 CA CYS A 60 6525 14076 14460 -1412 -515 1766 C
ATOM 290 C CYS A 60 -8.313 -37.488 38.841 1.00 95.72 C
ANISOU 290 C CYS A 60 7022 14371 14974 -1550 -652 1699 C
ATOM 291 O CYS A 60 -7.432 -37.395 37.985 1.00 94.81 O
ANISOU 291 O CYS A 60 7063 14177 14783 -1577 -661 1531 O
ATOM 292 CB CYS A 60 -7.695 -37.129 41.247 1.00 92.60 C
ANISOU 292 CB CYS A 60 6504 14139 14539 -1360 -430 1810 C
ATOM 293 SG CYS A 60 -6.935 -35.940 42.377 1.00 95.57 S
ANISOU 293 SG CYS A 60 6925 14623 14762 -1203 -277 1774 S
ATOM 294 N ILE A 61 -9.279 -38.432 38.811 1.00 92.73 N
ANISOU 294 N ILE A 61 6530 13958 14745 -1630 -759 1836 N
ATOM 295 CA ILE A 61 -9.407 -39.443 37.755 1.00 93.13 C
ANISOU 295 CA ILE A 61 6647 13860 14878 -1765 -916 1787 C
ATOM 296 C ILE A 61 -9.705 -38.723 36.420 1.00 96.28 C
ANISOU 296 C ILE A 61 7169 14223 15189 -1807 -1001 1692 C
ATOM 297 O ILE A 61 -9.092 -39.060 35.409 1.00 95.71 O
ANISOU 297 O ILE A 61 7261 14032 15072 -1862 -1064 1539 O
ATOM 298 CB ILE A 61 -10.485 -40.522 38.120 1.00 97.79 C
ANISOU 298 CB ILE A 61 7067 14425 15663 -1845 -1028 1986 C
ATOM 299 CG1 ILE A 61 -10.164 -41.277 39.449 1.00 98.07 C
ANISOU 299 CG1 ILE A 61 6980 14496 15787 -1799 -938 2085 C
ATOM 300 CG2 ILE A 61 -10.770 -41.506 36.973 1.00 99.94 C
ANISOU 300 CG2 ILE A 61 7422 14530 16021 -1993 -1225 1943 C
ATOM 301 CD1 ILE A 61 -8.808 -42.084 39.554 1.00103.75 C
ANISOU 301 CD1 ILE A 61 7809 15119 16491 -1805 -891 1939 C
ATOM 302 N PHE A 62 -10.585 -37.701 36.440 1.00 92.42 N
ANISOU 302 N PHE A 62 6607 13841 14667 -1767 -991 1783 N
ATOM 303 CA PHE A 62 -10.953 -36.903 35.266 1.00 92.03 C
ANISOU 303 CA PHE A 62 6655 13779 14535 -1797 -1063 1714 C
ATOM 304 C PHE A 62 -9.741 -36.121 34.728 1.00 92.98 C
ANISOU 304 C PHE A 62 6959 13884 14487 -1741 -974 1506 C
ATOM 305 O PHE A 62 -9.588 -36.041 33.509 1.00 92.67 O
ANISOU 305 O PHE A 62 7060 13763 14388 -1794 -1054 1390 O
ATOM 306 CB PHE A 62 -12.112 -35.942 35.595 1.00 94.37 C
ANISOU 306 CB PHE A 62 6816 14207 14835 -1745 -1042 1875 C
ATOM 307 CG PHE A 62 -12.591 -35.088 34.442 1.00 96.41 C
ANISOU 307 CG PHE A 62 7152 14463 15016 -1774 -1115 1827 C
ATOM 308 CD1 PHE A 62 -13.441 -35.611 33.473 1.00101.13 C
ANISOU 308 CD1 PHE A 62 7752 14979 15695 -1900 -1303 1871 C
ATOM 309 CD2 PHE A 62 -12.222 -33.751 34.345 1.00 97.77 C
ANISOU 309 CD2 PHE A 62 7395 14715 15039 -1677 -1006 1747 C
ATOM 310 CE1 PHE A 62 -13.889 -34.819 32.411 1.00102.41 C
ANISOU 310 CE1 PHE A 62 7986 15142 15782 -1926 -1374 1831 C
ATOM 311 CE2 PHE A 62 -12.671 -32.960 33.283 1.00101.01 C
ANISOU 311 CE2 PHE A 62 7871 15126 15381 -1702 -1070 1709 C
ATOM 312 CZ PHE A 62 -13.504 -33.498 32.326 1.00100.46 C
ANISOU 312 CZ PHE A 62 7801 14981 15386 -1824 -1250 1752 C
ATOM 313 N ILE A 63 -8.891 -35.557 35.627 1.00 87.20 N
ANISOU 313 N ILE A 63 6227 13225 13681 -1634 -817 1469 N
ATOM 314 CA ILE A 63 -7.679 -34.802 35.259 1.00 85.35 C
ANISOU 314 CA ILE A 63 6142 12981 13306 -1580 -729 1299 C
ATOM 315 C ILE A 63 -6.695 -35.747 34.538 1.00 88.76 C
ANISOU 315 C ILE A 63 6708 13277 13740 -1637 -764 1164 C
ATOM 316 O ILE A 63 -6.150 -35.382 33.496 1.00 87.79 O
ANISOU 316 O ILE A 63 6732 13100 13525 -1643 -773 1034 O
ATOM 317 CB ILE A 63 -7.018 -34.117 36.494 1.00 87.20 C
ANISOU 317 CB ILE A 63 6339 13311 13482 -1465 -580 1310 C
ATOM 318 CG1 ILE A 63 -7.970 -33.102 37.166 1.00 87.21 C
ANISOU 318 CG1 ILE A 63 6242 13440 13454 -1384 -537 1433 C
ATOM 319 CG2 ILE A 63 -5.697 -33.433 36.105 1.00 87.00 C
ANISOU 319 CG2 ILE A 63 6458 13261 13338 -1426 -508 1151 C
ATOM 320 CD1 ILE A 63 -7.572 -32.678 38.583 1.00 92.13 C
ANISOU 320 CD1 ILE A 63 6816 14151 14039 -1267 -411 1481 C
ATOM 321 N MET A 64 -6.522 -36.972 35.075 1.00 85.79 N
ANISOU 321 N MET A 64 6281 12844 13471 -1674 -782 1206 N
ATOM 322 CA MET A 64 -5.640 -38.012 34.536 1.00 85.83 C
ANISOU 322 CA MET A 64 6404 12715 13491 -1716 -807 1098 C
ATOM 323 C MET A 64 -6.177 -38.614 33.220 1.00 92.68 C
ANISOU 323 C MET A 64 7381 13458 14375 -1812 -968 1051 C
ATOM 324 O MET A 64 -5.448 -39.357 32.561 1.00 93.14 O
ANISOU 324 O MET A 64 7580 13393 14415 -1832 -991 943 O
ATOM 325 CB MET A 64 -5.427 -39.129 35.571 1.00 87.98 C
ANISOU 325 CB MET A 64 6578 12968 13883 -1725 -782 1174 C
ATOM 326 CG MET A 64 -4.513 -38.725 36.709 1.00 89.99 C
ANISOU 326 CG MET A 64 6782 13308 14102 -1632 -628 1177 C
ATOM 327 SD MET A 64 -4.420 -39.931 38.055 1.00 94.04 S
ANISOU 327 SD MET A 64 7153 13824 14754 -1633 -595 1294 S
ATOM 328 CE MET A 64 -3.538 -41.253 37.262 1.00 91.27 C
ANISOU 328 CE MET A 64 6939 13297 14442 -1696 -640 1178 C
ATOM 329 N LEU A 65 -7.426 -38.284 32.833 1.00 90.31 N
ANISOU 329 N LEU A 65 7026 13184 14105 -1863 -1080 1134 N
ATOM 330 CA LEU A 65 -8.038 -38.768 31.602 1.00 91.58 C
ANISOU 330 CA LEU A 65 7290 13228 14279 -1961 -1258 1100 C
ATOM 331 C LEU A 65 -8.153 -37.658 30.541 1.00 95.02 C
ANISOU 331 C LEU A 65 7836 13688 14579 -1942 -1273 1018 C
ATOM 332 O LEU A 65 -7.836 -37.912 29.378 1.00 95.14 O
ANISOU 332 O LEU A 65 8036 13592 14520 -1970 -1346 894 O
ATOM 333 CB LEU A 65 -9.418 -39.360 31.897 1.00 93.17 C
ANISOU 333 CB LEU A 65 7334 13428 14641 -2053 -1403 1281 C
ATOM 334 CG LEU A 65 -9.446 -40.861 32.088 1.00 99.36 C
ANISOU 334 CG LEU A 65 8106 14085 15562 -2135 -1506 1319 C
ATOM 335 CD1 LEU A 65 -9.162 -41.285 33.501 1.00 99.15 C
ANISOU 335 CD1 LEU A 65 7918 14126 15629 -2088 -1389 1420 C
ATOM 336 CD2 LEU A 65 -10.769 -41.422 31.631 1.00103.69 C
ANISOU 336 CD2 LEU A 65 8591 14568 16236 -2261 -1723 1444 C
ATOM 337 N ALA A 66 -8.605 -36.446 30.937 1.00 90.70 N
ANISOU 337 N ALA A 66 7188 13282 13992 -1886 -1201 1086 N
ATOM 338 CA ALA A 66 -8.785 -35.300 30.038 1.00 90.17 C
ANISOU 338 CA ALA A 66 7202 13253 13805 -1864 -1206 1027 C
ATOM 339 C ALA A 66 -7.439 -34.743 29.545 1.00 93.01 C
ANISOU 339 C ALA A 66 7723 13596 14021 -1788 -1089 859 C
ATOM 340 O ALA A 66 -7.317 -34.426 28.360 1.00 92.90 O
ANISOU 340 O ALA A 66 7854 13532 13911 -1796 -1136 762 O
ATOM 341 CB ALA A 66 -9.580 -34.205 30.733 1.00 90.42 C
ANISOU 341 CB ALA A 66 7079 13435 13840 -1812 -1147 1154 C
ATOM 342 N ASN A 67 -6.438 -34.628 30.443 1.00 88.51 N
ANISOU 342 N ASN A 67 7123 13068 13440 -1715 -943 838 N
ATOM 343 CA ASN A 67 -5.109 -34.118 30.089 1.00 87.43 C
ANISOU 343 CA ASN A 67 7110 12919 13190 -1644 -828 710 C
ATOM 344 C ASN A 67 -4.292 -35.175 29.338 1.00 91.86 C
ANISOU 344 C ASN A 67 7824 13341 13737 -1663 -851 604 C
ATOM 345 O ASN A 67 -3.388 -34.816 28.584 1.00 91.12 O
ANISOU 345 O ASN A 67 7865 13217 13541 -1614 -789 500 O
ATOM 346 CB ASN A 67 -4.358 -33.641 31.317 1.00 86.38 C
ANISOU 346 CB ASN A 67 6890 12871 13058 -1568 -684 737 C
ATOM 347 CG ASN A 67 -4.945 -32.386 31.901 1.00105.81 C
ANISOU 347 CG ASN A 67 9258 15459 15488 -1518 -641 809 C
ATOM 348 OD1 ASN A 67 -4.543 -31.268 31.555 1.00 98.04 O
ANISOU 348 OD1 ASN A 67 8332 14514 14406 -1468 -586 754 O
ATOM 349 ND2 ASN A 67 -5.936 -32.543 32.769 1.00 97.03 N
ANISOU 349 ND2 ASN A 67 8002 14409 14457 -1526 -667 941 N
ATOM 350 N LEU A 68 -4.618 -36.467 29.528 1.00 89.22 N
ANISOU 350 N LEU A 68 7473 12922 13506 -1728 -938 639 N
ATOM 351 CA LEU A 68 -3.960 -37.569 28.821 1.00 89.65 C
ANISOU 351 CA LEU A 68 7686 12828 13548 -1743 -974 543 C
ATOM 352 C LEU A 68 -4.469 -37.623 27.378 1.00 93.92 C
ANISOU 352 C LEU A 68 8395 13277 14015 -1785 -1112 470 C
ATOM 353 O LEU A 68 -3.705 -37.946 26.469 1.00 94.06 O
ANISOU 353 O LEU A 68 8602 13197 13940 -1746 -1097 355 O
ATOM 354 CB LEU A 68 -4.212 -38.907 29.543 1.00 90.30 C
ANISOU 354 CB LEU A 68 7693 12844 13773 -1801 -1033 611 C
ATOM 355 CG LEU A 68 -3.377 -40.120 29.100 1.00 95.66 C
ANISOU 355 CG LEU A 68 8524 13371 14450 -1797 -1038 521 C
ATOM 356 CD1 LEU A 68 -1.949 -40.043 29.638 1.00 94.98 C
ANISOU 356 CD1 LEU A 68 8443 13315 14329 -1702 -852 480 C
ATOM 357 CD2 LEU A 68 -4.013 -41.408 29.575 1.00 98.84 C
ANISOU 357 CD2 LEU A 68 8863 13691 15002 -1883 -1157 598 C
ATOM 358 N LEU A 69 -5.759 -37.289 27.179 1.00 90.19 N
ANISOU 358 N LEU A 69 7854 12837 13578 -1856 -1244 547 N
ATOM 359 CA LEU A 69 -6.435 -37.280 25.881 1.00 90.88 C
ANISOU 359 CA LEU A 69 8079 12847 13603 -1910 -1401 500 C
ATOM 360 C LEU A 69 -5.869 -36.185 24.963 1.00 93.82 C
ANISOU 360 C LEU A 69 8582 13256 13809 -1831 -1320 397 C
ATOM 361 O LEU A 69 -5.707 -36.432 23.767 1.00 94.54 O
ANISOU 361 O LEU A 69 8875 13244 13802 -1827 -1389 295 O
ATOM 362 CB LEU A 69 -7.952 -37.075 26.089 1.00 91.33 C
ANISOU 362 CB LEU A 69 7981 12962 13759 -2000 -1540 644 C
ATOM 363 CG LEU A 69 -8.885 -37.288 24.896 1.00 97.19 C
ANISOU 363 CG LEU A 69 8830 13611 14485 -2093 -1756 636 C
ATOM 364 CD1 LEU A 69 -9.047 -38.766 24.568 1.00 98.86 C
ANISOU 364 CD1 LEU A 69 9089 13667 14808 -2197 -1940 659 C
ATOM 365 CD2 LEU A 69 -10.261 -36.693 25.170 1.00 99.64 C
ANISOU 365 CD2 LEU A 69 8967 14034 14857 -2140 -1823 784 C
ATOM 366 N VAL A 70 -5.575 -34.987 25.515 1.00 88.33 N
ANISOU 366 N VAL A 70 7780 12701 13081 -1763 -1177 427 N
ATOM 367 CA VAL A 70 -5.045 -33.859 24.741 1.00 87.15 C
ANISOU 367 CA VAL A 70 7724 12598 12791 -1689 -1093 351 C
ATOM 368 C VAL A 70 -3.539 -34.114 24.429 1.00 89.28 C
ANISOU 368 C VAL A 70 8128 12811 12984 -1602 -961 247 C
ATOM 369 O VAL A 70 -3.065 -33.660 23.388 1.00 88.88 O
ANISOU 369 O VAL A 70 8221 12738 12810 -1547 -929 166 O
ATOM 370 CB VAL A 70 -5.304 -32.485 25.431 1.00 89.93 C
ANISOU 370 CB VAL A 70 7923 13107 13141 -1651 -1004 425 C
ATOM 371 CG1 VAL A 70 -4.531 -32.328 26.736 1.00 88.55 C
ANISOU 371 CG1 VAL A 70 7632 12999 13013 -1595 -858 461 C
ATOM 372 CG2 VAL A 70 -5.038 -31.314 24.487 1.00 89.45 C
ANISOU 372 CG2 VAL A 70 7955 13085 12948 -1597 -960 362 C
ATOM 373 N MET A 71 -2.822 -34.878 25.288 1.00 84.84 N
ANISOU 373 N MET A 71 7517 12223 12494 -1585 -886 259 N
ATOM 374 CA MET A 71 -1.409 -35.224 25.074 1.00 84.17 C
ANISOU 374 CA MET A 71 7539 12085 12355 -1502 -756 186 C
ATOM 375 C MET A 71 -1.254 -36.197 23.903 1.00 89.27 C
ANISOU 375 C MET A 71 8407 12580 12932 -1494 -829 91 C
ATOM 376 O MET A 71 -0.285 -36.087 23.152 1.00 88.80 O
ANISOU 376 O MET A 71 8488 12484 12767 -1402 -733 20 O
ATOM 377 CB MET A 71 -0.777 -35.819 26.338 1.00 85.78 C
ANISOU 377 CB MET A 71 7623 12304 12665 -1493 -670 237 C
ATOM 378 CG MET A 71 -0.296 -34.769 27.311 1.00 87.97 C
ANISOU 378 CG MET A 71 7757 12712 12956 -1449 -545 292 C
ATOM 379 SD MET A 71 0.752 -35.424 28.633 1.00 91.47 S
ANISOU 379 SD MET A 71 8100 13162 13495 -1420 -430 335 S
ATOM 380 CE MET A 71 -0.462 -36.198 29.679 1.00 88.53 C
ANISOU 380 CE MET A 71 7578 12803 13256 -1506 -536 431 C
ATOM 381 N VAL A 72 -2.213 -37.134 23.745 1.00 87.16 N
ANISOU 381 N VAL A 72 8173 12219 12724 -1584 -1001 100 N
ATOM 382 CA VAL A 72 -2.239 -38.117 22.656 1.00 88.42 C
ANISOU 382 CA VAL A 72 8564 12214 12818 -1588 -1109 8 C
ATOM 383 C VAL A 72 -2.645 -37.386 21.362 1.00 92.97 C
ANISOU 383 C VAL A 72 9286 12783 13253 -1572 -1178 -53 C
ATOM 384 O VAL A 72 -2.068 -37.658 20.308 1.00 93.35 O
ANISOU 384 O VAL A 72 9558 12738 13171 -1495 -1160 -152 O
ATOM 385 CB VAL A 72 -3.170 -39.328 22.978 1.00 93.18 C
ANISOU 385 CB VAL A 72 9146 12712 13547 -1705 -1295 50 C
ATOM 386 CG1 VAL A 72 -3.327 -40.263 21.782 1.00 94.74 C
ANISOU 386 CG1 VAL A 72 9610 12721 13664 -1715 -1442 -52 C
ATOM 387 CG2 VAL A 72 -2.659 -40.110 24.183 1.00 92.46 C
ANISOU 387 CG2 VAL A 72 8926 12621 13584 -1707 -1214 106 C
ATOM 388 N ALA A 73 -3.601 -36.432 21.465 1.00 89.30 N
ANISOU 388 N ALA A 73 8695 12423 12810 -1632 -1244 13 N
ATOM 389 CA ALA A 73 -4.134 -35.623 20.361 1.00 89.87 C
ANISOU 389 CA ALA A 73 8868 12511 12767 -1631 -1318 -23 C
ATOM 390 C ALA A 73 -3.038 -34.833 19.627 1.00 93.79 C
ANISOU 390 C ALA A 73 9480 13042 13112 -1499 -1154 -97 C
ATOM 391 O ALA A 73 -3.051 -34.785 18.399 1.00 94.15 O
ANISOU 391 O ALA A 73 9725 13023 13025 -1462 -1206 -175 O
ATOM 392 CB ALA A 73 -5.191 -34.660 20.886 1.00 89.95 C
ANISOU 392 CB ALA A 73 8675 12652 12848 -1700 -1368 86 C
ATOM 393 N ILE A 74 -2.097 -34.233 20.375 1.00 89.72 N
ANISOU 393 N ILE A 74 8843 12626 12620 -1429 -963 -65 N
ATOM 394 CA ILE A 74 -0.981 -33.444 19.839 1.00 89.44 C
ANISOU 394 CA ILE A 74 8877 12634 12472 -1308 -797 -104 C
ATOM 395 C ILE A 74 0.065 -34.398 19.206 1.00 95.29 C
ANISOU 395 C ILE A 74 9816 13255 13137 -1214 -726 -181 C
ATOM 396 O ILE A 74 0.665 -34.060 18.180 1.00 95.29 O
ANISOU 396 O ILE A 74 9969 13235 13000 -1113 -655 -234 O
ATOM 397 CB ILE A 74 -0.381 -32.550 20.971 1.00 90.80 C
ANISOU 397 CB ILE A 74 8844 12938 12717 -1283 -647 -29 C
ATOM 398 CG1 ILE A 74 -1.413 -31.476 21.409 1.00 90.48 C
ANISOU 398 CG1 ILE A 74 8652 13012 12715 -1345 -705 37 C
ATOM 399 CG2 ILE A 74 0.950 -31.894 20.552 1.00 90.95 C
ANISOU 399 CG2 ILE A 74 8916 12989 12654 -1163 -471 -47 C
ATOM 400 CD1 ILE A 74 -1.189 -30.844 22.780 1.00 96.86 C
ANISOU 400 CD1 ILE A 74 9257 13925 13619 -1348 -615 118 C
ATOM 401 N TYR A 75 0.236 -35.592 19.800 1.00 93.01 N
ANISOU 401 N TYR A 75 9524 12883 12932 -1239 -744 -181 N
ATOM 402 CA TYR A 75 1.181 -36.629 19.379 1.00 94.14 C
ANISOU 402 CA TYR A 75 9842 12906 13023 -1149 -674 -241 C
ATOM 403 C TYR A 75 0.786 -37.279 18.032 1.00100.69 C
ANISOU 403 C TYR A 75 10953 13588 13719 -1126 -803 -342 C
ATOM 404 O TYR A 75 1.680 -37.549 17.226 1.00101.07 O
ANISOU 404 O TYR A 75 11192 13567 13642 -994 -703 -402 O
ATOM 405 CB TYR A 75 1.284 -37.704 20.483 1.00 95.22 C
ANISOU 405 CB TYR A 75 9878 12998 13304 -1201 -680 -203 C
ATOM 406 CG TYR A 75 2.025 -38.971 20.109 1.00 98.34 C
ANISOU 406 CG TYR A 75 10455 13249 13660 -1121 -634 -262 C
ATOM 407 CD1 TYR A 75 3.417 -39.011 20.105 1.00 99.96 C
ANISOU 407 CD1 TYR A 75 10684 13469 13827 -989 -428 -255 C
ATOM 408 CD2 TYR A 75 1.338 -40.152 19.842 1.00100.76 C
ANISOU 408 CD2 TYR A 75 10899 13402 13983 -1179 -798 -312 C
ATOM 409 CE1 TYR A 75 4.105 -40.182 19.786 1.00101.96 C
ANISOU 409 CE1 TYR A 75 11104 13591 14043 -900 -371 -299 C
ATOM 410 CE2 TYR A 75 2.014 -41.328 19.524 1.00102.92 C
ANISOU 410 CE2 TYR A 75 11354 13533 14216 -1096 -755 -369 C
ATOM 411 CZ TYR A 75 3.399 -41.340 19.500 1.00109.83 C
ANISOU 411 CZ TYR A 75 12257 14432 15043 -950 -532 -362 C
ATOM 412 OH TYR A 75 4.067 -42.501 19.193 1.00112.09 O
ANISOU 412 OH TYR A 75 12724 14579 15285 -853 -475 -409 O
ATOM 413 N VAL A 76 -0.520 -37.548 17.796 1.00 98.62 N
ANISOU 413 N VAL A 76 10719 13271 13479 -1246 -1025 -353 N
ATOM 414 CA VAL A 76 -0.977 -38.228 16.571 1.00100.54 C
ANISOU 414 CA VAL A 76 11242 13357 13601 -1240 -1185 -450 C
ATOM 415 C VAL A 76 -1.265 -37.237 15.413 1.00105.28 C
ANISOU 415 C VAL A 76 11960 13997 14047 -1200 -1217 -490 C
ATOM 416 O VAL A 76 -1.000 -37.589 14.261 1.00106.25 O
ANISOU 416 O VAL A 76 12355 14008 14007 -1111 -1244 -583 O
ATOM 417 CB VAL A 76 -2.205 -39.162 16.784 1.00105.36 C
ANISOU 417 CB VAL A 76 11858 13857 14318 -1396 -1439 -439 C
ATOM 418 CG1 VAL A 76 -1.830 -40.394 17.602 1.00105.28 C
ANISOU 418 CG1 VAL A 76 11818 13759 14424 -1412 -1421 -427 C
ATOM 419 CG2 VAL A 76 -3.402 -38.431 17.399 1.00104.35 C
ANISOU 419 CG2 VAL A 76 11489 13846 14313 -1538 -1554 -335 C
ATOM 420 N ASN A 77 -1.812 -36.037 15.700 1.00101.10 N
ANISOU 420 N ASN A 77 11239 13617 13559 -1256 -1214 -419 N
ATOM 421 CA ASN A 77 -2.155 -35.060 14.663 1.00101.47 C
ANISOU 421 CA ASN A 77 11372 13710 13473 -1228 -1248 -445 C
ATOM 422 C ASN A 77 -0.903 -34.340 14.148 1.00104.62 C
ANISOU 422 C ASN A 77 11838 14167 13744 -1060 -1022 -468 C
ATOM 423 O ASN A 77 -0.080 -33.876 14.940 1.00102.42 O
ANISOU 423 O ASN A 77 11396 13986 13535 -1015 -841 -409 O
ATOM 424 CB ASN A 77 -3.183 -34.054 15.180 1.00102.78 C
ANISOU 424 CB ASN A 77 11310 14010 13733 -1341 -1320 -353 C
ATOM 425 CG ASN A 77 -3.886 -33.267 14.101 1.00131.35 C
ANISOU 425 CG ASN A 77 15020 17652 17233 -1347 -1417 -374 C
ATOM 426 OD1 ASN A 77 -3.320 -32.363 13.480 1.00126.65 O
ANISOU 426 OD1 ASN A 77 14478 17122 16522 -1243 -1291 -395 O
ATOM 427 ND2 ASN A 77 -5.159 -33.570 13.888 1.00124.82 N
ANISOU 427 ND2 ASN A 77 14197 16781 16448 -1475 -1647 -352 N
ATOM 428 N ARG A 78 -0.785 -34.255 12.808 1.00102.73 N
ANISOU 428 N ARG A 78 11845 13866 13321 -969 -1043 -544 N
ATOM 429 CA ARG A 78 0.326 -33.650 12.072 1.00102.67 C
ANISOU 429 CA ARG A 78 11940 13898 13171 -796 -845 -560 C
ATOM 430 C ARG A 78 0.408 -32.126 12.267 1.00105.33 C
ANISOU 430 C ARG A 78 12078 14410 13533 -793 -738 -482 C
ATOM 431 O ARG A 78 1.513 -31.598 12.405 1.00103.87 O
ANISOU 431 O ARG A 78 11829 14294 13342 -686 -533 -438 O
ATOM 432 CB ARG A 78 0.204 -33.965 10.573 1.00104.87 C
ANISOU 432 CB ARG A 78 12543 14063 13239 -708 -929 -659 C
ATOM 433 N ARG A 79 -0.747 -31.428 12.272 1.00102.20 N
ANISOU 433 N ARG A 79 11583 14079 13171 -908 -878 -455 N
ATOM 434 CA ARG A 79 -0.834 -29.968 12.408 1.00101.05 C
ANISOU 434 CA ARG A 79 11264 14086 13044 -910 -800 -386 C
ATOM 435 C ARG A 79 -0.419 -29.467 13.809 1.00103.71 C
ANISOU 435 C ARG A 79 11332 14530 13544 -946 -681 -297 C
ATOM 436 O ARG A 79 -0.112 -28.281 13.950 1.00102.21 O
ANISOU 436 O ARG A 79 11019 14453 13363 -917 -579 -243 O
ATOM 437 CB ARG A 79 -2.261 -29.487 12.095 1.00101.75 C
ANISOU 437 CB ARG A 79 11323 14204 13132 -1025 -991 -374 C
ATOM 438 N PHE A 80 -0.400 -30.352 14.830 1.00100.50 N
ANISOU 438 N PHE A 80 10840 14084 13262 -1005 -700 -282 N
ATOM 439 CA PHE A 80 -0.037 -29.961 16.193 1.00 98.98 C
ANISOU 439 CA PHE A 80 10411 13983 13213 -1036 -601 -202 C
ATOM 440 C PHE A 80 1.448 -30.285 16.519 1.00103.62 C
ANISOU 440 C PHE A 80 11004 14556 13812 -932 -415 -192 C
ATOM 441 O PHE A 80 1.811 -30.373 17.696 1.00102.25 O
ANISOU 441 O PHE A 80 10670 14420 13761 -961 -355 -139 O
ATOM 442 CB PHE A 80 -0.981 -30.611 17.228 1.00100.40 C
ANISOU 442 CB PHE A 80 10462 14151 13534 -1165 -730 -167 C
ATOM 443 CG PHE A 80 -2.436 -30.203 17.107 1.00102.02 C
ANISOU 443 CG PHE A 80 10611 14391 13761 -1271 -899 -137 C
ATOM 444 CD1 PHE A 80 -2.796 -28.865 16.985 1.00104.26 C
ANISOU 444 CD1 PHE A 80 10803 14789 14022 -1269 -875 -94 C
ATOM 445 CD2 PHE A 80 -3.448 -31.150 17.180 1.00105.02 C
ANISOU 445 CD2 PHE A 80 11012 14691 14198 -1375 -1082 -136 C
ATOM 446 CE1 PHE A 80 -4.137 -28.488 16.877 1.00105.31 C
ANISOU 446 CE1 PHE A 80 10876 14959 14180 -1359 -1021 -52 C
ATOM 447 CE2 PHE A 80 -4.789 -30.772 17.067 1.00108.05 C
ANISOU 447 CE2 PHE A 80 11327 15112 14617 -1473 -1239 -84 C
ATOM 448 CZ PHE A 80 -5.123 -29.443 16.920 1.00105.38 C
ANISOU 448 CZ PHE A 80 10901 14891 14246 -1460 -1201 -42 C
ATOM 449 N HIS A 81 2.312 -30.397 15.485 1.00101.71 N
ANISOU 449 N HIS A 81 10941 14264 13441 -804 -321 -232 N
ATOM 450 CA HIS A 81 3.745 -30.637 15.678 1.00101.63 C
ANISOU 450 CA HIS A 81 10933 14245 13436 -689 -133 -201 C
ATOM 451 C HIS A 81 4.504 -29.301 15.536 1.00103.61 C
ANISOU 451 C HIS A 81 11091 14605 13672 -618 11 -129 C
ATOM 452 O HIS A 81 5.350 -29.140 14.652 1.00103.89 O
ANISOU 452 O HIS A 81 11241 14629 13602 -487 128 -123 O
ATOM 453 CB HIS A 81 4.283 -31.711 14.708 1.00104.51 C
ANISOU 453 CB HIS A 81 11551 14480 13677 -573 -100 -270 C
ATOM 454 CG HIS A 81 3.791 -33.101 14.987 1.00109.09 C
ANISOU 454 CG HIS A 81 12217 14938 14294 -633 -221 -329 C
ATOM 455 ND1 HIS A 81 3.141 -33.843 14.019 1.00112.71 N
ANISOU 455 ND1 HIS A 81 12915 15272 14636 -630 -363 -425 N
ATOM 456 CD2 HIS A 81 3.875 -33.842 16.118 1.00110.51 C
ANISOU 456 CD2 HIS A 81 12275 15099 14615 -701 -227 -301 C
ATOM 457 CE1 HIS A 81 2.858 -35.006 14.585 1.00112.59 C
ANISOU 457 CE1 HIS A 81 12916 15161 14703 -697 -453 -450 C
ATOM 458 NE2 HIS A 81 3.274 -35.049 15.850 1.00111.60 N
ANISOU 458 NE2 HIS A 81 12572 15099 14733 -740 -370 -376 N
ATOM 459 N PHE A 82 4.177 -28.342 16.422 1.00 98.12 N
ANISOU 459 N PHE A 82 10190 14012 13081 -702 -4 -69 N
ATOM 460 CA PHE A 82 4.773 -27.004 16.460 1.00 96.85 C
ANISOU 460 CA PHE A 82 9918 13949 12931 -663 101 5 C
ATOM 461 C PHE A 82 5.194 -26.621 17.897 1.00 97.87 C
ANISOU 461 C PHE A 82 9836 14138 13211 -718 147 82 C
ATOM 462 O PHE A 82 4.542 -27.073 18.846 1.00 96.71 O
ANISOU 462 O PHE A 82 9606 13989 13149 -811 61 73 O
ATOM 463 CB PHE A 82 3.794 -25.966 15.890 1.00 98.70 C
ANISOU 463 CB PHE A 82 10150 14243 13108 -705 10 -7 C
ATOM 464 CG PHE A 82 3.708 -25.980 14.384 1.00101.84 C
ANISOU 464 CG PHE A 82 10747 14604 13344 -622 4 -58 C
ATOM 465 CD1 PHE A 82 4.597 -25.237 13.613 1.00105.50 C
ANISOU 465 CD1 PHE A 82 11240 15109 13737 -512 132 -13 C
ATOM 466 CD2 PHE A 82 2.746 -26.744 13.732 1.00105.35 C
ANISOU 466 CD2 PHE A 82 11352 14971 13707 -655 -139 -144 C
ATOM 467 CE1 PHE A 82 4.519 -25.249 12.217 1.00107.84 C
ANISOU 467 CE1 PHE A 82 11729 15375 13871 -422 133 -56 C
ATOM 468 CE2 PHE A 82 2.665 -26.753 12.335 1.00109.72 C
ANISOU 468 CE2 PHE A 82 12112 15483 14095 -570 -153 -196 C
ATOM 469 CZ PHE A 82 3.552 -26.005 11.588 1.00108.07 C
ANISOU 469 CZ PHE A 82 11932 15323 13805 -450 -11 -153 C
ATOM 470 N PRO A 83 6.256 -25.777 18.072 1.00 92.87 N
ANISOU 470 N PRO A 83 9116 13558 12613 -661 272 164 N
ATOM 471 CA PRO A 83 6.733 -25.422 19.428 1.00 91.11 C
ANISOU 471 CA PRO A 83 8712 13379 12526 -711 302 236 C
ATOM 472 C PRO A 83 5.655 -24.979 20.433 1.00 92.72 C
ANISOU 472 C PRO A 83 8799 13633 12796 -823 186 229 C
ATOM 473 O PRO A 83 5.798 -25.281 21.618 1.00 91.74 O
ANISOU 473 O PRO A 83 8569 13516 12770 -869 180 258 O
ATOM 474 CB PRO A 83 7.697 -24.250 19.175 1.00 92.73 C
ANISOU 474 CB PRO A 83 8858 13636 12739 -651 405 324 C
ATOM 475 CG PRO A 83 7.597 -23.929 17.709 1.00 98.30 C
ANISOU 475 CG PRO A 83 9704 14336 13311 -568 435 299 C
ATOM 476 CD PRO A 83 7.142 -25.183 17.051 1.00 94.96 C
ANISOU 476 CD PRO A 83 9448 13833 12800 -544 393 207 C
ATOM 477 N ILE A 84 4.597 -24.279 19.981 1.00 87.88 N
ANISOU 477 N ILE A 84 8206 13058 12128 -858 100 199 N
ATOM 478 CA ILE A 84 3.524 -23.793 20.855 1.00 86.24 C
ANISOU 478 CA ILE A 84 7894 12902 11970 -943 2 206 C
ATOM 479 C ILE A 84 2.658 -24.976 21.369 1.00 88.47 C
ANISOU 479 C ILE A 84 8174 13147 12293 -1010 -91 173 C
ATOM 480 O ILE A 84 2.320 -24.997 22.556 1.00 87.43 O
ANISOU 480 O ILE A 84 7926 13046 12246 -1060 -120 206 O
ATOM 481 CB ILE A 84 2.654 -22.688 20.165 1.00 89.54 C
ANISOU 481 CB ILE A 84 8330 13373 12319 -951 -54 199 C
ATOM 482 CG1 ILE A 84 1.497 -22.176 21.068 1.00 89.41 C
ANISOU 482 CG1 ILE A 84 8206 13414 12351 -1023 -142 221 C
ATOM 483 CG2 ILE A 84 2.141 -23.090 18.767 1.00 91.61 C
ANISOU 483 CG2 ILE A 84 8745 13594 12468 -931 -104 138 C
ATOM 484 CD1 ILE A 84 1.910 -21.522 22.389 1.00 96.61 C
ANISOU 484 CD1 ILE A 84 8995 14369 13345 -1030 -105 276 C
ATOM 485 N TYR A 85 2.330 -25.949 20.500 1.00 84.58 N
ANISOU 485 N TYR A 85 7813 12583 11742 -1006 -142 113 N
ATOM 486 CA TYR A 85 1.488 -27.091 20.865 1.00 83.94 C
ANISOU 486 CA TYR A 85 7736 12451 11705 -1077 -248 89 C
ATOM 487 C TYR A 85 2.242 -28.118 21.727 1.00 85.98 C
ANISOU 487 C TYR A 85 7957 12664 12047 -1074 -194 101 C
ATOM 488 O TYR A 85 1.596 -28.811 22.516 1.00 84.95 O
ANISOU 488 O TYR A 85 7760 12522 11996 -1142 -268 115 O
ATOM 489 CB TYR A 85 0.906 -27.767 19.618 1.00 86.17 C
ANISOU 489 CB TYR A 85 8192 12655 11894 -1079 -342 19 C
ATOM 490 CG TYR A 85 -0.053 -26.877 18.857 1.00 87.84 C
ANISOU 490 CG TYR A 85 8426 12912 12038 -1104 -426 15 C
ATOM 491 CD1 TYR A 85 -1.337 -26.634 19.329 1.00 89.59 C
ANISOU 491 CD1 TYR A 85 8546 13179 12316 -1193 -542 52 C
ATOM 492 CD2 TYR A 85 0.330 -26.274 17.661 1.00 89.08 C
ANISOU 492 CD2 TYR A 85 8701 13071 12075 -1029 -381 -15 C
ATOM 493 CE1 TYR A 85 -2.219 -25.809 18.635 1.00 90.76 C
ANISOU 493 CE1 TYR A 85 8705 13372 12408 -1214 -616 60 C
ATOM 494 CE2 TYR A 85 -0.546 -25.449 16.956 1.00 90.20 C
ANISOU 494 CE2 TYR A 85 8861 13257 12154 -1052 -459 -16 C
ATOM 495 CZ TYR A 85 -1.821 -25.222 17.445 1.00 97.64 C
ANISOU 495 CZ TYR A 85 9699 14242 13159 -1147 -578 21 C
ATOM 496 OH TYR A 85 -2.691 -24.415 16.751 1.00 99.27 O
ANISOU 496 OH TYR A 85 9917 14494 13309 -1167 -652 31 O
ATOM 497 N TYR A 86 3.587 -28.205 21.601 1.00 81.94 N
ANISOU 497 N TYR A 86 7477 12130 11526 -994 -65 112 N
ATOM 498 CA TYR A 86 4.400 -29.116 22.419 1.00 81.23 C
ANISOU 498 CA TYR A 86 7345 12002 11518 -985 -2 134 C
ATOM 499 C TYR A 86 4.433 -28.639 23.876 1.00 81.53 C
ANISOU 499 C TYR A 86 7201 12112 11664 -1034 6 201 C
ATOM 500 O TYR A 86 4.454 -29.462 24.794 1.00 80.54 O
ANISOU 500 O TYR A 86 7015 11967 11621 -1068 -6 218 O
ATOM 501 CB TYR A 86 5.832 -29.250 21.872 1.00 83.47 C
ANISOU 501 CB TYR A 86 7697 12250 11766 -879 141 151 C
ATOM 502 CG TYR A 86 5.969 -30.142 20.656 1.00 87.52 C
ANISOU 502 CG TYR A 86 8412 12668 12176 -807 152 85 C
ATOM 503 CD1 TYR A 86 5.872 -31.527 20.767 1.00 90.43 C
ANISOU 503 CD1 TYR A 86 8859 12940 12560 -816 115 42 C
ATOM 504 CD2 TYR A 86 6.308 -29.612 19.414 1.00 89.17 C
ANISOU 504 CD2 TYR A 86 8740 12875 12266 -717 208 71 C
ATOM 505 CE1 TYR A 86 6.029 -32.355 19.656 1.00 92.81 C
ANISOU 505 CE1 TYR A 86 9373 13139 12754 -736 124 -24 C
ATOM 506 CE2 TYR A 86 6.464 -30.429 18.294 1.00 91.56 C
ANISOU 506 CE2 TYR A 86 9250 13084 12453 -631 225 10 C
ATOM 507 CZ TYR A 86 6.327 -31.801 18.420 1.00 99.48 C
ANISOU 507 CZ TYR A 86 10348 13984 13466 -639 179 -42 C
ATOM 508 OH TYR A 86 6.493 -32.607 17.321 1.00101.40 O
ANISOU 508 OH TYR A 86 10823 14122 13582 -543 191 -109 O
ATOM 509 N LEU A 87 4.423 -27.305 24.074 1.00 76.03 N
ANISOU 509 N LEU A 87 6432 11494 10961 -1033 20 237 N
ATOM 510 CA LEU A 87 4.411 -26.644 25.380 1.00 74.21 C
ANISOU 510 CA LEU A 87 6060 11329 10806 -1066 17 294 C
ATOM 511 C LEU A 87 3.055 -26.823 26.066 1.00 76.64 C
ANISOU 511 C LEU A 87 6306 11667 11145 -1132 -86 296 C
ATOM 512 O LEU A 87 3.002 -26.879 27.296 1.00 75.99 O
ANISOU 512 O LEU A 87 6123 11617 11132 -1154 -90 338 O
ATOM 513 CB LEU A 87 4.740 -25.152 25.215 1.00 73.80 C
ANISOU 513 CB LEU A 87 5982 11335 10725 -1039 48 325 C
ATOM 514 CG LEU A 87 6.160 -24.696 25.587 1.00 78.49 C
ANISOU 514 CG LEU A 87 6529 11930 11364 -1001 140 386 C
ATOM 515 CD1 LEU A 87 7.229 -25.348 24.707 1.00 79.58 C
ANISOU 515 CD1 LEU A 87 6741 12013 11483 -936 235 391 C
ATOM 516 CD2 LEU A 87 6.284 -23.196 25.468 1.00 80.61 C
ANISOU 516 CD2 LEU A 87 6771 12246 11611 -990 140 418 C
ATOM 517 N MET A 88 1.966 -26.926 25.270 1.00 72.47 N
ANISOU 517 N MET A 88 5838 11130 10566 -1159 -171 261 N
ATOM 518 CA MET A 88 0.598 -27.146 25.758 1.00 71.83 C
ANISOU 518 CA MET A 88 5693 11077 10521 -1222 -274 284 C
ATOM 519 C MET A 88 0.457 -28.561 26.316 1.00 74.83 C
ANISOU 519 C MET A 88 6051 11401 10979 -1262 -309 290 C
ATOM 520 O MET A 88 -0.253 -28.761 27.301 1.00 74.26 O
ANISOU 520 O MET A 88 5872 11367 10978 -1299 -351 346 O
ATOM 521 CB MET A 88 -0.440 -26.907 24.646 1.00 74.75 C
ANISOU 521 CB MET A 88 6135 11444 10823 -1246 -365 256 C
ATOM 522 CG MET A 88 -0.611 -25.455 24.276 1.00 77.96 C
ANISOU 522 CG MET A 88 6534 11919 11167 -1216 -345 267 C
ATOM 523 SD MET A 88 -1.842 -25.226 22.979 1.00 82.94 S
ANISOU 523 SD MET A 88 7243 12549 11721 -1248 -458 243 S
ATOM 524 CE MET A 88 -1.754 -23.473 22.770 1.00 79.12 C
ANISOU 524 CE MET A 88 6734 12150 11179 -1199 -401 265 C
ATOM 525 N ALA A 89 1.137 -29.536 25.680 1.00 71.23 N
ANISOU 525 N ALA A 89 5701 10856 10509 -1245 -288 240 N
ATOM 526 CA ALA A 89 1.153 -30.943 26.086 1.00 71.18 C
ANISOU 526 CA ALA A 89 5696 10777 10573 -1276 -316 239 C
ATOM 527 C ALA A 89 1.912 -31.116 27.397 1.00 73.19 C
ANISOU 527 C ALA A 89 5834 11063 10912 -1264 -235 291 C
ATOM 528 O ALA A 89 1.540 -31.963 28.211 1.00 72.88 O
ANISOU 528 O ALA A 89 5723 11010 10956 -1305 -272 326 O
ATOM 529 CB ALA A 89 1.784 -31.795 24.997 1.00 72.89 C
ANISOU 529 CB ALA A 89 6079 10885 10730 -1237 -298 168 C
ATOM 530 N ASN A 90 2.972 -30.301 27.600 1.00 68.36 N
ANISOU 530 N ASN A 90 5202 10490 10283 -1209 -132 306 N
ATOM 531 CA ASN A 90 3.789 -30.303 28.815 1.00 67.26 C
ANISOU 531 CA ASN A 90 4960 10380 10215 -1197 -63 359 C
ATOM 532 C ASN A 90 2.999 -29.690 29.974 1.00 70.47 C
ANISOU 532 C ASN A 90 5248 10871 10658 -1225 -106 413 C
ATOM 533 O ASN A 90 3.170 -30.110 31.121 1.00 69.79 O
ANISOU 533 O ASN A 90 5076 10800 10641 -1233 -91 458 O
ATOM 534 CB ASN A 90 5.105 -29.555 28.599 1.00 65.83 C
ANISOU 534 CB ASN A 90 4795 10209 10009 -1139 36 371 C
ATOM 535 CG ASN A 90 6.176 -29.921 29.601 1.00 79.78 C
ANISOU 535 CG ASN A 90 6487 11973 11854 -1126 104 424 C
ATOM 536 OD1 ASN A 90 6.511 -31.096 29.798 1.00 72.56 O
ANISOU 536 OD1 ASN A 90 5576 11005 10988 -1127 127 426 O
ATOM 537 ND2 ASN A 90 6.777 -28.921 30.218 1.00 69.37 N
ANISOU 537 ND2 ASN A 90 5103 10704 10550 -1115 132 471 N
ATOM 538 N LEU A 91 2.119 -28.710 29.661 1.00 66.69 N
ANISOU 538 N LEU A 91 4769 10445 10127 -1230 -154 412 N
ATOM 539 CA LEU A 91 1.229 -28.052 30.620 1.00 66.07 C
ANISOU 539 CA LEU A 91 4596 10444 10063 -1236 -189 466 C
ATOM 540 C LEU A 91 0.178 -29.064 31.091 1.00 72.27 C
ANISOU 540 C LEU A 91 5319 11226 10914 -1282 -255 506 C
ATOM 541 O LEU A 91 -0.192 -29.069 32.267 1.00 71.99 O
ANISOU 541 O LEU A 91 5188 11243 10924 -1275 -252 571 O
ATOM 542 CB LEU A 91 0.581 -26.807 29.977 1.00 65.70 C
ANISOU 542 CB LEU A 91 4579 10445 9941 -1224 -217 457 C
ATOM 543 CG LEU A 91 -0.384 -25.971 30.832 1.00 69.74 C
ANISOU 543 CG LEU A 91 5012 11038 10447 -1209 -242 515 C
ATOM 544 CD1 LEU A 91 0.341 -25.236 31.943 1.00 68.94 C
ANISOU 544 CD1 LEU A 91 4878 10970 10347 -1164 -189 540 C
ATOM 545 CD2 LEU A 91 -1.132 -24.973 29.974 1.00 72.56 C
ANISOU 545 CD2 LEU A 91 5406 11427 10735 -1202 -276 505 C
ATOM 546 N ALA A 92 -0.266 -29.944 30.166 1.00 70.56 N
ANISOU 546 N ALA A 92 5164 10942 10702 -1325 -319 473 N
ATOM 547 CA ALA A 92 -1.209 -31.030 30.431 1.00 71.35 C
ANISOU 547 CA ALA A 92 5214 11017 10881 -1382 -402 516 C
ATOM 548 C ALA A 92 -0.529 -32.135 31.242 1.00 75.63 C
ANISOU 548 C ALA A 92 5716 11517 11503 -1386 -362 534 C
ATOM 549 O ALA A 92 -1.171 -32.754 32.094 1.00 75.53 O
ANISOU 549 O ALA A 92 5603 11522 11573 -1415 -397 606 O
ATOM 550 CB ALA A 92 -1.742 -31.585 29.126 1.00 73.06 C
ANISOU 550 CB ALA A 92 5536 11153 11070 -1429 -497 466 C
ATOM 551 N ALA A 93 0.781 -32.365 30.984 1.00 72.05 N
ANISOU 551 N ALA A 93 5334 11013 11030 -1352 -284 479 N
ATOM 552 CA ALA A 93 1.614 -33.337 31.693 1.00 71.78 C
ANISOU 552 CA ALA A 93 5268 10939 11066 -1346 -230 495 C
ATOM 553 C ALA A 93 1.824 -32.889 33.136 1.00 75.39 C
ANISOU 553 C ALA A 93 5603 11480 11563 -1323 -181 565 C
ATOM 554 O ALA A 93 1.875 -33.727 34.035 1.00 74.87 O
ANISOU 554 O ALA A 93 5463 11409 11575 -1335 -173 613 O
ATOM 555 CB ALA A 93 2.950 -33.503 30.985 1.00 72.52 C
ANISOU 555 CB ALA A 93 5464 10969 11119 -1301 -149 437 C
ATOM 556 N ALA A 94 1.917 -31.559 33.349 1.00 72.18 N
ANISOU 556 N ALA A 94 5184 11146 11097 -1287 -154 572 N
ATOM 557 CA ALA A 94 2.057 -30.926 34.660 1.00 71.93 C
ANISOU 557 CA ALA A 94 5068 11188 11076 -1254 -123 629 C
ATOM 558 C ALA A 94 0.764 -31.103 35.462 1.00 76.55 C
ANISOU 558 C ALA A 94 5560 11831 11695 -1262 -170 702 C
ATOM 559 O ALA A 94 0.818 -31.340 36.670 1.00 75.69 O
ANISOU 559 O ALA A 94 5374 11758 11626 -1240 -146 762 O
ATOM 560 CB ALA A 94 2.393 -29.450 34.496 1.00 72.28 C
ANISOU 560 CB ALA A 94 5148 11273 11040 -1216 -102 609 C
ATOM 561 N ASP A 95 -0.395 -31.019 34.770 1.00 74.45 N
ANISOU 561 N ASP A 95 5298 11571 11417 -1290 -237 709 N
ATOM 562 CA ASP A 95 -1.723 -31.228 35.349 1.00 75.12 C
ANISOU 562 CA ASP A 95 5285 11709 11548 -1300 -286 802 C
ATOM 563 C ASP A 95 -1.930 -32.717 35.638 1.00 79.88 C
ANISOU 563 C ASP A 95 5830 12261 12258 -1350 -319 845 C
ATOM 564 O ASP A 95 -2.561 -33.056 36.638 1.00 79.78 O
ANISOU 564 O ASP A 95 5707 12299 12308 -1339 -320 945 O
ATOM 565 CB ASP A 95 -2.823 -30.689 34.419 1.00 77.58 C
ANISOU 565 CB ASP A 95 5616 12037 11825 -1323 -355 807 C
ATOM 566 CG ASP A 95 -2.814 -29.182 34.211 1.00 90.36 C
ANISOU 566 CG ASP A 95 7277 13713 13344 -1270 -326 781 C
ATOM 567 OD1 ASP A 95 -2.608 -28.443 35.204 1.00 90.46 O
ANISOU 567 OD1 ASP A 95 7259 13785 13325 -1205 -271 813 O
ATOM 568 OD2 ASP A 95 -3.085 -28.739 33.072 1.00 98.52 O1-
ANISOU 568 OD2 ASP A 95 8378 14727 14327 -1292 -365 735 O1-
ATOM 569 N PHE A 96 -1.365 -33.601 34.779 1.00 76.83 N
ANISOU 569 N PHE A 96 5526 11773 11892 -1396 -341 774 N
ATOM 570 CA PHE A 96 -1.405 -35.060 34.943 1.00 77.19 C
ANISOU 570 CA PHE A 96 5544 11746 12039 -1445 -377 799 C
ATOM 571 C PHE A 96 -0.619 -35.448 36.200 1.00 80.07 C
ANISOU 571 C PHE A 96 5834 12136 12451 -1409 -296 840 C
ATOM 572 O PHE A 96 -1.043 -36.341 36.939 1.00 79.37 O
ANISOU 572 O PHE A 96 5653 12047 12456 -1431 -315 919 O
ATOM 573 CB PHE A 96 -0.848 -35.766 33.694 1.00 79.65 C
ANISOU 573 CB PHE A 96 5997 11936 12332 -1478 -407 698 C
ATOM 574 CG PHE A 96 -0.963 -37.273 33.705 1.00 82.27 C
ANISOU 574 CG PHE A 96 6328 12169 12760 -1531 -463 712 C
ATOM 575 CD1 PHE A 96 -2.129 -37.901 33.289 1.00 86.56 C
ANISOU 575 CD1 PHE A 96 6862 12663 13362 -1606 -596 749 C
ATOM 576 CD2 PHE A 96 0.107 -38.066 34.103 1.00 84.68 C
ANISOU 576 CD2 PHE A 96 6648 12424 13103 -1510 -391 693 C
ATOM 577 CE1 PHE A 96 -2.234 -39.297 33.296 1.00 88.44 C
ANISOU 577 CE1 PHE A 96 7109 12797 13697 -1662 -663 763 C
ATOM 578 CE2 PHE A 96 0.002 -39.462 34.108 1.00 88.43 C
ANISOU 578 CE2 PHE A 96 7132 12800 13668 -1557 -445 705 C
ATOM 579 CZ PHE A 96 -1.167 -40.068 33.701 1.00 87.44 C
ANISOU 579 CZ PHE A 96 7003 12619 13601 -1634 -584 737 C
ATOM 580 N PHE A 97 0.516 -34.748 36.445 1.00 76.01 N
ANISOU 580 N PHE A 97 5358 11645 11878 -1356 -211 797 N
ATOM 581 CA PHE A 97 1.360 -34.917 37.627 1.00 75.37 C
ANISOU 581 CA PHE A 97 5218 11592 11827 -1320 -140 834 C
ATOM 582 C PHE A 97 0.624 -34.366 38.852 1.00 80.39 C
ANISOU 582 C PHE A 97 5754 12331 12459 -1278 -135 925 C
ATOM 583 O PHE A 97 0.749 -34.929 39.941 1.00 79.96 O
ANISOU 583 O PHE A 97 5621 12300 12459 -1260 -108 991 O
ATOM 584 CB PHE A 97 2.724 -34.226 37.432 1.00 76.27 C
ANISOU 584 CB PHE A 97 5402 11695 11882 -1285 -73 774 C
ATOM 585 CG PHE A 97 3.640 -34.246 38.638 1.00 76.98 C
ANISOU 585 CG PHE A 97 5438 11814 11998 -1252 -16 816 C
ATOM 586 CD1 PHE A 97 4.406 -35.368 38.932 1.00 79.86 C
ANISOU 586 CD1 PHE A 97 5779 12127 12437 -1265 20 830 C
ATOM 587 CD2 PHE A 97 3.757 -33.134 39.461 1.00 78.28 C
ANISOU 587 CD2 PHE A 97 5584 12050 12108 -1207 -5 841 C
ATOM 588 CE1 PHE A 97 5.252 -35.384 40.045 1.00 80.29 C
ANISOU 588 CE1 PHE A 97 5780 12209 12518 -1239 64 876 C
ATOM 589 CE2 PHE A 97 4.601 -33.154 40.575 1.00 80.61 C
ANISOU 589 CE2 PHE A 97 5842 12365 12422 -1181 28 879 C
ATOM 590 CZ PHE A 97 5.349 -34.275 40.854 1.00 78.80 C
ANISOU 590 CZ PHE A 97 5577 12091 12272 -1200 62 899 C
ATOM 591 N ALA A 98 -0.148 -33.272 38.664 1.00 77.88 N
ANISOU 591 N ALA A 98 5446 12073 12072 -1251 -157 932 N
ATOM 592 CA ALA A 98 -0.960 -32.650 39.709 1.00 78.25 C
ANISOU 592 CA ALA A 98 5419 12217 12096 -1190 -145 1021 C
ATOM 593 C ALA A 98 -2.099 -33.589 40.114 1.00 84.62 C
ANISOU 593 C ALA A 98 6111 13044 12998 -1212 -180 1133 C
ATOM 594 O ALA A 98 -2.407 -33.691 41.301 1.00 84.71 O
ANISOU 594 O ALA A 98 6037 13120 13028 -1157 -145 1228 O
ATOM 595 CB ALA A 98 -1.506 -31.310 39.230 1.00 78.80 C
ANISOU 595 CB ALA A 98 5537 12332 12072 -1156 -158 1000 C
ATOM 596 N GLY A 99 -2.656 -34.311 39.133 1.00 82.39 N
ANISOU 596 N GLY A 99 5830 12698 12775 -1292 -254 1125 N
ATOM 597 CA GLY A 99 -3.707 -35.306 39.331 1.00 83.12 C
ANISOU 597 CA GLY A 99 5814 12786 12982 -1337 -315 1236 C
ATOM 598 C GLY A 99 -3.252 -36.446 40.223 1.00 87.03 C
ANISOU 598 C GLY A 99 6239 13260 13569 -1343 -285 1286 C
ATOM 599 O GLY A 99 -4.045 -36.989 40.994 1.00 86.87 O
ANISOU 599 O GLY A 99 6092 13281 13632 -1337 -295 1419 O
ATOM 600 N LEU A 100 -1.956 -36.794 40.130 1.00 83.64 N
ANISOU 600 N LEU A 100 5884 12768 13127 -1349 -243 1193 N
ATOM 601 CA LEU A 100 -1.296 -37.812 40.945 1.00 83.88 C
ANISOU 601 CA LEU A 100 5863 12773 13235 -1350 -204 1225 C
ATOM 602 C LEU A 100 -0.924 -37.240 42.314 1.00 87.60 C
ANISOU 602 C LEU A 100 6281 13341 13664 -1261 -123 1280 C
ATOM 603 O LEU A 100 -0.951 -37.969 43.307 1.00 87.68 O
ANISOU 603 O LEU A 100 6198 13374 13742 -1244 -97 1367 O
ATOM 604 CB LEU A 100 -0.034 -38.336 40.230 1.00 83.88 C
ANISOU 604 CB LEU A 100 5969 12669 13232 -1382 -185 1111 C
ATOM 605 CG LEU A 100 -0.247 -39.235 39.013 1.00 89.50 C
ANISOU 605 CG LEU A 100 6755 13260 13989 -1459 -263 1056 C
ATOM 606 CD1 LEU A 100 0.882 -39.073 38.015 1.00 89.47 C
ANISOU 606 CD1 LEU A 100 6897 13182 13914 -1451 -228 929 C
ATOM 607 CD2 LEU A 100 -0.396 -40.695 39.421 1.00 92.61 C
ANISOU 607 CD2 LEU A 100 7085 13591 14513 -1504 -295 1117 C
ATOM 608 N ALA A 101 -0.570 -35.935 42.358 1.00 83.54 N
ANISOU 608 N ALA A 101 5834 12875 13032 -1204 -90 1228 N
ATOM 609 CA ALA A 101 -0.182 -35.207 43.570 1.00 82.97 C
ANISOU 609 CA ALA A 101 5753 12880 12891 -1115 -32 1260 C
ATOM 610 C ALA A 101 -1.387 -34.987 44.500 1.00 87.30 C
ANISOU 610 C ALA A 101 6209 13526 13434 -1042 -20 1389 C
ATOM 611 O ALA A 101 -1.253 -35.195 45.707 1.00 87.36 O
ANISOU 611 O ALA A 101 6165 13583 13445 -980 24 1461 O
ATOM 612 CB ALA A 101 0.452 -33.874 43.201 1.00 83.09 C
ANISOU 612 CB ALA A 101 5880 12900 12791 -1085 -23 1168 C
ATOM 613 N TYR A 102 -2.553 -34.577 43.947 1.00 83.71 N
ANISOU 613 N TYR A 102 5733 13101 12972 -1044 -56 1428 N
ATOM 614 CA TYR A 102 -3.773 -34.351 44.729 1.00 83.86 C
ANISOU 614 CA TYR A 102 5655 13216 12991 -966 -35 1572 C
ATOM 615 C TYR A 102 -4.409 -35.683 45.162 1.00 89.31 C
ANISOU 615 C TYR A 102 6201 13908 13825 -1000 -49 1706 C
ATOM 616 O TYR A 102 -5.099 -35.715 46.180 1.00 89.57 O
ANISOU 616 O TYR A 102 6138 14027 13868 -914 -3 1846 O
ATOM 617 CB TYR A 102 -4.801 -33.502 43.957 1.00 84.75 C
ANISOU 617 CB TYR A 102 5779 13359 13062 -961 -69 1587 C
ATOM 618 CG TYR A 102 -4.406 -32.061 43.704 1.00 85.35 C
ANISOU 618 CG TYR A 102 5982 13451 12995 -905 -49 1488 C
ATOM 619 CD1 TYR A 102 -4.232 -31.171 44.759 1.00 87.11 C
ANISOU 619 CD1 TYR A 102 6248 13739 13112 -782 12 1506 C
ATOM 620 CD2 TYR A 102 -4.336 -31.555 42.411 1.00 85.75 C
ANISOU 620 CD2 TYR A 102 6111 13453 13016 -968 -98 1389 C
ATOM 621 CE1 TYR A 102 -3.896 -29.836 44.530 1.00 87.32 C
ANISOU 621 CE1 TYR A 102 6397 13768 13014 -735 16 1420 C
ATOM 622 CE2 TYR A 102 -4.008 -30.221 42.170 1.00 86.08 C
ANISOU 622 CE2 TYR A 102 6261 13509 12937 -919 -82 1311 C
ATOM 623 CZ TYR A 102 -3.796 -29.362 43.233 1.00 92.86 C
ANISOU 623 CZ TYR A 102 7161 14422 13701 -806 -29 1326 C
ATOM 624 OH TYR A 102 -3.481 -28.044 42.997 1.00 92.73 O
ANISOU 624 OH TYR A 102 7257 14406 13571 -762 -27 1251 O
ATOM 625 N PHE A 103 -4.181 -36.773 44.393 1.00 86.59 N
ANISOU 625 N PHE A 103 5846 13466 13588 -1117 -111 1668 N
ATOM 626 CA PHE A 103 -4.692 -38.122 44.679 1.00 87.34 C
ANISOU 626 CA PHE A 103 5814 13534 13835 -1171 -146 1783 C
ATOM 627 C PHE A 103 -4.074 -38.663 45.974 1.00 91.70 C
ANISOU 627 C PHE A 103 6310 14122 14410 -1112 -70 1840 C
ATOM 628 O PHE A 103 -4.781 -39.251 46.794 1.00 91.86 O
ANISOU 628 O PHE A 103 6195 14195 14513 -1080 -53 1997 O
ATOM 629 CB PHE A 103 -4.393 -39.073 43.504 1.00 89.22 C
ANISOU 629 CB PHE A 103 6105 13637 14157 -1302 -235 1696 C
ATOM 630 CG PHE A 103 -5.120 -40.398 43.536 1.00 91.59 C
ANISOU 630 CG PHE A 103 6289 13887 14623 -1379 -308 1812 C
ATOM 631 CD1 PHE A 103 -6.370 -40.536 42.950 1.00 95.33 C
ANISOU 631 CD1 PHE A 103 6696 14350 15173 -1440 -407 1904 C
ATOM 632 CD2 PHE A 103 -4.535 -41.519 44.111 1.00 93.81 C
ANISOU 632 CD2 PHE A 103 6528 14123 14994 -1399 -287 1835 C
ATOM 633 CE1 PHE A 103 -7.036 -41.767 42.963 1.00 97.23 C
ANISOU 633 CE1 PHE A 103 6828 14535 15583 -1522 -494 2024 C
ATOM 634 CE2 PHE A 103 -5.206 -42.748 44.129 1.00 97.60 C
ANISOU 634 CE2 PHE A 103 6900 14548 15637 -1474 -364 1949 C
ATOM 635 CZ PHE A 103 -6.451 -42.863 43.553 1.00 96.46 C
ANISOU 635 CZ PHE A 103 6690 14389 15571 -1538 -472 2043 C
ATOM 636 N TYR A 104 -2.755 -38.442 46.157 1.00 87.89 N
ANISOU 636 N TYR A 104 5925 13612 13857 -1095 -26 1723 N
ATOM 637 CA TYR A 104 -1.995 -38.852 47.338 1.00 87.77 C
ANISOU 637 CA TYR A 104 5878 13623 13848 -1043 38 1757 C
ATOM 638 C TYR A 104 -2.364 -37.954 48.532 1.00 91.21 C
ANISOU 638 C TYR A 104 6297 14179 14179 -904 103 1839 C
ATOM 639 O TYR A 104 -2.289 -38.399 49.680 1.00 91.01 O
ANISOU 639 O TYR A 104 6205 14203 14172 -841 153 1930 O
ATOM 640 CB TYR A 104 -0.481 -38.805 47.035 1.00 88.56 C
ANISOU 640 CB TYR A 104 6089 13651 13908 -1076 52 1615 C
ATOM 641 CG TYR A 104 0.419 -39.295 48.152 1.00 90.74 C
ANISOU 641 CG TYR A 104 6335 13941 14200 -1039 105 1644 C
ATOM 642 CD1 TYR A 104 0.448 -40.639 48.515 1.00 93.39 C
ANISOU 642 CD1 TYR A 104 6574 14243 14665 -1079 109 1716 C
ATOM 643 CD2 TYR A 104 1.313 -38.433 48.778 1.00 91.01 C
ANISOU 643 CD2 TYR A 104 6444 14008 14126 -976 140 1597 C
ATOM 644 CE1 TYR A 104 1.287 -41.097 49.530 1.00 94.13 C
ANISOU 644 CE1 TYR A 104 6638 14352 14774 -1046 159 1748 C
ATOM 645 CE2 TYR A 104 2.160 -38.880 49.791 1.00 91.79 C
ANISOU 645 CE2 TYR A 104 6519 14117 14240 -948 177 1628 C
ATOM 646 CZ TYR A 104 2.145 -40.213 50.163 1.00 99.47 C
ANISOU 646 CZ TYR A 104 7388 15069 15338 -981 191 1703 C
ATOM 647 OH TYR A 104 2.983 -40.658 51.155 1.00100.04 O
ANISOU 647 OH TYR A 104 7433 15153 15426 -954 228 1738 O
ATOM 648 N LEU A 105 -2.792 -36.708 48.249 1.00 87.33 N
ANISOU 648 N LEU A 105 5876 13731 13575 -849 104 1808 N
ATOM 649 CA LEU A 105 -3.218 -35.724 49.242 1.00 87.48 C
ANISOU 649 CA LEU A 105 5914 13852 13473 -704 161 1873 C
ATOM 650 C LEU A 105 -4.599 -36.096 49.815 1.00 93.30 C
ANISOU 650 C LEU A 105 6505 14674 14272 -638 192 2068 C
ATOM 651 O LEU A 105 -4.767 -36.099 51.036 1.00 93.01 O
ANISOU 651 O LEU A 105 6430 14715 14195 -518 261 2172 O
ATOM 652 CB LEU A 105 -3.245 -34.318 48.599 1.00 87.05 C
ANISOU 652 CB LEU A 105 5984 13799 13291 -678 145 1775 C
ATOM 653 CG LEU A 105 -4.046 -33.225 49.315 1.00 92.30 C
ANISOU 653 CG LEU A 105 6677 14561 13833 -527 195 1849 C
ATOM 654 CD1 LEU A 105 -3.261 -32.590 50.424 1.00 92.38 C
ANISOU 654 CD1 LEU A 105 6793 14594 13713 -418 232 1813 C
ATOM 655 CD2 LEU A 105 -4.474 -32.173 48.350 1.00 94.80 C
ANISOU 655 CD2 LEU A 105 7066 14870 14083 -536 164 1784 C
ATOM 656 N MET A 106 -5.574 -36.403 48.928 1.00 91.49 N
ANISOU 656 N MET A 106 6195 14429 14139 -713 139 2125 N
ATOM 657 CA MET A 106 -6.949 -36.764 49.290 1.00 92.90 C
ANISOU 657 CA MET A 106 6213 14681 14404 -670 153 2332 C
ATOM 658 C MET A 106 -7.017 -38.130 49.979 1.00 97.44 C
ANISOU 658 C MET A 106 6646 15254 15122 -694 163 2459 C
ATOM 659 O MET A 106 -7.944 -38.368 50.752 1.00 97.61 O
ANISOU 659 O MET A 106 6533 15362 15192 -610 212 2655 O
ATOM 660 CB MET A 106 -7.865 -36.757 48.067 1.00 95.91 C
ANISOU 660 CB MET A 106 6552 15028 14864 -770 65 2353 C
ATOM 661 CG MET A 106 -8.111 -35.370 47.490 1.00 99.58 C
ANISOU 661 CG MET A 106 7122 15519 15195 -724 67 2279 C
ATOM 662 SD MET A 106 -9.008 -34.231 48.579 1.00104.81 S
ANISOU 662 SD MET A 106 7762 16329 15732 -509 181 2428 S
ATOM 663 CE MET A 106 -8.956 -32.771 47.594 1.00100.87 C
ANISOU 663 CE MET A 106 7417 15813 15094 -504 156 2282 C
ATOM 664 N PHE A 107 -6.031 -39.007 49.731 1.00 94.24 N
ANISOU 664 N PHE A 107 6269 14754 14785 -799 125 2359 N
ATOM 665 CA PHE A 107 -5.960 -40.317 50.373 1.00 95.09 C
ANISOU 665 CA PHE A 107 6254 14847 15028 -826 133 2465 C
ATOM 666 C PHE A 107 -5.432 -40.182 51.811 1.00 99.16 C
ANISOU 666 C PHE A 107 6778 15445 15455 -689 237 2505 C
ATOM 667 O PHE A 107 -5.624 -41.092 52.623 1.00 99.79 O
ANISOU 667 O PHE A 107 6734 15556 15626 -663 272 2643 O
ATOM 668 CB PHE A 107 -5.073 -41.270 49.559 1.00 96.82 C
ANISOU 668 CB PHE A 107 6517 14928 15344 -978 58 2339 C
ATOM 669 CG PHE A 107 -5.623 -42.674 49.464 1.00 99.72 C
ANISOU 669 CG PHE A 107 6747 15246 15896 -1052 23 2456 C
ATOM 670 CD1 PHE A 107 -6.492 -43.029 48.437 1.00104.36 C
ANISOU 670 CD1 PHE A 107 7222 15802 16628 -1133 -66 2576 C
ATOM 671 CD2 PHE A 107 -5.265 -43.645 50.392 1.00102.12 C
ANISOU 671 CD2 PHE A 107 7036 15527 16237 -1047 66 2448 C
ATOM 672 CE1 PHE A 107 -7.007 -44.326 48.349 1.00106.35 C
ANISOU 672 CE1 PHE A 107 7349 15998 17061 -1207 -112 2690 C
ATOM 673 CE2 PHE A 107 -5.778 -44.947 50.302 1.00105.98 C
ANISOU 673 CE2 PHE A 107 7402 15964 16901 -1117 31 2555 C
ATOM 674 CZ PHE A 107 -6.644 -45.277 49.279 1.00105.24 C
ANISOU 674 CZ PHE A 107 7199 15834 16951 -1196 -60 2675 C
ATOM 675 N ASN A 108 -4.785 -39.038 52.122 1.00 94.56 N
ANISOU 675 N ASN A 108 6340 14894 14693 -599 279 2396 N
ATOM 676 CA ASN A 108 -4.209 -38.741 53.428 1.00 93.83 C
ANISOU 676 CA ASN A 108 6294 14866 14490 -469 355 2414 C
ATOM 677 C ASN A 108 -4.816 -37.441 54.033 1.00 96.60 C
ANISOU 677 C ASN A 108 6715 15317 14672 -298 416 2459 C
ATOM 678 O ASN A 108 -4.087 -36.637 54.616 1.00 95.75 O
ANISOU 678 O ASN A 108 6749 15220 14412 -214 437 2371 O
ATOM 679 CB ASN A 108 -2.688 -38.636 53.303 1.00 94.12 C
ANISOU 679 CB ASN A 108 6461 14824 14474 -528 330 2235 C
ATOM 680 CG ASN A 108 -2.004 -39.949 53.004 1.00122.40 C
ANISOU 680 CG ASN A 108 9980 18321 18207 -655 299 2212 C
ATOM 681 OD1 ASN A 108 -1.766 -40.766 53.899 1.00118.37 O
ANISOU 681 OD1 ASN A 108 9391 17830 17753 -630 336 2296 O
ATOM 682 ND2 ASN A 108 -1.669 -40.181 51.741 1.00115.70 N
ANISOU 682 ND2 ASN A 108 9173 17372 17417 -784 236 2098 N
ATOM 683 N THR A 109 -6.156 -37.261 53.921 1.00 92.93 N
ANISOU 683 N THR A 109 6153 14920 14237 -242 439 2606 N
ATOM 684 CA THR A 109 -6.893 -36.101 54.464 1.00 92.83 C
ANISOU 684 CA THR A 109 6195 15005 14072 -62 511 2677 C
ATOM 685 C THR A 109 -7.855 -36.558 55.578 1.00 96.48 C
ANISOU 685 C THR A 109 6509 15581 14569 84 608 2924 C
ATOM 686 O THR A 109 -8.310 -37.704 55.569 1.00 96.63 O
ANISOU 686 O THR A 109 6349 15600 14765 14 597 3059 O
ATOM 687 CB THR A 109 -7.657 -35.366 53.339 1.00101.79 C
ANISOU 687 CB THR A 109 7345 16129 15201 -103 469 2651 C
ATOM 688 OG1 THR A 109 -6.788 -35.111 52.243 1.00102.86 O
ANISOU 688 OG1 THR A 109 7599 16160 15324 -242 384 2440 O
ATOM 689 CG2 THR A 109 -8.288 -34.046 53.787 1.00100.33 C
ANISOU 689 CG2 THR A 109 7243 16031 14847 83 543 2700 C
ATOM 690 N GLY A 110 -8.146 -35.652 56.515 1.00 92.36 N
ANISOU 690 N GLY A 110 6071 15148 13873 292 700 2982 N
ATOM 691 CA GLY A 110 -9.050 -35.894 57.632 1.00 92.95 C
ANISOU 691 CA GLY A 110 6034 15343 13941 474 815 3220 C
ATOM 692 C GLY A 110 -8.441 -36.768 58.710 1.00 95.38 C
ANISOU 692 C GLY A 110 6305 15667 14268 511 853 3269 C
ATOM 693 O GLY A 110 -7.461 -36.357 59.340 1.00 93.94 O
ANISOU 693 O GLY A 110 6289 15467 13936 573 857 3143 O
ATOM 694 N PRO A 111 -8.984 -37.989 58.949 1.00 92.26 N
ANISOU 694 N PRO A 111 5691 15303 14060 472 873 3458 N
ATOM 695 CA PRO A 111 -8.401 -38.851 59.994 1.00 92.04 C
ANISOU 695 CA PRO A 111 5621 15294 14057 508 913 3512 C
ATOM 696 C PRO A 111 -7.093 -39.517 59.548 1.00 93.71 C
ANISOU 696 C PRO A 111 5880 15384 14342 316 815 3321 C
ATOM 697 O PRO A 111 -6.302 -39.902 60.408 1.00 93.56 O
ANISOU 697 O PRO A 111 5892 15369 14286 352 840 3305 O
ATOM 698 CB PRO A 111 -9.496 -39.887 60.260 1.00 95.18 C
ANISOU 698 CB PRO A 111 5758 15756 14649 516 959 3787 C
ATOM 699 CG PRO A 111 -10.281 -39.946 59.014 1.00 99.76 C
ANISOU 699 CG PRO A 111 6239 16292 15375 372 877 3811 C
ATOM 700 CD PRO A 111 -10.160 -38.624 58.315 1.00 94.66 C
ANISOU 700 CD PRO A 111 5777 15621 14567 389 851 3638 C
ATOM 701 N ASN A 112 -6.852 -39.624 58.220 1.00 88.33 N
ANISOU 701 N ASN A 112 5209 14597 13755 122 710 3184 N
ATOM 702 CA ASN A 112 -5.643 -40.224 57.639 1.00 86.54 C
ANISOU 702 CA ASN A 112 5032 14250 13599 -55 624 3006 C
ATOM 703 C ASN A 112 -4.434 -39.257 57.682 1.00 88.72 C
ANISOU 703 C ASN A 112 5528 14485 13698 -38 602 2794 C
ATOM 704 O ASN A 112 -3.310 -39.679 57.393 1.00 87.37 O
ANISOU 704 O ASN A 112 5403 14227 13567 -155 550 2664 O
ATOM 705 CB ASN A 112 -5.905 -40.673 56.198 1.00 85.84 C
ANISOU 705 CB ASN A 112 4887 14065 13662 -244 526 2951 C
ATOM 706 CG ASN A 112 -6.787 -41.893 56.056 1.00104.32 C
ANISOU 706 CG ASN A 112 7017 16399 16221 -321 503 3131 C
ATOM 707 OD1 ASN A 112 -7.759 -42.101 56.795 1.00101.19 O
ANISOU 707 OD1 ASN A 112 6479 16100 15869 -215 568 3351 O
ATOM 708 ND2 ASN A 112 -6.493 -42.705 55.058 1.00 93.09 N
ANISOU 708 ND2 ASN A 112 5574 14856 14940 -504 405 3048 N
ATOM 709 N THR A 113 -4.665 -37.978 58.061 1.00 85.16 N
ANISOU 709 N THR A 113 5210 14091 13056 111 640 2772 N
ATOM 710 CA THR A 113 -3.631 -36.942 58.195 1.00 84.15 C
ANISOU 710 CA THR A 113 5296 13923 12754 139 607 2592 C
ATOM 711 C THR A 113 -2.737 -37.288 59.392 1.00 88.76 C
ANISOU 711 C THR A 113 5923 14520 13283 200 627 2596 C
ATOM 712 O THR A 113 -1.526 -37.065 59.331 1.00 87.97 O
ANISOU 712 O THR A 113 5937 14349 13140 132 566 2449 O
ATOM 713 CB THR A 113 -4.265 -35.543 58.329 1.00 91.43 C
ANISOU 713 CB THR A 113 6348 14898 13494 292 638 2587 C
ATOM 714 OG1 THR A 113 -5.283 -35.383 57.343 1.00 90.70 O
ANISOU 714 OG1 THR A 113 6172 14816 13473 251 635 2637 O
ATOM 715 CG2 THR A 113 -3.250 -34.418 58.173 1.00 89.47 C
ANISOU 715 CG2 THR A 113 6319 14582 13095 280 572 2388 C
ATOM 716 N ARG A 114 -3.340 -37.853 60.467 1.00 86.36 N
ANISOU 716 N ARG A 114 5515 14307 12991 326 712 2779 N
ATOM 717 CA ARG A 114 -2.661 -38.290 61.693 1.00 86.42 C
ANISOU 717 CA ARG A 114 5540 14342 12952 399 742 2817 C
ATOM 718 C ARG A 114 -1.694 -39.453 61.417 1.00 89.22 C
ANISOU 718 C ARG A 114 5801 14619 13478 222 693 2772 C
ATOM 719 O ARG A 114 -0.652 -39.552 62.069 1.00 88.33 O
ANISOU 719 O ARG A 114 5760 14486 13316 225 673 2718 O
ATOM 720 CB ARG A 114 -3.685 -38.714 62.759 1.00 88.25 C
ANISOU 720 CB ARG A 114 5667 14698 13166 584 857 3044 C
ATOM 721 CG ARG A 114 -4.045 -37.608 63.733 1.00100.69 C
ANISOU 721 CG ARG A 114 7431 16340 14488 814 909 3050 C
ATOM 722 CD ARG A 114 -4.170 -38.121 65.144 1.00113.95 C
ANISOU 722 CD ARG A 114 9048 18137 16112 1018 1026 3256 C
ATOM 723 NE ARG A 114 -4.365 -37.000 66.057 1.00125.92 N
ANISOU 723 NE ARG A 114 10778 19703 17364 1250 1072 3246 N
ATOM 724 CZ ARG A 114 -4.825 -37.108 67.298 1.00142.93 C
ANISOU 724 CZ ARG A 114 12957 21959 19392 1481 1179 3399 C
ATOM 725 NH1 ARG A 114 -5.157 -38.296 67.788 1.00132.04 N
ANISOU 725 NH1 ARG A 114 11383 20649 18136 1509 1256 3586 N
ATOM 726 NH2 ARG A 114 -4.978 -36.029 68.048 1.00131.02 N1+
ANISOU 726 NH2 ARG A 114 11676 20479 17628 1696 1212 3371 N1+
ATOM 727 N ARG A 115 -2.039 -40.323 60.437 1.00 85.27 N
ANISOU 727 N ARG A 115 5157 14069 13173 70 665 2791 N
ATOM 728 CA ARG A 115 -1.249 -41.489 60.016 1.00 84.27 C
ANISOU 728 CA ARG A 115 4948 13856 13214 -94 622 2750 C
ATOM 729 C ARG A 115 0.065 -41.093 59.326 1.00 85.80 C
ANISOU 729 C ARG A 115 5280 13946 13375 -211 546 2542 C
ATOM 730 O ARG A 115 0.996 -41.901 59.303 1.00 85.25 O
ANISOU 730 O ARG A 115 5179 13814 13397 -307 525 2503 O
ATOM 731 CB ARG A 115 -2.065 -42.396 59.077 1.00 85.49 C
ANISOU 731 CB ARG A 115 4937 13974 13571 -212 600 2828 C
ATOM 732 CG ARG A 115 -2.844 -43.457 59.833 1.00 99.87 C
ANISOU 732 CG ARG A 115 6570 15863 15512 -158 661 3048 C
ATOM 733 CD ARG A 115 -3.621 -44.402 58.936 1.00114.37 C
ANISOU 733 CD ARG A 115 8241 17654 17561 -280 618 3143 C
ATOM 734 NE ARG A 115 -4.466 -45.301 59.733 1.00127.52 N
ANISOU 734 NE ARG A 115 9717 19400 19335 -206 680 3387 N
ATOM 735 CZ ARG A 115 -4.068 -46.456 60.266 1.00143.94 C
ANISOU 735 CZ ARG A 115 11691 21469 21530 -231 699 3470 C
ATOM 736 NH1 ARG A 115 -2.822 -46.882 60.092 1.00130.69 N
ANISOU 736 NH1 ARG A 115 10078 19702 19876 -328 663 3329 N
ATOM 737 NH2 ARG A 115 -4.912 -47.191 60.979 1.00132.58 N1+
ANISOU 737 NH2 ARG A 115 10074 20112 20190 -154 758 3708 N1+
ATOM 738 N LEU A 116 0.142 -39.863 58.775 1.00 80.64 N
ANISOU 738 N LEU A 116 4772 13274 12593 -198 509 2422 N
ATOM 739 CA LEU A 116 1.330 -39.345 58.088 1.00 78.80 C
ANISOU 739 CA LEU A 116 4667 12950 12323 -297 439 2243 C
ATOM 740 C LEU A 116 2.484 -39.067 59.048 1.00 82.13 C
ANISOU 740 C LEU A 116 5186 13368 12650 -254 422 2203 C
ATOM 741 O LEU A 116 2.278 -38.522 60.136 1.00 82.48 O
ANISOU 741 O LEU A 116 5299 13483 12558 -109 447 2255 O
ATOM 742 CB LEU A 116 1.007 -38.045 57.323 1.00 78.21 C
ANISOU 742 CB LEU A 116 4717 12866 12135 -280 405 2147 C
ATOM 743 CG LEU A 116 0.079 -38.140 56.121 1.00 82.14 C
ANISOU 743 CG LEU A 116 5149 13344 12715 -351 394 2148 C
ATOM 744 CD1 LEU A 116 -0.557 -36.808 55.842 1.00 82.05 C
ANISOU 744 CD1 LEU A 116 5243 13366 12565 -270 390 2112 C
ATOM 745 CD2 LEU A 116 0.811 -38.644 54.886 1.00 83.37 C
ANISOU 745 CD2 LEU A 116 5304 13390 12982 -520 339 2033 C
ATOM 746 N THR A 117 3.699 -39.430 58.623 1.00 77.37 N
ANISOU 746 N THR A 117 4600 12682 12116 -375 377 2112 N
ATOM 747 CA THR A 117 4.944 -39.184 59.350 1.00 76.84 C
ANISOU 747 CA THR A 117 4619 12594 11983 -368 339 2071 C
ATOM 748 C THR A 117 5.524 -37.845 58.860 1.00 78.86 C
ANISOU 748 C THR A 117 5040 12800 12124 -386 263 1939 C
ATOM 749 O THR A 117 4.942 -37.225 57.965 1.00 78.49 O
ANISOU 749 O THR A 117 5028 12741 12055 -401 255 1885 O
ATOM 750 CB THR A 117 5.923 -40.363 59.179 1.00 86.63 C
ANISOU 750 CB THR A 117 5763 13775 13379 -483 341 2077 C
ATOM 751 OG1 THR A 117 6.134 -40.613 57.788 1.00 85.96 O
ANISOU 751 OG1 THR A 117 5654 13607 13399 -609 327 1997 O
ATOM 752 CG2 THR A 117 5.443 -41.632 59.875 1.00 86.69 C
ANISOU 752 CG2 THR A 117 5618 13830 13490 -454 407 2215 C
ATOM 753 N VAL A 118 6.651 -37.395 59.445 1.00 73.90 N
ANISOU 753 N VAL A 118 4508 12140 11429 -389 201 1898 N
ATOM 754 CA VAL A 118 7.311 -36.131 59.094 1.00 72.98 C
ANISOU 754 CA VAL A 118 4546 11968 11216 -412 112 1789 C
ATOM 755 C VAL A 118 7.764 -36.175 57.612 1.00 75.66 C
ANISOU 755 C VAL A 118 4851 12230 11666 -552 99 1708 C
ATOM 756 O VAL A 118 7.559 -35.200 56.882 1.00 74.76 O
ANISOU 756 O VAL A 118 4822 12091 11491 -561 65 1632 O
ATOM 757 CB VAL A 118 8.493 -35.832 60.059 1.00 77.11 C
ANISOU 757 CB VAL A 118 5158 12465 11674 -404 31 1785 C
ATOM 758 CG1 VAL A 118 9.208 -34.533 59.694 1.00 76.80 C
ANISOU 758 CG1 VAL A 118 5272 12357 11553 -440 -79 1686 C
ATOM 759 CG2 VAL A 118 8.019 -35.788 61.511 1.00 77.75 C
ANISOU 759 CG2 VAL A 118 5295 12622 11625 -249 45 1861 C
ATOM 760 N SER A 119 8.327 -37.320 57.173 1.00 71.86 N
ANISOU 760 N SER A 119 4251 11713 11341 -649 133 1730 N
ATOM 761 CA SER A 119 8.816 -37.540 55.809 1.00 70.89 C
ANISOU 761 CA SER A 119 4098 11514 11321 -765 136 1665 C
ATOM 762 C SER A 119 7.671 -37.601 54.779 1.00 73.64 C
ANISOU 762 C SER A 119 4420 11867 11694 -776 170 1638 C
ATOM 763 O SER A 119 7.791 -36.988 53.715 1.00 72.71 O
ANISOU 763 O SER A 119 4359 11704 11564 -825 146 1557 O
ATOM 764 CB SER A 119 9.636 -38.826 55.740 1.00 74.35 C
ANISOU 764 CB SER A 119 4429 11914 11908 -838 174 1707 C
ATOM 765 OG SER A 119 8.874 -39.957 56.134 1.00 83.91 O
ANISOU 765 OG SER A 119 5528 13163 13192 -814 235 1787 O
ATOM 766 N THR A 120 6.578 -38.335 55.090 1.00 70.00 N
ANISOU 766 N THR A 120 3868 11458 11269 -733 220 1716 N
ATOM 767 CA THR A 120 5.424 -38.506 54.194 1.00 69.69 C
ANISOU 767 CA THR A 120 3786 11423 11269 -750 239 1716 C
ATOM 768 C THR A 120 4.605 -37.209 54.073 1.00 73.00 C
ANISOU 768 C THR A 120 4297 11887 11555 -677 219 1687 C
ATOM 769 O THR A 120 3.982 -36.995 53.031 1.00 71.88 O
ANISOU 769 O THR A 120 4156 11725 11429 -716 211 1648 O
ATOM 770 CB THR A 120 4.525 -39.668 54.643 1.00 78.42 C
ANISOU 770 CB THR A 120 4755 12570 12471 -731 286 1834 C
ATOM 771 OG1 THR A 120 4.106 -39.460 55.988 1.00 79.11 O
ANISOU 771 OG1 THR A 120 4833 12748 12477 -608 314 1928 O
ATOM 772 CG2 THR A 120 5.199 -41.025 54.502 1.00 76.93 C
ANISOU 772 CG2 THR A 120 4477 12321 12432 -815 304 1856 C
ATOM 773 N TRP A 121 4.606 -36.352 55.120 1.00 70.14 N
ANISOU 773 N TRP A 121 4018 11576 11055 -569 207 1704 N
ATOM 774 CA TRP A 121 3.904 -35.059 55.104 1.00 70.26 C
ANISOU 774 CA TRP A 121 4141 11626 10929 -483 191 1675 C
ATOM 775 C TRP A 121 4.574 -34.128 54.100 1.00 72.64 C
ANISOU 775 C TRP A 121 4545 11855 11199 -557 130 1550 C
ATOM 776 O TRP A 121 3.886 -33.478 53.311 1.00 72.07 O
ANISOU 776 O TRP A 121 4506 11785 11091 -554 126 1513 O
ATOM 777 CB TRP A 121 3.882 -34.415 56.501 1.00 69.96 C
ANISOU 777 CB TRP A 121 4198 11644 10740 -340 187 1715 C
ATOM 778 CG TRP A 121 2.896 -33.293 56.643 1.00 71.43 C
ANISOU 778 CG TRP A 121 4479 11878 10783 -217 197 1718 C
ATOM 779 CD1 TRP A 121 1.636 -33.376 57.154 1.00 75.20 C
ANISOU 779 CD1 TRP A 121 4908 12443 11221 -93 270 1829 C
ATOM 780 CD2 TRP A 121 3.087 -31.919 56.269 1.00 71.26 C
ANISOU 780 CD2 TRP A 121 4616 11818 10643 -201 137 1618 C
ATOM 781 NE1 TRP A 121 1.031 -32.142 57.132 1.00 75.04 N
ANISOU 781 NE1 TRP A 121 5010 12443 11058 9 266 1802 N
ATOM 782 CE2 TRP A 121 1.895 -31.230 56.583 1.00 75.95 C
ANISOU 782 CE2 TRP A 121 5257 12479 11122 -58 181 1667 C
ATOM 783 CE3 TRP A 121 4.152 -31.200 55.696 1.00 71.92 C
ANISOU 783 CE3 TRP A 121 4799 11816 10712 -290 51 1504 C
ATOM 784 CZ2 TRP A 121 1.733 -29.859 56.341 1.00 75.45 C
ANISOU 784 CZ2 TRP A 121 5347 12394 10926 -3 141 1593 C
ATOM 785 CZ3 TRP A 121 3.986 -29.847 55.447 1.00 73.49 C
ANISOU 785 CZ3 TRP A 121 5141 11993 10787 -243 4 1435 C
ATOM 786 CH2 TRP A 121 2.794 -29.187 55.778 1.00 74.80 C
ANISOU 786 CH2 TRP A 121 5364 12221 10835 -100 47 1473 C
ATOM 787 N LEU A 122 5.923 -34.088 54.123 1.00 68.13 N
ANISOU 787 N LEU A 122 4013 11223 10650 -623 85 1501 N
ATOM 788 CA LEU A 122 6.754 -33.291 53.219 1.00 67.23 C
ANISOU 788 CA LEU A 122 3978 11037 10527 -698 29 1406 C
ATOM 789 C LEU A 122 6.681 -33.831 51.784 1.00 70.86 C
ANISOU 789 C LEU A 122 4373 11453 11097 -796 58 1366 C
ATOM 790 O LEU A 122 6.897 -33.074 50.836 1.00 69.88 O
ANISOU 790 O LEU A 122 4311 11288 10950 -836 30 1294 O
ATOM 791 CB LEU A 122 8.214 -33.270 53.705 1.00 67.10 C
ANISOU 791 CB LEU A 122 3991 10972 10530 -743 -23 1401 C
ATOM 792 CG LEU A 122 8.508 -32.493 54.989 1.00 71.86 C
ANISOU 792 CG LEU A 122 4704 11591 11007 -660 -90 1416 C
ATOM 793 CD1 LEU A 122 9.814 -32.933 55.592 1.00 72.16 C
ANISOU 793 CD1 LEU A 122 4721 11593 11105 -714 -134 1448 C
ATOM 794 CD2 LEU A 122 8.505 -30.990 54.749 1.00 73.76 C
ANISOU 794 CD2 LEU A 122 5097 11802 11126 -632 -168 1344 C
ATOM 795 N LEU A 123 6.364 -35.131 51.628 1.00 68.00 N
ANISOU 795 N LEU A 123 3895 11094 10846 -830 110 1415 N
ATOM 796 CA LEU A 123 6.220 -35.780 50.328 1.00 67.81 C
ANISOU 796 CA LEU A 123 3827 11019 10919 -913 129 1379 C
ATOM 797 C LEU A 123 4.934 -35.290 49.631 1.00 72.85 C
ANISOU 797 C LEU A 123 4480 11684 11515 -895 123 1363 C
ATOM 798 O LEU A 123 5.031 -34.799 48.503 1.00 72.28 O
ANISOU 798 O LEU A 123 4462 11570 11432 -941 104 1288 O
ATOM 799 CB LEU A 123 6.221 -37.319 50.474 1.00 68.00 C
ANISOU 799 CB LEU A 123 3738 11026 11073 -951 170 1440 C
ATOM 800 CG LEU A 123 6.143 -38.151 49.183 1.00 72.62 C
ANISOU 800 CG LEU A 123 4298 11538 11758 -1035 180 1401 C
ATOM 801 CD1 LEU A 123 7.433 -38.057 48.377 1.00 72.46 C
ANISOU 801 CD1 LEU A 123 4332 11441 11758 -1088 186 1332 C
ATOM 802 CD2 LEU A 123 5.833 -39.607 49.491 1.00 75.61 C
ANISOU 802 CD2 LEU A 123 4570 11904 12256 -1057 207 1474 C
ATOM 803 N ARG A 124 3.750 -35.385 50.306 1.00 70.19 N
ANISOU 803 N ARG A 124 4092 11420 11155 -822 142 1445 N
ATOM 804 CA ARG A 124 2.471 -34.951 49.728 1.00 70.54 C
ANISOU 804 CA ARG A 124 4132 11498 11170 -801 137 1456 C
ATOM 805 C ARG A 124 2.459 -33.432 49.498 1.00 74.97 C
ANISOU 805 C ARG A 124 4817 12070 11598 -754 110 1388 C
ATOM 806 O ARG A 124 1.879 -32.983 48.510 1.00 74.62 O
ANISOU 806 O ARG A 124 4794 12016 11542 -780 93 1349 O
ATOM 807 CB ARG A 124 1.243 -35.381 50.569 1.00 71.38 C
ANISOU 807 CB ARG A 124 4141 11688 11292 -722 174 1589 C
ATOM 808 CG ARG A 124 1.038 -34.724 51.932 1.00 80.82 C
ANISOU 808 CG ARG A 124 5375 12964 12368 -582 203 1651 C
ATOM 809 CD ARG A 124 -0.436 -34.774 52.296 1.00 90.04 C
ANISOU 809 CD ARG A 124 6462 14217 13531 -492 246 1780 C
ATOM 810 NE ARG A 124 -0.728 -34.214 53.614 1.00100.50 N
ANISOU 810 NE ARG A 124 7831 15622 14731 -333 290 1853 N
ATOM 811 CZ ARG A 124 -0.998 -32.934 53.851 1.00115.70 C
ANISOU 811 CZ ARG A 124 9879 17578 16504 -228 291 1825 C
ATOM 812 NH1 ARG A 124 -0.982 -32.050 52.861 1.00102.44 N
ANISOU 812 NH1 ARG A 124 8279 15856 14786 -275 249 1725 N
ATOM 813 NH2 ARG A 124 -1.256 -32.525 55.082 1.00103.54 N1+
ANISOU 813 NH2 ARG A 124 8394 16104 14842 -68 334 1894 N1+
ATOM 814 N GLN A 125 3.115 -32.659 50.384 1.00 71.76 N
ANISOU 814 N GLN A 125 4495 11674 11095 -691 95 1372 N
ATOM 815 CA GLN A 125 3.195 -31.204 50.284 1.00 71.49 C
ANISOU 815 CA GLN A 125 4593 11637 10935 -646 56 1308 C
ATOM 816 C GLN A 125 4.194 -30.802 49.191 1.00 75.02 C
ANISOU 816 C GLN A 125 5093 12004 11408 -744 15 1210 C
ATOM 817 O GLN A 125 3.975 -29.800 48.507 1.00 74.85 O
ANISOU 817 O GLN A 125 5144 11970 11326 -743 -10 1154 O
ATOM 818 CB GLN A 125 3.580 -30.591 51.642 1.00 73.12 C
ANISOU 818 CB GLN A 125 4888 11866 11029 -547 36 1327 C
ATOM 819 CG GLN A 125 3.261 -29.103 51.772 1.00 87.40 C
ANISOU 819 CG GLN A 125 6839 13680 12688 -461 0 1285 C
ATOM 820 CD GLN A 125 1.787 -28.791 51.679 1.00107.25 C
ANISOU 820 CD GLN A 125 9337 16264 15150 -370 50 1336 C
ATOM 821 OE1 GLN A 125 0.975 -29.199 52.518 1.00104.63 O
ANISOU 821 OE1 GLN A 125 8954 16004 14795 -270 107 1436 O
ATOM 822 NE2 GLN A 125 1.418 -28.048 50.653 1.00 96.79 N
ANISOU 822 NE2 GLN A 125 8050 14921 13804 -397 33 1281 N
ATOM 823 N GLY A 126 5.257 -31.594 49.035 1.00 70.94 N
ANISOU 823 N GLY A 126 4532 11436 10985 -822 17 1201 N
ATOM 824 CA GLY A 126 6.295 -31.381 48.033 1.00 70.21 C
ANISOU 824 CA GLY A 126 4472 11271 10935 -906 -3 1135 C
ATOM 825 C GLY A 126 5.820 -31.604 46.612 1.00 73.43 C
ANISOU 825 C GLY A 126 4864 11652 11383 -961 16 1091 C
ATOM 826 O GLY A 126 6.143 -30.806 45.730 1.00 72.82 O
ANISOU 826 O GLY A 126 4850 11542 11276 -986 -5 1032 O
ATOM 827 N LEU A 127 5.037 -32.684 46.384 1.00 69.54 N
ANISOU 827 N LEU A 127 4290 11171 10961 -978 47 1125 N
ATOM 828 CA LEU A 127 4.475 -33.049 45.076 1.00 69.29 C
ANISOU 828 CA LEU A 127 4250 11107 10969 -1031 48 1089 C
ATOM 829 C LEU A 127 3.505 -31.975 44.553 1.00 74.31 C
ANISOU 829 C LEU A 127 4937 11777 11521 -1002 22 1063 C
ATOM 830 O LEU A 127 3.415 -31.772 43.339 1.00 73.76 O
ANISOU 830 O LEU A 127 4905 11671 11450 -1045 9 1006 O
ATOM 831 CB LEU A 127 3.750 -34.406 45.157 1.00 69.58 C
ANISOU 831 CB LEU A 127 4190 11144 11102 -1056 62 1147 C
ATOM 832 CG LEU A 127 4.612 -35.660 45.343 1.00 74.05 C
ANISOU 832 CG LEU A 127 4708 11658 11770 -1098 90 1164 C
ATOM 833 CD1 LEU A 127 3.804 -36.785 45.974 1.00 74.69 C
ANISOU 833 CD1 LEU A 127 4682 11762 11933 -1097 98 1254 C
ATOM 834 CD2 LEU A 127 5.243 -36.108 44.033 1.00 76.15 C
ANISOU 834 CD2 LEU A 127 5019 11835 12079 -1162 95 1094 C
ATOM 835 N ILE A 128 2.788 -31.295 45.469 1.00 72.05 N
ANISOU 835 N ILE A 128 4655 11560 11159 -920 20 1110 N
ATOM 836 CA ILE A 128 1.832 -30.232 45.151 1.00 72.24 C
ANISOU 836 CA ILE A 128 4726 11625 11098 -872 5 1102 C
ATOM 837 C ILE A 128 2.610 -28.955 44.767 1.00 75.98 C
ANISOU 837 C ILE A 128 5312 12065 11492 -871 -24 1022 C
ATOM 838 O ILE A 128 2.234 -28.280 43.806 1.00 75.77 O
ANISOU 838 O ILE A 128 5327 12031 11433 -886 -40 978 O
ATOM 839 CB ILE A 128 0.856 -30.015 46.341 1.00 76.08 C
ANISOU 839 CB ILE A 128 5184 12196 11528 -762 28 1194 C
ATOM 840 CG1 ILE A 128 -0.101 -31.224 46.468 1.00 77.35 C
ANISOU 840 CG1 ILE A 128 5213 12391 11787 -774 52 1294 C
ATOM 841 CG2 ILE A 128 0.058 -28.704 46.193 1.00 77.04 C
ANISOU 841 CG2 ILE A 128 5378 12356 11538 -688 20 1186 C
ATOM 842 CD1 ILE A 128 -0.900 -31.304 47.753 1.00 88.17 C
ANISOU 842 CD1 ILE A 128 6525 13846 13130 -662 95 1416 C
ATOM 843 N ASP A 129 3.701 -28.646 45.497 1.00 72.16 N
ANISOU 843 N ASP A 129 4874 11558 10987 -859 -40 1011 N
ATOM 844 CA ASP A 129 4.557 -27.485 45.234 1.00 71.60 C
ANISOU 844 CA ASP A 129 4901 11445 10861 -868 -84 953 C
ATOM 845 C ASP A 129 5.302 -27.649 43.902 1.00 74.81 C
ANISOU 845 C ASP A 129 5303 11790 11330 -956 -79 902 C
ATOM 846 O ASP A 129 5.525 -26.658 43.206 1.00 74.42 O
ANISOU 846 O ASP A 129 5318 11718 11239 -965 -104 858 O
ATOM 847 CB ASP A 129 5.550 -27.268 46.386 1.00 73.50 C
ANISOU 847 CB ASP A 129 5179 11667 11081 -847 -119 971 C
ATOM 848 CG ASP A 129 4.922 -26.830 47.699 1.00 83.29 C
ANISOU 848 CG ASP A 129 6468 12956 12220 -738 -131 1009 C
ATOM 849 OD1 ASP A 129 3.679 -26.869 47.811 1.00 83.88 O
ANISOU 849 OD1 ASP A 129 6522 13091 12256 -672 -93 1041 O
ATOM 850 OD2 ASP A 129 5.674 -26.476 48.622 1.00 90.10 O1-
ANISOU 850 OD2 ASP A 129 7396 13797 13042 -713 -181 1014 O1-
ATOM 851 N THR A 130 5.656 -28.903 43.548 1.00 70.60 N
ANISOU 851 N THR A 130 4700 11232 10894 -1009 -42 914 N
ATOM 852 CA THR A 130 6.337 -29.271 42.303 1.00 69.54 C
ANISOU 852 CA THR A 130 4568 11040 10815 -1072 -19 875 C
ATOM 853 C THR A 130 5.369 -29.081 41.121 1.00 71.87 C
ANISOU 853 C THR A 130 4887 11338 11082 -1083 -21 832 C
ATOM 854 O THR A 130 5.760 -28.493 40.114 1.00 71.64 O
ANISOU 854 O THR A 130 4910 11278 11031 -1101 -22 788 O
ATOM 855 CB THR A 130 6.868 -30.720 42.393 1.00 76.42 C
ANISOU 855 CB THR A 130 5371 11879 11787 -1107 23 903 C
ATOM 856 OG1 THR A 130 7.705 -30.838 43.543 1.00 75.59 O
ANISOU 856 OG1 THR A 130 5239 11777 11705 -1096 18 950 O
ATOM 857 CG2 THR A 130 7.647 -31.150 41.153 1.00 74.82 C
ANISOU 857 CG2 THR A 130 5188 11611 11630 -1149 59 868 C
ATOM 858 N SER A 131 4.112 -29.553 41.265 1.00 66.88 N
ANISOU 858 N SER A 131 4212 10745 10452 -1070 -25 858 N
ATOM 859 CA SER A 131 3.069 -29.486 40.239 1.00 66.34 C
ANISOU 859 CA SER A 131 4155 10683 10368 -1087 -42 835 C
ATOM 860 C SER A 131 2.664 -28.041 39.889 1.00 69.54 C
ANISOU 860 C SER A 131 4625 11118 10680 -1052 -65 808 C
ATOM 861 O SER A 131 2.333 -27.782 38.730 1.00 69.35 O
ANISOU 861 O SER A 131 4635 11077 10636 -1078 -78 767 O
ATOM 862 CB SER A 131 1.832 -30.260 40.684 1.00 70.23 C
ANISOU 862 CB SER A 131 4568 11217 10901 -1081 -51 901 C
ATOM 863 OG SER A 131 1.219 -29.702 41.833 1.00 78.61 O
ANISOU 863 OG SER A 131 5603 12351 11914 -1006 -46 964 O
ATOM 864 N LEU A 132 2.675 -27.115 40.876 1.00 65.24 N
ANISOU 864 N LEU A 132 4105 10611 10072 -990 -73 830 N
ATOM 865 CA LEU A 132 2.306 -25.711 40.663 1.00 64.39 C
ANISOU 865 CA LEU A 132 4069 10525 9873 -947 -97 806 C
ATOM 866 C LEU A 132 3.352 -25.017 39.780 1.00 67.19 C
ANISOU 866 C LEU A 132 4488 10824 10218 -986 -109 747 C
ATOM 867 O LEU A 132 3.004 -24.528 38.702 1.00 66.73 O
ANISOU 867 O LEU A 132 4460 10761 10133 -1000 -115 713 O
ATOM 868 CB LEU A 132 2.135 -24.967 42.009 1.00 64.45 C
ANISOU 868 CB LEU A 132 4111 10570 9807 -859 -107 842 C
ATOM 869 CG LEU A 132 1.954 -23.435 41.953 1.00 68.88 C
ANISOU 869 CG LEU A 132 4771 11135 10267 -806 -137 813 C
ATOM 870 CD1 LEU A 132 0.645 -23.043 41.299 1.00 69.22 C
ANISOU 870 CD1 LEU A 132 4802 11224 10273 -778 -126 826 C
ATOM 871 CD2 LEU A 132 2.034 -22.827 43.330 1.00 71.12 C
ANISOU 871 CD2 LEU A 132 5119 11432 10473 -717 -156 837 C
ATOM 872 N THR A 133 4.629 -25.021 40.216 1.00 63.01 N
ANISOU 872 N THR A 133 3969 10254 9719 -1003 -113 748 N
ATOM 873 CA THR A 133 5.757 -24.409 39.507 1.00 62.65 C
ANISOU 873 CA THR A 133 3965 10156 9685 -1037 -122 723 C
ATOM 874 C THR A 133 5.990 -25.093 38.145 1.00 65.46 C
ANISOU 874 C THR A 133 4305 10482 10086 -1083 -79 696 C
ATOM 875 O THR A 133 6.597 -24.472 37.270 1.00 65.73 O
ANISOU 875 O THR A 133 4376 10487 10112 -1096 -74 679 O
ATOM 876 CB THR A 133 7.037 -24.418 40.361 1.00 72.82 C
ANISOU 876 CB THR A 133 5246 11408 11016 -1052 -141 756 C
ATOM 877 OG1 THR A 133 7.106 -25.612 41.145 1.00 74.96 O
ANISOU 877 OG1 THR A 133 5506 11706 11269 -1014 -161 788 O
ATOM 878 CG2 THR A 133 7.148 -23.191 41.259 1.00 71.02 C
ANISOU 878 CG2 THR A 133 5075 11140 10769 -1062 -191 754 C
ATOM 879 N ALA A 134 5.492 -26.343 37.960 1.00 59.89 N
ANISOU 879 N ALA A 134 3555 9778 9423 -1100 -50 698 N
ATOM 880 CA ALA A 134 5.570 -27.059 36.682 1.00 59.04 C
ANISOU 880 CA ALA A 134 3462 9631 9340 -1132 -20 664 C
ATOM 881 C ALA A 134 4.642 -26.387 35.670 1.00 62.29 C
ANISOU 881 C ALA A 134 3921 10059 9686 -1128 -43 625 C
ATOM 882 O ALA A 134 5.018 -26.215 34.514 1.00 61.40 O
ANISOU 882 O ALA A 134 3858 9915 9556 -1137 -25 591 O
ATOM 883 CB ALA A 134 5.202 -28.520 36.865 1.00 59.90 C
ANISOU 883 CB ALA A 134 3523 9725 9510 -1153 -6 676 C
ATOM 884 N SER A 135 3.450 -25.958 36.131 1.00 59.37 N
ANISOU 884 N SER A 135 3536 9745 9278 -1107 -79 640 N
ATOM 885 CA SER A 135 2.439 -25.267 35.327 1.00 59.30 C
ANISOU 885 CA SER A 135 3558 9763 9210 -1100 -107 620 C
ATOM 886 C SER A 135 2.744 -23.767 35.221 1.00 62.82 C
ANISOU 886 C SER A 135 4058 10220 9591 -1069 -116 606 C
ATOM 887 O SER A 135 2.448 -23.159 34.189 1.00 62.28 O
ANISOU 887 O SER A 135 4032 10153 9480 -1072 -124 577 O
ATOM 888 CB SER A 135 1.049 -25.476 35.921 1.00 62.54 C
ANISOU 888 CB SER A 135 3914 10230 9620 -1083 -133 669 C
ATOM 889 OG SER A 135 0.683 -26.847 35.915 1.00 71.37 O
ANISOU 889 OG SER A 135 4978 11330 10808 -1123 -140 690 O
ATOM 890 N VAL A 136 3.337 -23.178 36.284 1.00 58.98 N
ANISOU 890 N VAL A 136 3576 9737 9097 -1040 -123 628 N
ATOM 891 CA VAL A 136 3.704 -21.760 36.360 1.00 58.70 C
ANISOU 891 CA VAL A 136 3599 9695 9008 -1013 -149 620 C
ATOM 892 C VAL A 136 4.825 -21.478 35.335 1.00 61.93 C
ANISOU 892 C VAL A 136 4035 10055 9442 -1048 -134 602 C
ATOM 893 O VAL A 136 4.704 -20.527 34.560 1.00 61.32 O
ANISOU 893 O VAL A 136 4000 9977 9322 -1041 -145 584 O
ATOM 894 CB VAL A 136 4.091 -21.347 37.813 1.00 62.95 C
ANISOU 894 CB VAL A 136 4154 10233 9533 -975 -179 648 C
ATOM 895 CG1 VAL A 136 4.865 -20.034 37.850 1.00 62.67 C
ANISOU 895 CG1 VAL A 136 4187 10157 9466 -970 -225 640 C
ATOM 896 CG2 VAL A 136 2.853 -21.254 38.705 1.00 63.11 C
ANISOU 896 CG2 VAL A 136 4170 10311 9497 -909 -184 675 C
ATOM 897 N ALA A 137 5.877 -22.322 35.308 1.00 58.46 N
ANISOU 897 N ALA A 137 3563 9576 9072 -1078 -101 617 N
ATOM 898 CA ALA A 137 6.996 -22.187 34.368 1.00 58.43 C
ANISOU 898 CA ALA A 137 3571 9530 9100 -1097 -68 624 C
ATOM 899 C ALA A 137 6.562 -22.517 32.933 1.00 62.51 C
ANISOU 899 C ALA A 137 4119 10045 9588 -1097 -31 585 C
ATOM 900 O ALA A 137 7.119 -21.949 31.989 1.00 62.06 O
ANISOU 900 O ALA A 137 4091 9970 9518 -1091 -8 588 O
ATOM 901 CB ALA A 137 8.153 -23.083 34.784 1.00 59.25 C
ANISOU 901 CB ALA A 137 3627 9598 9286 -1116 -32 665 C
ATOM 902 N ASN A 138 5.567 -23.425 32.773 1.00 59.21 N
ANISOU 902 N ASN A 138 3696 9642 9158 -1104 -32 556 N
ATOM 903 CA ASN A 138 5.022 -23.811 31.469 1.00 59.41 C
ANISOU 903 CA ASN A 138 3768 9657 9148 -1109 -22 513 C
ATOM 904 C ASN A 138 4.279 -22.637 30.838 1.00 65.09 C
ANISOU 904 C ASN A 138 4526 10411 9796 -1096 -55 495 C
ATOM 905 O ASN A 138 4.548 -22.310 29.682 1.00 65.01 O
ANISOU 905 O ASN A 138 4567 10385 9751 -1087 -33 475 O
ATOM 906 CB ASN A 138 4.103 -25.026 31.582 1.00 57.13 C
ANISOU 906 CB ASN A 138 3461 9367 8879 -1132 -45 499 C
ATOM 907 CG ASN A 138 4.755 -26.343 31.242 1.00 64.07 C
ANISOU 907 CG ASN A 138 4352 10186 9804 -1143 -5 488 C
ATOM 908 OD1 ASN A 138 5.380 -26.507 30.188 1.00 46.38 O
ANISOU 908 OD1 ASN A 138 2176 7904 7541 -1127 37 464 O
ATOM 909 ND2 ASN A 138 4.527 -27.346 32.077 1.00 58.81 N
ANISOU 909 ND2 ASN A 138 3634 9516 9197 -1163 -15 508 N
ATOM 910 N LEU A 139 3.389 -21.971 31.614 1.00 62.65 N
ANISOU 910 N LEU A 139 4194 10149 9462 -1084 -98 509 N
ATOM 911 CA LEU A 139 2.624 -20.795 31.180 1.00 63.09 C
ANISOU 911 CA LEU A 139 4281 10240 9452 -1064 -127 501 C
ATOM 912 C LEU A 139 3.554 -19.608 30.912 1.00 68.51 C
ANISOU 912 C LEU A 139 5002 10907 10123 -1049 -118 507 C
ATOM 913 O LEU A 139 3.268 -18.799 30.029 1.00 68.32 O
ANISOU 913 O LEU A 139 5014 10893 10051 -1038 -124 494 O
ATOM 914 CB LEU A 139 1.560 -20.409 32.223 1.00 63.05 C
ANISOU 914 CB LEU A 139 4246 10286 9426 -1035 -160 531 C
ATOM 915 CG LEU A 139 0.309 -21.303 32.306 1.00 68.06 C
ANISOU 915 CG LEU A 139 4832 10954 10073 -1048 -180 550 C
ATOM 916 CD1 LEU A 139 -0.369 -21.170 33.654 1.00 68.21 C
ANISOU 916 CD1 LEU A 139 4806 11021 10090 -1003 -186 604 C
ATOM 917 CD2 LEU A 139 -0.680 -21.007 31.174 1.00 69.99 C
ANISOU 917 CD2 LEU A 139 5097 11220 10276 -1059 -209 540 C
ATOM 918 N LEU A 140 4.671 -19.523 31.666 1.00 66.09 N
ANISOU 918 N LEU A 140 4678 10569 9865 -1052 -112 536 N
ATOM 919 CA LEU A 140 5.702 -18.493 31.518 1.00 66.66 C
ANISOU 919 CA LEU A 140 4768 10610 9950 -1050 -118 562 C
ATOM 920 C LEU A 140 6.431 -18.686 30.186 1.00 73.17 C
ANISOU 920 C LEU A 140 5603 11411 10787 -1054 -61 568 C
ATOM 921 O LEU A 140 6.682 -17.706 29.482 1.00 72.96 O
ANISOU 921 O LEU A 140 5601 11381 10741 -1044 -61 581 O
ATOM 922 CB LEU A 140 6.691 -18.544 32.703 1.00 66.44 C
ANISOU 922 CB LEU A 140 4712 10549 9982 -1063 -140 604 C
ATOM 923 CG LEU A 140 7.757 -17.445 32.796 1.00 70.65 C
ANISOU 923 CG LEU A 140 5256 11039 10548 -1074 -177 650 C
ATOM 924 CD1 LEU A 140 7.161 -16.131 33.280 1.00 70.67 C
ANISOU 924 CD1 LEU A 140 5318 11044 10491 -1051 -251 636 C
ATOM 925 CD2 LEU A 140 8.854 -17.854 33.747 1.00 72.68 C
ANISOU 925 CD2 LEU A 140 5474 11259 10884 -1100 -196 701 C
ATOM 926 N ALA A 141 6.740 -19.955 29.836 1.00 71.22 N
ANISOU 926 N ALA A 141 5345 11147 10569 -1060 -9 561 N
ATOM 927 CA ALA A 141 7.403 -20.336 28.588 1.00 71.90 C
ANISOU 927 CA ALA A 141 5458 11209 10653 -1042 60 567 C
ATOM 928 C ALA A 141 6.475 -20.113 27.384 1.00 76.42 C
ANISOU 928 C ALA A 141 6095 11802 11140 -1025 57 516 C
ATOM 929 O ALA A 141 6.958 -19.738 26.314 1.00 76.48 O
ANISOU 929 O ALA A 141 6138 11800 11121 -995 102 529 O
ATOM 930 CB ALA A 141 7.845 -21.790 28.653 1.00 72.92 C
ANISOU 930 CB ALA A 141 5576 11307 10823 -1042 110 565 C
ATOM 931 N ILE A 142 5.150 -20.328 27.566 1.00 72.94 N
ANISOU 931 N ILE A 142 5664 11391 10660 -1041 3 471 N
ATOM 932 CA ILE A 142 4.122 -20.122 26.535 1.00 73.36 C
ANISOU 932 CA ILE A 142 5771 11465 10638 -1037 -22 431 C
ATOM 933 C ILE A 142 3.995 -18.606 26.266 1.00 77.63 C
ANISOU 933 C ILE A 142 6319 12035 11141 -1020 -38 448 C
ATOM 934 O ILE A 142 3.881 -18.197 25.107 1.00 77.72 O
ANISOU 934 O ILE A 142 6380 12052 11098 -1001 -24 435 O
ATOM 935 CB ILE A 142 2.763 -20.779 26.943 1.00 76.55 C
ANISOU 935 CB ILE A 142 6158 11893 11035 -1067 -84 407 C
ATOM 936 CG1 ILE A 142 2.878 -22.325 26.959 1.00 77.40 C
ANISOU 936 CG1 ILE A 142 6271 11957 11179 -1087 -77 388 C
ATOM 937 CG2 ILE A 142 1.626 -20.351 26.005 1.00 77.39 C
ANISOU 937 CG2 ILE A 142 6304 12028 11072 -1070 -131 384 C
ATOM 938 CD1 ILE A 142 1.806 -23.085 27.777 1.00 83.37 C
ANISOU 938 CD1 ILE A 142 6974 12731 11971 -1124 -135 396 C
ATOM 939 N ALA A 143 4.062 -17.785 27.336 1.00 73.96 N
ANISOU 939 N ALA A 143 5816 11583 10703 -1021 -68 477 N
ATOM 940 CA ALA A 143 3.995 -16.322 27.267 1.00 73.86 C
ANISOU 940 CA ALA A 143 5816 11584 10662 -1005 -93 496 C
ATOM 941 C ALA A 143 5.178 -15.743 26.478 1.00 78.94 C
ANISOU 941 C ALA A 143 6471 12198 11326 -993 -51 533 C
ATOM 942 O ALA A 143 4.994 -14.778 25.737 1.00 78.61 O
ANISOU 942 O ALA A 143 6454 12169 11245 -977 -55 539 O
ATOM 943 CB ALA A 143 3.966 -15.734 28.667 1.00 74.26 C
ANISOU 943 CB ALA A 143 5847 11633 10734 -1002 -139 516 C
ATOM 944 N ILE A 144 6.378 -16.350 26.621 1.00 76.43 N
ANISOU 944 N ILE A 144 6124 11843 11074 -999 -8 570 N
ATOM 945 CA ILE A 144 7.600 -15.959 25.909 1.00 77.07 C
ANISOU 945 CA ILE A 144 6195 11898 11192 -982 45 635 C
ATOM 946 C ILE A 144 7.475 -16.428 24.445 1.00 83.47 C
ANISOU 946 C ILE A 144 7057 12717 11939 -941 114 613 C
ATOM 947 O ILE A 144 7.811 -15.664 23.539 1.00 83.40 O
ANISOU 947 O ILE A 144 7064 12714 11911 -911 145 650 O
ATOM 948 CB ILE A 144 8.870 -16.513 26.624 1.00 80.04 C
ANISOU 948 CB ILE A 144 6511 12234 11665 -997 70 699 C
ATOM 949 CG1 ILE A 144 9.034 -15.865 28.020 1.00 79.84 C
ANISOU 949 CG1 ILE A 144 6455 12191 11690 -1034 -17 722 C
ATOM 950 CG2 ILE A 144 10.138 -16.299 25.779 1.00 81.60 C
ANISOU 950 CG2 ILE A 144 6683 12410 11912 -969 143 792 C
ATOM 951 CD1 ILE A 144 9.910 -16.638 29.020 1.00 86.66 C
ANISOU 951 CD1 ILE A 144 7266 13025 12638 -1059 -17 765 C
ATOM 952 N GLU A 145 6.948 -17.659 24.227 1.00 81.66 N
ANISOU 952 N GLU A 145 6865 12486 11674 -938 128 554 N
ATOM 953 CA GLU A 145 6.720 -18.276 22.912 1.00 82.69 C
ANISOU 953 CA GLU A 145 7077 12612 11728 -898 174 516 C
ATOM 954 C GLU A 145 5.807 -17.385 22.052 1.00 87.94 C
ANISOU 954 C GLU A 145 7790 13313 12309 -889 138 487 C
ATOM 955 O GLU A 145 6.105 -17.171 20.875 1.00 88.03 O
ANISOU 955 O GLU A 145 7858 13325 12265 -839 189 497 O
ATOM 956 CB GLU A 145 6.122 -19.692 23.088 1.00 84.27 C
ANISOU 956 CB GLU A 145 7313 12790 11915 -914 157 453 C
ATOM 957 CG GLU A 145 5.541 -20.349 21.840 1.00 98.32 C
ANISOU 957 CG GLU A 145 9204 14554 13600 -887 156 390 C
ATOM 958 CD GLU A 145 6.469 -20.655 20.679 1.00126.84 C
ANISOU 958 CD GLU A 145 12902 18136 17156 -806 249 403 C
ATOM 959 OE1 GLU A 145 7.681 -20.877 20.912 1.00127.58 O
ANISOU 959 OE1 GLU A 145 12963 18209 17303 -767 338 467 O
ATOM 960 OE2 GLU A 145 5.965 -20.729 19.534 1.00122.24 O1-
ANISOU 960 OE2 GLU A 145 12424 17549 16473 -778 233 355 O1-
ATOM 961 N ARG A 146 4.722 -16.850 22.648 1.00 85.14 N
ANISOU 961 N ARG A 146 7413 12992 11946 -927 58 462 N
ATOM 962 CA ARG A 146 3.782 -15.975 21.945 1.00 85.49 C
ANISOU 962 CA ARG A 146 7489 13074 11918 -920 21 444 C
ATOM 963 C ARG A 146 4.381 -14.575 21.741 1.00 91.29 C
ANISOU 963 C ARG A 146 8203 13816 12665 -898 41 502 C
ATOM 964 O ARG A 146 4.048 -13.918 20.756 1.00 91.28 O
ANISOU 964 O ARG A 146 8240 13839 12604 -873 47 502 O
ATOM 965 CB ARG A 146 2.428 -15.876 22.682 1.00 83.70 C
ANISOU 965 CB ARG A 146 7237 12883 11683 -957 -60 418 C
ATOM 966 CG ARG A 146 1.642 -17.191 22.821 1.00 88.38 C
ANISOU 966 CG ARG A 146 7839 13470 12272 -988 -99 378 C
ATOM 967 CD ARG A 146 1.438 -17.964 21.521 1.00 91.63 C
ANISOU 967 CD ARG A 146 8338 13859 12618 -981 -102 334 C
ATOM 968 NE ARG A 146 0.634 -17.246 20.528 1.00 95.35 N
ANISOU 968 NE ARG A 146 8852 14364 13014 -973 -138 325 N
ATOM 969 CZ ARG A 146 0.366 -17.699 19.309 1.00107.85 C
ANISOU 969 CZ ARG A 146 10530 15929 14520 -963 -157 287 C
ATOM 970 NH1 ARG A 146 0.841 -18.872 18.911 1.00 92.81 N
ANISOU 970 NH1 ARG A 146 8698 13967 12600 -952 -140 249 N
ATOM 971 NH2 ARG A 146 -0.376 -16.979 18.475 1.00 95.57 N1+
ANISOU 971 NH2 ARG A 146 9006 14407 12897 -958 -196 286 N1+
ATOM 972 N HIS A 147 5.275 -14.133 22.652 1.00 88.89 N
ANISOU 972 N HIS A 147 7841 13489 12444 -910 44 555 N
ATOM 973 CA HIS A 147 5.926 -12.822 22.581 1.00 89.58 C
ANISOU 973 CA HIS A 147 7903 13568 12567 -902 43 621 C
ATOM 974 C HIS A 147 6.941 -12.762 21.426 1.00 95.91 C
ANISOU 974 C HIS A 147 8708 14358 13374 -858 128 684 C
ATOM 975 O HIS A 147 7.197 -11.676 20.907 1.00 95.94 O
ANISOU 975 O HIS A 147 8702 14366 13384 -842 134 739 O
ATOM 976 CB HIS A 147 6.616 -12.486 23.912 1.00 90.17 C
ANISOU 976 CB HIS A 147 7925 13606 12731 -936 -1 663 C
ATOM 977 CG HIS A 147 6.993 -11.046 24.048 1.00 93.80 C
ANISOU 977 CG HIS A 147 8371 14044 13225 -942 -45 719 C
ATOM 978 ND1 HIS A 147 8.254 -10.593 23.699 1.00 96.15 N
ANISOU 978 ND1 HIS A 147 8626 14306 13599 -942 -19 815 N
ATOM 979 CD2 HIS A 147 6.255 -9.998 24.480 1.00 95.44 C
ANISOU 979 CD2 HIS A 147 8605 14255 13404 -946 -115 699 C
ATOM 980 CE1 HIS A 147 8.245 -9.292 23.935 1.00 95.69 C
ANISOU 980 CE1 HIS A 147 8571 14225 13562 -957 -87 846 C
ATOM 981 NE2 HIS A 147 7.063 -8.888 24.406 1.00 95.65 N
ANISOU 981 NE2 HIS A 147 8615 14240 13488 -955 -144 772 N
ATOM 982 N ILE A 148 7.501 -13.916 21.021 1.00 94.01 N
ANISOU 982 N ILE A 148 8487 14104 13129 -829 200 683 N
ATOM 983 CA ILE A 148 8.474 -13.992 19.931 1.00 95.34 C
ANISOU 983 CA ILE A 148 8668 14264 13292 -763 302 751 C
ATOM 984 C ILE A 148 7.726 -14.108 18.584 1.00101.92 C
ANISOU 984 C ILE A 148 9601 15126 13999 -711 328 697 C
ATOM 985 O ILE A 148 7.982 -13.298 17.691 1.00102.23 O
ANISOU 985 O ILE A 148 9647 15183 14012 -666 368 752 O
ATOM 986 CB ILE A 148 9.489 -15.160 20.143 1.00 98.69 C
ANISOU 986 CB ILE A 148 9077 14655 13767 -740 376 784 C
ATOM 987 CG1 ILE A 148 10.301 -14.972 21.448 1.00 98.65 C
ANISOU 987 CG1 ILE A 148 8968 14623 13893 -794 343 856 C
ATOM 988 CG2 ILE A 148 10.435 -15.308 18.934 1.00100.36 C
ANISOU 988 CG2 ILE A 148 9318 14863 13951 -644 502 858 C
ATOM 989 CD1 ILE A 148 10.950 -16.253 22.013 1.00104.80 C
ANISOU 989 CD1 ILE A 148 9720 15371 14727 -795 385 868 C
ATOM 990 N THR A 149 6.805 -15.095 18.454 1.00 99.82 N
ANISOU 990 N THR A 149 9409 14859 13658 -720 294 597 N
ATOM 991 CA THR A 149 6.034 -15.406 17.237 1.00100.93 C
ANISOU 991 CA THR A 149 9663 15012 13673 -680 292 535 C
ATOM 992 C THR A 149 5.203 -14.222 16.699 1.00106.78 C
ANISOU 992 C THR A 149 10411 15799 14362 -686 247 534 C
ATOM 993 O THR A 149 4.995 -14.152 15.486 1.00107.18 O
ANISOU 993 O THR A 149 10544 15863 14316 -630 275 524 O
ATOM 994 CB THR A 149 5.092 -16.599 17.466 1.00108.97 C
ANISOU 994 CB THR A 149 10740 16012 14651 -722 221 437 C
ATOM 995 OG1 THR A 149 4.308 -16.385 18.639 1.00107.72 O
ANISOU 995 OG1 THR A 149 10504 15873 14553 -800 134 419 O
ATOM 996 CG2 THR A 149 5.833 -17.924 17.556 1.00107.72 C
ANISOU 996 CG2 THR A 149 10620 15801 14507 -693 276 424 C
ATOM 997 N VAL A 150 4.722 -13.317 17.576 1.00104.03 N
ANISOU 997 N VAL A 150 9986 15472 14069 -744 178 544 N
ATOM 998 CA VAL A 150 3.929 -12.144 17.174 1.00104.45 C
ANISOU 998 CA VAL A 150 10038 15566 14083 -749 134 550 C
ATOM 999 C VAL A 150 4.863 -11.140 16.455 1.00110.72 C
ANISOU 999 C VAL A 150 10810 16363 14895 -699 203 640 C
ATOM 1000 O VAL A 150 4.512 -10.651 15.379 1.00110.75 O
ANISOU 1000 O VAL A 150 10860 16397 14823 -659 218 645 O
ATOM 1001 CB VAL A 150 3.177 -11.514 18.387 1.00107.53 C
ANISOU 1001 CB VAL A 150 10366 15969 14520 -807 51 539 C
ATOM 1002 CG1 VAL A 150 2.748 -10.071 18.119 1.00107.20 C
ANISOU 1002 CG1 VAL A 150 10312 15957 14464 -799 26 571 C
ATOM 1003 CG2 VAL A 150 1.974 -12.367 18.776 1.00107.19 C
ANISOU 1003 CG2 VAL A 150 10342 15941 14444 -845 -16 470 C
ATOM 1004 N PHE A 151 6.062 -10.884 17.020 1.00108.80 N
ANISOU 1004 N PHE A 151 10495 16090 14755 -700 241 719 N
ATOM 1005 CA PHE A 151 7.060 -9.980 16.446 1.00110.03 C
ANISOU 1005 CA PHE A 151 10607 16243 14957 -660 301 833 C
ATOM 1006 C PHE A 151 7.848 -10.654 15.295 1.00116.69 C
ANISOU 1006 C PHE A 151 11491 17088 15756 -570 422 882 C
ATOM 1007 O PHE A 151 8.533 -9.958 14.543 1.00116.68 O
ANISOU 1007 O PHE A 151 11463 17098 15773 -516 489 985 O
ATOM 1008 CB PHE A 151 8.021 -9.481 17.536 1.00111.70 C
ANISOU 1008 CB PHE A 151 10719 16412 15309 -707 276 915 C
ATOM 1009 CG PHE A 151 7.417 -8.438 18.447 1.00112.75 C
ANISOU 1009 CG PHE A 151 10829 16535 15474 -767 168 896 C
ATOM 1010 CD1 PHE A 151 6.719 -8.808 19.591 1.00114.95 C
ANISOU 1010 CD1 PHE A 151 11117 16807 15751 -814 93 815 C
ATOM 1011 CD2 PHE A 151 7.556 -7.082 18.166 1.00115.31 C
ANISOU 1011 CD2 PHE A 151 11128 16856 15828 -766 144 963 C
ATOM 1012 CE1 PHE A 151 6.166 -7.839 20.435 1.00115.44 C
ANISOU 1012 CE1 PHE A 151 11176 16858 15830 -848 5 801 C
ATOM 1013 CE2 PHE A 151 7.003 -6.113 19.010 1.00117.66 C
ANISOU 1013 CE2 PHE A 151 11426 17135 16145 -808 46 941 C
ATOM 1014 CZ PHE A 151 6.308 -6.498 20.136 1.00114.95 C
ANISOU 1014 CZ PHE A 151 11104 16783 15789 -843 -20 859 C
ATOM 1015 N ARG A 152 7.726 -11.990 15.151 1.00115.13 N
ANISOU 1015 N ARG A 152 11367 16878 15499 -545 451 812 N
ATOM 1016 CA ARG A 152 8.376 -12.763 14.087 1.00116.75 C
ANISOU 1016 CA ARG A 152 11647 17077 15637 -440 568 843 C
ATOM 1017 C ARG A 152 7.344 -13.201 13.018 1.00123.07 C
ANISOU 1017 C ARG A 152 12591 17895 16274 -398 550 744 C
ATOM 1018 O ARG A 152 7.711 -13.903 12.076 1.00123.69 O
ANISOU 1018 O ARG A 152 12768 17966 16262 -298 635 751 O
ATOM 1019 CB ARG A 152 9.114 -13.986 14.675 1.00117.23 C
ANISOU 1019 CB ARG A 152 11707 17095 15739 -430 615 839 C
ATOM 1020 N MET A 153 6.069 -12.768 13.178 1.00120.49 N
ANISOU 1020 N MET A 153 12278 17592 15912 -468 437 665 N
ATOM 1021 CA MET A 153 4.893 -13.020 12.329 1.00121.31 C
ANISOU 1021 CA MET A 153 12497 17715 15881 -462 374 576 C
ATOM 1022 C MET A 153 4.482 -14.506 12.249 1.00127.02 C
ANISOU 1022 C MET A 153 13340 18394 16529 -453 350 481 C
ATOM 1023 O MET A 153 3.330 -14.816 12.571 1.00126.49 O
ANISOU 1023 O MET A 153 13297 18321 16441 -527 236 400 O
ATOM 1024 CB MET A 153 5.060 -12.456 10.900 1.00124.54 C
ANISOU 1024 CB MET A 153 12962 18157 16198 -375 435 624 C
ATOM 1025 CG MET A 153 4.656 -11.006 10.776 1.00127.99 C
ANISOU 1025 CG MET A 153 13369 18643 16618 -416 362 624 C
ATOM 1026 SD MET A 153 5.769 -9.888 11.659 1.00131.29 S
ANISOU 1026 SD MET A 153 13622 19076 17186 -497 318 690 S
ATOM 1027 CE MET A 153 4.931 -8.315 11.400 1.00128.61 C
ANISOU 1027 CE MET A 153 13240 18759 16867 -419 416 824 C
ATOM 1028 N GLN A 154 5.389 -15.408 11.827 1.00125.25 N
ANISOU 1028 N GLN A 154 13191 18132 16266 -361 453 499 N
ATOM 1029 CA GLN A 154 5.082 -16.835 11.685 1.00126.16 C
ANISOU 1029 CA GLN A 154 13448 18190 16295 -334 435 411 C
ATOM 1030 C GLN A 154 5.977 -17.725 12.583 1.00130.78 C
ANISOU 1030 C GLN A 154 13992 18727 16972 -335 490 426 C
ATOM 1031 O GLN A 154 6.931 -17.235 13.193 1.00129.68 O
ANISOU 1031 O GLN A 154 13713 18603 16959 -354 543 513 O
ATOM 1032 CB GLN A 154 5.233 -17.248 10.203 1.00128.89 C
ANISOU 1032 CB GLN A 154 13967 18524 16482 -199 509 406 C
ATOM 1033 CG GLN A 154 4.298 -18.377 9.748 1.00143.36 C
ANISOU 1033 CG GLN A 154 15991 20302 18177 -196 412 282 C
ATOM 1034 CD GLN A 154 2.835 -18.001 9.802 1.00160.68 C
ANISOU 1034 CD GLN A 154 18182 22520 20348 -306 246 217 C
ATOM 1035 OE1 GLN A 154 2.380 -17.046 9.157 1.00155.03 O
ANISOU 1035 OE1 GLN A 154 17446 21863 19596 -305 228 245 O
ATOM 1036 NE2 GLN A 154 2.054 -18.772 10.550 1.00153.16 N
ANISOU 1036 NE2 GLN A 154 17252 21523 19419 -399 121 139 N
ATOM 1037 N LEU A 155 5.638 -19.044 12.660 1.00128.64 N
ANISOU 1037 N LEU A 155 13849 18393 16637 -316 468 344 N
ATOM 1038 CA LEU A 155 6.310 -20.094 13.437 1.00128.65 C
ANISOU 1038 CA LEU A 155 13841 18339 16703 -314 508 340 C
ATOM 1039 C LEU A 155 7.772 -20.300 12.993 1.00133.41 C
ANISOU 1039 C LEU A 155 14428 18934 17329 -192 684 448 C
ATOM 1040 O LEU A 155 8.174 -19.846 11.919 1.00133.70 O
ANISOU 1040 O LEU A 155 14498 18999 17303 -89 779 516 O
ATOM 1041 CB LEU A 155 5.547 -21.447 13.335 1.00129.52 C
ANISOU 1041 CB LEU A 155 14125 18370 16716 -311 432 224 C
ATOM 1042 CG LEU A 155 4.158 -21.604 14.014 1.00133.79 C
ANISOU 1042 CG LEU A 155 14665 18900 17271 -445 249 134 C
ATOM 1043 CD1 LEU A 155 4.144 -21.096 15.466 1.00132.61 C
ANISOU 1043 CD1 LEU A 155 14322 18784 17278 -559 205 165 C
ATOM 1044 CD2 LEU A 155 3.029 -21.017 13.170 1.00136.69 C
ANISOU 1044 CD2 LEU A 155 15104 19297 17536 -465 151 94 C
ATOM 1045 N HIS A 156 8.552 -21.004 13.830 1.00129.91 N
ANISOU 1045 N HIS A 156 13925 18454 16981 -203 727 473 N
ATOM 1046 CA HIS A 156 9.972 -21.269 13.609 1.00130.30 C
ANISOU 1046 CA HIS A 156 13933 18491 17082 -102 886 588 C
ATOM 1047 C HIS A 156 10.206 -22.628 12.906 1.00134.33 C
ANISOU 1047 C HIS A 156 14635 18930 17475 25 966 543 C
ATOM 1048 O HIS A 156 9.247 -23.353 12.612 1.00134.41 O
ANISOU 1048 O HIS A 156 14812 18893 17363 24 879 417 O
ATOM 1049 CB HIS A 156 10.737 -21.230 14.944 1.00130.31 C
ANISOU 1049 CB HIS A 156 13764 18493 17256 -194 873 640 C
ATOM 1050 CG HIS A 156 10.101 -20.369 15.993 1.00132.53 C
ANISOU 1050 CG HIS A 156 13920 18813 17624 -339 739 614 C
ATOM 1051 ND1 HIS A 156 9.289 -20.912 16.975 1.00133.61 N
ANISOU 1051 ND1 HIS A 156 14052 18930 17784 -441 621 517 N
ATOM 1052 CD2 HIS A 156 10.149 -19.026 16.160 1.00133.78 C
ANISOU 1052 CD2 HIS A 156 13962 19023 17846 -385 714 682 C
ATOM 1053 CE1 HIS A 156 8.892 -19.892 17.715 1.00132.05 C
ANISOU 1053 CE1 HIS A 156 13740 18778 17655 -533 539 530 C
ATOM 1054 NE2 HIS A 156 9.381 -18.737 17.263 1.00132.45 N
ANISOU 1054 NE2 HIS A 156 13729 18866 17728 -505 586 620 N
ATOM 1055 N THR A 157 11.494 -22.957 12.644 1.00130.56 N
ANISOU 1055 N THR A 157 14134 18436 17036 137 1126 653 N
ATOM 1056 CA THR A 157 11.943 -24.179 11.965 1.00131.25 C
ANISOU 1056 CA THR A 157 14407 18450 17013 281 1225 625 C
ATOM 1057 C THR A 157 12.146 -25.343 12.970 1.00133.32 C
ANISOU 1057 C THR A 157 14657 18645 17353 216 1184 570 C
ATOM 1058 O THR A 157 11.709 -25.250 14.123 1.00131.51 O
ANISOU 1058 O THR A 157 14301 18431 17238 60 1064 533 O
ATOM 1059 CB THR A 157 13.237 -23.901 11.171 1.00140.30 C
ANISOU 1059 CB THR A 157 15538 19618 18151 460 1439 793 C
ATOM 1060 OG1 THR A 157 14.241 -23.386 12.050 1.00139.12 O
ANISOU 1060 OG1 THR A 157 15153 19511 18196 406 1493 943 O
ATOM 1061 CG2 THR A 157 13.020 -22.947 9.998 1.00139.39 C
ANISOU 1061 CG2 THR A 157 15477 19557 17928 554 1492 842 C
ATOM 1062 N ARG A 158 12.791 -26.444 12.507 1.00130.02 N
ANISOU 1062 N ARG A 158 14378 18155 16867 350 1292 569 N
ATOM 1063 CA ARG A 158 13.079 -27.670 13.261 1.00129.18 C
ANISOU 1063 CA ARG A 158 14287 17976 16820 322 1280 527 C
ATOM 1064 C ARG A 158 14.015 -27.423 14.458 1.00130.27 C
ANISOU 1064 C ARG A 158 14180 18156 17160 258 1336 657 C
ATOM 1065 O ARG A 158 13.918 -28.147 15.452 1.00129.25 O
ANISOU 1065 O ARG A 158 14000 17992 17119 168 1273 616 O
ATOM 1066 CB ARG A 158 13.701 -28.731 12.338 1.00131.43 C
ANISOU 1066 CB ARG A 158 14795 18173 16969 513 1408 514 C
ATOM 1067 N MET A 159 14.911 -26.407 14.365 1.00125.24 N
ANISOU 1067 N MET A 159 13394 17592 16600 299 1444 821 N
ATOM 1068 CA MET A 159 15.864 -26.043 15.422 1.00123.57 C
ANISOU 1068 CA MET A 159 12951 17420 16580 238 1485 965 C
ATOM 1069 C MET A 159 15.127 -25.742 16.742 1.00123.72 C
ANISOU 1069 C MET A 159 12839 17459 16708 37 1307 894 C
ATOM 1070 O MET A 159 15.571 -26.208 17.795 1.00122.88 O
ANISOU 1070 O MET A 159 12623 17342 16725 -25 1298 931 O
ATOM 1071 CB MET A 159 16.734 -24.841 14.992 1.00126.30 C
ANISOU 1071 CB MET A 159 13170 17835 16983 300 1592 1149 C
ATOM 1072 CG MET A 159 17.793 -24.426 16.017 1.00129.50 C
ANISOU 1072 CG MET A 159 13340 18272 17593 236 1621 1318 C
ATOM 1073 SD MET A 159 19.006 -25.716 16.407 1.00134.61 S
ANISOU 1073 SD MET A 159 13955 18871 18319 325 1764 1422 S
ATOM 1074 CE MET A 159 19.810 -24.985 17.802 1.00130.27 C
ANISOU 1074 CE MET A 159 13123 18364 18009 178 1704 1579 C
ATOM 1075 N SER A 160 13.989 -25.014 16.672 1.00117.60 N
ANISOU 1075 N SER A 160 12087 16713 15881 -53 1172 795 N
ATOM 1076 CA SER A 160 13.172 -24.659 17.833 1.00115.04 C
ANISOU 1076 CA SER A 160 11660 16413 15638 -221 1011 729 C
ATOM 1077 C SER A 160 12.510 -25.881 18.473 1.00116.43 C
ANISOU 1077 C SER A 160 11890 16532 15816 -283 930 616 C
ATOM 1078 O SER A 160 12.341 -25.886 19.692 1.00115.07 O
ANISOU 1078 O SER A 160 11594 16374 15753 -392 856 617 O
ATOM 1079 CB SER A 160 12.106 -23.642 17.452 1.00118.00 C
ANISOU 1079 CB SER A 160 12063 16830 15941 -274 908 662 C
ATOM 1080 OG SER A 160 12.711 -22.381 17.220 1.00126.29 O
ANISOU 1080 OG SER A 160 13008 17937 17041 -260 953 779 O
ATOM 1081 N ASN A 161 12.156 -26.913 17.670 1.00112.03 N
ANISOU 1081 N ASN A 161 11523 15906 15139 -210 940 524 N
ATOM 1082 CA ASN A 161 11.548 -28.157 18.163 1.00110.81 C
ANISOU 1082 CA ASN A 161 11432 15682 14990 -264 860 425 C
ATOM 1083 C ASN A 161 12.546 -28.917 19.051 1.00111.76 C
ANISOU 1083 C ASN A 161 11450 15781 15232 -257 941 503 C
ATOM 1084 O ASN A 161 12.142 -29.495 20.063 1.00110.62 O
ANISOU 1084 O ASN A 161 11241 15621 15167 -355 858 465 O
ATOM 1085 CB ASN A 161 11.056 -29.038 17.006 1.00113.05 C
ANISOU 1085 CB ASN A 161 11961 15877 15115 -173 855 322 C
ATOM 1086 CG ASN A 161 9.916 -28.437 16.208 1.00136.80 C
ANISOU 1086 CG ASN A 161 15103 18889 17987 -173 765 237 C
ATOM 1087 OD1 ASN A 161 8.835 -28.146 16.725 1.00130.40 O
ANISOU 1087 OD1 ASN A 161 14241 18115 17191 -292 624 186 O
ATOM 1088 ND2 ASN A 161 10.137 -28.240 14.921 1.00130.50 N
ANISOU 1088 ND2 ASN A 161 14503 18042 17041 -28 842 215 N
ATOM 1089 N ARG A 162 13.847 -28.870 18.692 1.00106.87 N
ANISOU 1089 N ARG A 162 10809 15166 14631 -137 1106 626 N
ATOM 1090 CA ARG A 162 14.940 -29.470 19.460 1.00105.74 C
ANISOU 1090 CA ARG A 162 10558 15009 14608 -116 1200 729 C
ATOM 1091 C ARG A 162 15.213 -28.633 20.711 1.00105.91 C
ANISOU 1091 C ARG A 162 10354 15100 14785 -237 1147 815 C
ATOM 1092 O ARG A 162 15.582 -29.185 21.748 1.00105.00 O
ANISOU 1092 O ARG A 162 10141 14975 14780 -288 1142 851 O
ATOM 1093 CB ARG A 162 16.208 -29.599 18.603 1.00107.16 C
ANISOU 1093 CB ARG A 162 10779 15179 14759 60 1397 855 C
ATOM 1094 N ARG A 163 15.019 -27.299 20.606 1.00100.05 N
ANISOU 1094 N ARG A 163 9544 14423 14048 -280 1101 846 N
ATOM 1095 CA ARG A 163 15.181 -26.339 21.700 1.00 97.86 C
ANISOU 1095 CA ARG A 163 9085 14200 13897 -392 1028 915 C
ATOM 1096 C ARG A 163 14.057 -26.486 22.724 1.00 98.50 C
ANISOU 1096 C ARG A 163 9140 14286 14001 -522 876 805 C
ATOM 1097 O ARG A 163 14.297 -26.256 23.906 1.00 97.54 O
ANISOU 1097 O ARG A 163 8888 14185 13989 -601 827 852 O
ATOM 1098 CB ARG A 163 15.218 -24.893 21.178 1.00 98.04 C
ANISOU 1098 CB ARG A 163 9069 14276 13904 -392 1017 968 C
ATOM 1099 CG ARG A 163 16.518 -24.493 20.499 1.00109.58 C
ANISOU 1099 CG ARG A 163 10479 15753 15405 -288 1160 1137 C
ATOM 1100 CD ARG A 163 16.451 -23.063 19.995 1.00118.89 C
ANISOU 1100 CD ARG A 163 11621 16979 16571 -293 1140 1189 C
ATOM 1101 NE ARG A 163 17.688 -22.659 19.325 1.00127.30 N
ANISOU 1101 NE ARG A 163 12618 18060 17690 -192 1279 1376 N
ATOM 1102 CZ ARG A 163 17.887 -21.471 18.761 1.00141.15 C
ANISOU 1102 CZ ARG A 163 14329 19853 19448 -169 1296 1465 C
ATOM 1103 NH1 ARG A 163 16.931 -20.550 18.777 1.00127.46 N
ANISOU 1103 NH1 ARG A 163 12624 18143 17660 -237 1185 1374 N
ATOM 1104 NH2 ARG A 163 19.044 -21.196 18.176 1.00129.30 N1+
ANISOU 1104 NH2 ARG A 163 12750 18366 18011 -74 1430 1658 N1+
ATOM 1105 N VAL A 164 12.835 -26.858 22.268 1.00 93.11 N
ANISOU 1105 N VAL A 164 8580 13583 13215 -540 799 669 N
ATOM 1106 CA VAL A 164 11.640 -27.062 23.099 1.00 91.26 C
ANISOU 1106 CA VAL A 164 8325 13354 12995 -650 661 577 C
ATOM 1107 C VAL A 164 11.907 -28.203 24.097 1.00 92.73 C
ANISOU 1107 C VAL A 164 8461 13504 13267 -680 664 584 C
ATOM 1108 O VAL A 164 11.546 -28.072 25.267 1.00 91.55 O
ANISOU 1108 O VAL A 164 8208 13384 13192 -767 587 587 O
ATOM 1109 CB VAL A 164 10.376 -27.314 22.222 1.00 95.70 C
ANISOU 1109 CB VAL A 164 9032 13894 13437 -654 582 455 C
ATOM 1110 CG1 VAL A 164 9.298 -28.113 22.954 1.00 95.14 C
ANISOU 1110 CG1 VAL A 164 8955 13803 13392 -744 465 379 C
ATOM 1111 CG2 VAL A 164 9.802 -25.997 21.714 1.00 95.27 C
ANISOU 1111 CG2 VAL A 164 8976 13896 13325 -669 536 448 C
ATOM 1112 N VAL A 165 12.578 -29.283 23.642 1.00 88.51 N
ANISOU 1112 N VAL A 165 8002 12908 12720 -598 761 595 N
ATOM 1113 CA VAL A 165 12.957 -30.444 24.461 1.00 87.63 C
ANISOU 1113 CA VAL A 165 7852 12754 12688 -610 783 610 C
ATOM 1114 C VAL A 165 13.821 -29.956 25.645 1.00 88.76 C
ANISOU 1114 C VAL A 165 7815 12946 12964 -655 801 726 C
ATOM 1115 O VAL A 165 13.584 -30.367 26.781 1.00 87.83 O
ANISOU 1115 O VAL A 165 7618 12833 12921 -729 742 720 O
ATOM 1116 CB VAL A 165 13.679 -31.538 23.619 1.00 92.87 C
ANISOU 1116 CB VAL A 165 8643 13341 13303 -485 908 618 C
ATOM 1117 CG1 VAL A 165 14.038 -32.757 24.469 1.00 92.74 C
ANISOU 1117 CG1 VAL A 165 8589 13276 13372 -497 931 634 C
ATOM 1118 CG2 VAL A 165 12.834 -31.960 22.418 1.00 93.54 C
ANISOU 1118 CG2 VAL A 165 8933 13366 13242 -438 870 498 C
ATOM 1119 N VAL A 166 14.769 -29.032 25.371 1.00 83.77 N
ANISOU 1119 N VAL A 166 7120 12349 12360 -614 872 836 N
ATOM 1120 CA VAL A 166 15.668 -28.415 26.354 1.00 82.27 C
ANISOU 1120 CA VAL A 166 6768 12195 12295 -659 873 961 C
ATOM 1121 C VAL A 166 14.842 -27.534 27.318 1.00 83.76 C
ANISOU 1121 C VAL A 166 6891 12429 12506 -772 728 917 C
ATOM 1122 O VAL A 166 15.079 -27.584 28.524 1.00 82.97 O
ANISOU 1122 O VAL A 166 6692 12339 12493 -834 680 956 O
ATOM 1123 CB VAL A 166 16.805 -27.612 25.662 1.00 86.42 C
ANISOU 1123 CB VAL A 166 7251 12740 12847 -588 971 1098 C
ATOM 1124 CG1 VAL A 166 17.724 -26.944 26.681 1.00 85.86 C
ANISOU 1124 CG1 VAL A 166 7013 12695 12917 -650 943 1237 C
ATOM 1125 CG2 VAL A 166 17.616 -28.504 24.726 1.00 87.42 C
ANISOU 1125 CG2 VAL A 166 7451 12825 12941 -451 1133 1154 C
ATOM 1126 N VAL A 167 13.861 -26.766 26.785 1.00 78.85 N
ANISOU 1126 N VAL A 167 6330 11832 11797 -789 661 838 N
ATOM 1127 CA VAL A 167 12.970 -25.878 27.551 1.00 77.10 C
ANISOU 1127 CA VAL A 167 6067 11652 11574 -874 536 795 C
ATOM 1128 C VAL A 167 12.114 -26.734 28.517 1.00 79.23 C
ANISOU 1128 C VAL A 167 6327 11919 11860 -929 466 726 C
ATOM 1129 O VAL A 167 12.009 -26.376 29.690 1.00 78.18 O
ANISOU 1129 O VAL A 167 6115 11812 11778 -985 399 747 O
ATOM 1130 CB VAL A 167 12.102 -24.976 26.620 1.00 80.77 C
ANISOU 1130 CB VAL A 167 6607 12143 11939 -866 496 732 C
ATOM 1131 CG1 VAL A 167 11.034 -24.206 27.396 1.00 79.82 C
ANISOU 1131 CG1 VAL A 167 6457 12063 11808 -938 377 684 C
ATOM 1132 CG2 VAL A 167 12.977 -24.003 25.838 1.00 81.00 C
ANISOU 1132 CG2 VAL A 167 6624 12183 11968 -816 559 819 C
ATOM 1133 N ILE A 168 11.564 -27.880 28.041 1.00 75.21 N
ANISOU 1133 N ILE A 168 5898 11371 11306 -910 480 654 N
ATOM 1134 CA ILE A 168 10.757 -28.824 28.830 1.00 74.18 C
ANISOU 1134 CA ILE A 168 5756 11230 11200 -960 418 602 C
ATOM 1135 C ILE A 168 11.587 -29.316 30.040 1.00 77.40 C
ANISOU 1135 C ILE A 168 6059 11635 11713 -979 443 675 C
ATOM 1136 O ILE A 168 11.059 -29.351 31.154 1.00 76.08 O
ANISOU 1136 O ILE A 168 5827 11495 11582 -1032 374 672 O
ATOM 1137 CB ILE A 168 10.237 -29.997 27.939 1.00 77.89 C
ANISOU 1137 CB ILE A 168 6346 11637 11614 -932 427 525 C
ATOM 1138 CG1 ILE A 168 9.101 -29.503 27.005 1.00 78.34 C
ANISOU 1138 CG1 ILE A 168 6493 11702 11569 -941 357 447 C
ATOM 1139 CG2 ILE A 168 9.765 -31.204 28.782 1.00 78.77 C
ANISOU 1139 CG2 ILE A 168 6428 11719 11782 -977 383 504 C
ATOM 1140 CD1 ILE A 168 8.679 -30.461 25.866 1.00 86.82 C
ANISOU 1140 CD1 ILE A 168 7720 12701 12566 -905 352 371 C
ATOM 1141 N VAL A 169 12.886 -29.635 29.823 1.00 74.74 N
ANISOU 1141 N VAL A 169 5704 11269 11423 -928 543 753 N
ATOM 1142 CA VAL A 169 13.828 -30.086 30.861 1.00 74.37 C
ANISOU 1142 CA VAL A 169 5556 11218 11482 -941 574 840 C
ATOM 1143 C VAL A 169 13.981 -28.971 31.925 1.00 77.70 C
ANISOU 1143 C VAL A 169 5880 11689 11951 -1001 495 892 C
ATOM 1144 O VAL A 169 13.836 -29.262 33.111 1.00 76.76 O
ANISOU 1144 O VAL A 169 5700 11584 11881 -1045 444 902 O
ATOM 1145 CB VAL A 169 15.196 -30.520 30.254 1.00 78.89 C
ANISOU 1145 CB VAL A 169 6126 11755 12096 -864 707 934 C
ATOM 1146 CG1 VAL A 169 16.253 -30.749 31.334 1.00 78.79 C
ANISOU 1146 CG1 VAL A 169 5987 11746 12204 -886 728 1048 C
ATOM 1147 CG2 VAL A 169 15.045 -31.769 29.392 1.00 79.36 C
ANISOU 1147 CG2 VAL A 169 6302 11750 12102 -794 780 875 C
ATOM 1148 N VAL A 170 14.208 -27.706 31.492 1.00 74.43 N
ANISOU 1148 N VAL A 170 5466 11298 11516 -999 478 923 N
ATOM 1149 CA VAL A 170 14.357 -26.518 32.354 1.00 73.89 C
ANISOU 1149 CA VAL A 170 5336 11259 11481 -1050 390 968 C
ATOM 1150 C VAL A 170 13.083 -26.328 33.228 1.00 77.24 C
ANISOU 1150 C VAL A 170 5774 11714 11858 -1093 287 884 C
ATOM 1151 O VAL A 170 13.213 -26.090 34.431 1.00 76.58 O
ANISOU 1151 O VAL A 170 5640 11642 11814 -1128 224 915 O
ATOM 1152 CB VAL A 170 14.681 -25.242 31.517 1.00 77.89 C
ANISOU 1152 CB VAL A 170 5857 11773 11965 -1034 390 1005 C
ATOM 1153 CG1 VAL A 170 14.618 -23.969 32.362 1.00 77.37 C
ANISOU 1153 CG1 VAL A 170 5758 11723 11917 -1089 276 1029 C
ATOM 1154 CG2 VAL A 170 16.041 -25.363 30.835 1.00 78.46 C
ANISOU 1154 CG2 VAL A 170 5889 11822 12101 -985 497 1125 C
ATOM 1155 N ILE A 171 11.875 -26.469 32.628 1.00 73.60 N
ANISOU 1155 N ILE A 171 5383 11266 11314 -1084 272 790 N
ATOM 1156 CA ILE A 171 10.571 -26.328 33.300 1.00 72.85 C
ANISOU 1156 CA ILE A 171 5297 11209 11176 -1111 191 728 C
ATOM 1157 C ILE A 171 10.435 -27.394 34.419 1.00 76.91 C
ANISOU 1157 C ILE A 171 5758 11722 11741 -1130 182 738 C
ATOM 1158 O ILE A 171 10.094 -27.037 35.550 1.00 76.03 O
ANISOU 1158 O ILE A 171 5614 11642 11632 -1145 122 750 O
ATOM 1159 CB ILE A 171 9.391 -26.401 32.277 1.00 75.74 C
ANISOU 1159 CB ILE A 171 5737 11582 11458 -1100 180 647 C
ATOM 1160 CG1 ILE A 171 9.403 -25.178 31.330 1.00 76.15 C
ANISOU 1160 CG1 ILE A 171 5835 11645 11452 -1082 178 640 C
ATOM 1161 CG2 ILE A 171 8.030 -26.511 32.982 1.00 75.95 C
ANISOU 1161 CG2 ILE A 171 5751 11646 11459 -1124 109 610 C
ATOM 1162 CD1 ILE A 171 8.581 -25.334 30.021 1.00 84.47 C
ANISOU 1162 CD1 ILE A 171 6973 12695 12426 -1064 183 573 C
ATOM 1163 N TRP A 172 10.718 -28.678 34.106 1.00 74.04 N
ANISOU 1163 N TRP A 172 5396 11321 11413 -1120 242 736 N
ATOM 1164 CA TRP A 172 10.615 -29.777 35.068 1.00 74.00 C
ANISOU 1164 CA TRP A 172 5339 11311 11466 -1137 240 750 C
ATOM 1165 C TRP A 172 11.733 -29.725 36.125 1.00 78.22 C
ANISOU 1165 C TRP A 172 5797 11848 12076 -1146 248 833 C
ATOM 1166 O TRP A 172 11.467 -30.078 37.275 1.00 78.04 O
ANISOU 1166 O TRP A 172 5725 11848 12079 -1164 211 850 O
ATOM 1167 CB TRP A 172 10.615 -31.140 34.362 1.00 73.28 C
ANISOU 1167 CB TRP A 172 5287 11165 11392 -1121 297 723 C
ATOM 1168 CG TRP A 172 9.300 -31.470 33.712 1.00 74.51 C
ANISOU 1168 CG TRP A 172 5506 11312 11491 -1133 251 646 C
ATOM 1169 CD1 TRP A 172 9.014 -31.451 32.379 1.00 77.83 C
ANISOU 1169 CD1 TRP A 172 6025 11700 11846 -1112 260 590 C
ATOM 1170 CD2 TRP A 172 8.080 -31.819 34.380 1.00 74.09 C
ANISOU 1170 CD2 TRP A 172 5418 11287 11445 -1168 180 630 C
ATOM 1171 NE1 TRP A 172 7.695 -31.788 32.172 1.00 77.46 N
ANISOU 1171 NE1 TRP A 172 6009 11653 11770 -1143 185 538 N
ATOM 1172 CE2 TRP A 172 7.096 -32.012 33.384 1.00 78.42 C
ANISOU 1172 CE2 TRP A 172 6040 11813 11942 -1178 139 570 C
ATOM 1173 CE3 TRP A 172 7.721 -31.994 35.728 1.00 74.97 C
ANISOU 1173 CE3 TRP A 172 5443 11442 11601 -1187 148 673 C
ATOM 1174 CZ2 TRP A 172 5.779 -32.368 33.692 1.00 77.74 C
ANISOU 1174 CZ2 TRP A 172 5927 11745 11864 -1215 63 563 C
ATOM 1175 CZ3 TRP A 172 6.418 -32.344 36.032 1.00 76.47 C
ANISOU 1175 CZ3 TRP A 172 5608 11655 11791 -1210 88 667 C
ATOM 1176 CH2 TRP A 172 5.462 -32.525 35.023 1.00 77.48 C
ANISOU 1176 CH2 TRP A 172 5795 11761 11885 -1228 45 619 C
ATOM 1177 N THR A 173 12.955 -29.265 35.756 1.00 74.66 N
ANISOU 1177 N THR A 173 5330 11375 11661 -1134 291 898 N
ATOM 1178 CA THR A 173 14.089 -29.145 36.688 1.00 74.32 C
ANISOU 1178 CA THR A 173 5209 11329 11701 -1152 284 994 C
ATOM 1179 C THR A 173 13.758 -28.070 37.739 1.00 78.01 C
ANISOU 1179 C THR A 173 5668 11829 12143 -1183 174 996 C
ATOM 1180 O THR A 173 13.955 -28.315 38.931 1.00 77.74 O
ANISOU 1180 O THR A 173 5589 11803 12143 -1202 132 1031 O
ATOM 1181 CB THR A 173 15.400 -28.854 35.925 1.00 78.92 C
ANISOU 1181 CB THR A 173 5768 11882 12335 -1131 352 1082 C
ATOM 1182 OG1 THR A 173 15.600 -29.891 34.961 1.00 76.57 O
ANISOU 1182 OG1 THR A 173 5505 11550 12037 -1079 463 1071 O
ATOM 1183 CG2 THR A 173 16.621 -28.779 36.843 1.00 76.41 C
ANISOU 1183 CG2 THR A 173 5357 11555 12119 -1158 336 1201 C
ATOM 1184 N MET A 174 13.206 -26.922 37.294 1.00 74.36 N
ANISOU 1184 N MET A 174 5261 11382 11611 -1181 126 955 N
ATOM 1185 CA MET A 174 12.784 -25.815 38.155 1.00 74.26 C
ANISOU 1185 CA MET A 174 5271 11389 11556 -1195 22 948 C
ATOM 1186 C MET A 174 11.698 -26.293 39.137 1.00 76.06 C
ANISOU 1186 C MET A 174 5508 11657 11735 -1182 -12 899 C
ATOM 1187 O MET A 174 11.758 -25.966 40.321 1.00 75.21 O
ANISOU 1187 O MET A 174 5399 11558 11619 -1183 -78 921 O
ATOM 1188 CB MET A 174 12.275 -24.637 37.298 1.00 77.13 C
ANISOU 1188 CB MET A 174 5692 11753 11859 -1187 -6 918 C
ATOM 1189 CG MET A 174 11.896 -23.405 38.100 1.00 81.19 C
ANISOU 1189 CG MET A 174 6270 12306 12274 -1166 -41 835 C
ATOM 1190 SD MET A 174 11.191 -22.104 37.077 1.00 86.30 S
ANISOU 1190 SD MET A 174 6975 12943 12870 -1165 -105 832 S
ATOM 1191 CE MET A 174 10.656 -20.959 38.351 1.00 83.29 C
ANISOU 1191 CE MET A 174 6624 12555 12465 -1168 -219 844 C
ATOM 1192 N ALA A 175 10.740 -27.095 38.639 1.00 71.69 N
ANISOU 1192 N ALA A 175 4961 11121 11158 -1168 33 847 N
ATOM 1193 CA ALA A 175 9.638 -27.665 39.406 1.00 71.08 C
ANISOU 1193 CA ALA A 175 4870 11082 11053 -1154 15 824 C
ATOM 1194 C ALA A 175 10.146 -28.585 40.529 1.00 74.42 C
ANISOU 1194 C ALA A 175 5230 11505 11541 -1161 23 876 C
ATOM 1195 O ALA A 175 9.662 -28.475 41.657 1.00 74.03 O
ANISOU 1195 O ALA A 175 5173 11491 11463 -1140 -18 890 O
ATOM 1196 CB ALA A 175 8.715 -28.435 38.480 1.00 71.87 C
ANISOU 1196 CB ALA A 175 4982 11184 11142 -1155 51 777 C
ATOM 1197 N ILE A 176 11.122 -29.470 40.226 1.00 70.76 N
ANISOU 1197 N ILE A 176 4725 11002 11160 -1179 82 911 N
ATOM 1198 CA ILE A 176 11.719 -30.422 41.179 1.00 70.32 C
ANISOU 1198 CA ILE A 176 4602 10942 11176 -1187 99 968 C
ATOM 1199 C ILE A 176 12.486 -29.645 42.269 1.00 73.39 C
ANISOU 1199 C ILE A 176 4979 11335 11571 -1195 32 1024 C
ATOM 1200 O ILE A 176 12.319 -29.960 43.447 1.00 72.89 O
ANISOU 1200 O ILE A 176 4891 11297 11507 -1186 2 1048 O
ATOM 1201 CB ILE A 176 12.623 -31.479 40.457 1.00 73.55 C
ANISOU 1201 CB ILE A 176 4980 11300 11666 -1193 187 996 C
ATOM 1202 CG1 ILE A 176 11.766 -32.398 39.551 1.00 74.10 C
ANISOU 1202 CG1 ILE A 176 5082 11351 11723 -1185 230 933 C
ATOM 1203 CG2 ILE A 176 13.419 -32.333 41.468 1.00 74.08 C
ANISOU 1203 CG2 ILE A 176 4969 11359 11817 -1203 206 1071 C
ATOM 1204 CD1 ILE A 176 12.510 -33.140 38.427 1.00 81.48 C
ANISOU 1204 CD1 ILE A 176 6041 12223 12693 -1169 317 934 C
ATOM 1205 N VAL A 177 13.283 -28.625 41.877 1.00 69.73 N
ANISOU 1205 N VAL A 177 4539 10845 11110 -1212 0 1047 N
ATOM 1206 CA VAL A 177 14.084 -27.794 42.790 1.00 69.81 C
ANISOU 1206 CA VAL A 177 4552 10841 11132 -1233 -91 1103 C
ATOM 1207 C VAL A 177 13.148 -26.997 43.735 1.00 74.05 C
ANISOU 1207 C VAL A 177 5163 11410 11565 -1202 -180 1058 C
ATOM 1208 O VAL A 177 13.328 -27.082 44.954 1.00 73.66 O
ANISOU 1208 O VAL A 177 5113 11365 11507 -1196 -235 1088 O
ATOM 1209 CB VAL A 177 15.072 -26.861 42.021 1.00 73.93 C
ANISOU 1209 CB VAL A 177 5077 11322 11693 -1262 -111 1150 C
ATOM 1210 CG1 VAL A 177 15.705 -25.818 42.943 1.00 74.05 C
ANISOU 1210 CG1 VAL A 177 5116 11310 11711 -1293 -242 1200 C
ATOM 1211 CG2 VAL A 177 16.159 -27.671 41.314 1.00 74.03 C
ANISOU 1211 CG2 VAL A 177 5010 11307 11812 -1273 -15 1227 C
ATOM 1212 N MET A 178 12.138 -26.272 43.178 1.00 70.79 N
ANISOU 1212 N MET A 178 4816 11017 11066 -1174 -187 989 N
ATOM 1213 CA MET A 178 11.165 -25.468 43.940 1.00 70.65 C
ANISOU 1213 CA MET A 178 4876 11028 10938 -1124 -253 950 C
ATOM 1214 C MET A 178 10.340 -26.337 44.909 1.00 73.48 C
ANISOU 1214 C MET A 178 5209 11438 11270 -1079 -226 954 C
ATOM 1215 O MET A 178 9.934 -25.855 45.970 1.00 73.33 O
ANISOU 1215 O MET A 178 5248 11440 11174 -1027 -281 955 O
ATOM 1216 CB MET A 178 10.223 -24.689 43.004 1.00 73.05 C
ANISOU 1216 CB MET A 178 5235 11348 11171 -1102 -243 889 C
ATOM 1217 CG MET A 178 10.901 -23.550 42.255 1.00 77.24 C
ANISOU 1217 CG MET A 178 5808 11833 11707 -1132 -289 890 C
ATOM 1218 SD MET A 178 11.406 -22.174 43.313 1.00 82.39 S
ANISOU 1218 SD MET A 178 6557 12440 12305 -1125 -432 905 S
ATOM 1219 CE MET A 178 12.481 -21.298 42.198 1.00 79.41 C
ANISOU 1219 CE MET A 178 6173 12002 11996 -1188 -464 942 C
ATOM 1220 N GLY A 179 10.126 -27.599 44.539 1.00 68.94 N
ANISOU 1220 N GLY A 179 4554 10878 10760 -1093 -145 962 N
ATOM 1221 CA GLY A 179 9.408 -28.572 45.354 1.00 68.42 C
ANISOU 1221 CA GLY A 179 4441 10858 10698 -1059 -114 985 C
ATOM 1222 C GLY A 179 10.300 -29.340 46.312 1.00 71.76 C
ANISOU 1222 C GLY A 179 4808 11270 11186 -1074 -114 1045 C
ATOM 1223 O GLY A 179 9.829 -30.243 47.005 1.00 71.76 O
ANISOU 1223 O GLY A 179 4757 11307 11204 -1049 -82 1076 O
ATOM 1224 N ALA A 180 11.598 -28.988 46.358 1.00 67.78 N
ANISOU 1224 N ALA A 180 4309 10720 10726 -1116 -154 1076 N
ATOM 1225 CA ALA A 180 12.595 -29.613 47.230 1.00 67.34 C
ANISOU 1225 CA ALA A 180 4198 10648 10739 -1138 -166 1146 C
ATOM 1226 C ALA A 180 13.169 -28.616 48.246 1.00 70.48 C
ANISOU 1226 C ALA A 180 4666 11029 11086 -1133 -284 1170 C
ATOM 1227 O ALA A 180 13.573 -29.043 49.326 1.00 70.42 O
ANISOU 1227 O ALA A 180 4639 11027 11090 -1126 -315 1218 O
ATOM 1228 CB ALA A 180 13.721 -30.203 46.399 1.00 68.06 C
ANISOU 1228 CB ALA A 180 4218 10694 10946 -1195 -112 1187 C
ATOM 1229 N ILE A 181 13.190 -27.297 47.908 1.00 66.05 N
ANISOU 1229 N ILE A 181 4194 10438 10463 -1136 -359 1135 N
ATOM 1230 CA ILE A 181 13.702 -26.196 48.746 1.00 65.95 C
ANISOU 1230 CA ILE A 181 4278 10386 10395 -1136 -496 1148 C
ATOM 1231 C ILE A 181 13.171 -26.314 50.220 1.00 70.25 C
ANISOU 1231 C ILE A 181 4884 10964 10842 -1061 -539 1148 C
ATOM 1232 O ILE A 181 14.011 -26.288 51.125 1.00 70.38 O
ANISOU 1232 O ILE A 181 4918 10949 10872 -1081 -626 1197 O
ATOM 1233 CB ILE A 181 13.385 -24.800 48.120 1.00 68.77 C
ANISOU 1233 CB ILE A 181 4736 10714 10681 -1130 -556 1093 C
ATOM 1234 CG1 ILE A 181 14.228 -24.573 46.840 1.00 69.14 C
ANISOU 1234 CG1 ILE A 181 4723 10717 10829 -1204 -534 1121 C
ATOM 1235 CG2 ILE A 181 13.616 -23.656 49.128 1.00 69.61 C
ANISOU 1235 CG2 ILE A 181 4979 10772 10697 -1108 -710 1088 C
ATOM 1236 CD1 ILE A 181 13.777 -23.429 45.923 1.00 76.78 C
ANISOU 1236 CD1 ILE A 181 5760 11669 11745 -1198 -553 1069 C
ATOM 1237 N PRO A 182 11.853 -26.497 50.510 1.00 67.05 N
ANISOU 1237 N PRO A 182 4507 10624 10346 -973 -480 1110 N
ATOM 1238 CA PRO A 182 11.439 -26.614 51.923 1.00 67.41 C
ANISOU 1238 CA PRO A 182 4611 10704 10297 -887 -510 1128 C
ATOM 1239 C PRO A 182 11.844 -27.946 52.563 1.00 70.88 C
ANISOU 1239 C PRO A 182 4941 11172 10818 -901 -461 1195 C
ATOM 1240 O PRO A 182 11.916 -28.031 53.790 1.00 71.02 O
ANISOU 1240 O PRO A 182 5006 11204 10774 -847 -505 1225 O
ATOM 1241 CB PRO A 182 9.917 -26.482 51.863 1.00 69.17 C
ANISOU 1241 CB PRO A 182 4863 10993 10424 -788 -438 1095 C
ATOM 1242 CG PRO A 182 9.555 -26.956 50.513 1.00 73.15 C
ANISOU 1242 CG PRO A 182 5269 11510 11015 -843 -349 1075 C
ATOM 1243 CD PRO A 182 10.682 -26.566 49.608 1.00 68.54 C
ANISOU 1243 CD PRO A 182 4676 10857 10512 -943 -390 1064 C
ATOM 1244 N SER A 183 12.108 -28.975 51.733 1.00 66.53 N
ANISOU 1244 N SER A 183 4254 10624 10398 -967 -369 1217 N
ATOM 1245 CA SER A 183 12.513 -30.306 52.180 1.00 66.19 C
ANISOU 1245 CA SER A 183 4098 10601 10451 -987 -311 1281 C
ATOM 1246 C SER A 183 14.050 -30.428 52.249 1.00 70.38 C
ANISOU 1246 C SER A 183 4586 11074 11081 -1070 -363 1339 C
ATOM 1247 O SER A 183 14.559 -31.523 52.507 1.00 70.45 O
ANISOU 1247 O SER A 183 4495 11090 11182 -1095 -314 1399 O
ATOM 1248 CB SER A 183 11.934 -31.370 51.251 1.00 69.11 C
ANISOU 1248 CB SER A 183 4362 10993 10903 -1006 -190 1274 C
ATOM 1249 OG SER A 183 12.148 -32.671 51.771 1.00 77.12 O
ANISOU 1249 OG SER A 183 5275 12026 12002 -1013 -133 1334 O
ATOM 1250 N VAL A 184 14.786 -29.313 52.019 1.00 66.59 N
ANISOU 1250 N VAL A 184 4175 10536 10590 -1113 -465 1333 N
ATOM 1251 CA VAL A 184 16.253 -29.267 52.096 1.00 66.50 C
ANISOU 1251 CA VAL A 184 4119 10467 10680 -1195 -533 1410 C
ATOM 1252 C VAL A 184 16.634 -28.101 53.063 1.00 71.75 C
ANISOU 1252 C VAL A 184 4917 11088 11258 -1192 -710 1413 C
ATOM 1253 O VAL A 184 17.340 -27.169 52.680 1.00 71.67 O
ANISOU 1253 O VAL A 184 4945 11013 11275 -1250 -808 1429 O
ATOM 1254 CB VAL A 184 16.968 -29.171 50.701 1.00 69.61 C
ANISOU 1254 CB VAL A 184 4443 10820 11185 -1265 -485 1431 C
ATOM 1255 CG1 VAL A 184 18.488 -29.253 50.847 1.00 69.93 C
ANISOU 1255 CG1 VAL A 184 4410 10810 11350 -1342 -540 1544 C
ATOM 1256 CG2 VAL A 184 16.499 -30.263 49.749 1.00 68.67 C
ANISOU 1256 CG2 VAL A 184 4237 10732 11124 -1254 -326 1410 C
ATOM 1257 N GLY A 185 16.125 -28.164 54.297 1.00 68.90 N
ANISOU 1257 N GLY A 185 4634 10757 10789 -1117 -752 1402 N
ATOM 1258 CA GLY A 185 16.431 -27.191 55.344 1.00 69.55 C
ANISOU 1258 CA GLY A 185 4868 10790 10766 -1097 -924 1398 C
ATOM 1259 C GLY A 185 15.467 -26.049 55.615 1.00 73.33 C
ANISOU 1259 C GLY A 185 5532 11262 11069 -1005 -986 1310 C
ATOM 1260 O GLY A 185 15.361 -25.622 56.770 1.00 73.17 O
ANISOU 1260 O GLY A 185 5652 11225 10924 -938 -1090 1301 O
ATOM 1261 N TRP A 186 14.783 -25.509 54.577 1.00 69.90 N
ANISOU 1261 N TRP A 186 5111 10834 10613 -993 -927 1247 N
ATOM 1262 CA TRP A 186 13.885 -24.360 54.772 1.00 70.29 C
ANISOU 1262 CA TRP A 186 5335 10874 10498 -900 -979 1170 C
ATOM 1263 C TRP A 186 12.484 -24.811 55.260 1.00 75.61 C
ANISOU 1263 C TRP A 186 6029 11642 11058 -762 -861 1144 C
ATOM 1264 O TRP A 186 11.491 -24.706 54.534 1.00 74.56 O
ANISOU 1264 O TRP A 186 5877 11553 10899 -720 -765 1106 O
ATOM 1265 CB TRP A 186 13.771 -23.493 53.497 1.00 68.25 C
ANISOU 1265 CB TRP A 186 5087 10580 10264 -944 -977 1124 C
ATOM 1266 CG TRP A 186 13.324 -22.074 53.744 1.00 69.92 C
ANISOU 1266 CG TRP A 186 5496 10741 10329 -880 -1087 1059 C
ATOM 1267 CD1 TRP A 186 12.844 -21.552 54.911 1.00 73.30 C
ANISOU 1267 CD1 TRP A 186 6102 11158 10589 -766 -1162 1028 C
ATOM 1268 CD2 TRP A 186 13.320 -20.999 52.793 1.00 69.22 C
ANISOU 1268 CD2 TRP A 186 5460 10599 10241 -916 -1132 1018 C
ATOM 1269 NE1 TRP A 186 12.542 -20.221 54.748 1.00 73.32 N
ANISOU 1269 NE1 TRP A 186 6269 11099 10489 -729 -1251 967 N
ATOM 1270 CE2 TRP A 186 12.828 -19.853 53.459 1.00 74.12 C
ANISOU 1270 CE2 TRP A 186 6291 11174 10698 -826 -1238 961 C
ATOM 1271 CE3 TRP A 186 13.694 -20.887 51.443 1.00 69.87 C
ANISOU 1271 CE3 TRP A 186 5436 10667 10445 -1009 -1089 1029 C
ATOM 1272 CZ2 TRP A 186 12.693 -18.614 52.819 1.00 73.51 C
ANISOU 1272 CZ2 TRP A 186 6313 11034 10582 -833 -1306 914 C
ATOM 1273 CZ3 TRP A 186 13.556 -19.661 50.810 1.00 71.40 C
ANISOU 1273 CZ3 TRP A 186 5721 10807 10600 -1016 -1154 987 C
ATOM 1274 CH2 TRP A 186 13.062 -18.542 51.495 1.00 72.83 C
ANISOU 1274 CH2 TRP A 186 6104 10940 10627 -934 -1263 930 C
ATOM 1275 N ASN A 187 12.416 -25.259 56.522 1.00 74.13 N
ANISOU 1275 N ASN A 187 5885 11482 10798 -687 -880 1177 N
ATOM 1276 CA ASN A 187 11.194 -25.691 57.204 1.00 74.57 C
ANISOU 1276 CA ASN A 187 5960 11628 10747 -543 -778 1184 C
ATOM 1277 C ASN A 187 11.294 -25.348 58.700 1.00 82.33 C
ANISOU 1277 C ASN A 187 7110 12596 11575 -437 -876 1195 C
ATOM 1278 O ASN A 187 12.402 -25.204 59.222 1.00 82.96 O
ANISOU 1278 O ASN A 187 7242 12605 11673 -501 -1013 1212 O
ATOM 1279 CB ASN A 187 10.928 -27.182 56.977 1.00 73.02 C
ANISOU 1279 CB ASN A 187 5557 11511 10677 -569 -629 1244 C
ATOM 1280 CG ASN A 187 12.090 -28.132 57.193 1.00 96.69 C
ANISOU 1280 CG ASN A 187 8433 14486 13820 -677 -646 1306 C
ATOM 1281 OD1 ASN A 187 13.258 -27.744 57.303 1.00 95.79 O
ANISOU 1281 OD1 ASN A 187 8363 14296 13735 -754 -772 1316 O
ATOM 1282 ND2 ASN A 187 11.802 -29.425 57.212 1.00 88.09 N
ANISOU 1282 ND2 ASN A 187 7191 13461 12818 -676 -527 1362 N
ATOM 1283 N CYS A 188 10.143 -25.185 59.383 1.00 81.32 N
ANISOU 1283 N CYS A 188 7073 12532 11293 -268 -809 1192 N
ATOM 1284 CA CYS A 188 10.077 -24.794 60.799 1.00 83.48 C
ANISOU 1284 CA CYS A 188 7538 12798 11384 -128 -885 1197 C
ATOM 1285 C CYS A 188 10.244 -26.016 61.751 1.00 89.31 C
ANISOU 1285 C CYS A 188 8180 13603 12151 -96 -828 1282 C
ATOM 1286 O CYS A 188 9.767 -25.981 62.892 1.00 90.14 O
ANISOU 1286 O CYS A 188 8402 13747 12100 63 -817 1307 O
ATOM 1287 CB CYS A 188 8.778 -24.038 61.086 1.00 84.49 C
ANISOU 1287 CB CYS A 188 7814 12964 11324 60 -825 1168 C
ATOM 1288 SG CYS A 188 7.287 -25.070 61.097 1.00 88.09 S
ANISOU 1288 SG CYS A 188 8101 13576 11793 184 -589 1252 S
ATOM 1289 N ILE A 189 10.971 -27.057 61.302 1.00 85.91 N
ANISOU 1289 N ILE A 189 7548 13181 11914 -239 -795 1329 N
ATOM 1290 CA ILE A 189 11.242 -28.267 62.082 1.00 86.31 C
ANISOU 1290 CA ILE A 189 7484 13287 12023 -233 -743 1413 C
ATOM 1291 C ILE A 189 12.198 -27.928 63.262 1.00 92.77 C
ANISOU 1291 C ILE A 189 8453 14047 12749 -216 -906 1426 C
ATOM 1292 O ILE A 189 11.967 -28.402 64.374 1.00 92.91 O
ANISOU 1292 O ILE A 189 8502 14120 12681 -105 -876 1477 O
ATOM 1293 CB ILE A 189 11.793 -29.402 61.169 1.00 88.32 C
ANISOU 1293 CB ILE A 189 7498 13550 12510 -392 -668 1454 C
ATOM 1294 CG1 ILE A 189 11.893 -30.757 61.892 1.00 88.54 C
ANISOU 1294 CG1 ILE A 189 7386 13643 12611 -379 -585 1546 C
ATOM 1295 CG2 ILE A 189 13.096 -29.027 60.462 1.00 89.37 C
ANISOU 1295 CG2 ILE A 189 7616 13584 12757 -554 -784 1434 C
ATOM 1296 CD1 ILE A 189 10.676 -31.626 61.753 1.00 92.87 C
ANISOU 1296 CD1 ILE A 189 7804 14289 13192 -307 -413 1589 C
ATOM 1297 N CYS A 190 13.234 -27.095 63.017 1.00 91.19 N
ANISOU 1297 N CYS A 190 8347 13734 12567 -324 -1081 1387 N
ATOM 1298 CA CYS A 190 14.206 -26.669 64.025 1.00 93.08 C
ANISOU 1298 CA CYS A 190 8741 13896 12731 -334 -1274 1398 C
ATOM 1299 C CYS A 190 13.981 -25.179 64.372 1.00 97.23 C
ANISOU 1299 C CYS A 190 9552 14336 13054 -244 -1421 1312 C
ATOM 1300 O CYS A 190 14.843 -24.531 64.976 1.00 98.00 O
ANISOU 1300 O CYS A 190 9819 14335 13082 -269 -1625 1301 O
ATOM 1301 CB CYS A 190 15.631 -26.938 63.548 1.00 93.95 C
ANISOU 1301 CB CYS A 190 8728 13935 13034 -533 -1378 1445 C
ATOM 1302 SG CYS A 190 15.963 -28.680 63.168 1.00 97.19 S
ANISOU 1302 SG CYS A 190 8826 14430 13672 -625 -1206 1544 S
ATOM 1303 N ASP A 191 12.787 -24.670 64.010 1.00 92.70 N
ANISOU 1303 N ASP A 191 9038 13800 12384 -133 -1319 1257 N
ATOM 1304 CA ASP A 191 12.296 -23.311 64.245 1.00 93.02 C
ANISOU 1304 CA ASP A 191 9346 13774 12225 -17 -1413 1174 C
ATOM 1305 C ASP A 191 10.790 -23.420 64.542 1.00 96.09 C
ANISOU 1305 C ASP A 191 9767 14272 12469 193 -1228 1177 C
ATOM 1306 O ASP A 191 9.965 -22.747 63.920 1.00 95.34 O
ANISOU 1306 O ASP A 191 9720 14184 12322 252 -1169 1130 O
ATOM 1307 CB ASP A 191 12.616 -22.417 63.022 1.00 94.28 C
ANISOU 1307 CB ASP A 191 9505 13846 12473 -147 -1489 1115 C
ATOM 1308 CG ASP A 191 12.457 -20.918 63.226 1.00104.93 C
ANISOU 1308 CG ASP A 191 11138 15085 13643 -72 -1641 1029 C
ATOM 1309 OD1 ASP A 191 12.463 -20.468 64.397 1.00107.34 O
ANISOU 1309 OD1 ASP A 191 11682 15344 13759 52 -1754 1008 O
ATOM 1310 OD2 ASP A 191 12.365 -20.190 62.214 1.00109.11 O
ANISOU 1310 OD2 ASP A 191 11665 15571 14222 -135 -1655 982 O
ATOM 1311 N ILE A 192 10.454 -24.302 65.508 1.00 92.73 N
ANISOU 1311 N ILE A 192 9305 13938 11990 307 -1135 1249 N
ATOM 1312 CA ILE A 192 9.115 -24.712 65.952 1.00 92.60 C
ANISOU 1312 CA ILE A 192 9267 14047 11869 507 -943 1302 C
ATOM 1313 C ILE A 192 8.208 -23.512 66.352 1.00 97.23 C
ANISOU 1313 C ILE A 192 10119 14614 12209 716 -948 1249 C
ATOM 1314 O ILE A 192 6.984 -23.634 66.244 1.00 96.71 O
ANISOU 1314 O ILE A 192 10001 14647 12097 854 -774 1292 O
ATOM 1315 CB ILE A 192 9.235 -25.745 67.123 1.00 96.33 C
ANISOU 1315 CB ILE A 192 9692 14592 12316 583 -897 1395 C
ATOM 1316 CG1 ILE A 192 8.005 -26.665 67.253 1.00 96.71 C
ANISOU 1316 CG1 ILE A 192 9569 14792 12385 709 -664 1496 C
ATOM 1317 CG2 ILE A 192 9.665 -25.145 68.466 1.00 98.64 C
ANISOU 1317 CG2 ILE A 192 10272 14821 12384 713 -1048 1372 C
ATOM 1318 CD1 ILE A 192 7.964 -27.811 66.238 1.00104.18 C
ANISOU 1318 CD1 ILE A 192 10198 15796 13591 545 -545 1547 C
ATOM 1319 N GLU A 193 8.788 -22.379 66.790 1.00 94.69 N
ANISOU 1319 N GLU A 193 10076 14162 11740 739 -1148 1166 N
ATOM 1320 CA GLU A 193 8.011 -21.201 67.182 1.00 95.59 C
ANISOU 1320 CA GLU A 193 10471 14239 11612 942 -1165 1108 C
ATOM 1321 C GLU A 193 7.538 -20.405 65.963 1.00 97.86 C
ANISOU 1321 C GLU A 193 10737 14495 11950 889 -1140 1046 C
ATOM 1322 O GLU A 193 6.495 -19.750 66.042 1.00 98.22 O
ANISOU 1322 O GLU A 193 10915 14564 11838 1071 -1058 1032 O
ATOM 1323 CB GLU A 193 8.817 -20.293 68.119 1.00 98.79 C
ANISOU 1323 CB GLU A 193 11203 14499 11834 985 -1407 1037 C
ATOM 1324 CG GLU A 193 8.957 -20.833 69.538 1.00111.54 C
ANISOU 1324 CG GLU A 193 12930 16152 13299 1136 -1412 1091 C
ATOM 1325 CD GLU A 193 7.700 -20.905 70.389 1.00133.29 C
ANISOU 1325 CD GLU A 193 15793 19014 15836 1439 -1227 1144 C
ATOM 1326 OE1 GLU A 193 6.807 -20.043 70.227 1.00128.96 O
ANISOU 1326 OE1 GLU A 193 15399 18454 15146 1589 -1175 1104 O
ATOM 1327 OE2 GLU A 193 7.636 -21.801 71.261 1.00127.80 O1-
ANISOU 1327 OE2 GLU A 193 15035 18414 15108 1534 -1138 1234 O1-
ATOM 1328 N ASN A 194 8.285 -20.474 64.838 1.00 92.36 N
ANISOU 1328 N ASN A 194 9874 13750 11469 650 -1202 1020 N
ATOM 1329 CA ASN A 194 7.945 -19.762 63.602 1.00 91.01 C
ANISOU 1329 CA ASN A 194 9669 13550 11363 581 -1185 965 C
ATOM 1330 C ASN A 194 7.226 -20.689 62.589 1.00 91.78 C
ANISOU 1330 C ASN A 194 9464 13774 11635 522 -976 1023 C
ATOM 1331 O ASN A 194 7.433 -20.574 61.376 1.00 89.78 O
ANISOU 1331 O ASN A 194 9085 13498 11530 370 -976 994 O
ATOM 1332 CB ASN A 194 9.196 -19.131 62.975 1.00 92.30 C
ANISOU 1332 CB ASN A 194 9861 13572 11638 371 -1391 906 C
ATOM 1333 CG ASN A 194 9.760 -17.984 63.781 1.00119.42 C
ANISOU 1333 CG ASN A 194 13619 16857 14899 424 -1620 837 C
ATOM 1334 OD1 ASN A 194 10.274 -18.178 64.884 1.00115.94 O
ANISOU 1334 OD1 ASN A 194 13337 16388 14327 513 -1707 846 O
ATOM 1335 ND2 ASN A 194 9.695 -16.769 63.246 1.00111.99 N
ANISOU 1335 ND2 ASN A 194 12792 15809 13950 371 -1731 767 N
ATOM 1336 N CYS A 195 6.337 -21.565 63.095 1.00 87.83 N
ANISOU 1336 N CYS A 195 8860 13403 11108 652 -803 1110 N
ATOM 1337 CA CYS A 195 5.527 -22.459 62.267 1.00 86.20 C
ANISOU 1337 CA CYS A 195 8388 13312 11051 615 -617 1177 C
ATOM 1338 C CYS A 195 4.241 -21.755 61.871 1.00 89.22 C
ANISOU 1338 C CYS A 195 8822 13740 11336 755 -513 1177 C
ATOM 1339 O CYS A 195 3.644 -21.047 62.687 1.00 90.12 O
ANISOU 1339 O CYS A 195 9145 13856 11242 961 -503 1179 O
ATOM 1340 CB CYS A 195 5.237 -23.778 62.979 1.00 86.62 C
ANISOU 1340 CB CYS A 195 8285 13475 11151 668 -496 1288 C
ATOM 1341 SG CYS A 195 6.635 -24.929 63.021 1.00 89.89 S
ANISOU 1341 SG CYS A 195 8535 13860 11759 461 -570 1309 S
ATOM 1342 N SER A 196 3.811 -21.960 60.622 1.00 83.80 N
ANISOU 1342 N SER A 196 7954 13089 10796 650 -434 1181 N
ATOM 1343 CA SER A 196 2.586 -21.367 60.103 1.00 83.38 C
ANISOU 1343 CA SER A 196 7910 13086 10684 757 -332 1195 C
ATOM 1344 C SER A 196 1.344 -22.152 60.571 1.00 86.76 C
ANISOU 1344 C SER A 196 8212 13655 11097 910 -149 1330 C
ATOM 1345 O SER A 196 1.421 -23.358 60.815 1.00 85.49 O
ANISOU 1345 O SER A 196 7876 13557 11048 864 -89 1408 O
ATOM 1346 CB SER A 196 2.635 -21.289 58.583 1.00 85.48 C
ANISOU 1346 CB SER A 196 8033 13333 11112 580 -332 1151 C
ATOM 1347 OG SER A 196 2.736 -22.566 57.980 1.00 92.58 O
ANISOU 1347 OG SER A 196 8688 14276 12211 430 -280 1196 O
ATOM 1348 N ASN A 197 0.207 -21.445 60.708 1.00 84.10 N
ANISOU 1348 N ASN A 197 7965 13365 10624 1097 -62 1369 N
ATOM 1349 CA ASN A 197 -1.076 -22.001 61.150 1.00 84.42 C
ANISOU 1349 CA ASN A 197 7897 13541 10639 1269 117 1522 C
ATOM 1350 C ASN A 197 -1.676 -22.949 60.104 1.00 86.92 C
ANISOU 1350 C ASN A 197 7913 13937 11177 1136 212 1601 C
ATOM 1351 O ASN A 197 -2.307 -23.933 60.482 1.00 86.44 O
ANISOU 1351 O ASN A 197 7685 13977 11182 1189 326 1739 O
ATOM 1352 CB ASN A 197 -2.073 -20.880 61.470 1.00 85.47 C
ANISOU 1352 CB ASN A 197 8212 13692 10569 1504 181 1545 C
ATOM 1353 CG ASN A 197 -1.662 -19.988 62.618 1.00108.09 C
ANISOU 1353 CG ASN A 197 11400 16483 13188 1681 101 1482 C
ATOM 1354 OD1 ASN A 197 -1.407 -20.443 63.738 1.00102.14 O
ANISOU 1354 OD1 ASN A 197 10712 15749 12348 1783 106 1525 O
ATOM 1355 ND2 ASN A 197 -1.624 -18.687 62.376 1.00100.99 N
ANISOU 1355 ND2 ASN A 197 10722 15490 12161 1729 20 1379 N
ATOM 1356 N MET A 198 -1.482 -22.659 58.802 1.00 82.38 N
ANISOU 1356 N MET A 198 7275 13310 10713 964 158 1519 N
ATOM 1357 CA MET A 198 -2.002 -23.480 57.707 1.00 81.22 C
ANISOU 1357 CA MET A 198 6879 13215 10766 826 220 1572 C
ATOM 1358 C MET A 198 -1.141 -24.739 57.518 1.00 85.19 C
ANISOU 1358 C MET A 198 7223 13700 11444 644 186 1566 C
ATOM 1359 O MET A 198 -1.675 -25.841 57.548 1.00 84.74 O
ANISOU 1359 O MET A 198 6977 13718 11502 629 268 1676 O
ATOM 1360 CB MET A 198 -2.056 -22.661 56.421 1.00 82.76 C
ANISOU 1360 CB MET A 198 7097 13357 10993 725 170 1480 C
ATOM 1361 CG MET A 198 -2.942 -23.262 55.366 1.00 85.77 C
ANISOU 1361 CG MET A 198 7263 13799 11528 638 241 1548 C
ATOM 1362 SD MET A 198 -4.136 -22.071 54.722 1.00 90.15 S
ANISOU 1362 SD MET A 198 7873 14384 11996 746 291 1570 S
ATOM 1363 CE MET A 198 -3.038 -20.873 53.932 1.00 86.23 C
ANISOU 1363 CE MET A 198 7559 13753 11452 634 149 1378 C
ATOM 1364 N ALA A 199 0.180 -24.579 57.312 1.00 81.81 N
ANISOU 1364 N ALA A 199 6868 13173 11044 509 64 1448 N
ATOM 1365 CA ALA A 199 1.108 -25.702 57.164 1.00 81.16 C
ANISOU 1365 CA ALA A 199 6650 13068 11119 348 34 1443 C
ATOM 1366 C ALA A 199 1.967 -25.818 58.440 1.00 86.55 C
ANISOU 1366 C ALA A 199 7440 13725 11720 401 -23 1442 C
ATOM 1367 O ALA A 199 2.846 -24.980 58.661 1.00 86.42 O
ANISOU 1367 O ALA A 199 7595 13621 11622 383 -142 1352 O
ATOM 1368 CB ALA A 199 1.968 -25.521 55.924 1.00 80.82 C
ANISOU 1368 CB ALA A 199 6582 12939 11188 154 -47 1337 C
ATOM 1369 N PRO A 200 1.694 -26.811 59.324 1.00 84.05 N
ANISOU 1369 N PRO A 200 7031 13483 11423 471 52 1550 N
ATOM 1370 CA PRO A 200 2.418 -26.882 60.609 1.00 84.75 C
ANISOU 1370 CA PRO A 200 7235 13554 11412 543 -1 1555 C
ATOM 1371 C PRO A 200 3.892 -27.298 60.504 1.00 87.95 C
ANISOU 1371 C PRO A 200 7618 13877 11923 368 -112 1493 C
ATOM 1372 O PRO A 200 4.614 -27.129 61.488 1.00 88.53 O
ANISOU 1372 O PRO A 200 7818 13915 11903 411 -192 1481 O
ATOM 1373 CB PRO A 200 1.632 -27.933 61.404 1.00 87.12 C
ANISOU 1373 CB PRO A 200 7403 13967 11733 655 128 1705 C
ATOM 1374 CG PRO A 200 0.320 -28.070 60.696 1.00 91.53 C
ANISOU 1374 CG PRO A 200 7828 14601 12348 693 243 1783 C
ATOM 1375 CD PRO A 200 0.646 -27.847 59.257 1.00 85.77 C
ANISOU 1375 CD PRO A 200 7044 13803 11740 505 185 1683 C
ATOM 1376 N LEU A 201 4.348 -27.818 59.347 1.00 82.78 N
ANISOU 1376 N LEU A 201 6814 13188 11450 180 -121 1460 N
ATOM 1377 CA LEU A 201 5.744 -28.235 59.170 1.00 81.73 C
ANISOU 1377 CA LEU A 201 6644 12982 11430 19 -209 1420 C
ATOM 1378 C LEU A 201 6.531 -27.249 58.280 1.00 85.09 C
ANISOU 1378 C LEU A 201 7157 13306 11867 -94 -321 1314 C
ATOM 1379 O LEU A 201 7.752 -27.357 58.202 1.00 84.28 O
ANISOU 1379 O LEU A 201 7049 13135 11838 -211 -410 1291 O
ATOM 1380 CB LEU A 201 5.832 -29.659 58.586 1.00 80.88 C
ANISOU 1380 CB LEU A 201 6306 12902 11522 -100 -131 1472 C
ATOM 1381 CG LEU A 201 5.613 -30.829 59.554 1.00 85.81 C
ANISOU 1381 CG LEU A 201 6823 13599 12184 -42 -57 1581 C
ATOM 1382 CD1 LEU A 201 4.131 -31.162 59.709 1.00 86.37 C
ANISOU 1382 CD1 LEU A 201 6815 13768 12233 80 65 1674 C
ATOM 1383 CD2 LEU A 201 6.317 -32.070 59.052 1.00 87.19 C
ANISOU 1383 CD2 LEU A 201 6823 13750 12555 -194 -37 1603 C
ATOM 1384 N TYR A 202 5.842 -26.281 57.637 1.00 81.95 N
ANISOU 1384 N TYR A 202 6835 12901 11402 -55 -317 1265 N
ATOM 1385 CA TYR A 202 6.454 -25.262 56.769 1.00 81.44 C
ANISOU 1385 CA TYR A 202 6855 12746 11342 -147 -416 1174 C
ATOM 1386 C TYR A 202 6.637 -23.938 57.517 1.00 85.92 C
ANISOU 1386 C TYR A 202 7667 13250 11727 -49 -533 1123 C
ATOM 1387 O TYR A 202 5.751 -23.530 58.276 1.00 86.52 O
ANISOU 1387 O TYR A 202 7857 13368 11647 123 -495 1141 O
ATOM 1388 CB TYR A 202 5.599 -25.040 55.507 1.00 82.05 C
ANISOU 1388 CB TYR A 202 6862 12849 11465 -173 -343 1151 C
ATOM 1389 CG TYR A 202 5.915 -25.941 54.327 1.00 82.89 C
ANISOU 1389 CG TYR A 202 6785 12952 11756 -326 -296 1153 C
ATOM 1390 CD1 TYR A 202 6.178 -27.297 54.506 1.00 84.60 C
ANISOU 1390 CD1 TYR A 202 6853 13200 12092 -379 -241 1212 C
ATOM 1391 CD2 TYR A 202 5.856 -25.458 53.023 1.00 83.05 C
ANISOU 1391 CD2 TYR A 202 6789 12942 11824 -405 -300 1097 C
ATOM 1392 CE1 TYR A 202 6.450 -28.133 53.424 1.00 84.65 C
ANISOU 1392 CE1 TYR A 202 6716 13192 12254 -504 -198 1208 C
ATOM 1393 CE2 TYR A 202 6.111 -26.287 51.931 1.00 83.17 C
ANISOU 1393 CE2 TYR A 202 6662 12950 11990 -527 -255 1095 C
ATOM 1394 CZ TYR A 202 6.418 -27.622 52.137 1.00 90.18 C
ANISOU 1394 CZ TYR A 202 7419 13858 12988 -574 -205 1148 C
ATOM 1395 OH TYR A 202 6.656 -28.445 51.062 1.00 89.93 O
ANISOU 1395 OH TYR A 202 7269 13808 13091 -680 -161 1142 O
ATOM 1396 N SER A 203 7.783 -23.273 57.292 1.00 82.00 N
ANISOU 1396 N SER A 203 7253 12648 11254 -155 -678 1068 N
ATOM 1397 CA SER A 203 8.138 -21.998 57.922 1.00 82.68 C
ANISOU 1397 CA SER A 203 7582 12644 11189 -95 -828 1013 C
ATOM 1398 C SER A 203 7.369 -20.840 57.295 1.00 85.73 C
ANISOU 1398 C SER A 203 8077 13009 11485 -34 -824 954 C
ATOM 1399 O SER A 203 7.075 -20.881 56.097 1.00 84.48 O
ANISOU 1399 O SER A 203 7796 12873 11429 -111 -757 942 O
ATOM 1400 CB SER A 203 9.640 -21.752 57.800 1.00 86.85 C
ANISOU 1400 CB SER A 203 8127 13063 11811 -253 -991 997 C
ATOM 1401 OG SER A 203 10.052 -20.580 58.486 1.00 98.12 O
ANISOU 1401 OG SER A 203 9795 14386 13100 -208 -1165 950 O
ATOM 1402 N ASP A 204 7.056 -19.803 58.109 1.00 82.67 N
ANISOU 1402 N ASP A 204 7932 12576 10902 110 -900 916 N
ATOM 1403 CA ASP A 204 6.350 -18.587 57.683 1.00 82.46 C
ANISOU 1403 CA ASP A 204 8046 12519 10768 191 -907 860 C
ATOM 1404 C ASP A 204 7.169 -17.815 56.640 1.00 84.37 C
ANISOU 1404 C ASP A 204 8289 12658 11108 28 -1023 803 C
ATOM 1405 O ASP A 204 6.598 -17.278 55.690 1.00 83.35 O
ANISOU 1405 O ASP A 204 8137 12539 10992 23 -973 775 O
ATOM 1406 CB ASP A 204 6.052 -17.652 58.880 1.00 86.06 C
ANISOU 1406 CB ASP A 204 8792 12922 10985 381 -985 829 C
ATOM 1407 CG ASP A 204 5.524 -18.269 60.159 1.00 98.46 C
ANISOU 1407 CG ASP A 204 10411 14571 12427 560 -903 890 C
ATOM 1408 OD1 ASP A 204 4.457 -18.903 60.112 1.00 98.30 O1-
ANISOU 1408 OD1 ASP A 204 10253 14677 12419 649 -721 962 O1-
ATOM 1409 OD2 ASP A 204 6.103 -17.994 61.230 1.00106.97 O
ANISOU 1409 OD2 ASP A 204 11688 15579 13376 627 -1026 870 O
ATOM 1410 N SER A 205 8.511 -17.767 56.827 1.00 80.04 N
ANISOU 1410 N SER A 205 7761 12015 10634 -103 -1180 797 N
ATOM 1411 CA SER A 205 9.465 -17.089 55.941 1.00 78.92 C
ANISOU 1411 CA SER A 205 7608 11771 10606 -266 -1304 770 C
ATOM 1412 C SER A 205 9.458 -17.704 54.536 1.00 79.86 C
ANISOU 1412 C SER A 205 7485 11951 10907 -388 -1182 793 C
ATOM 1413 O SER A 205 9.669 -16.983 53.558 1.00 79.04 O
ANISOU 1413 O SER A 205 7376 11798 10859 -464 -1218 767 O
ATOM 1414 CB SER A 205 10.875 -17.140 56.525 1.00 82.45 C
ANISOU 1414 CB SER A 205 8089 12122 11116 -377 -1482 796 C
ATOM 1415 OG SER A 205 11.316 -18.473 56.723 1.00 88.92 O
ANISOU 1415 OG SER A 205 8723 13010 12054 -440 -1409 864 O
ATOM 1416 N TYR A 206 9.203 -19.026 54.441 1.00 74.41 N
ANISOU 1416 N TYR A 206 6606 11362 10303 -402 -1039 844 N
ATOM 1417 CA TYR A 206 9.138 -19.744 53.170 1.00 72.41 C
ANISOU 1417 CA TYR A 206 6143 11162 10206 -503 -922 862 C
ATOM 1418 C TYR A 206 7.827 -19.439 52.454 1.00 76.22 C
ANISOU 1418 C TYR A 206 6616 11710 10636 -427 -809 835 C
ATOM 1419 O TYR A 206 7.858 -19.174 51.254 1.00 75.42 O
ANISOU 1419 O TYR A 206 6450 11597 10610 -505 -788 813 O
ATOM 1420 CB TYR A 206 9.303 -21.268 53.368 1.00 72.30 C
ANISOU 1420 CB TYR A 206 5952 11219 10299 -541 -825 924 C
ATOM 1421 CG TYR A 206 9.105 -22.071 52.097 1.00 71.76 C
ANISOU 1421 CG TYR A 206 5695 11201 10370 -623 -701 936 C
ATOM 1422 CD1 TYR A 206 10.118 -22.182 51.150 1.00 73.11 C
ANISOU 1422 CD1 TYR A 206 5776 11322 10680 -760 -725 944 C
ATOM 1423 CD2 TYR A 206 7.894 -22.705 51.835 1.00 71.74 C
ANISOU 1423 CD2 TYR A 206 5610 11290 10359 -561 -567 947 C
ATOM 1424 CE1 TYR A 206 9.934 -22.900 49.970 1.00 72.40 C
ANISOU 1424 CE1 TYR A 206 5541 11269 10698 -820 -614 948 C
ATOM 1425 CE2 TYR A 206 7.696 -23.418 50.654 1.00 71.64 C
ANISOU 1425 CE2 TYR A 206 5449 11307 10463 -637 -475 950 C
ATOM 1426 CZ TYR A 206 8.722 -23.521 49.728 1.00 76.97 C
ANISOU 1426 CZ TYR A 206 6059 11928 11257 -762 -497 944 C
ATOM 1427 OH TYR A 206 8.545 -24.239 48.570 1.00 75.49 O
ANISOU 1427 OH TYR A 206 5751 11763 11169 -824 -409 942 O
ATOM 1428 N LEU A 207 6.684 -19.509 53.174 1.00 73.21 N
ANISOU 1428 N LEU A 207 6291 11398 10128 -271 -733 848 N
ATOM 1429 CA LEU A 207 5.348 -19.283 52.613 1.00 72.79 C
ANISOU 1429 CA LEU A 207 6215 11416 10025 -186 -621 846 C
ATOM 1430 C LEU A 207 5.172 -17.851 52.094 1.00 76.93 C
ANISOU 1430 C LEU A 207 6881 11877 10472 -164 -687 785 C
ATOM 1431 O LEU A 207 4.506 -17.677 51.076 1.00 75.43 O
ANISOU 1431 O LEU A 207 6622 11724 10314 -179 -616 777 O
ATOM 1432 CB LEU A 207 4.239 -19.605 53.626 1.00 73.49 C
ANISOU 1432 CB LEU A 207 6335 11592 9995 -9 -527 900 C
ATOM 1433 CG LEU A 207 4.056 -21.078 54.039 1.00 78.03 C
ANISOU 1433 CG LEU A 207 6743 12252 10652 -13 -430 979 C
ATOM 1434 CD1 LEU A 207 2.845 -21.228 54.906 1.00 78.86 C
ANISOU 1434 CD1 LEU A 207 6875 12449 10641 174 -329 1050 C
ATOM 1435 CD2 LEU A 207 3.885 -22.003 52.834 1.00 79.95 C
ANISOU 1435 CD2 LEU A 207 6773 12538 11067 -140 -349 998 C
ATOM 1436 N VAL A 208 5.776 -16.845 52.770 1.00 75.13 N
ANISOU 1436 N VAL A 208 6853 11548 10144 -132 -829 743 N
ATOM 1437 CA VAL A 208 5.745 -15.433 52.347 1.00 75.56 C
ANISOU 1437 CA VAL A 208 7060 11521 10129 -117 -915 684 C
ATOM 1438 C VAL A 208 6.544 -15.316 51.035 1.00 78.96 C
ANISOU 1438 C VAL A 208 7372 11909 10721 -296 -952 672 C
ATOM 1439 O VAL A 208 6.081 -14.660 50.103 1.00 78.08 O
ANISOU 1439 O VAL A 208 7258 11797 10611 -302 -924 646 O
ATOM 1440 CB VAL A 208 6.261 -14.460 53.453 1.00 80.74 C
ANISOU 1440 CB VAL A 208 7974 12062 10643 -46 -1082 644 C
ATOM 1441 CG1 VAL A 208 6.475 -13.042 52.921 1.00 80.90 C
ANISOU 1441 CG1 VAL A 208 8139 11972 10628 -70 -1199 586 C
ATOM 1442 CG2 VAL A 208 5.312 -14.428 54.638 1.00 81.53 C
ANISOU 1442 CG2 VAL A 208 8215 12209 10552 168 -1022 656 C
ATOM 1443 N PHE A 209 7.701 -16.008 50.954 1.00 75.71 N
ANISOU 1443 N PHE A 209 6854 11467 10444 -432 -1000 701 N
ATOM 1444 CA PHE A 209 8.576 -16.045 49.779 1.00 75.18 C
ANISOU 1444 CA PHE A 209 6662 11365 10537 -590 -1020 712 C
ATOM 1445 C PHE A 209 7.901 -16.785 48.612 1.00 78.52 C
ANISOU 1445 C PHE A 209 6911 11883 11040 -617 -860 720 C
ATOM 1446 O PHE A 209 7.944 -16.291 47.487 1.00 77.62 O
ANISOU 1446 O PHE A 209 6763 11753 10976 -675 -852 704 O
ATOM 1447 CB PHE A 209 9.927 -16.706 50.130 1.00 77.07 C
ANISOU 1447 CB PHE A 209 6826 11561 10895 -703 -1093 762 C
ATOM 1448 CG PHE A 209 10.806 -17.074 48.955 1.00 77.99 C
ANISOU 1448 CG PHE A 209 6780 11666 11187 -846 -1069 801 C
ATOM 1449 CD1 PHE A 209 11.571 -16.111 48.307 1.00 81.36 C
ANISOU 1449 CD1 PHE A 209 7236 12005 11672 -929 -1172 808 C
ATOM 1450 CD2 PHE A 209 10.891 -18.390 48.514 1.00 79.29 C
ANISOU 1450 CD2 PHE A 209 6767 11902 11459 -891 -944 838 C
ATOM 1451 CE1 PHE A 209 12.383 -16.454 47.220 1.00 81.72 C
ANISOU 1451 CE1 PHE A 209 7130 12046 11873 -1042 -1133 860 C
ATOM 1452 CE2 PHE A 209 11.704 -18.732 47.428 1.00 81.53 C
ANISOU 1452 CE2 PHE A 209 6918 12172 11889 -1001 -909 877 C
ATOM 1453 CZ PHE A 209 12.445 -17.763 46.790 1.00 79.88 C
ANISOU 1453 CZ PHE A 209 6734 11886 11729 -1070 -998 892 C
ATOM 1454 N TRP A 210 7.299 -17.962 48.880 1.00 75.19 N
ANISOU 1454 N TRP A 210 6385 11553 10632 -579 -745 750 N
ATOM 1455 CA TRP A 210 6.620 -18.812 47.896 1.00 74.37 C
ANISOU 1455 CA TRP A 210 6124 11530 10604 -607 -611 763 C
ATOM 1456 C TRP A 210 5.410 -18.102 47.274 1.00 78.57 C
ANISOU 1456 C TRP A 210 6692 12100 11059 -536 -560 737 C
ATOM 1457 O TRP A 210 5.231 -18.170 46.056 1.00 77.49 O
ANISOU 1457 O TRP A 210 6476 11980 10989 -599 -513 725 O
ATOM 1458 CB TRP A 210 6.182 -20.132 48.553 1.00 73.01 C
ANISOU 1458 CB TRP A 210 5853 11435 10454 -571 -524 811 C
ATOM 1459 CG TRP A 210 5.457 -21.077 47.644 1.00 73.49 C
ANISOU 1459 CG TRP A 210 5763 11564 10594 -603 -409 829 C
ATOM 1460 CD1 TRP A 210 4.111 -21.267 47.573 1.00 76.46 C
ANISOU 1460 CD1 TRP A 210 6106 12017 10927 -525 -328 850 C
ATOM 1461 CD2 TRP A 210 6.041 -21.971 46.684 1.00 72.77 C
ANISOU 1461 CD2 TRP A 210 5545 11465 10639 -718 -370 833 C
ATOM 1462 NE1 TRP A 210 3.816 -22.226 46.633 1.00 75.40 N
ANISOU 1462 NE1 TRP A 210 5835 11916 10898 -597 -260 864 N
ATOM 1463 CE2 TRP A 210 4.982 -22.680 46.076 1.00 76.34 C
ANISOU 1463 CE2 TRP A 210 5906 11982 11120 -709 -281 846 C
ATOM 1464 CE3 TRP A 210 7.361 -22.252 46.284 1.00 73.97 C
ANISOU 1464 CE3 TRP A 210 5654 11559 10894 -821 -402 837 C
ATOM 1465 CZ2 TRP A 210 5.198 -23.649 45.090 1.00 75.18 C
ANISOU 1465 CZ2 TRP A 210 5650 11831 11083 -798 -232 845 C
ATOM 1466 CZ3 TRP A 210 7.574 -23.218 45.311 1.00 75.00 C
ANISOU 1466 CZ3 TRP A 210 5670 11696 11132 -894 -333 844 C
ATOM 1467 CH2 TRP A 210 6.501 -23.906 44.728 1.00 75.35 C
ANISOU 1467 CH2 TRP A 210 5648 11794 11187 -881 -253 840 C
ATOM 1468 N ALA A 211 4.583 -17.439 48.105 1.00 76.21 N
ANISOU 1468 N ALA A 211 6520 11817 10618 -399 -565 733 N
ATOM 1469 CA ALA A 211 3.391 -16.725 47.655 1.00 76.34 C
ANISOU 1469 CA ALA A 211 6578 11874 10554 -312 -512 723 C
ATOM 1470 C ALA A 211 3.750 -15.485 46.834 1.00 81.09 C
ANISOU 1470 C ALA A 211 7263 12401 11146 -357 -587 671 C
ATOM 1471 O ALA A 211 3.112 -15.252 45.810 1.00 80.56 O
ANISOU 1471 O ALA A 211 7143 12368 11098 -370 -533 664 O
ATOM 1472 CB ALA A 211 2.530 -16.329 48.842 1.00 77.97 C
ANISOU 1472 CB ALA A 211 6911 12109 10604 -135 -493 744 C
ATOM 1473 N ILE A 212 4.772 -14.707 47.258 1.00 78.58 N
ANISOU 1473 N ILE A 212 7068 11979 10810 -389 -719 641 N
ATOM 1474 CA ILE A 212 5.185 -13.489 46.553 1.00 78.74 C
ANISOU 1474 CA ILE A 212 7168 11916 10832 -436 -805 603 C
ATOM 1475 C ILE A 212 5.940 -13.859 45.247 1.00 82.62 C
ANISOU 1475 C ILE A 212 7509 12402 11480 -587 -788 614 C
ATOM 1476 O ILE A 212 5.945 -13.053 44.316 1.00 82.10 O
ANISOU 1476 O ILE A 212 7456 12309 11430 -620 -804 596 O
ATOM 1477 CB ILE A 212 6.014 -12.527 47.466 1.00 82.76 C
ANISOU 1477 CB ILE A 212 7865 12302 11278 -425 -972 579 C
ATOM 1478 CG1 ILE A 212 5.860 -11.046 47.061 1.00 83.72 C
ANISOU 1478 CG1 ILE A 212 8128 12346 11337 -400 -1051 538 C
ATOM 1479 CG2 ILE A 212 7.483 -12.939 47.642 1.00 83.34 C
ANISOU 1479 CG2 ILE A 212 7887 12309 11472 -558 -1072 607 C
ATOM 1480 CD1 ILE A 212 4.542 -10.366 47.509 1.00 91.58 C
ANISOU 1480 CD1 ILE A 212 9268 13370 12160 -221 -1001 513 C
ATOM 1481 N PHE A 213 6.543 -15.070 45.175 1.00 79.38 N
ANISOU 1481 N PHE A 213 6963 12020 11179 -665 -747 648 N
ATOM 1482 CA PHE A 213 7.269 -15.545 43.991 1.00 78.90 C
ANISOU 1482 CA PHE A 213 6768 11957 11255 -785 -713 667 C
ATOM 1483 C PHE A 213 6.291 -15.928 42.874 1.00 81.76 C
ANISOU 1483 C PHE A 213 7042 12397 11626 -778 -595 655 C
ATOM 1484 O PHE A 213 6.527 -15.577 41.719 1.00 81.37 O
ANISOU 1484 O PHE A 213 6959 12333 11624 -834 -584 648 O
ATOM 1485 CB PHE A 213 8.179 -16.738 44.342 1.00 80.88 C
ANISOU 1485 CB PHE A 213 6915 12208 11606 -852 -700 710 C
ATOM 1486 CG PHE A 213 8.986 -17.309 43.198 1.00 82.42 C
ANISOU 1486 CG PHE A 213 6982 12399 11936 -955 -652 740 C
ATOM 1487 CD1 PHE A 213 10.157 -16.691 42.774 1.00 86.08 C
ANISOU 1487 CD1 PHE A 213 7443 12787 12475 -1032 -727 774 C
ATOM 1488 CD2 PHE A 213 8.597 -18.485 42.570 1.00 84.48 C
ANISOU 1488 CD2 PHE A 213 7128 12724 12246 -968 -535 743 C
ATOM 1489 CE1 PHE A 213 10.909 -17.227 41.723 1.00 86.83 C
ANISOU 1489 CE1 PHE A 213 7422 12883 12687 -1105 -664 815 C
ATOM 1490 CE2 PHE A 213 9.358 -19.024 41.530 1.00 87.16 C
ANISOU 1490 CE2 PHE A 213 7374 13053 12692 -1042 -484 768 C
ATOM 1491 CZ PHE A 213 10.501 -18.387 41.105 1.00 85.50 C
ANISOU 1491 CZ PHE A 213 7161 12777 12547 -1102 -539 807 C
ATOM 1492 N ASN A 214 5.208 -16.654 43.216 1.00 77.27 N
ANISOU 1492 N ASN A 214 6434 11909 11016 -710 -513 662 N
ATOM 1493 CA ASN A 214 4.200 -17.093 42.254 1.00 76.25 C
ANISOU 1493 CA ASN A 214 6222 11851 10898 -707 -421 661 C
ATOM 1494 C ASN A 214 3.303 -15.930 41.808 1.00 80.05 C
ANISOU 1494 C ASN A 214 6780 12343 11293 -644 -425 639 C
ATOM 1495 O ASN A 214 2.839 -15.933 40.665 1.00 79.51 O
ANISOU 1495 O ASN A 214 6658 12304 11249 -676 -382 630 O
ATOM 1496 CB ASN A 214 3.353 -18.223 42.835 1.00 75.93 C
ANISOU 1496 CB ASN A 214 6106 11886 10858 -660 -349 698 C
ATOM 1497 CG ASN A 214 4.097 -19.529 42.973 1.00 91.23 C
ANISOU 1497 CG ASN A 214 7946 13820 12898 -732 -327 720 C
ATOM 1498 OD1 ASN A 214 4.491 -20.166 41.985 1.00 83.61 O
ANISOU 1498 OD1 ASN A 214 6903 12847 12020 -814 -296 712 O
ATOM 1499 ND2 ASN A 214 4.284 -19.970 44.204 1.00 82.31 N
ANISOU 1499 ND2 ASN A 214 6825 12697 11753 -692 -338 749 N
ATOM 1500 N LEU A 215 3.063 -14.941 42.693 1.00 76.83 N
ANISOU 1500 N LEU A 215 6505 11907 10779 -552 -477 629 N
ATOM 1501 CA LEU A 215 2.224 -13.784 42.376 1.00 76.81 C
ANISOU 1501 CA LEU A 215 6588 11909 10687 -478 -478 613 C
ATOM 1502 C LEU A 215 2.957 -12.785 41.474 1.00 80.45 C
ANISOU 1502 C LEU A 215 7092 12296 11177 -549 -545 580 C
ATOM 1503 O LEU A 215 2.320 -12.212 40.589 1.00 80.03 O
ANISOU 1503 O LEU A 215 7036 12267 11106 -538 -515 571 O
ATOM 1504 CB LEU A 215 1.720 -13.073 43.645 1.00 77.61 C
ANISOU 1504 CB LEU A 215 6838 11997 10652 -337 -506 615 C
ATOM 1505 CG LEU A 215 0.513 -13.706 44.352 1.00 82.32 C
ANISOU 1505 CG LEU A 215 7399 12690 11189 -218 -411 669 C
ATOM 1506 CD1 LEU A 215 0.373 -13.179 45.760 1.00 83.24 C
ANISOU 1506 CD1 LEU A 215 7676 12780 11172 -76 -442 673 C
ATOM 1507 CD2 LEU A 215 -0.781 -13.473 43.580 1.00 84.92 C
ANISOU 1507 CD2 LEU A 215 7673 13095 11499 -170 -329 701 C
ATOM 1508 N VAL A 216 4.280 -12.588 41.672 1.00 76.99 N
ANISOU 1508 N VAL A 216 6683 11773 10797 -624 -634 575 N
ATOM 1509 CA VAL A 216 5.065 -11.662 40.846 1.00 76.94 C
ANISOU 1509 CA VAL A 216 6702 11695 10838 -696 -702 567 C
ATOM 1510 C VAL A 216 5.224 -12.271 39.427 1.00 80.55 C
ANISOU 1510 C VAL A 216 7019 12195 11391 -780 -622 580 C
ATOM 1511 O VAL A 216 5.340 -11.517 38.458 1.00 80.01 O
ANISOU 1511 O VAL A 216 6955 12106 11338 -808 -631 576 O
ATOM 1512 CB VAL A 216 6.429 -11.266 41.492 1.00 81.39 C
ANISOU 1512 CB VAL A 216 7325 12150 11448 -757 -832 582 C
ATOM 1513 CG1 VAL A 216 7.474 -12.382 41.401 1.00 80.91 C
ANISOU 1513 CG1 VAL A 216 7137 12093 11512 -852 -815 624 C
ATOM 1514 CG2 VAL A 216 6.968 -9.967 40.902 1.00 81.59 C
ANISOU 1514 CG2 VAL A 216 7414 12090 11496 -800 -924 583 C
ATOM 1515 N THR A 217 5.175 -13.622 39.313 1.00 77.05 N
ANISOU 1515 N THR A 217 6463 11808 11002 -808 -545 594 N
ATOM 1516 CA THR A 217 5.261 -14.336 38.038 1.00 76.58 C
ANISOU 1516 CA THR A 217 6297 11785 11015 -871 -469 599 C
ATOM 1517 C THR A 217 3.955 -14.103 37.265 1.00 80.62 C
ANISOU 1517 C THR A 217 6806 12360 11468 -828 -415 579 C
ATOM 1518 O THR A 217 3.999 -13.929 36.046 1.00 80.01 O
ANISOU 1518 O THR A 217 6699 12287 11412 -864 -389 572 O
ATOM 1519 CB THR A 217 5.571 -15.829 38.248 1.00 85.88 C
ANISOU 1519 CB THR A 217 7380 12990 12262 -906 -416 617 C
ATOM 1520 OG1 THR A 217 6.699 -15.962 39.117 1.00 88.05 O
ANISOU 1520 OG1 THR A 217 7661 13209 12585 -937 -473 645 O
ATOM 1521 CG2 THR A 217 5.866 -16.557 36.935 1.00 84.31 C
ANISOU 1521 CG2 THR A 217 7099 12804 12132 -965 -348 619 C
ATOM 1522 N PHE A 218 2.806 -14.060 37.978 1.00 77.67 N
ANISOU 1522 N PHE A 218 6461 12034 11015 -744 -398 580 N
ATOM 1523 CA PHE A 218 1.493 -13.806 37.374 1.00 77.58 C
ANISOU 1523 CA PHE A 218 6439 12087 10952 -697 -352 582 C
ATOM 1524 C PHE A 218 1.412 -12.382 36.816 1.00 81.36 C
ANISOU 1524 C PHE A 218 6998 12535 11381 -675 -387 564 C
ATOM 1525 O PHE A 218 0.840 -12.186 35.745 1.00 80.81 O
ANISOU 1525 O PHE A 218 6897 12499 11307 -687 -356 561 O
ATOM 1526 CB PHE A 218 0.346 -14.033 38.384 1.00 79.84 C
ANISOU 1526 CB PHE A 218 6732 12433 11172 -597 -321 614 C
ATOM 1527 CG PHE A 218 0.147 -15.427 38.941 1.00 81.47 C
ANISOU 1527 CG PHE A 218 6846 12682 11425 -606 -279 648 C
ATOM 1528 CD1 PHE A 218 0.599 -16.546 38.248 1.00 84.03 C
ANISOU 1528 CD1 PHE A 218 7077 13006 11843 -701 -258 642 C
ATOM 1529 CD2 PHE A 218 -0.564 -15.627 40.119 1.00 84.24 C
ANISOU 1529 CD2 PHE A 218 7209 13075 11722 -510 -255 692 C
ATOM 1530 CE1 PHE A 218 0.402 -17.830 38.758 1.00 84.87 C
ANISOU 1530 CE1 PHE A 218 7101 13145 11998 -712 -225 676 C
ATOM 1531 CE2 PHE A 218 -0.778 -16.914 40.618 1.00 87.02 C
ANISOU 1531 CE2 PHE A 218 7466 13470 12127 -518 -216 735 C
ATOM 1532 CZ PHE A 218 -0.288 -18.007 39.937 1.00 84.55 C
ANISOU 1532 CZ PHE A 218 7060 13148 11917 -625 -206 724 C
ATOM 1533 N VAL A 219 2.002 -11.402 37.535 1.00 78.06 N
ANISOU 1533 N VAL A 219 6687 12045 10927 -647 -462 552 N
ATOM 1534 CA VAL A 219 2.017 -9.985 37.161 1.00 78.08 C
ANISOU 1534 CA VAL A 219 6783 11999 10887 -624 -512 537 C
ATOM 1535 C VAL A 219 2.866 -9.793 35.881 1.00 81.40 C
ANISOU 1535 C VAL A 219 7149 12390 11388 -721 -519 539 C
ATOM 1536 O VAL A 219 2.366 -9.192 34.929 1.00 80.55 O
ANISOU 1536 O VAL A 219 7040 12305 11261 -714 -496 535 O
ATOM 1537 CB VAL A 219 2.507 -9.080 38.330 1.00 82.76 C
ANISOU 1537 CB VAL A 219 7519 12502 11424 -576 -611 524 C
ATOM 1538 CG1 VAL A 219 2.701 -7.631 37.883 1.00 83.03 C
ANISOU 1538 CG1 VAL A 219 7651 12465 11434 -571 -681 511 C
ATOM 1539 CG2 VAL A 219 1.544 -9.142 39.513 1.00 83.01 C
ANISOU 1539 CG2 VAL A 219 7624 12568 11348 -449 -587 527 C
ATOM 1540 N VAL A 220 4.113 -10.328 35.845 1.00 78.18 N
ANISOU 1540 N VAL A 220 6692 11939 11073 -802 -542 555 N
ATOM 1541 CA VAL A 220 5.009 -10.187 34.683 1.00 78.03 C
ANISOU 1541 CA VAL A 220 6619 11894 11135 -878 -537 578 C
ATOM 1542 C VAL A 220 4.419 -10.924 33.454 1.00 81.69 C
ANISOU 1542 C VAL A 220 7001 12433 11603 -891 -439 569 C
ATOM 1543 O VAL A 220 4.666 -10.487 32.327 1.00 81.58 O
ANISOU 1543 O VAL A 220 6972 12417 11608 -915 -422 580 O
ATOM 1544 CB VAL A 220 6.491 -10.601 34.931 1.00 81.97 C
ANISOU 1544 CB VAL A 220 7073 12333 11737 -952 -574 621 C
ATOM 1545 CG1 VAL A 220 7.168 -9.671 35.937 1.00 82.36 C
ANISOU 1545 CG1 VAL A 220 7214 12289 11790 -957 -701 636 C
ATOM 1546 CG2 VAL A 220 6.633 -12.063 35.348 1.00 81.42 C
ANISOU 1546 CG2 VAL A 220 6930 12301 11703 -968 -519 624 C
ATOM 1547 N MET A 221 3.619 -11.998 33.669 1.00 77.52 N
ANISOU 1547 N MET A 221 6430 11969 11056 -872 -385 555 N
ATOM 1548 CA MET A 221 2.964 -12.725 32.578 1.00 76.82 C
ANISOU 1548 CA MET A 221 6283 11940 10967 -888 -319 544 C
ATOM 1549 C MET A 221 1.841 -11.874 31.977 1.00 79.95 C
ANISOU 1549 C MET A 221 6709 12375 11293 -846 -315 535 C
ATOM 1550 O MET A 221 1.694 -11.854 30.758 1.00 79.61 O
ANISOU 1550 O MET A 221 6648 12352 11249 -868 -288 529 O
ATOM 1551 CB MET A 221 2.430 -14.088 33.036 1.00 79.08 C
ANISOU 1551 CB MET A 221 6511 12268 11266 -889 -283 542 C
ATOM 1552 CG MET A 221 3.484 -15.170 33.017 1.00 82.79 C
ANISOU 1552 CG MET A 221 6933 12709 11815 -942 -260 549 C
ATOM 1553 SD MET A 221 2.852 -16.842 33.292 1.00 87.14 S
ANISOU 1553 SD MET A 221 7415 13301 12393 -955 -219 547 S
ATOM 1554 CE MET A 221 2.473 -16.784 35.043 1.00 83.89 C
ANISOU 1554 CE MET A 221 7013 12904 11957 -900 -248 571 C
ATOM 1555 N VAL A 222 1.087 -11.139 32.826 1.00 75.79 N
ANISOU 1555 N VAL A 222 6238 11858 10702 -776 -340 539 N
ATOM 1556 CA VAL A 222 0.008 -10.235 32.404 1.00 75.22 C
ANISOU 1556 CA VAL A 222 6197 11822 10561 -722 -334 543 C
ATOM 1557 C VAL A 222 0.625 -9.111 31.541 1.00 78.38 C
ANISOU 1557 C VAL A 222 6638 12176 10967 -744 -361 537 C
ATOM 1558 O VAL A 222 0.091 -8.812 30.472 1.00 77.73 O
ANISOU 1558 O VAL A 222 6538 12129 10865 -748 -337 539 O
ATOM 1559 CB VAL A 222 -0.802 -9.693 33.622 1.00 79.30 C
ANISOU 1559 CB VAL A 222 6778 12350 11004 -622 -345 558 C
ATOM 1560 CG1 VAL A 222 -1.641 -8.465 33.261 1.00 79.37 C
ANISOU 1560 CG1 VAL A 222 6841 12373 10943 -556 -344 567 C
ATOM 1561 CG2 VAL A 222 -1.684 -10.784 34.222 1.00 79.10 C
ANISOU 1561 CG2 VAL A 222 6687 12393 10975 -591 -300 588 C
ATOM 1562 N VAL A 223 1.779 -8.554 31.979 1.00 75.03 N
ANISOU 1562 N VAL A 223 6259 11671 10577 -766 -417 540 N
ATOM 1563 CA VAL A 223 2.539 -7.494 31.295 1.00 75.08 C
ANISOU 1563 CA VAL A 223 6295 11620 10611 -795 -456 554 C
ATOM 1564 C VAL A 223 2.957 -7.983 29.887 1.00 78.52 C
ANISOU 1564 C VAL A 223 6654 12083 11097 -851 -400 568 C
ATOM 1565 O VAL A 223 2.847 -7.217 28.927 1.00 78.12 O
ANISOU 1565 O VAL A 223 6611 12037 11035 -849 -392 579 O
ATOM 1566 CB VAL A 223 3.766 -7.032 32.140 1.00 79.32 C
ANISOU 1566 CB VAL A 223 6881 12059 11200 -824 -543 571 C
ATOM 1567 CG1 VAL A 223 4.674 -6.082 31.361 1.00 79.40 C
ANISOU 1567 CG1 VAL A 223 6892 12007 11269 -870 -586 610 C
ATOM 1568 CG2 VAL A 223 3.321 -6.378 33.446 1.00 79.62 C
ANISOU 1568 CG2 VAL A 223 7032 12058 11163 -753 -609 549 C
ATOM 1569 N LEU A 224 3.390 -9.258 29.771 1.00 74.93 N
ANISOU 1569 N LEU A 224 6135 11646 10688 -889 -357 568 N
ATOM 1570 CA LEU A 224 3.808 -9.879 28.510 1.00 74.78 C
ANISOU 1570 CA LEU A 224 6065 11648 10701 -923 -296 577 C
ATOM 1571 C LEU A 224 2.669 -9.885 27.480 1.00 79.59 C
ANISOU 1571 C LEU A 224 6676 12321 11245 -902 -260 553 C
ATOM 1572 O LEU A 224 2.899 -9.460 26.349 1.00 79.52 O
ANISOU 1572 O LEU A 224 6667 12315 11230 -906 -236 567 O
ATOM 1573 CB LEU A 224 4.320 -11.313 28.736 1.00 74.55 C
ANISOU 1573 CB LEU A 224 5986 11621 10719 -952 -258 574 C
ATOM 1574 CG LEU A 224 5.750 -11.455 29.254 1.00 79.09 C
ANISOU 1574 CG LEU A 224 6535 12135 11380 -987 -274 620 C
ATOM 1575 CD1 LEU A 224 5.920 -12.736 30.042 1.00 78.92 C
ANISOU 1575 CD1 LEU A 224 6478 12118 11389 -1001 -256 610 C
ATOM 1576 CD2 LEU A 224 6.761 -11.382 28.121 1.00 81.87 C
ANISOU 1576 CD2 LEU A 224 6853 12468 11784 -1005 -228 671 C
ATOM 1577 N TYR A 225 1.447 -10.326 27.870 1.00 76.71 N
ANISOU 1577 N TYR A 225 6307 12006 10832 -879 -259 530 N
ATOM 1578 CA TYR A 225 0.289 -10.358 26.964 1.00 76.89 C
ANISOU 1578 CA TYR A 225 6325 12089 10801 -867 -243 520 C
ATOM 1579 C TYR A 225 -0.257 -8.947 26.714 1.00 82.07 C
ANISOU 1579 C TYR A 225 7019 12754 11410 -828 -263 535 C
ATOM 1580 O TYR A 225 -0.697 -8.669 25.597 1.00 81.44 O
ANISOU 1580 O TYR A 225 6939 12704 11298 -829 -249 536 O
ATOM 1581 CB TYR A 225 -0.828 -11.277 27.484 1.00 77.85 C
ANISOU 1581 CB TYR A 225 6413 12260 10908 -860 -244 518 C
ATOM 1582 CG TYR A 225 -0.419 -12.730 27.596 1.00 79.29 C
ANISOU 1582 CG TYR A 225 6558 12431 11137 -902 -228 503 C
ATOM 1583 CD1 TYR A 225 -0.339 -13.544 26.467 1.00 81.08 C
ANISOU 1583 CD1 TYR A 225 6783 12658 11366 -938 -210 481 C
ATOM 1584 CD2 TYR A 225 -0.154 -13.306 28.833 1.00 79.99 C
ANISOU 1584 CD2 TYR A 225 6625 12506 11262 -898 -231 510 C
ATOM 1585 CE1 TYR A 225 0.041 -14.883 26.564 1.00 81.09 C
ANISOU 1585 CE1 TYR A 225 6764 12639 11408 -970 -196 466 C
ATOM 1586 CE2 TYR A 225 0.233 -14.641 28.944 1.00 80.82 C
ANISOU 1586 CE2 TYR A 225 6695 12598 11414 -936 -215 500 C
ATOM 1587 CZ TYR A 225 0.318 -15.429 27.808 1.00 87.33 C
ANISOU 1587 CZ TYR A 225 7520 13417 12244 -971 -197 477 C
ATOM 1588 OH TYR A 225 0.691 -16.747 27.931 1.00 87.53 O
ANISOU 1588 OH TYR A 225 7524 13420 12315 -1002 -181 466 O
ATOM 1589 N ALA A 226 -0.197 -8.053 27.730 1.00 80.14 N
ANISOU 1589 N ALA A 226 6818 12477 11156 -789 -298 544 N
ATOM 1590 CA ALA A 226 -0.635 -6.654 27.612 1.00 80.99 C
ANISOU 1590 CA ALA A 226 6978 12577 11219 -743 -320 557 C
ATOM 1591 C ALA A 226 0.214 -5.900 26.579 1.00 87.02 C
ANISOU 1591 C ALA A 226 7748 13304 12011 -773 -324 572 C
ATOM 1592 O ALA A 226 -0.300 -5.023 25.880 1.00 86.86 O
ANISOU 1592 O ALA A 226 7745 13302 11955 -750 -322 584 O
ATOM 1593 CB ALA A 226 -0.557 -5.956 28.961 1.00 81.94 C
ANISOU 1593 CB ALA A 226 7167 12645 11320 -692 -366 557 C
ATOM 1594 N HIS A 227 1.508 -6.272 26.475 1.00 84.76 N
ANISOU 1594 N HIS A 227 7439 12970 11794 -821 -324 584 N
ATOM 1595 CA HIS A 227 2.457 -5.718 25.512 1.00 85.39 C
ANISOU 1595 CA HIS A 227 7506 13018 11918 -847 -316 622 C
ATOM 1596 C HIS A 227 2.132 -6.233 24.104 1.00 90.05 C
ANISOU 1596 C HIS A 227 8068 13670 12479 -850 -251 619 C
ATOM 1597 O HIS A 227 2.334 -5.505 23.133 1.00 89.96 O
ANISOU 1597 O HIS A 227 8058 13659 12463 -843 -236 650 O
ATOM 1598 CB HIS A 227 3.899 -6.077 25.910 1.00 86.42 C
ANISOU 1598 CB HIS A 227 7609 13087 12140 -891 -330 657 C
ATOM 1599 CG HIS A 227 4.943 -5.430 25.056 1.00 90.35 C
ANISOU 1599 CG HIS A 227 8080 13548 12701 -912 -323 726 C
ATOM 1600 ND1 HIS A 227 5.474 -6.076 23.954 1.00 92.29 N
ANISOU 1600 ND1 HIS A 227 8277 13822 12966 -918 -244 757 N
ATOM 1601 CD2 HIS A 227 5.518 -4.211 25.169 1.00 92.64 C
ANISOU 1601 CD2 HIS A 227 8389 13774 13037 -923 -387 778 C
ATOM 1602 CE1 HIS A 227 6.353 -5.235 23.435 1.00 92.25 C
ANISOU 1602 CE1 HIS A 227 8249 13779 13024 -928 -251 837 C
ATOM 1603 NE2 HIS A 227 6.414 -4.099 24.132 1.00 92.79 N
ANISOU 1603 NE2 HIS A 227 8350 13788 13117 -939 -342 854 N
ATOM 1604 N ILE A 228 1.623 -7.485 24.002 1.00 86.87 N
ANISOU 1604 N ILE A 228 7645 13310 12050 -858 -220 583 N
ATOM 1605 CA ILE A 228 1.242 -8.123 22.739 1.00 87.08 C
ANISOU 1605 CA ILE A 228 7668 13383 12034 -860 -177 568 C
ATOM 1606 C ILE A 228 -0.066 -7.490 22.238 1.00 92.00 C
ANISOU 1606 C ILE A 228 8309 14059 12588 -836 -195 562 C
ATOM 1607 O ILE A 228 -0.086 -6.977 21.117 1.00 92.23 O
ANISOU 1607 O ILE A 228 8352 14105 12586 -825 -176 577 O
ATOM 1608 CB ILE A 228 1.132 -9.673 22.873 1.00 90.04 C
ANISOU 1608 CB ILE A 228 8030 13770 12413 -883 -160 532 C
ATOM 1609 CG1 ILE A 228 2.510 -10.303 23.167 1.00 90.29 C
ANISOU 1609 CG1 ILE A 228 8040 13751 12514 -900 -128 548 C
ATOM 1610 CG2 ILE A 228 0.496 -10.305 21.615 1.00 91.26 C
ANISOU 1610 CG2 ILE A 228 8208 13961 12506 -884 -144 505 C
ATOM 1611 CD1 ILE A 228 2.469 -11.712 23.797 1.00 96.97 C
ANISOU 1611 CD1 ILE A 228 8868 14593 13382 -922 -123 518 C
ATOM 1612 N PHE A 229 -1.140 -7.514 23.067 1.00 88.76 N
ANISOU 1612 N PHE A 229 7892 13677 12154 -822 -225 552 N
ATOM 1613 CA PHE A 229 -2.457 -6.959 22.730 1.00 88.82 C
ANISOU 1613 CA PHE A 229 7902 13740 12105 -795 -240 565 C
ATOM 1614 C PHE A 229 -2.382 -5.463 22.408 1.00 93.21 C
ANISOU 1614 C PHE A 229 8487 14282 12644 -762 -245 592 C
ATOM 1615 O PHE A 229 -3.064 -5.013 21.488 1.00 93.03 O
ANISOU 1615 O PHE A 229 8467 14302 12578 -750 -241 607 O
ATOM 1616 CB PHE A 229 -3.473 -7.196 23.860 1.00 90.55 C
ANISOU 1616 CB PHE A 229 8100 13988 12316 -770 -259 576 C
ATOM 1617 CG PHE A 229 -4.037 -8.597 23.912 1.00 92.19 C
ANISOU 1617 CG PHE A 229 8264 14227 12535 -804 -265 568 C
ATOM 1618 CD1 PHE A 229 -4.979 -9.022 22.982 1.00 95.72 C
ANISOU 1618 CD1 PHE A 229 8691 14723 12955 -827 -284 578 C
ATOM 1619 CD2 PHE A 229 -3.664 -9.476 24.920 1.00 94.21 C
ANISOU 1619 CD2 PHE A 229 8500 14461 12833 -814 -262 558 C
ATOM 1620 CE1 PHE A 229 -5.505 -10.315 23.036 1.00 96.83 C
ANISOU 1620 CE1 PHE A 229 8794 14880 13117 -867 -310 578 C
ATOM 1621 CE2 PHE A 229 -4.193 -10.767 24.976 1.00 97.15 C
ANISOU 1621 CE2 PHE A 229 8829 14857 13225 -848 -274 558 C
ATOM 1622 CZ PHE A 229 -5.111 -11.178 24.035 1.00 95.61 C
ANISOU 1622 CZ PHE A 229 8615 14701 13010 -877 -302 570 C
ATOM 1623 N GLY A 230 -1.543 -4.728 23.147 1.00 90.05 N
ANISOU 1623 N GLY A 230 8113 13820 12283 -751 -261 602 N
ATOM 1624 CA GLY A 230 -1.317 -3.298 22.951 1.00 90.21 C
ANISOU 1624 CA GLY A 230 8168 13805 12304 -726 -280 631 C
ATOM 1625 C GLY A 230 -0.683 -2.989 21.609 1.00 94.31 C
ANISOU 1625 C GLY A 230 8674 14324 12836 -745 -253 657 C
ATOM 1626 O GLY A 230 -1.093 -2.045 20.931 1.00 93.92 O
ANISOU 1626 O GLY A 230 8636 14291 12757 -721 -252 682 O
ATOM 1627 N TYR A 231 0.299 -3.818 21.203 1.00 91.35 N
ANISOU 1627 N TYR A 231 8273 13935 12501 -779 -222 660 N
ATOM 1628 CA TYR A 231 1.021 -3.711 19.934 1.00 91.73 C
ANISOU 1628 CA TYR A 231 8307 13987 12559 -781 -177 697 C
ATOM 1629 C TYR A 231 0.122 -4.104 18.753 1.00 95.77 C
ANISOU 1629 C TYR A 231 8832 14571 12987 -765 -147 677 C
ATOM 1630 O TYR A 231 0.206 -3.466 17.702 1.00 95.78 O
ANISOU 1630 O TYR A 231 8838 14589 12964 -744 -122 711 O
ATOM 1631 CB TYR A 231 2.289 -4.582 19.966 1.00 93.12 C
ANISOU 1631 CB TYR A 231 8457 14129 12798 -804 -142 715 C
ATOM 1632 CG TYR A 231 3.060 -4.644 18.665 1.00 95.77 C
ANISOU 1632 CG TYR A 231 8780 14476 13132 -786 -73 763 C
ATOM 1633 CD1 TYR A 231 3.763 -3.534 18.197 1.00 98.32 C
ANISOU 1633 CD1 TYR A 231 9081 14774 13501 -774 -63 845 C
ATOM 1634 CD2 TYR A 231 3.147 -5.825 17.937 1.00 96.78 C
ANISOU 1634 CD2 TYR A 231 8924 14633 13215 -773 -16 734 C
ATOM 1635 CE1 TYR A 231 4.494 -3.591 17.010 1.00 99.86 C
ANISOU 1635 CE1 TYR A 231 9262 14987 13695 -741 15 906 C
ATOM 1636 CE2 TYR A 231 3.887 -5.898 16.757 1.00 98.32 C
ANISOU 1636 CE2 TYR A 231 9125 14838 13395 -734 59 782 C
ATOM 1637 CZ TYR A 231 4.554 -4.775 16.294 1.00106.30 C
ANISOU 1637 CZ TYR A 231 10104 15836 14448 -713 82 873 C
ATOM 1638 OH TYR A 231 5.277 -4.832 15.128 1.00108.09 O
ANISOU 1638 OH TYR A 231 10334 16080 14654 -659 170 934 O
ATOM 1639 N VAL A 232 -0.731 -5.141 18.925 1.00 92.18 N
ANISOU 1639 N VAL A 232 8380 14154 12490 -777 -157 628 N
ATOM 1640 CA VAL A 232 -1.671 -5.606 17.895 1.00 92.44 C
ANISOU 1640 CA VAL A 232 8432 14244 12446 -775 -158 607 C
ATOM 1641 C VAL A 232 -2.699 -4.480 17.659 1.00 96.72 C
ANISOU 1641 C VAL A 232 8973 14827 12950 -752 -184 633 C
ATOM 1642 O VAL A 232 -3.013 -4.173 16.507 1.00 96.47 O
ANISOU 1642 O VAL A 232 8959 14829 12867 -738 -174 648 O
ATOM 1643 CB VAL A 232 -2.328 -6.976 18.263 1.00 96.33 C
ANISOU 1643 CB VAL A 232 8921 14753 12926 -806 -184 562 C
ATOM 1644 CG1 VAL A 232 -3.494 -7.330 17.335 1.00 96.60 C
ANISOU 1644 CG1 VAL A 232 8975 14838 12889 -815 -220 550 C
ATOM 1645 CG2 VAL A 232 -1.291 -8.094 18.246 1.00 96.12 C
ANISOU 1645 CG2 VAL A 232 8907 14687 12928 -821 -150 537 C
ATOM 1646 N ALA A1001 -3.135 -3.812 18.750 1.00 93.39 N
ANISOU 1646 N ALA A1001 8537 14399 12548 -738 -212 643 N
ATOM 1647 CA ALA A1001 -4.070 -2.687 18.720 1.00 93.45 C
ANISOU 1647 CA ALA A1001 8546 14437 12524 -701 -228 676 C
ATOM 1648 C ALA A1001 -3.468 -1.475 18.001 1.00 97.64 C
ANISOU 1648 C ALA A1001 9095 14943 13062 -680 -213 711 C
ATOM 1649 O ALA A1001 -4.200 -0.759 17.318 1.00 97.67 O
ANISOU 1649 O ALA A1001 9100 14987 13024 -657 -214 739 O
ATOM 1650 CB ALA A1001 -4.468 -2.299 20.135 1.00 94.01 C
ANISOU 1650 CB ALA A1001 8617 14492 12609 -670 -248 681 C
ATOM 1651 N ASP A1002 -2.145 -1.253 18.149 1.00 94.06 N
ANISOU 1651 N ASP A1002 8646 14422 12669 -691 -204 722 N
ATOM 1652 CA ASP A1002 -1.440 -0.131 17.527 1.00 94.25 C
ANISOU 1652 CA ASP A1002 8674 14412 12725 -679 -196 773 C
ATOM 1653 C ASP A1002 -1.281 -0.325 16.013 1.00 97.91 C
ANISOU 1653 C ASP A1002 9130 14924 13147 -673 -147 795 C
ATOM 1654 O ASP A1002 -1.330 0.664 15.281 1.00 97.80 O
ANISOU 1654 O ASP A1002 9116 14923 13120 -649 -139 839 O
ATOM 1655 CB ASP A1002 -0.066 0.092 18.178 1.00 96.37 C
ANISOU 1655 CB ASP A1002 8935 14595 13085 -703 -210 798 C
ATOM 1656 CG ASP A1002 -0.116 0.842 19.500 1.00108.37 C
ANISOU 1656 CG ASP A1002 10491 16045 14638 -697 -275 791 C
ATOM 1657 OD1 ASP A1002 -0.743 1.926 19.547 1.00109.07 O
ANISOU 1657 OD1 ASP A1002 10615 16131 14696 -660 -300 799 O
ATOM 1658 OD2 ASP A1002 0.539 0.389 20.464 1.00115.46 O1-
ANISOU 1658 OD2 ASP A1002 11392 16887 15592 -723 -303 783 O1-
ATOM 1659 N LEU A1003 -1.100 -1.578 15.542 1.00 93.94 N
ANISOU 1659 N LEU A1003 8631 14445 12618 -686 -118 763 N
ATOM 1660 CA LEU A1003 -0.967 -1.853 14.108 1.00 93.95 C
ANISOU 1660 CA LEU A1003 8653 14488 12557 -665 -73 774 C
ATOM 1661 C LEU A1003 -2.331 -1.769 13.421 1.00 97.35 C
ANISOU 1661 C LEU A1003 9104 14985 12899 -658 -103 754 C
ATOM 1662 O LEU A1003 -2.411 -1.251 12.307 1.00 97.51 O
ANISOU 1662 O LEU A1003 9144 15039 12866 -630 -81 783 O
ATOM 1663 CB LEU A1003 -0.309 -3.217 13.833 1.00 94.14 C
ANISOU 1663 CB LEU A1003 8696 14502 12570 -672 -37 741 C
ATOM 1664 CG LEU A1003 1.193 -3.350 14.137 1.00 99.04 C
ANISOU 1664 CG LEU A1003 9291 15069 13273 -667 13 785 C
ATOM 1665 CD1 LEU A1003 1.630 -4.793 14.067 1.00 99.32 C
ANISOU 1665 CD1 LEU A1003 9351 15094 13290 -669 45 742 C
ATOM 1666 CD2 LEU A1003 2.050 -2.513 13.185 1.00102.09 C
ANISOU 1666 CD2 LEU A1003 9664 15456 13669 -623 75 872 C
ATOM 1667 N GLU A1004 -3.401 -2.242 14.098 1.00 93.08 N
ANISOU 1667 N GLU A1004 8556 14465 12347 -682 -153 719 N
ATOM 1668 CA GLU A1004 -4.779 -2.200 13.597 1.00 93.02 C
ANISOU 1668 CA GLU A1004 8550 14519 12272 -686 -195 719 C
ATOM 1669 C GLU A1004 -5.292 -0.754 13.516 1.00 96.23 C
ANISOU 1669 C GLU A1004 8938 14950 12673 -653 -198 772 C
ATOM 1670 O GLU A1004 -6.070 -0.443 12.614 1.00 96.27 O
ANISOU 1670 O GLU A1004 8952 15009 12619 -645 -212 792 O
ATOM 1671 CB GLU A1004 -5.721 -3.048 14.470 1.00 94.27 C
ANISOU 1671 CB GLU A1004 8685 14692 12442 -718 -243 693 C
ATOM 1672 CG GLU A1004 -5.552 -4.551 14.286 1.00105.53 C
ANISOU 1672 CG GLU A1004 10139 16107 13850 -756 -260 642 C
ATOM 1673 CD GLU A1004 -6.488 -5.457 15.069 1.00125.23 C
ANISOU 1673 CD GLU A1004 12604 18614 16365 -796 -315 628 C
ATOM 1674 OE1 GLU A1004 -7.046 -5.011 16.099 1.00115.54 O
ANISOU 1674 OE1 GLU A1004 11325 17392 15183 -787 -318 654 O
ATOM 1675 OE2 GLU A1004 -6.634 -6.634 14.668 1.00119.87 O1-
ANISOU 1675 OE2 GLU A1004 11957 17932 15656 -832 -355 595 O1-
ATOM 1676 N ASP A1005 -4.852 0.122 14.448 1.00 91.90 N
ANISOU 1676 N ASP A1005 8376 14358 12183 -633 -192 794 N
ATOM 1677 CA ASP A1005 -5.214 1.544 14.487 1.00 91.70 C
ANISOU 1677 CA ASP A1005 8347 14339 12155 -594 -194 843 C
ATOM 1678 C ASP A1005 -4.571 2.276 13.307 1.00 95.06 C
ANISOU 1678 C ASP A1005 8781 14761 12578 -579 -161 883 C
ATOM 1679 O ASP A1005 -5.225 3.101 12.667 1.00 94.94 O
ANISOU 1679 O ASP A1005 8761 14779 12531 -552 -160 924 O
ATOM 1680 CB ASP A1005 -4.789 2.183 15.826 1.00 93.43 C
ANISOU 1680 CB ASP A1005 8577 14496 12427 -571 -209 847 C
ATOM 1681 CG ASP A1005 -5.108 3.662 15.967 1.00105.87 C
ANISOU 1681 CG ASP A1005 10170 16046 14010 -526 -213 894 C
ATOM 1682 OD1 ASP A1005 -6.261 4.057 15.671 1.00107.45 O
ANISOU 1682 OD1 ASP A1005 10358 16305 14162 -500 -207 928 O
ATOM 1683 OD2 ASP A1005 -4.226 4.416 16.423 1.00111.81 O1-
ANISOU 1683 OD2 ASP A1005 10952 16715 14816 -518 -230 899 O1-
ATOM 1684 N ASN A1006 -3.298 1.955 13.012 1.00 91.01 N
ANISOU 1684 N ASN A1006 8271 14209 12101 -590 -128 884 N
ATOM 1685 CA ASN A1006 -2.547 2.519 11.891 1.00 91.00 C
ANISOU 1685 CA ASN A1006 8266 14206 12102 -567 -83 941 C
ATOM 1686 C ASN A1006 -3.103 1.985 10.567 1.00 95.19 C
ANISOU 1686 C ASN A1006 8824 14811 12532 -549 -62 935 C
ATOM 1687 O ASN A1006 -3.055 2.689 9.559 1.00 95.32 O
ANISOU 1687 O ASN A1006 8841 14857 12519 -515 -37 987 O
ATOM 1688 CB ASN A1006 -1.049 2.208 12.021 1.00 90.16 C
ANISOU 1688 CB ASN A1006 8146 14044 12069 -576 -46 964 C
ATOM 1689 CG ASN A1006 -0.358 2.888 13.185 1.00103.12 C
ANISOU 1689 CG ASN A1006 9764 15599 13818 -595 -79 996 C
ATOM 1690 OD1 ASN A1006 -0.551 4.077 13.465 1.00 94.70 O
ANISOU 1690 OD1 ASN A1006 8699 14503 12779 -586 -114 1027 O
ATOM 1691 ND2 ASN A1006 0.516 2.160 13.857 1.00 93.18 N
ANISOU 1691 ND2 ASN A1006 8490 14291 12622 -621 -74 994 N
ATOM 1692 N TRP A1007 -3.643 0.747 10.584 1.00 91.48 N
ANISOU 1692 N TRP A1007 8383 14367 12008 -571 -83 872 N
ATOM 1693 CA TRP A1007 -4.254 0.108 9.419 1.00 91.79 C
ANISOU 1693 CA TRP A1007 8472 14462 11941 -563 -94 851 C
ATOM 1694 C TRP A1007 -5.616 0.740 9.129 1.00 94.75 C
ANISOU 1694 C TRP A1007 8834 14894 12273 -566 -144 872 C
ATOM 1695 O TRP A1007 -6.003 0.859 7.962 1.00 94.70 O
ANISOU 1695 O TRP A1007 8861 14934 12187 -545 -147 890 O
ATOM 1696 CB TRP A1007 -4.396 -1.406 9.623 1.00 90.71 C
ANISOU 1696 CB TRP A1007 8373 14317 11777 -598 -127 779 C
ATOM 1697 CG TRP A1007 -4.547 -2.152 8.334 1.00 92.66 C
ANISOU 1697 CG TRP A1007 8702 14590 11913 -581 -134 752 C
ATOM 1698 CD1 TRP A1007 -5.703 -2.374 7.644 1.00 96.13 C
ANISOU 1698 CD1 TRP A1007 9179 15075 12270 -597 -205 740 C
ATOM 1699 CD2 TRP A1007 -3.493 -2.721 7.543 1.00 93.11 C
ANISOU 1699 CD2 TRP A1007 8826 14626 11925 -532 -66 745 C
ATOM 1700 NE1 TRP A1007 -5.438 -3.062 6.482 1.00 96.48 N
ANISOU 1700 NE1 TRP A1007 9327 15120 12210 -564 -198 711 N
ATOM 1701 CE2 TRP A1007 -4.088 -3.290 6.396 1.00 97.96 C
ANISOU 1701 CE2 TRP A1007 9537 15269 12412 -514 -103 714 C
ATOM 1702 CE3 TRP A1007 -2.096 -2.815 7.700 1.00 94.35 C
ANISOU 1702 CE3 TRP A1007 8972 14741 12136 -497 21 770 C
ATOM 1703 CZ2 TRP A1007 -3.341 -3.945 5.409 1.00 98.12 C
ANISOU 1703 CZ2 TRP A1007 9661 15274 12344 -448 -48 698 C
ATOM 1704 CZ3 TRP A1007 -1.356 -3.466 6.725 1.00 96.63 C
ANISOU 1704 CZ3 TRP A1007 9342 15024 12350 -431 87 770 C
ATOM 1705 CH2 TRP A1007 -1.975 -4.021 5.595 1.00 98.15 C
ANISOU 1705 CH2 TRP A1007 9648 15243 12401 -401 57 729 C
ATOM 1706 N GLU A1008 -6.339 1.144 10.196 1.00 90.26 N
ANISOU 1706 N GLU A1008 8219 14322 11754 -583 -179 878 N
ATOM 1707 CA GLU A1008 -7.642 1.808 10.116 1.00 89.97 C
ANISOU 1707 CA GLU A1008 8153 14337 11696 -577 -217 917 C
ATOM 1708 C GLU A1008 -7.459 3.222 9.550 1.00 93.10 C
ANISOU 1708 C GLU A1008 8539 14739 12094 -532 -182 979 C
ATOM 1709 O GLU A1008 -8.258 3.654 8.718 1.00 92.95 O
ANISOU 1709 O GLU A1008 8516 14778 12021 -520 -199 1017 O
ATOM 1710 CB GLU A1008 -8.319 1.841 11.503 1.00 90.94 C
ANISOU 1710 CB GLU A1008 8235 14446 11873 -583 -240 918 C
ATOM 1711 CG GLU A1008 -9.749 2.367 11.492 1.00102.14 C
ANISOU 1711 CG GLU A1008 9614 15926 13270 -571 -274 972 C
ATOM 1712 CD GLU A1008 -10.463 2.406 12.831 1.00121.53 C
ANISOU 1712 CD GLU A1008 12033 18374 15769 -553 -278 989 C
ATOM 1713 OE1 GLU A1008 -9.844 2.836 13.831 1.00115.16 O
ANISOU 1713 OE1 GLU A1008 11241 17512 15001 -512 -247 987 O
ATOM 1714 OE2 GLU A1008 -11.666 2.058 12.866 1.00114.48 O1-
ANISOU 1714 OE2 GLU A1008 11100 17526 14871 -575 -318 1011 O1-
ATOM 1715 N THR A1009 -6.385 3.920 9.990 1.00 88.59 N
ANISOU 1715 N THR A1009 7964 14106 11591 -514 -142 997 N
ATOM 1716 CA THR A1009 -6.021 5.276 9.566 1.00 88.21 C
ANISOU 1716 CA THR A1009 7904 14045 11567 -477 -114 1062 C
ATOM 1717 C THR A1009 -5.618 5.258 8.080 1.00 92.04 C
ANISOU 1717 C THR A1009 8406 14572 11994 -455 -75 1094 C
ATOM 1718 O THR A1009 -5.937 6.198 7.349 1.00 91.77 O
ANISOU 1718 O THR A1009 8362 14573 11935 -425 -64 1150 O
ATOM 1719 CB THR A1009 -4.887 5.817 10.466 1.00 95.25 C
ANISOU 1719 CB THR A1009 8788 14842 12559 -477 -105 1076 C
ATOM 1720 OG1 THR A1009 -5.204 5.583 11.840 1.00 93.40 O
ANISOU 1720 OG1 THR A1009 8561 14570 12358 -488 -141 1036 O
ATOM 1721 CG2 THR A1009 -4.617 7.306 10.257 1.00 94.48 C
ANISOU 1721 CG2 THR A1009 8679 14714 12505 -447 -95 1151 C
ATOM 1722 N LEU A1010 -4.946 4.176 7.643 1.00 88.62 N
ANISOU 1722 N LEU A1010 8004 14136 11530 -461 -50 1060 N
ATOM 1723 CA LEU A1010 -4.463 3.990 6.275 1.00 89.19 C
ANISOU 1723 CA LEU A1010 8113 14244 11530 -420 -1 1086 C
ATOM 1724 C LEU A1010 -5.616 3.739 5.288 1.00 93.84 C
ANISOU 1724 C LEU A1010 8748 14908 11999 -416 -43 1067 C
ATOM 1725 O LEU A1010 -5.568 4.261 4.174 1.00 93.82 O
ANISOU 1725 O LEU A1010 8771 14947 11931 -370 -13 1112 O
ATOM 1726 CB LEU A1010 -3.468 2.816 6.230 1.00 89.33 C
ANISOU 1726 CB LEU A1010 8165 14229 11545 -414 42 1053 C
ATOM 1727 CG LEU A1010 -2.488 2.776 5.055 1.00 94.92 C
ANISOU 1727 CG LEU A1010 8907 14954 12203 -345 126 1106 C
ATOM 1728 CD1 LEU A1010 -1.302 3.708 5.293 1.00 95.14 C
ANISOU 1728 CD1 LEU A1010 8863 14942 12343 -322 187 1207 C
ATOM 1729 CD2 LEU A1010 -1.969 1.371 4.841 1.00 97.83 C
ANISOU 1729 CD2 LEU A1010 9345 15310 12517 -328 156 1053 C
ATOM 1730 N ASN A1011 -6.632 2.941 5.688 1.00 90.63 N
ANISOU 1730 N ASN A1011 8350 14518 11569 -464 -118 1013 N
ATOM 1731 CA ASN A1011 -7.784 2.591 4.848 1.00 91.17 C
ANISOU 1731 CA ASN A1011 8458 14647 11537 -478 -186 1003 C
ATOM 1732 C ASN A1011 -8.837 3.709 4.780 1.00 95.19 C
ANISOU 1732 C ASN A1011 8911 15206 12050 -476 -216 1067 C
ATOM 1733 O ASN A1011 -9.413 3.916 3.709 1.00 95.39 O
ANISOU 1733 O ASN A1011 8965 15286 11992 -462 -243 1095 O
ATOM 1734 CB ASN A1011 -8.452 1.305 5.345 1.00 92.24 C
ANISOU 1734 CB ASN A1011 8613 14774 11662 -539 -265 937 C
ATOM 1735 CG ASN A1011 -7.749 0.024 4.949 1.00115.33 C
ANISOU 1735 CG ASN A1011 11632 17668 14520 -540 -269 869 C
ATOM 1736 OD1 ASN A1011 -6.518 -0.062 4.893 1.00109.60 O
ANISOU 1736 OD1 ASN A1011 10939 16907 13798 -497 -189 859 O
ATOM 1737 ND2 ASN A1011 -8.532 -1.016 4.694 1.00107.46 N
ANISOU 1737 ND2 ASN A1011 10671 16675 13484 -594 -367 826 N
ATOM 1738 N ASP A1012 -9.106 4.403 5.910 1.00 91.22 N
ANISOU 1738 N ASP A1012 8339 14683 11636 -481 -212 1093 N
ATOM 1739 CA ASP A1012 -10.106 5.474 5.985 1.00 91.32 C
ANISOU 1739 CA ASP A1012 8301 14738 11659 -466 -229 1160 C
ATOM 1740 C ASP A1012 -9.689 6.711 5.168 1.00 95.64 C
ANISOU 1740 C ASP A1012 8842 15294 12202 -414 -176 1224 C
ATOM 1741 O ASP A1012 -10.489 7.194 4.363 1.00 95.53 O
ANISOU 1741 O ASP A1012 8816 15341 12142 -399 -195 1277 O
ATOM 1742 CB ASP A1012 -10.384 5.879 7.448 1.00 92.71 C
ANISOU 1742 CB ASP A1012 8428 14880 11918 -464 -229 1168 C
ATOM 1743 CG ASP A1012 -11.226 4.900 8.260 1.00103.12 C
ANISOU 1743 CG ASP A1012 9728 16209 13245 -507 -282 1137 C
ATOM 1744 OD1 ASP A1012 -12.042 4.165 7.654 1.00103.86 O
ANISOU 1744 OD1 ASP A1012 9820 16354 13286 -544 -345 1143 O
ATOM 1745 OD2 ASP A1012 -11.122 4.921 9.507 1.00108.76 O1-
ANISOU 1745 OD2 ASP A1012 10427 16876 14019 -502 -267 1117 O1-
ATOM 1746 N ASN A1013 -8.447 7.205 5.360 1.00 92.31 N
ANISOU 1746 N ASN A1013 8424 14814 11837 -389 -115 1231 N
ATOM 1747 CA ASN A1013 -7.919 8.386 4.666 1.00 92.56 C
ANISOU 1747 CA ASN A1013 8440 14843 11886 -344 -65 1305 C
ATOM 1748 C ASN A1013 -7.693 8.133 3.164 1.00 97.29 C
ANISOU 1748 C ASN A1013 9079 15501 12387 -313 -39 1327 C
ATOM 1749 O ASN A1013 -7.662 9.096 2.394 1.00 97.49 O
ANISOU 1749 O ASN A1013 9086 15553 12402 -273 -7 1400 O
ATOM 1750 CB ASN A1013 -6.624 8.869 5.310 1.00 93.19 C
ANISOU 1750 CB ASN A1013 8504 14835 12070 -337 -23 1321 C
ATOM 1751 CG ASN A1013 -6.844 9.619 6.600 1.00116.78 C
ANISOU 1751 CG ASN A1013 11471 17757 15144 -344 -51 1321 C
ATOM 1752 OD1 ASN A1013 -6.703 9.070 7.697 1.00112.39 O
ANISOU 1752 OD1 ASN A1013 10924 17152 14627 -371 -74 1266 O
ATOM 1753 ND2 ASN A1013 -7.203 10.891 6.500 1.00108.10 N
ANISOU 1753 ND2 ASN A1013 10354 16653 14067 -313 -49 1382 N
ATOM 1754 N LEU A1014 -7.556 6.857 2.751 1.00 94.06 N
ANISOU 1754 N LEU A1014 8732 15108 11900 -326 -54 1266 N
ATOM 1755 CA LEU A1014 -7.384 6.470 1.347 1.00 94.91 C
ANISOU 1755 CA LEU A1014 8909 15263 11887 -284 -35 1273 C
ATOM 1756 C LEU A1014 -8.684 6.720 0.576 1.00 99.78 C
ANISOU 1756 C LEU A1014 9539 15955 12418 -290 -102 1295 C
ATOM 1757 O LEU A1014 -8.645 7.107 -0.593 1.00100.15 O
ANISOU 1757 O LEU A1014 9620 16049 12384 -240 -78 1340 O
ATOM 1758 CB LEU A1014 -6.968 4.990 1.253 1.00 95.13 C
ANISOU 1758 CB LEU A1014 9022 15270 11853 -293 -45 1190 C
ATOM 1759 CG LEU A1014 -6.274 4.540 -0.035 1.00100.84 C
ANISOU 1759 CG LEU A1014 9843 16015 12457 -219 9 1195 C
ATOM 1760 CD1 LEU A1014 -5.178 3.545 0.264 1.00100.90 C
ANISOU 1760 CD1 LEU A1014 9891 15968 12479 -196 70 1157 C
ATOM 1761 CD2 LEU A1014 -7.262 3.941 -1.027 1.00104.41 C
ANISOU 1761 CD2 LEU A1014 10396 16512 12761 -225 -79 1150 C
ATOM 1762 N LYS A1015 -9.831 6.512 1.249 1.00 96.32 N
ANISOU 1762 N LYS A1015 9065 15530 12002 -347 -183 1278 N
ATOM 1763 CA LYS A1015 -11.172 6.713 0.706 1.00 96.88 C
ANISOU 1763 CA LYS A1015 9125 15670 12015 -366 -259 1316 C
ATOM 1764 C LYS A1015 -11.482 8.209 0.547 1.00101.70 C
ANISOU 1764 C LYS A1015 9664 16310 12668 -327 -219 1410 C
ATOM 1765 O LYS A1015 -12.274 8.573 -0.324 1.00102.00 O
ANISOU 1765 O LYS A1015 9700 16413 12643 -320 -256 1462 O
ATOM 1766 CB LYS A1015 -12.220 6.042 1.607 1.00 99.03 C
ANISOU 1766 CB LYS A1015 9361 15945 12322 -436 -349 1293 C
ATOM 1767 CG LYS A1015 -12.142 4.515 1.603 1.00112.40 C
ANISOU 1767 CG LYS A1015 11129 17615 13964 -484 -417 1209 C
ATOM 1768 CD LYS A1015 -13.222 3.853 2.459 1.00121.83 C
ANISOU 1768 CD LYS A1015 12270 18810 15210 -556 -506 1205 C
ATOM 1769 CE LYS A1015 -12.867 3.759 3.925 1.00131.72 C
ANISOU 1769 CE LYS A1015 13467 20011 16570 -562 -458 1181 C
ATOM 1770 NZ LYS A1015 -13.931 3.075 4.705 1.00141.07 N1+
ANISOU 1770 NZ LYS A1015 14604 21199 17795 -624 -540 1183 N1+
ATOM 1771 N VAL A1016 -10.857 9.066 1.386 1.00 98.32 N
ANISOU 1771 N VAL A1016 9185 15827 12345 -304 -153 1433 N
ATOM 1772 CA VAL A1016 -11.021 10.528 1.377 1.00 98.43 C
ANISOU 1772 CA VAL A1016 9142 15844 12413 -264 -114 1517 C
ATOM 1773 C VAL A1016 -10.412 11.095 0.076 1.00103.34 C
ANISOU 1773 C VAL A1016 9784 16498 12985 -213 -61 1574 C
ATOM 1774 O VAL A1016 -11.030 11.955 -0.555 1.00103.38 O
ANISOU 1774 O VAL A1016 9759 16550 12971 -185 -59 1648 O
ATOM 1775 CB VAL A1016 -10.403 11.193 2.647 1.00101.70 C
ANISOU 1775 CB VAL A1016 9524 16168 12950 -257 -77 1515 C
ATOM 1776 CG1 VAL A1016 -10.612 12.707 2.647 1.00101.71 C
ANISOU 1776 CG1 VAL A1016 9485 16156 13005 -214 -47 1599 C
ATOM 1777 CG2 VAL A1016 -10.973 10.586 3.928 1.00100.95 C
ANISOU 1777 CG2 VAL A1016 9418 16047 12891 -293 -119 1463 C
ATOM 1778 N ILE A1017 -9.219 10.590 -0.323 1.00100.28 N
ANISOU 1778 N ILE A1017 9443 16088 12573 -192 -13 1550 N
ATOM 1779 CA ILE A1017 -8.494 11.004 -1.534 1.00100.99 C
ANISOU 1779 CA ILE A1017 9554 16208 12610 -126 54 1613 C
ATOM 1780 C ILE A1017 -9.313 10.611 -2.782 1.00106.15 C
ANISOU 1780 C ILE A1017 10272 16948 13111 -110 9 1612 C
ATOM 1781 O ILE A1017 -9.392 11.404 -3.725 1.00106.39 O
ANISOU 1781 O ILE A1017 10298 17029 13097 -58 42 1689 O
ATOM 1782 CB ILE A1017 -7.050 10.416 -1.577 1.00104.12 C
ANISOU 1782 CB ILE A1017 9981 16558 13021 -97 125 1599 C
ATOM 1783 CG1 ILE A1017 -6.279 10.746 -0.275 1.00103.81 C
ANISOU 1783 CG1 ILE A1017 9882 16426 13136 -130 142 1596 C
ATOM 1784 CG2 ILE A1017 -6.281 10.928 -2.811 1.00105.69 C
ANISOU 1784 CG2 ILE A1017 10188 16793 13178 -11 214 1693 C
ATOM 1785 CD1 ILE A1017 -4.979 9.976 -0.041 1.00111.96 C
ANISOU 1785 CD1 ILE A1017 10937 17409 14194 -125 188 1566 C
ATOM 1786 N GLU A1018 -9.949 9.418 -2.764 1.00103.04 N
ANISOU 1786 N GLU A1018 9941 16567 12643 -158 -76 1530 N
ATOM 1787 CA GLU A1018 -10.786 8.906 -3.857 1.00103.97 C
ANISOU 1787 CA GLU A1018 10138 16750 12616 -161 -156 1517 C
ATOM 1788 C GLU A1018 -11.953 9.868 -4.166 1.00108.42 C
ANISOU 1788 C GLU A1018 10636 17377 13180 -171 -200 1598 C
ATOM 1789 O GLU A1018 -12.348 9.982 -5.328 1.00108.96 O
ANISOU 1789 O GLU A1018 10756 17506 13137 -142 -230 1631 O
ATOM 1790 CB GLU A1018 -11.323 7.504 -3.527 1.00105.39 C
ANISOU 1790 CB GLU A1018 10379 16909 12754 -231 -261 1422 C
ATOM 1791 CG GLU A1018 -10.259 6.420 -3.546 1.00116.31 C
ANISOU 1791 CG GLU A1018 11858 18239 14094 -209 -225 1341 C
ATOM 1792 CD GLU A1018 -10.754 5.039 -3.161 1.00137.60 C
ANISOU 1792 CD GLU A1018 14626 20907 16751 -278 -335 1247 C
ATOM 1793 OE1 GLU A1018 -10.447 4.593 -2.032 1.00128.45 O
ANISOU 1793 OE1 GLU A1018 13433 19693 15680 -317 -326 1199 O
ATOM 1794 OE2 GLU A1018 -11.458 4.406 -3.982 1.00134.67 O1-
ANISOU 1794 OE2 GLU A1018 14347 20562 16261 -295 -439 1225 O1-
ATOM 1795 N LYS A1019 -12.471 10.577 -3.135 1.00104.29 N
ANISOU 1795 N LYS A1019 10009 16839 12779 -200 -200 1634 N
ATOM 1796 CA LYS A1019 -13.535 11.573 -3.275 1.00104.34 C
ANISOU 1796 CA LYS A1019 9942 16899 12805 -198 -224 1723 C
ATOM 1797 C LYS A1019 -12.969 12.841 -3.931 1.00108.58 C
ANISOU 1797 C LYS A1019 10453 17451 13353 -126 -134 1807 C
ATOM 1798 O LYS A1019 -11.956 13.370 -3.466 1.00107.33 O
ANISOU 1798 O LYS A1019 10274 17232 13273 -94 -51 1814 O
ATOM 1799 CB LYS A1019 -14.171 11.894 -1.907 1.00106.11 C
ANISOU 1799 CB LYS A1019 10080 17091 13147 -230 -234 1735 C
ATOM 1800 CG LYS A1019 -15.342 12.873 -1.980 1.00122.28 C
ANISOU 1800 CG LYS A1019 12051 19196 15214 -221 -257 1833 C
ATOM 1801 CD LYS A1019 -15.865 13.259 -0.605 1.00132.91 C
ANISOU 1801 CD LYS A1019 13327 20505 16669 -220 -240 1854 C
ATOM 1802 CE LYS A1019 -17.013 14.238 -0.704 1.00145.34 C
ANISOU 1802 CE LYS A1019 14827 22136 18259 -193 -245 1966 C
ATOM 1803 NZ LYS A1019 -17.541 14.609 0.633 1.00154.18 N1+
ANISOU 1803 NZ LYS A1019 15895 23216 19470 -164 -211 1993 N1+
ATOM 1804 N ALA A1020 -13.627 13.313 -5.014 1.00106.49 N
ANISOU 1804 N ALA A1020 10185 17263 13015 -103 -158 1878 N
ATOM 1805 CA ALA A1020 -13.246 14.509 -5.773 1.00106.88 C
ANISOU 1805 CA ALA A1020 10205 17339 13066 -33 -80 1971 C
ATOM 1806 C ALA A1020 -13.340 15.763 -4.889 1.00110.59 C
ANISOU 1806 C ALA A1020 10577 17764 13679 -22 -31 2033 C
ATOM 1807 O ALA A1020 -14.424 16.326 -4.696 1.00110.48 O
ANISOU 1807 O ALA A1020 10506 17778 13691 -34 -65 2082 O
ATOM 1808 CB ALA A1020 -14.127 14.653 -7.008 1.00108.62 C
ANISOU 1808 CB ALA A1020 10447 17654 13170 -20 -135 2029 C
ATOM 1809 N ASP A1021 -12.191 16.162 -4.317 1.00106.62 N
ANISOU 1809 N ASP A1021 10059 17183 13268 3 45 2036 N
ATOM 1810 CA ASP A1021 -12.071 17.312 -3.422 1.00105.90 C
ANISOU 1810 CA ASP A1021 9904 17019 13313 14 80 2082 C
ATOM 1811 C ASP A1021 -10.910 18.226 -3.861 1.00109.07 C
ANISOU 1811 C ASP A1021 10282 17381 13778 62 158 2157 C
ATOM 1812 O ASP A1021 -10.250 17.945 -4.866 1.00109.36 O
ANISOU 1812 O ASP A1021 10346 17457 13750 96 200 2179 O
ATOM 1813 CB ASP A1021 -11.866 16.827 -1.970 1.00107.07 C
ANISOU 1813 CB ASP A1021 10058 17080 13543 -29 58 2000 C
ATOM 1814 CG ASP A1021 -12.965 15.927 -1.427 1.00118.03 C
ANISOU 1814 CG ASP A1021 11448 18501 14895 -72 -12 1948 C
ATOM 1815 OD1 ASP A1021 -14.144 16.356 -1.428 1.00119.21 O
ANISOU 1815 OD1 ASP A1021 11555 18681 15058 -61 -30 2002 O
ATOM 1816 OD2 ASP A1021 -12.640 14.821 -0.948 1.00123.08 O1-
ANISOU 1816 OD2 ASP A1021 12128 19132 15504 -113 -45 1864 O1-
ATOM 1817 N ASN A1022 -10.673 19.320 -3.112 1.00104.33 N
ANISOU 1817 N ASN A1022 9637 16699 13306 69 175 2203 N
ATOM 1818 CA ASN A1022 -9.605 20.284 -3.384 1.00103.96 C
ANISOU 1818 CA ASN A1022 9553 16593 13353 101 230 2291 C
ATOM 1819 C ASN A1022 -8.235 19.727 -2.945 1.00105.95 C
ANISOU 1819 C ASN A1022 9817 16772 13669 81 252 2259 C
ATOM 1820 O ASN A1022 -8.177 18.707 -2.255 1.00104.62 O
ANISOU 1820 O ASN A1022 9689 16589 13473 43 224 2159 O
ATOM 1821 CB ASN A1022 -9.899 21.621 -2.690 1.00105.31 C
ANISOU 1821 CB ASN A1022 9691 16681 13640 108 216 2341 C
ATOM 1822 CG ASN A1022 -10.154 21.512 -1.207 1.00130.44 C
ANISOU 1822 CG ASN A1022 12905 19774 16880 75 167 2257 C
ATOM 1823 OD1 ASN A1022 -9.232 21.349 -0.401 1.00125.53 O
ANISOU 1823 OD1 ASN A1022 12304 19059 16334 45 153 2211 O
ATOM 1824 ND2 ASN A1022 -11.415 21.609 -0.816 1.00121.95 N
ANISOU 1824 ND2 ASN A1022 11834 18729 15770 87 142 2245 N
ATOM 1825 N ALA A1023 -7.141 20.410 -3.353 1.00102.14 N
ANISOU 1825 N ALA A1023 9289 16242 13279 106 300 2359 N
ATOM 1826 CA ALA A1023 -5.746 20.057 -3.069 1.00101.55 C
ANISOU 1826 CA ALA A1023 9201 16099 13284 93 328 2373 C
ATOM 1827 C ALA A1023 -5.457 19.937 -1.564 1.00104.00 C
ANISOU 1827 C ALA A1023 9526 16288 13703 30 265 2298 C
ATOM 1828 O ALA A1023 -4.731 19.025 -1.166 1.00103.27 O
ANISOU 1828 O ALA A1023 9448 16166 13626 5 270 2251 O
ATOM 1829 CB ALA A1023 -4.818 21.095 -3.678 1.00103.11 C
ANISOU 1829 CB ALA A1023 9324 16270 13582 130 382 2529 C
ATOM 1830 N ALA A1024 -6.024 20.845 -0.738 1.00 99.91 N
ANISOU 1830 N ALA A1024 9013 15697 13252 13 209 2289 N
ATOM 1831 CA ALA A1024 -5.836 20.882 0.719 1.00 98.96 C
ANISOU 1831 CA ALA A1024 8927 15452 13221 -33 143 2219 C
ATOM 1832 C ALA A1024 -6.433 19.650 1.417 1.00100.91 C
ANISOU 1832 C ALA A1024 9226 15730 13385 -60 118 2086 C
ATOM 1833 O ALA A1024 -5.918 19.235 2.457 1.00100.00 O
ANISOU 1833 O ALA A1024 9136 15532 13328 -99 83 2026 O
ATOM 1834 CB ALA A1024 -6.457 22.144 1.292 1.00 99.95 C
ANISOU 1834 CB ALA A1024 9070 15502 13403 -18 98 2242 C
ATOM 1835 N GLN A1025 -7.509 19.076 0.851 1.00 96.55 N
ANISOU 1835 N GLN A1025 8688 15292 12705 -44 128 2048 N
ATOM 1836 CA GLN A1025 -8.164 17.882 1.385 1.00 95.39 C
ANISOU 1836 CA GLN A1025 8580 15185 12481 -72 99 1939 C
ATOM 1837 C GLN A1025 -7.310 16.630 1.132 1.00 97.67 C
ANISOU 1837 C GLN A1025 8885 15490 12735 -96 119 1890 C
ATOM 1838 O GLN A1025 -7.321 15.714 1.951 1.00 96.54 O
ANISOU 1838 O GLN A1025 8770 15319 12590 -132 90 1802 O
ATOM 1839 CB GLN A1025 -9.562 17.703 0.769 1.00 97.12 C
ANISOU 1839 CB GLN A1025 8797 15517 12586 -56 89 1938 C
ATOM 1840 CG GLN A1025 -10.615 18.712 1.248 1.00118.41 C
ANISOU 1840 CG GLN A1025 11482 18203 15306 -29 70 1972 C
ATOM 1841 CD GLN A1025 -11.180 18.396 2.616 1.00142.79 C
ANISOU 1841 CD GLN A1025 14597 21242 18413 -41 34 1903 C
ATOM 1842 OE1 GLN A1025 -11.842 17.370 2.827 1.00138.60 O
ANISOU 1842 OE1 GLN A1025 14074 20761 17827 -69 10 1843 O
ATOM 1843 NE2 GLN A1025 -10.987 19.302 3.563 1.00137.02 N
ANISOU 1843 NE2 GLN A1025 13886 20418 17755 -9 28 1920 N
ATOM 1844 N VAL A1026 -6.573 16.601 0.001 1.00 93.98 N
ANISOU 1844 N VAL A1026 8402 15069 12236 -64 176 1954 N
ATOM 1845 CA VAL A1026 -5.704 15.489 -0.411 1.00 93.58 C
ANISOU 1845 CA VAL A1026 8375 15038 12141 -60 215 1928 C
ATOM 1846 C VAL A1026 -4.446 15.450 0.492 1.00 96.73 C
ANISOU 1846 C VAL A1026 8749 15329 12673 -89 220 1937 C
ATOM 1847 O VAL A1026 -4.064 14.367 0.947 1.00 95.99 O
ANISOU 1847 O VAL A1026 8684 15219 12567 -114 218 1866 O
ATOM 1848 CB VAL A1026 -5.327 15.573 -1.922 1.00 98.25 C
ANISOU 1848 CB VAL A1026 8966 15712 12652 7 287 2012 C
ATOM 1849 CG1 VAL A1026 -4.535 14.347 -2.373 1.00 98.25 C
ANISOU 1849 CG1 VAL A1026 9011 15732 12586 33 338 1984 C
ATOM 1850 CG2 VAL A1026 -6.567 15.739 -2.793 1.00 98.41 C
ANISOU 1850 CG2 VAL A1026 9013 15832 12545 30 265 2009 C
ATOM 1851 N LYS A1027 -3.825 16.629 0.750 1.00 92.77 N
ANISOU 1851 N LYS A1027 8196 14750 12303 -90 217 2030 N
ATOM 1852 CA LYS A1027 -2.624 16.782 1.584 1.00 92.13 C
ANISOU 1852 CA LYS A1027 8084 14554 12368 -127 199 2064 C
ATOM 1853 C LYS A1027 -2.852 16.286 3.014 1.00 95.64 C
ANISOU 1853 C LYS A1027 8573 14923 12843 -183 125 1950 C
ATOM 1854 O LYS A1027 -2.049 15.489 3.502 1.00 95.10 O
ANISOU 1854 O LYS A1027 8503 14805 12828 -214 121 1928 O
ATOM 1855 CB LYS A1027 -2.151 18.249 1.634 1.00 94.57 C
ANISOU 1855 CB LYS A1027 8340 14783 12811 -127 178 2184 C
ATOM 1856 CG LYS A1027 -1.614 18.805 0.326 1.00103.73 C
ANISOU 1856 CG LYS A1027 9433 15996 13985 -73 256 2331 C
ATOM 1857 CD LYS A1027 -1.083 20.221 0.523 1.00110.06 C
ANISOU 1857 CD LYS A1027 10181 16702 14937 -86 216 2450 C
ATOM 1858 CE LYS A1027 -0.737 20.889 -0.782 1.00116.79 C
ANISOU 1858 CE LYS A1027 10954 17611 15810 -29 296 2612 C
ATOM 1859 NZ LYS A1027 -0.144 22.237 -0.575 1.00123.82 N1+
ANISOU 1859 NZ LYS A1027 11786 18395 16864 -50 245 2737 N1+
ATOM 1860 N ASP A1028 -3.951 16.735 3.674 1.00 92.01 N
ANISOU 1860 N ASP A1028 8153 14458 12348 -186 75 1887 N
ATOM 1861 CA ASP A1028 -4.272 16.390 5.062 1.00 91.34 C
ANISOU 1861 CA ASP A1028 8117 14306 12281 -219 12 1788 C
ATOM 1862 C ASP A1028 -4.501 14.875 5.220 1.00 94.03 C
ANISOU 1862 C ASP A1028 8482 14704 12541 -241 22 1690 C
ATOM 1863 O ASP A1028 -4.135 14.328 6.258 1.00 93.24 O
ANISOU 1863 O ASP A1028 8405 14538 12486 -276 -12 1630 O
ATOM 1864 CB ASP A1028 -5.476 17.205 5.595 1.00 93.51 C
ANISOU 1864 CB ASP A1028 8426 14572 12531 -192 -22 1770 C
ATOM 1865 CG ASP A1028 -6.863 16.589 5.491 1.00106.70 C
ANISOU 1865 CG ASP A1028 10114 16339 14086 -174 -19 1711 C
ATOM 1866 OD1 ASP A1028 -7.228 15.796 6.387 1.00107.17 O
ANISOU 1866 OD1 ASP A1028 10211 16375 14135 -185 -50 1634 O
ATOM 1867 OD2 ASP A1028 -7.629 16.999 4.593 1.00114.17 O1-
ANISOU 1867 OD2 ASP A1028 11037 17374 14969 -144 7 1756 O1-
ATOM 1868 N ALA A1029 -5.053 14.203 4.193 1.00 90.25 N
ANISOU 1868 N ALA A1029 8005 14339 11947 -222 61 1676 N
ATOM 1869 CA ALA A1029 -5.288 12.761 4.228 1.00 89.54 C
ANISOU 1869 CA ALA A1029 7947 14297 11777 -243 61 1588 C
ATOM 1870 C ALA A1029 -3.968 11.989 4.123 1.00 93.15 C
ANISOU 1870 C ALA A1029 8401 14728 12265 -249 103 1594 C
ATOM 1871 O ALA A1029 -3.752 11.066 4.910 1.00 92.18 O
ANISOU 1871 O ALA A1029 8301 14583 12141 -281 87 1519 O
ATOM 1872 CB ALA A1029 -6.230 12.353 3.109 1.00 90.58 C
ANISOU 1872 CB ALA A1029 8098 14542 11778 -222 68 1578 C
ATOM 1873 N LEU A1030 -3.078 12.388 3.186 1.00 90.18 N
ANISOU 1873 N LEU A1030 7988 14355 11920 -213 161 1695 N
ATOM 1874 CA LEU A1030 -1.769 11.761 2.968 1.00 90.31 C
ANISOU 1874 CA LEU A1030 7988 14354 11972 -200 220 1736 C
ATOM 1875 C LEU A1030 -0.836 11.953 4.172 1.00 93.83 C
ANISOU 1875 C LEU A1030 8398 14686 12568 -251 184 1752 C
ATOM 1876 O LEU A1030 -0.066 11.042 4.486 1.00 93.50 O
ANISOU 1876 O LEU A1030 8354 14623 12547 -262 208 1737 O
ATOM 1877 CB LEU A1030 -1.094 12.318 1.703 1.00 91.36 C
ANISOU 1877 CB LEU A1030 8082 14529 12101 -134 301 1867 C
ATOM 1878 CG LEU A1030 -1.670 11.884 0.354 1.00 96.62 C
ANISOU 1878 CG LEU A1030 8801 15309 12601 -68 351 1859 C
ATOM 1879 CD1 LEU A1030 -1.400 12.925 -0.707 1.00 97.79 C
ANISOU 1879 CD1 LEU A1030 8903 15494 12758 -2 418 2000 C
ATOM 1880 CD2 LEU A1030 -1.113 10.541 -0.087 1.00 99.08 C
ANISOU 1880 CD2 LEU A1030 9176 15651 12820 -36 401 1807 C
ATOM 1881 N THR A1031 -0.909 13.129 4.842 1.00 89.87 N
ANISOU 1881 N THR A1031 7876 14105 12167 -279 121 1784 N
ATOM 1882 CA THR A1031 -0.095 13.455 6.025 1.00 89.27 C
ANISOU 1882 CA THR A1031 7783 13903 12231 -332 58 1799 C
ATOM 1883 C THR A1031 -0.482 12.510 7.175 1.00 91.46 C
ANISOU 1883 C THR A1031 8115 14157 12480 -371 11 1668 C
ATOM 1884 O THR A1031 0.400 12.023 7.885 1.00 90.98 O
ANISOU 1884 O THR A1031 8043 14029 12497 -409 -10 1666 O
ATOM 1885 CB THR A1031 -0.253 14.939 6.413 1.00 98.07 C
ANISOU 1885 CB THR A1031 8895 14933 13435 -342 -10 1853 C
ATOM 1886 OG1 THR A1031 -0.159 15.753 5.242 1.00 98.49 O
ANISOU 1886 OG1 THR A1031 8892 15022 13509 -304 41 1978 O
ATOM 1887 CG2 THR A1031 0.789 15.395 7.435 1.00 97.07 C
ANISOU 1887 CG2 THR A1031 8764 14660 13457 -400 -97 1881 C
ATOM 1888 N LYS A1032 -1.798 12.228 7.320 1.00 86.83 N
ANISOU 1888 N LYS A1032 7579 13628 11786 -360 -4 1573 N
ATOM 1889 CA LYS A1032 -2.354 11.308 8.317 1.00 85.50 C
ANISOU 1889 CA LYS A1032 7454 13450 11583 -388 -42 1461 C
ATOM 1890 C LYS A1032 -1.884 9.872 8.037 1.00 88.34 C
ANISOU 1890 C LYS A1032 7813 13857 11894 -398 2 1417 C
ATOM 1891 O LYS A1032 -1.715 9.096 8.978 1.00 87.47 O
ANISOU 1891 O LYS A1032 7719 13708 11809 -432 -24 1355 O
ATOM 1892 CB LYS A1032 -3.896 11.375 8.329 1.00 87.52 C
ANISOU 1892 CB LYS A1032 7743 13761 11749 -367 -63 1405 C
ATOM 1893 CG LYS A1032 -4.495 12.621 8.990 1.00 98.27 C
ANISOU 1893 CG LYS A1032 9128 15058 13152 -346 -109 1429 C
ATOM 1894 CD LYS A1032 -4.707 12.461 10.500 1.00107.03 C
ANISOU 1894 CD LYS A1032 10292 16111 14262 -345 -160 1355 C
ATOM 1895 CE LYS A1032 -5.369 13.657 11.141 1.00117.39 C
ANISOU 1895 CE LYS A1032 11649 17377 15579 -297 -189 1376 C
ATOM 1896 NZ LYS A1032 -4.477 14.846 11.181 1.00126.22 N1+
ANISOU 1896 NZ LYS A1032 12790 18371 16797 -303 -236 1428 N1+
ATOM 1897 N MET A1033 -1.665 9.531 6.746 1.00 84.74 N
ANISOU 1897 N MET A1033 7350 13481 11367 -361 69 1451 N
ATOM 1898 CA MET A1033 -1.194 8.215 6.307 1.00 84.31 C
ANISOU 1898 CA MET A1033 7317 13465 11253 -353 117 1414 C
ATOM 1899 C MET A1033 0.307 8.059 6.540 1.00 87.79 C
ANISOU 1899 C MET A1033 7716 13845 11795 -358 155 1479 C
ATOM 1900 O MET A1033 0.742 6.980 6.945 1.00 86.91 O
ANISOU 1900 O MET A1033 7621 13725 11678 -371 171 1432 O
ATOM 1901 CB MET A1033 -1.515 7.957 4.826 1.00 87.23 C
ANISOU 1901 CB MET A1033 7717 13929 11497 -297 172 1432 C
ATOM 1902 CG MET A1033 -2.996 7.803 4.530 1.00 90.66 C
ANISOU 1902 CG MET A1033 8197 14430 11821 -304 124 1362 C
ATOM 1903 SD MET A1033 -3.361 6.725 3.123 1.00 95.46 S
ANISOU 1903 SD MET A1033 8885 15127 12257 -257 154 1332 S
ATOM 1904 CE MET A1033 -2.606 7.632 1.786 1.00 93.05 C
ANISOU 1904 CE MET A1033 8556 14857 11941 -177 238 1460 C
ATOM 1905 N ARG A1034 1.097 9.127 6.274 1.00 84.96 N
ANISOU 1905 N ARG A1034 7298 13446 11538 -348 169 1600 N
ATOM 1906 CA ARG A1034 2.552 9.126 6.467 1.00 85.34 C
ANISOU 1906 CA ARG A1034 7283 13434 11710 -355 199 1701 C
ATOM 1907 C ARG A1034 2.886 8.963 7.953 1.00 89.33 C
ANISOU 1907 C ARG A1034 7784 13840 12319 -428 116 1658 C
ATOM 1908 O ARG A1034 3.811 8.224 8.286 1.00 88.77 O
ANISOU 1908 O ARG A1034 7685 13741 12301 -442 140 1680 O
ATOM 1909 CB ARG A1034 3.193 10.407 5.908 1.00 85.78 C
ANISOU 1909 CB ARG A1034 7267 13465 11860 -335 215 1855 C
ATOM 1910 CG ARG A1034 4.661 10.231 5.524 1.00 95.31 C
ANISOU 1910 CG ARG A1034 8392 14654 13166 -312 287 2001 C
ATOM 1911 CD ARG A1034 5.358 11.551 5.250 1.00105.77 C
ANISOU 1911 CD ARG A1034 9629 15932 14626 -314 276 2169 C
ATOM 1912 NE ARG A1034 5.720 12.253 6.484 1.00112.84 N
ANISOU 1912 NE ARG A1034 10502 16698 15675 -404 148 2184 N
ATOM 1913 CZ ARG A1034 6.911 12.178 7.070 1.00126.25 C
ANISOU 1913 CZ ARG A1034 12131 18312 17525 -452 113 2279 C
ATOM 1914 NH1 ARG A1034 7.878 11.440 6.537 1.00113.47 N
ANISOU 1914 NH1 ARG A1034 10446 16731 15936 -414 211 2378 N
ATOM 1915 NH2 ARG A1034 7.147 12.847 8.190 1.00113.26 N1+
ANISOU 1915 NH2 ARG A1034 10490 16539 16004 -535 -26 2282 N1+
ATOM 1916 N ALA A1035 2.105 9.627 8.836 1.00 86.30 N
ANISOU 1916 N ALA A1035 7434 13403 11955 -465 23 1601 N
ATOM 1917 CA ALA A1035 2.241 9.562 10.295 1.00 86.11 C
ANISOU 1917 CA ALA A1035 7431 13282 12006 -523 -66 1549 C
ATOM 1918 C ALA A1035 1.882 8.167 10.829 1.00 90.17 C
ANISOU 1918 C ALA A1035 7984 13828 12447 -536 -58 1431 C
ATOM 1919 O ALA A1035 2.507 7.703 11.785 1.00 89.38 O
ANISOU 1919 O ALA A1035 7880 13664 12415 -577 -95 1414 O
ATOM 1920 CB ALA A1035 1.357 10.614 10.949 1.00 86.73 C
ANISOU 1920 CB ALA A1035 7560 13304 12090 -530 -152 1516 C
ATOM 1921 N ALA A1036 0.886 7.502 10.203 1.00 87.36 N
ANISOU 1921 N ALA A1036 7664 13567 11960 -504 -19 1357 N
ATOM 1922 CA ALA A1036 0.420 6.163 10.573 1.00 87.17 C
ANISOU 1922 CA ALA A1036 7676 13580 11866 -517 -15 1252 C
ATOM 1923 C ALA A1036 1.405 5.069 10.129 1.00 92.88 C
ANISOU 1923 C ALA A1036 8383 14319 12590 -508 54 1270 C
ATOM 1924 O ALA A1036 1.526 4.050 10.811 1.00 92.18 O
ANISOU 1924 O ALA A1036 8306 14212 12505 -535 45 1209 O
ATOM 1925 CB ALA A1036 -0.947 5.900 9.964 1.00 87.71 C
ANISOU 1925 CB ALA A1036 7782 13735 11808 -494 -12 1191 C
ATOM 1926 N ALA A1037 2.100 5.278 8.993 1.00 91.08 N
ANISOU 1926 N ALA A1037 8129 14124 12355 -461 129 1360 N
ATOM 1927 CA ALA A1037 3.062 4.325 8.436 1.00 91.69 C
ANISOU 1927 CA ALA A1037 8197 14219 12423 -425 216 1398 C
ATOM 1928 C ALA A1037 4.378 4.289 9.235 1.00 96.53 C
ANISOU 1928 C ALA A1037 8743 14752 13183 -459 213 1475 C
ATOM 1929 O ALA A1037 4.995 3.225 9.324 1.00 96.07 O
ANISOU 1929 O ALA A1037 8684 14692 13126 -450 260 1468 O
ATOM 1930 CB ALA A1037 3.350 4.671 6.986 1.00 93.32 C
ANISOU 1930 CB ALA A1037 8398 14485 12574 -347 303 1489 C
ATOM 1931 N LEU A1038 4.812 5.439 9.796 1.00 94.13 N
ANISOU 1931 N LEU A1038 8385 14376 13004 -499 149 1552 N
ATOM 1932 CA LEU A1038 6.050 5.553 10.581 1.00 94.73 C
ANISOU 1932 CA LEU A1038 8394 14363 13236 -547 114 1639 C
ATOM 1933 C LEU A1038 5.924 4.855 11.943 1.00 99.35 C
ANISOU 1933 C LEU A1038 9013 14896 13838 -607 39 1533 C
ATOM 1934 O LEU A1038 6.919 4.339 12.459 1.00 99.07 O
ANISOU 1934 O LEU A1038 8934 14812 13894 -638 35 1579 O
ATOM 1935 CB LEU A1038 6.438 7.030 10.789 1.00 95.26 C
ANISOU 1935 CB LEU A1038 8413 14355 13427 -580 40 1747 C
ATOM 1936 CG LEU A1038 6.885 7.822 9.553 1.00100.78 C
ANISOU 1936 CG LEU A1038 9043 15089 14160 -527 116 1902 C
ATOM 1937 CD1 LEU A1038 6.790 9.312 9.797 1.00101.25 C
ANISOU 1937 CD1 LEU A1038 9085 15082 14303 -559 28 1965 C
ATOM 1938 CD2 LEU A1038 8.295 7.445 9.117 1.00104.09 C
ANISOU 1938 CD2 LEU A1038 9365 15499 14686 -509 190 2058 C
ATOM 1939 N ASP A1039 4.707 4.858 12.522 1.00 96.31 N
ANISOU 1939 N ASP A1039 8701 14527 13364 -618 -13 1403 N
ATOM 1940 CA ASP A1039 4.400 4.225 13.807 1.00 95.97 C
ANISOU 1940 CA ASP A1039 8698 14451 13316 -659 -74 1299 C
ATOM 1941 C ASP A1039 4.251 2.712 13.635 1.00100.13 C
ANISOU 1941 C ASP A1039 9245 15041 13759 -642 -7 1225 C
ATOM 1942 O ASP A1039 4.603 1.958 14.548 1.00 99.31 O
ANISOU 1942 O ASP A1039 9150 14910 13674 -674 -34 1169 O
ATOM 1943 CB ASP A1039 3.126 4.835 14.415 1.00 97.58 C
ANISOU 1943 CB ASP A1039 8965 14648 13463 -661 -146 1216 C
ATOM 1944 CG ASP A1039 3.255 6.294 14.834 1.00109.77 C
ANISOU 1944 CG ASP A1039 10519 16105 15084 -677 -230 1269 C
ATOM 1945 OD1 ASP A1039 4.096 7.016 14.244 1.00111.54 O1-
ANISOU 1945 OD1 ASP A1039 10691 16293 15398 -684 -228 1383 O1-
ATOM 1946 OD2 ASP A1039 2.503 6.720 15.736 1.00115.29 O
ANISOU 1946 OD2 ASP A1039 11282 16770 15752 -675 -296 1203 O
ATOM 1947 N ALA A1040 3.761 2.272 12.458 1.00 97.35 N
ANISOU 1947 N ALA A1040 8908 14768 13311 -588 73 1224 N
ATOM 1948 CA ALA A1040 3.592 0.863 12.092 1.00 97.22 C
ANISOU 1948 CA ALA A1040 8933 14803 13202 -565 128 1154 C
ATOM 1949 C ALA A1040 4.954 0.174 11.889 1.00101.92 C
ANISOU 1949 C ALA A1040 9496 15379 13850 -544 204 1218 C
ATOM 1950 O ALA A1040 5.054 -1.044 12.065 1.00101.42 O
ANISOU 1950 O ALA A1040 9465 15321 13748 -544 225 1152 O
ATOM 1951 CB ALA A1040 2.757 0.751 10.825 1.00 98.29 C
ANISOU 1951 CB ALA A1040 9120 15017 13210 -512 168 1133 C
ATOM 1952 N GLN A1041 5.992 0.968 11.527 1.00 99.13 N
ANISOU 1952 N GLN A1041 9073 15001 13590 -523 246 1359 N
ATOM 1953 CA GLN A1041 7.374 0.546 11.277 1.00 99.51 C
ANISOU 1953 CA GLN A1041 9069 15035 13707 -491 332 1461 C
ATOM 1954 C GLN A1041 8.068 0.069 12.571 1.00102.63 C
ANISOU 1954 C GLN A1041 9407 15350 14238 -566 266 1482 C
ATOM 1955 O GLN A1041 8.848 -0.885 12.520 1.00102.61 O
ANISOU 1955 O GLN A1041 9352 15332 14305 -550 327 1567 O
ATOM 1956 CB GLN A1041 8.161 1.717 10.648 1.00101.92 C
ANISOU 1956 CB GLN A1041 9310 15356 14060 -431 407 1627 C
ATOM 1957 CG GLN A1041 9.507 1.318 10.044 1.00118.03 C
ANISOU 1957 CG GLN A1041 11231 17337 16277 -450 419 1801 C
ATOM 1958 CD GLN A1041 10.252 2.497 9.464 1.00138.45 C
ANISOU 1958 CD GLN A1041 13743 19938 18924 -403 472 1973 C
ATOM 1959 OE1 GLN A1041 10.547 3.490 10.143 1.00133.02 O
ANISOU 1959 OE1 GLN A1041 12985 19190 18368 -463 388 2064 O
ATOM 1960 NE2 GLN A1041 10.619 2.381 8.201 1.00133.17 N
ANISOU 1960 NE2 GLN A1041 13091 19342 18165 -290 610 2033 N
ATOM 1961 N LYS A1042 7.788 0.739 13.714 1.00 98.09 N
ANISOU 1961 N LYS A1042 8849 14729 13691 -637 147 1408 N
ATOM 1962 CA LYS A1042 8.359 0.424 15.032 1.00 97.37 C
ANISOU 1962 CA LYS A1042 8727 14559 13709 -707 68 1412 C
ATOM 1963 C LYS A1042 7.815 -0.925 15.545 1.00100.46 C
ANISOU 1963 C LYS A1042 9169 14969 14033 -719 69 1284 C
ATOM 1964 O LYS A1042 6.597 -1.099 15.653 1.00 99.34 O
ANISOU 1964 O LYS A1042 9092 14859 13793 -719 38 1167 O
ATOM 1965 CB LYS A1042 8.060 1.556 16.040 1.00 99.17 C
ANISOU 1965 CB LYS A1042 8970 14719 13993 -762 -62 1404 C
ATOM 1966 CG LYS A1042 8.651 2.904 15.641 1.00108.57 C
ANISOU 1966 CG LYS A1042 10104 15867 15283 -768 -87 1544 C
ATOM 1967 CD LYS A1042 8.140 4.031 16.518 1.00116.11 C
ANISOU 1967 CD LYS A1042 11107 16740 16270 -817 -226 1509 C
ATOM 1968 CE LYS A1042 8.611 5.368 16.011 1.00125.84 C
ANISOU 1968 CE LYS A1042 12295 17908 17612 -837 -281 1640 C
ATOM 1969 NZ LYS A1042 8.162 6.485 16.882 1.00133.95 N1+
ANISOU 1969 NZ LYS A1042 13398 18837 18659 -878 -427 1589 N1+
ATOM 1970 N ALA A1043 8.722 -1.887 15.815 1.00 97.11 N
ANISOU 1970 N ALA A1043 8706 14527 13665 -722 113 1322 N
ATOM 1971 CA ALA A1043 8.371 -3.229 16.282 1.00128.46 C
ANISOU 1971 CA ALA A1043 12710 18507 17591 -732 124 1223 C
ATOM 1972 C ALA A1043 9.126 -3.593 17.568 1.00163.06 C
ANISOU 1972 C ALA A1043 17038 22822 22097 -788 74 1268 C
ATOM 1973 O ALA A1043 10.350 -3.498 17.624 1.00128.58 O
ANISOU 1973 O ALA A1043 12593 18422 17841 -792 98 1404 O
ATOM 1974 CB ALA A1043 8.667 -4.255 15.193 1.00129.54 C
ANISOU 1974 CB ALA A1043 12873 18697 17650 -659 247 1219 C
ATOM 1975 N MET A1058 11.808 -12.782 7.356 1.00144.36 N1+
ANISOU 1975 N MET A1058 15539 20668 18642 331 1267 1239 N1+
ATOM 1976 CA MET A1058 12.172 -11.908 8.469 1.00143.20 C
ANISOU 1976 CA MET A1058 15184 20526 18698 205 1209 1326 C
ATOM 1977 C MET A1058 12.312 -10.452 7.983 1.00147.16 C
ANISOU 1977 C MET A1058 15586 21077 19251 216 1229 1458 C
ATOM 1978 O MET A1058 11.692 -9.557 8.563 1.00145.79 O
ANISOU 1978 O MET A1058 15338 20911 19144 96 1107 1427 O
ATOM 1979 CB MET A1058 13.477 -12.399 9.137 1.00145.76 C
ANISOU 1979 CB MET A1058 15404 20819 19159 221 1294 1441 C
ATOM 1980 CG MET A1058 13.827 -11.680 10.434 1.00148.45 C
ANISOU 1980 CG MET A1058 15552 21146 19705 79 1207 1515 C
ATOM 1981 SD MET A1058 12.701 -12.038 11.807 1.00150.97 S
ANISOU 1981 SD MET A1058 15871 21431 20061 -98 1019 1330 S
ATOM 1982 CE MET A1058 13.366 -10.960 13.051 1.00147.08 C
ANISOU 1982 CE MET A1058 15175 20921 19787 -214 947 1462 C
ATOM 1983 N LYS A1059 13.116 -10.226 6.919 1.00144.83 N
ANISOU 1983 N LYS A1059 15298 20813 18917 369 1385 1606 N
ATOM 1984 CA LYS A1059 13.370 -8.905 6.325 1.00144.83 C
ANISOU 1984 CA LYS A1059 15200 20860 18969 392 1416 1752 C
ATOM 1985 C LYS A1059 12.311 -8.551 5.245 1.00148.59 C
ANISOU 1985 C LYS A1059 15805 21376 19277 421 1373 1651 C
ATOM 1986 O LYS A1059 12.467 -7.548 4.541 1.00148.65 O
ANISOU 1986 O LYS A1059 15744 21424 19313 434 1385 1751 O
ATOM 1987 CB LYS A1059 14.796 -8.839 5.727 1.00148.61 C
ANISOU 1987 CB LYS A1059 15609 21362 19493 549 1609 1983 C
ATOM 1988 CG LYS A1059 15.087 -9.849 4.615 1.00160.96 C
ANISOU 1988 CG LYS A1059 17354 22940 20865 753 1769 1976 C
ATOM 1989 CD LYS A1059 16.511 -9.715 4.083 1.00170.05 C
ANISOU 1989 CD LYS A1059 18406 24117 22090 910 1971 2235 C
ATOM 1990 CE LYS A1059 16.830 -10.718 2.997 1.00179.76 C
ANISOU 1990 CE LYS A1059 19825 25351 23126 1135 2147 2238 C
ATOM 1991 NZ LYS A1059 16.893 -12.113 3.512 1.00187.34 N1+
ANISOU 1991 NZ LYS A1059 20876 26250 24056 1136 2149 2128 N1+
ATOM 1992 N ASP A1060 11.234 -9.361 5.140 1.00144.36 N
ANISOU 1992 N ASP A1060 15447 20826 18579 419 1307 1459 N
ATOM 1993 CA ASP A1060 10.149 -9.185 4.171 1.00143.99 C
ANISOU 1993 CA ASP A1060 15541 20810 18360 442 1249 1351 C
ATOM 1994 C ASP A1060 9.194 -8.049 4.582 1.00145.47 C
ANISOU 1994 C ASP A1060 15647 21018 18608 293 1096 1297 C
ATOM 1995 O ASP A1060 8.767 -7.284 3.713 1.00145.35 O
ANISOU 1995 O ASP A1060 15683 21045 18498 323 1078 1289 O
ATOM 1996 CB ASP A1060 9.358 -10.496 3.994 1.00146.07 C
ANISOU 1996 CB ASP A1060 16012 21032 18455 464 1198 1171 C
ATOM 1997 CG ASP A1060 10.175 -11.663 3.464 1.00156.77 C
ANISOU 1997 CG ASP A1060 17482 22353 19730 616 1339 1199 C
ATOM 1998 OD1 ASP A1060 10.731 -11.544 2.345 1.00158.52 O1-
ANISOU 1998 OD1 ASP A1060 17765 22604 19863 787 1488 1307 O1-
ATOM 1999 OD2 ASP A1060 10.225 -12.708 4.145 1.00162.07 O
ANISOU 1999 OD2 ASP A1060 18187 22967 20425 573 1306 1116 O
ATOM 2000 N PHE A1061 8.859 -7.940 5.886 1.00139.81 N
ANISOU 2000 N PHE A1061 14816 20271 18035 146 990 1262 N
ATOM 2001 CA PHE A1061 7.953 -6.908 6.399 1.00138.11 C
ANISOU 2001 CA PHE A1061 14530 20070 17874 24 859 1221 C
ATOM 2002 C PHE A1061 8.711 -5.628 6.770 1.00140.45 C
ANISOU 2002 C PHE A1061 14656 20367 18343 -11 874 1376 C
ATOM 2003 O PHE A1061 8.147 -4.541 6.643 1.00139.47 O
ANISOU 2003 O PHE A1061 14485 20260 18248 -68 800 1381 O
ATOM 2004 CB PHE A1061 7.161 -7.418 7.615 1.00138.77 C
ANISOU 2004 CB PHE A1061 14618 20121 17988 -103 726 1080 C
ATOM 2005 CG PHE A1061 5.859 -6.686 7.849 1.00139.60 C
ANISOU 2005 CG PHE A1061 14720 20248 18071 -194 595 999 C
ATOM 2006 CD1 PHE A1061 4.690 -7.086 7.208 1.00142.93 C
ANISOU 2006 CD1 PHE A1061 15266 20693 18347 -186 537 893 C
ATOM 2007 CD2 PHE A1061 5.797 -5.604 8.719 1.00140.90 C
ANISOU 2007 CD2 PHE A1061 14766 20405 18364 -285 525 1030 C
ATOM 2008 CE1 PHE A1061 3.486 -6.412 7.427 1.00143.19 C
ANISOU 2008 CE1 PHE A1061 15282 20752 18372 -268 421 836 C
ATOM 2009 CE2 PHE A1061 4.590 -4.927 8.935 1.00143.04 C
ANISOU 2009 CE2 PHE A1061 15039 20698 18613 -353 417 963 C
ATOM 2010 CZ PHE A1061 3.444 -5.337 8.289 1.00141.35 C
ANISOU 2010 CZ PHE A1061 14927 20517 18263 -343 372 874 C
ATOM 2011 N ARG A1062 9.979 -5.757 7.233 1.00136.57 N
ANISOU 2011 N ARG A1062 14074 19853 17963 29 968 1514 N
ATOM 2012 CA ARG A1062 10.854 -4.641 7.628 1.00135.94 C
ANISOU 2012 CA ARG A1062 13827 19758 18064 -14 966 1680 C
ATOM 2013 C ARG A1062 11.152 -3.726 6.421 1.00139.61 C
ANISOU 2013 C ARG A1062 14263 20272 18510 74 1044 1817 C
ATOM 2014 O ARG A1062 11.233 -2.506 6.582 1.00138.90 O
ANISOU 2014 O ARG A1062 14061 20172 18544 16 993 1915 O
ATOM 2015 CB ARG A1062 12.165 -5.175 8.240 1.00136.43 C
ANISOU 2015 CB ARG A1062 13797 19783 18256 1 1038 1801 C
ATOM 2016 CG ARG A1062 13.030 -4.138 8.967 1.00146.20 C
ANISOU 2016 CG ARG A1062 14858 20981 19710 -85 985 1956 C
ATOM 2017 CD ARG A1062 12.488 -3.769 10.340 1.00153.93 C
ANISOU 2017 CD ARG A1062 15812 21910 20765 -241 810 1847 C
ATOM 2018 NE ARG A1062 13.321 -2.772 11.017 1.00161.54 N
ANISOU 2018 NE ARG A1062 16634 22822 21922 -321 739 1992 N
ATOM 2019 CZ ARG A1062 13.136 -1.457 10.941 1.00174.83 C
ANISOU 2019 CZ ARG A1062 18271 24497 23661 -355 677 2056 C
ATOM 2020 NH1 ARG A1062 12.145 -0.959 10.210 1.00161.80 N
ANISOU 2020 NH1 ARG A1062 16694 22897 21886 -312 688 1993 N
ATOM 2021 NH2 ARG A1062 13.941 -0.629 11.592 1.00161.40 N1+
ANISOU 2021 NH2 ARG A1062 16452 22731 22141 -434 594 2189 N1+
ATOM 2022 N HIS A1063 11.291 -4.323 5.218 1.00136.46 N
ANISOU 2022 N HIS A1063 13977 19918 17952 218 1162 1821 N
ATOM 2023 CA HIS A1063 11.546 -3.627 3.956 1.00137.03 C
ANISOU 2023 CA HIS A1063 14051 20047 17967 336 1264 1948 C
ATOM 2024 C HIS A1063 10.297 -3.658 3.038 1.00139.51 C
ANISOU 2024 C HIS A1063 14525 20403 18078 372 1227 1805 C
ATOM 2025 O HIS A1063 10.411 -3.440 1.829 1.00140.22 O
ANISOU 2025 O HIS A1063 14678 20544 18055 501 1324 1871 O
ATOM 2026 CB HIS A1063 12.762 -4.246 3.240 1.00139.41 C
ANISOU 2026 CB HIS A1063 14363 20367 18241 508 1457 2098 C
ATOM 2027 CG HIS A1063 14.055 -4.083 3.973 1.00143.20 C
ANISOU 2027 CG HIS A1063 14665 20814 18928 488 1509 2284 C
ATOM 2028 ND1 HIS A1063 14.880 -2.997 3.746 1.00145.63 N
ANISOU 2028 ND1 HIS A1063 14803 21132 19397 487 1541 2504 N
ATOM 2029 CD2 HIS A1063 14.637 -4.891 4.888 1.00144.88 C
ANISOU 2029 CD2 HIS A1063 14851 20986 19212 475 1535 2292 C
ATOM 2030 CE1 HIS A1063 15.926 -3.168 4.539 1.00145.33 C
ANISOU 2030 CE1 HIS A1063 14635 21056 19527 464 1573 2640 C
ATOM 2031 NE2 HIS A1063 15.824 -4.295 5.246 1.00145.22 N
ANISOU 2031 NE2 HIS A1063 14701 21013 19462 458 1575 2518 N
ATOM 2032 N GLY A1064 9.129 -3.900 3.632 1.00133.83 N
ANISOU 2032 N GLY A1064 13875 19663 17311 263 1088 1618 N
ATOM 2033 CA GLY A1064 7.857 -3.968 2.922 1.00133.07 C
ANISOU 2033 CA GLY A1064 13924 19598 17037 270 1021 1477 C
ATOM 2034 C GLY A1064 6.975 -2.747 3.094 1.00134.73 C
ANISOU 2034 C GLY A1064 14077 19832 17283 176 910 1456 C
ATOM 2035 O GLY A1064 6.394 -2.261 2.119 1.00134.62 O
ANISOU 2035 O GLY A1064 14139 19865 17146 220 901 1433 O
ATOM 2036 N PHE A1065 6.863 -2.252 4.340 1.00129.18 N
ANISOU 2036 N PHE A1065 13249 19092 16742 52 823 1463 N
ATOM 2037 CA PHE A1065 6.047 -1.091 4.704 1.00127.68 C
ANISOU 2037 CA PHE A1065 13006 18911 16597 -35 717 1445 C
ATOM 2038 C PHE A1065 6.684 0.227 4.247 1.00130.58 C
ANISOU 2038 C PHE A1065 13267 19292 17055 -4 766 1612 C
ATOM 2039 O PHE A1065 5.950 1.179 3.978 1.00129.84 O
ANISOU 2039 O PHE A1065 13164 19222 16948 -31 710 1607 O
ATOM 2040 CB PHE A1065 5.811 -1.054 6.218 1.00128.28 C
ANISOU 2040 CB PHE A1065 13020 18932 16789 -165 603 1376 C
ATOM 2041 N ASP A1066 8.036 0.284 4.151 1.00126.85 N
ANISOU 2041 N ASP A1066 12712 18806 16680 55 871 1772 N
ATOM 2042 CA ASP A1066 8.774 1.486 3.735 1.00126.75 C
ANISOU 2042 CA ASP A1066 12580 18800 16780 83 918 1961 C
ATOM 2043 C ASP A1066 8.525 1.819 2.250 1.00129.71 C
ANISOU 2043 C ASP A1066 13015 19252 17017 204 1006 2013 C
ATOM 2044 O ASP A1066 8.713 2.970 1.851 1.00129.60 O
ANISOU 2044 O ASP A1066 12917 19252 17074 210 1013 2136 O
ATOM 2045 CB ASP A1066 10.289 1.347 4.008 1.00129.33 C
ANISOU 2045 CB ASP A1066 12787 19093 17261 112 1003 2140 C
ATOM 2046 CG ASP A1066 11.020 0.191 3.341 1.00140.39 C
ANISOU 2046 CG ASP A1066 14241 20523 18577 250 1161 2192 C
ATOM 2047 OD1 ASP A1066 10.399 -0.517 2.516 1.00141.39 O
ANISOU 2047 OD1 ASP A1066 14517 20697 18506 346 1216 2097 O
ATOM 2048 OD2 ASP A1066 12.221 0.004 3.634 1.00146.65 O1-
ANISOU 2048 OD2 ASP A1066 14930 21288 19501 269 1229 2338 O1-
ATOM 2049 N ILE A1067 8.093 0.817 1.448 1.00125.38 N
ANISOU 2049 N ILE A1067 12620 18746 16273 299 1064 1918 N
ATOM 2050 CA ILE A1067 7.757 0.983 0.029 1.00125.63 C
ANISOU 2050 CA ILE A1067 12746 18849 16138 424 1139 1943 C
ATOM 2051 C ILE A1067 6.527 1.901 -0.060 1.00127.36 C
ANISOU 2051 C ILE A1067 12971 19094 16327 348 1023 1874 C
ATOM 2052 O ILE A1067 6.499 2.811 -0.892 1.00127.57 O
ANISOU 2052 O ILE A1067 12965 19165 16340 403 1064 1977 O
ATOM 2053 CB ILE A1067 7.527 -0.379 -0.698 1.00129.42 C
ANISOU 2053 CB ILE A1067 13423 19347 16406 528 1191 1828 C
ATOM 2054 CG1 ILE A1067 8.606 -1.430 -0.328 1.00130.40 C
ANISOU 2054 CG1 ILE A1067 13549 19433 16563 592 1293 1871 C
ATOM 2055 CG2 ILE A1067 7.426 -0.176 -2.225 1.00131.44 C
ANISOU 2055 CG2 ILE A1067 13792 19672 16478 676 1273 1867 C
ATOM 2056 CD1 ILE A1067 8.263 -2.900 -0.701 1.00138.71 C
ANISOU 2056 CD1 ILE A1067 14808 20469 17426 655 1298 1712 C
ATOM 2057 N LEU A1068 5.537 1.677 0.839 1.00121.41 N
ANISOU 2057 N LEU A1068 12250 18310 15569 226 884 1712 N
ATOM 2058 CA LEU A1068 4.302 2.460 0.955 1.00119.80 C
ANISOU 2058 CA LEU A1068 12050 18125 15344 147 768 1638 C
ATOM 2059 C LEU A1068 4.609 3.891 1.392 1.00121.35 C
ANISOU 2059 C LEU A1068 12103 18299 15707 91 739 1752 C
ATOM 2060 O LEU A1068 3.957 4.818 0.912 1.00121.05 O
ANISOU 2060 O LEU A1068 12058 18295 15640 88 706 1766 O
ATOM 2061 CB LEU A1068 3.307 1.812 1.941 1.00118.76 C
ANISOU 2061 CB LEU A1068 11965 17963 15195 38 642 1469 C
ATOM 2062 CG LEU A1068 2.604 0.533 1.484 1.00123.79 C
ANISOU 2062 CG LEU A1068 12758 18619 15659 67 619 1337 C
ATOM 2063 CD1 LEU A1068 3.352 -0.706 1.956 1.00123.99 C
ANISOU 2063 CD1 LEU A1068 12818 18596 15695 79 658 1297 C
ATOM 2064 CD2 LEU A1068 1.193 0.479 2.027 1.00125.50 C
ANISOU 2064 CD2 LEU A1068 13002 18840 15842 -33 479 1214 C
ATOM 2065 N VAL A1069 5.616 4.066 2.281 1.00115.92 N
ANISOU 2065 N VAL A1069 11305 17546 15193 45 744 1834 N
ATOM 2066 CA VAL A1069 6.072 5.365 2.799 1.00114.81 C
ANISOU 2066 CA VAL A1069 11035 17358 15230 -17 698 1949 C
ATOM 2067 C VAL A1069 6.600 6.215 1.621 1.00117.49 C
ANISOU 2067 C VAL A1069 11321 17742 15576 74 792 2119 C
ATOM 2068 O VAL A1069 6.290 7.405 1.536 1.00117.24 O
ANISOU 2068 O VAL A1069 11244 17710 15594 46 744 2166 O
ATOM 2069 CB VAL A1069 7.135 5.205 3.928 1.00118.62 C
ANISOU 2069 CB VAL A1069 11424 17755 15891 -83 673 2010 C
ATOM 2070 CG1 VAL A1069 7.596 6.561 4.467 1.00118.43 C
ANISOU 2070 CG1 VAL A1069 11290 17662 16044 -158 593 2115 C
ATOM 2071 CG2 VAL A1069 6.607 4.338 5.068 1.00117.43 C
ANISOU 2071 CG2 VAL A1069 11331 17568 15721 -160 594 1846 C
ATOM 2072 N GLY A1070 7.347 5.578 0.718 1.00112.87 N
ANISOU 2072 N GLY A1070 10749 17199 14937 193 930 2211 N
ATOM 2073 CA GLY A1070 7.893 6.211 -0.475 1.00112.88 C
ANISOU 2073 CA GLY A1070 10707 17256 14926 309 1047 2386 C
ATOM 2074 C GLY A1070 6.815 6.625 -1.456 1.00114.16 C
ANISOU 2074 C GLY A1070 10959 17492 14926 359 1043 2330 C
ATOM 2075 O GLY A1070 6.845 7.748 -1.963 1.00114.12 O
ANISOU 2075 O GLY A1070 10882 17509 14971 378 1057 2450 O
ATOM 2076 N GLN A1071 5.835 5.725 -1.700 1.00108.42 N
ANISOU 2076 N GLN A1071 10385 16798 14013 370 1009 2152 N
ATOM 2077 CA GLN A1071 4.703 5.933 -2.614 1.00107.59 C
ANISOU 2077 CA GLN A1071 10383 16761 13736 408 984 2080 C
ATOM 2078 C GLN A1071 3.767 7.057 -2.125 1.00108.76 C
ANISOU 2078 C GLN A1071 10471 16899 13954 302 864 2051 C
ATOM 2079 O GLN A1071 3.211 7.771 -2.961 1.00108.65 O
ANISOU 2079 O GLN A1071 10468 16941 13871 344 872 2092 O
ATOM 2080 CB GLN A1071 3.904 4.632 -2.805 1.00108.68 C
ANISOU 2080 CB GLN A1071 10693 16913 13687 420 944 1898 C
ATOM 2081 CG GLN A1071 4.639 3.574 -3.634 1.00121.97 C
ANISOU 2081 CG GLN A1071 12486 18619 15239 567 1073 1925 C
ATOM 2082 CD GLN A1071 3.888 2.268 -3.799 1.00139.13 C
ANISOU 2082 CD GLN A1071 14842 20785 17238 571 1016 1743 C
ATOM 2083 OE1 GLN A1071 2.803 2.045 -3.246 1.00133.27 O
ANISOU 2083 OE1 GLN A1071 14125 20016 16498 450 879 1602 O
ATOM 2084 NE2 GLN A1071 4.459 1.364 -4.580 1.00132.09 N
ANISOU 2084 NE2 GLN A1071 14079 19906 16204 714 1123 1755 N
ATOM 2085 N ILE A1072 3.603 7.216 -0.789 1.00102.90 N
ANISOU 2085 N ILE A1072 9671 16085 13340 176 760 1988 N
ATOM 2086 CA ILE A1072 2.775 8.267 -0.177 1.00101.36 C
ANISOU 2086 CA ILE A1072 9426 15865 13219 85 652 1964 C
ATOM 2087 C ILE A1072 3.517 9.619 -0.307 1.00105.03 C
ANISOU 2087 C ILE A1072 9766 16304 13838 93 682 2143 C
ATOM 2088 O ILE A1072 2.901 10.608 -0.712 1.00104.65 O
ANISOU 2088 O ILE A1072 9697 16276 13790 90 652 2176 O
ATOM 2089 CB ILE A1072 2.399 7.921 1.303 1.00103.00 C
ANISOU 2089 CB ILE A1072 9633 16003 13501 -30 541 1841 C
ATOM 2090 CG1 ILE A1072 1.360 6.774 1.348 1.00102.70 C
ANISOU 2090 CG1 ILE A1072 9708 15998 13313 -46 495 1676 C
ATOM 2091 CG2 ILE A1072 1.867 9.154 2.070 1.00103.09 C
ANISOU 2091 CG2 ILE A1072 9588 15968 13611 -105 445 1845 C
ATOM 2092 CD1 ILE A1072 1.220 6.043 2.703 1.00107.34 C
ANISOU 2092 CD1 ILE A1072 10301 16527 13958 -132 420 1567 C
ATOM 2093 N ASP A1073 4.837 9.646 0.001 1.00101.60 N
ANISOU 2093 N ASP A1073 9244 15821 13539 103 737 2269 N
ATOM 2094 CA ASP A1073 5.686 10.841 -0.091 1.00101.87 C
ANISOU 2094 CA ASP A1073 9145 15817 13742 105 759 2466 C
ATOM 2095 C ASP A1073 5.742 11.382 -1.523 1.00106.04 C
ANISOU 2095 C ASP A1073 9662 16432 14196 219 862 2591 C
ATOM 2096 O ASP A1073 5.763 12.600 -1.702 1.00105.79 O
ANISOU 2096 O ASP A1073 9553 16384 14260 201 836 2697 O
ATOM 2097 CB ASP A1073 7.103 10.552 0.417 1.00104.18 C
ANISOU 2097 CB ASP A1073 9348 16055 14180 103 806 2589 C
ATOM 2098 CG ASP A1073 7.296 10.914 1.875 1.00114.48 C
ANISOU 2098 CG ASP A1073 10598 17242 15657 -30 675 2563 C
ATOM 2099 OD1 ASP A1073 7.186 10.010 2.731 1.00114.33 O1-
ANISOU 2099 OD1 ASP A1073 10644 17197 15600 -82 622 2413 O1-
ATOM 2100 OD2 ASP A1073 7.542 12.105 2.163 1.00121.00 O
ANISOU 2100 OD2 ASP A1073 11322 17997 16655 -81 619 2696 O
ATOM 2101 N ASP A1074 5.732 10.485 -2.533 1.00102.86 N
ANISOU 2101 N ASP A1074 9348 16115 13617 338 974 2576 N
ATOM 2102 CA ASP A1074 5.733 10.852 -3.951 1.00103.73 C
ANISOU 2102 CA ASP A1074 9475 16317 13619 467 1080 2683 C
ATOM 2103 C ASP A1074 4.360 11.405 -4.359 1.00106.49 C
ANISOU 2103 C ASP A1074 9891 16712 13858 444 1005 2585 C
ATOM 2104 O ASP A1074 4.294 12.316 -5.187 1.00106.82 O
ANISOU 2104 O ASP A1074 9893 16801 13891 501 1048 2699 O
ATOM 2105 CB ASP A1074 6.125 9.655 -4.838 1.00106.60 C
ANISOU 2105 CB ASP A1074 9950 16746 13806 610 1211 2674 C
ATOM 2106 CG ASP A1074 7.576 9.210 -4.723 1.00118.31 C
ANISOU 2106 CG ASP A1074 11359 18203 15390 670 1323 2815 C
ATOM 2107 OD1 ASP A1074 8.466 10.088 -4.593 1.00119.26 O
ANISOU 2107 OD1 ASP A1074 11317 18293 15704 659 1354 3013 O
ATOM 2108 OD2 ASP A1074 7.831 7.991 -4.828 1.00124.83 O1-
ANISOU 2108 OD2 ASP A1074 12289 19040 16101 736 1382 2741 O1-
ATOM 2109 N ALA A1075 3.273 10.870 -3.760 1.00101.28 N
ANISOU 2109 N ALA A1075 9321 16039 13124 360 893 2389 N
ATOM 2110 CA ALA A1075 1.901 11.325 -4.000 1.00100.33 C
ANISOU 2110 CA ALA A1075 9253 15956 12910 326 809 2297 C
ATOM 2111 C ALA A1075 1.654 12.675 -3.315 1.00103.16 C
ANISOU 2111 C ALA A1075 9506 16259 13430 242 732 2351 C
ATOM 2112 O ALA A1075 0.837 13.464 -3.795 1.00102.86 O
ANISOU 2112 O ALA A1075 9469 16263 13351 250 708 2366 O
ATOM 2113 CB ALA A1075 0.908 10.291 -3.495 1.00100.11 C
ANISOU 2113 CB ALA A1075 9334 15926 12777 263 717 2099 C
ATOM 2114 N LEU A1076 2.373 12.933 -2.199 1.00 98.72 N
ANISOU 2114 N LEU A1076 8863 15597 13048 164 687 2380 N
ATOM 2115 CA LEU A1076 2.299 14.169 -1.417 1.00 97.94 C
ANISOU 2115 CA LEU A1076 8684 15415 13111 84 601 2427 C
ATOM 2116 C LEU A1076 2.933 15.333 -2.190 1.00102.96 C
ANISOU 2116 C LEU A1076 9221 16058 13842 134 659 2628 C
ATOM 2117 O LEU A1076 2.390 16.437 -2.164 1.00102.39 O
ANISOU 2117 O LEU A1076 9118 15961 13825 105 604 2660 O
ATOM 2118 CB LEU A1076 2.990 13.977 -0.052 1.00 97.28 C
ANISOU 2118 CB LEU A1076 8564 15218 13181 -6 532 2405 C
ATOM 2119 CG LEU A1076 2.851 15.105 0.982 1.00101.46 C
ANISOU 2119 CG LEU A1076 9052 15635 13861 -94 414 2416 C
ATOM 2120 CD1 LEU A1076 1.440 15.174 1.550 1.00100.56 C
ANISOU 2120 CD1 LEU A1076 9024 15521 13665 -136 327 2252 C
ATOM 2121 CD2 LEU A1076 3.834 14.916 2.119 1.00103.77 C
ANISOU 2121 CD2 LEU A1076 9295 15815 14317 -164 360 2452 C
ATOM 2122 N LYS A1077 4.067 15.077 -2.887 1.00100.87 N
ANISOU 2122 N LYS A1077 8904 15826 13597 216 776 2770 N
ATOM 2123 CA LYS A1077 4.796 16.061 -3.703 1.00102.09 C
ANISOU 2123 CA LYS A1077 8949 15997 13844 279 853 2991 C
ATOM 2124 C LYS A1077 3.950 16.544 -4.894 1.00106.37 C
ANISOU 2124 C LYS A1077 9531 16640 14245 358 897 3005 C
ATOM 2125 O LYS A1077 4.102 17.692 -5.314 1.00106.65 O
ANISOU 2125 O LYS A1077 9481 16667 14375 365 900 3143 O
ATOM 2126 CB LYS A1077 6.126 15.482 -4.218 1.00105.80 C
ANISOU 2126 CB LYS A1077 9364 16496 14340 372 988 3141 C
ATOM 2127 CG LYS A1077 7.189 15.267 -3.146 1.00122.52 C
ANISOU 2127 CG LYS A1077 11395 18509 16648 295 949 3199 C
ATOM 2128 CD LYS A1077 8.413 14.552 -3.718 1.00135.05 C
ANISOU 2128 CD LYS A1077 12931 20139 18244 402 1099 3350 C
ATOM 2129 CE LYS A1077 9.443 14.219 -2.665 1.00145.52 C
ANISOU 2129 CE LYS A1077 14165 21364 19760 322 1056 3415 C
ATOM 2130 NZ LYS A1077 10.599 13.480 -3.241 1.00155.24 N1+
ANISOU 2130 NZ LYS A1077 15346 22643 20997 437 1215 3570 N1+
ATOM 2131 N LEU A1078 3.067 15.668 -5.430 1.00102.35 N
ANISOU 2131 N LEU A1078 9154 16219 13514 412 921 2865 N
ATOM 2132 CA LEU A1078 2.174 15.966 -6.557 1.00102.39 C
ANISOU 2132 CA LEU A1078 9219 16325 13358 483 949 2858 C
ATOM 2133 C LEU A1078 1.079 16.953 -6.149 1.00105.15 C
ANISOU 2133 C LEU A1078 9556 16649 13747 398 834 2800 C
ATOM 2134 O LEU A1078 0.704 17.809 -6.952 1.00105.25 O
ANISOU 2134 O LEU A1078 9544 16713 13733 441 856 2882 O
ATOM 2135 CB LEU A1078 1.538 14.677 -7.115 1.00102.41 C
ANISOU 2135 CB LEU A1078 9382 16406 13124 542 968 2711 C
ATOM 2136 CG LEU A1078 2.475 13.679 -7.815 1.00108.12 C
ANISOU 2136 CG LEU A1078 10157 17171 13751 668 1102 2766 C
ATOM 2137 CD1 LEU A1078 1.854 12.303 -7.877 1.00107.89 C
ANISOU 2137 CD1 LEU A1078 10292 17161 13540 675 1070 2579 C
ATOM 2138 CD2 LEU A1078 2.860 14.150 -9.213 1.00111.97 C
ANISOU 2138 CD2 LEU A1078 10646 17751 14145 817 1226 2920 C
ATOM 2139 N ALA A1079 0.576 16.835 -4.903 1.00100.42 N
ANISOU 2139 N ALA A1079 8976 15972 13207 287 721 2667 N
ATOM 2140 CA ALA A1079 -0.463 17.705 -4.344 1.00 99.48 C
ANISOU 2140 CA ALA A1079 8855 15817 13126 215 618 2607 C
ATOM 2141 C ALA A1079 0.091 19.100 -4.016 1.00103.43 C
ANISOU 2141 C ALA A1079 9248 16230 13822 184 592 2747 C
ATOM 2142 O ALA A1079 -0.634 20.089 -4.149 1.00102.60 O
ANISOU 2142 O ALA A1079 9132 16124 13728 175 552 2764 O
ATOM 2143 CB ALA A1079 -1.057 17.074 -3.095 1.00 99.02 C
ANISOU 2143 CB ALA A1079 8854 15701 13068 127 522 2439 C
ATOM 2144 N ASN A1080 1.372 19.173 -3.594 1.00100.64 N
ANISOU 2144 N ASN A1080 8815 15798 13627 165 607 2855 N
ATOM 2145 CA ASN A1080 2.060 20.418 -3.244 1.00101.09 C
ANISOU 2145 CA ASN A1080 8769 15751 13891 124 564 3003 C
ATOM 2146 C ASN A1080 2.312 21.282 -4.487 1.00106.15 C
ANISOU 2146 C ASN A1080 9334 16456 14544 204 645 3183 C
ATOM 2147 O ASN A1080 2.324 22.510 -4.378 1.00106.18 O
ANISOU 2147 O ASN A1080 9279 16392 14674 172 591 3273 O
ATOM 2148 CB ASN A1080 3.379 20.122 -2.526 1.00102.53 C
ANISOU 2148 CB ASN A1080 8880 15840 14236 80 553 3085 C
ATOM 2149 CG ASN A1080 3.224 19.424 -1.191 1.00126.22 C
ANISOU 2149 CG ASN A1080 11943 18755 17260 -8 456 2928 C
ATOM 2150 OD1 ASN A1080 2.451 19.837 -0.318 1.00119.01 O
ANISOU 2150 OD1 ASN A1080 11084 17769 16364 -73 346 2820 O
ATOM 2151 ND2 ASN A1080 4.006 18.379 -0.980 1.00119.57 N
ANISOU 2151 ND2 ASN A1080 11092 17914 16425 -6 497 2925 N
ATOM 2152 N GLU A1081 2.501 20.642 -5.659 1.00103.26 N
ANISOU 2152 N GLU A1081 8978 16215 14042 313 774 3236 N
ATOM 2153 CA GLU A1081 2.719 21.316 -6.940 1.00104.29 C
ANISOU 2153 CA GLU A1081 9046 16426 14152 412 873 3409 C
ATOM 2154 C GLU A1081 1.418 21.952 -7.448 1.00108.78 C
ANISOU 2154 C GLU A1081 9665 17054 14614 422 840 3350 C
ATOM 2155 O GLU A1081 1.445 23.065 -7.977 1.00108.86 O
ANISOU 2155 O GLU A1081 9599 17065 14699 444 853 3488 O
ATOM 2156 CB GLU A1081 3.274 20.337 -7.988 1.00106.33 C
ANISOU 2156 CB GLU A1081 9336 16800 14264 543 1021 3462 C
ATOM 2157 CG GLU A1081 4.725 19.944 -7.764 1.00115.33 C
ANISOU 2157 CG GLU A1081 10397 17899 15522 563 1089 3586 C
ATOM 2158 CD GLU A1081 5.286 18.928 -8.741 1.00127.96 C
ANISOU 2158 CD GLU A1081 12056 19606 16958 708 1242 3619 C
ATOM 2159 OE1 GLU A1081 5.744 17.858 -8.280 1.00116.65 O
ANISOU 2159 OE1 GLU A1081 10672 18152 15499 701 1255 3539 O
ATOM 2160 OE2 GLU A1081 5.281 19.203 -9.963 1.00118.51 O1-
ANISOU 2160 OE2 GLU A1081 10867 18510 15651 835 1350 3722 O1-
ATOM 2161 N GLY A1082 0.305 21.239 -7.271 1.00105.34 N
ANISOU 2161 N GLY A1082 9348 16665 14013 405 795 3157 N
ATOM 2162 CA GLY A1082 -1.025 21.672 -7.691 1.00105.42 C
ANISOU 2162 CA GLY A1082 9407 16737 13908 411 757 3093 C
ATOM 2163 C GLY A1082 -1.788 20.632 -8.489 1.00109.88 C
ANISOU 2163 C GLY A1082 10090 17421 14237 465 782 2977 C
ATOM 2164 O GLY A1082 -2.937 20.868 -8.879 1.00108.92 O
ANISOU 2164 O GLY A1082 10019 17351 14015 453 730 2903 O
ATOM 2165 N LYS A1083 -1.145 19.471 -8.732 1.00107.40 N
ANISOU 2165 N LYS A1083 9826 17147 13835 526 857 2968 N
ATOM 2166 CA LYS A1083 -1.697 18.346 -9.489 1.00107.63 C
ANISOU 2166 CA LYS A1083 9991 17270 13635 584 873 2858 C
ATOM 2167 C LYS A1083 -2.532 17.462 -8.556 1.00111.19 C
ANISOU 2167 C LYS A1083 10520 17684 14041 486 762 2660 C
ATOM 2168 O LYS A1083 -2.004 16.548 -7.919 1.00110.15 O
ANISOU 2168 O LYS A1083 10411 17499 13943 454 756 2591 O
ATOM 2169 CB LYS A1083 -0.567 17.545 -10.173 1.00110.88 C
ANISOU 2169 CB LYS A1083 10438 17717 13974 695 997 2922 C
ATOM 2170 CG LYS A1083 0.240 18.355 -11.187 1.00123.99 C
ANISOU 2170 CG LYS A1083 12020 19429 15660 813 1124 3136 C
ATOM 2171 CD LYS A1083 1.386 17.556 -11.785 1.00132.31 C
ANISOU 2171 CD LYS A1083 13100 20510 16663 933 1260 3217 C
ATOM 2172 CE LYS A1083 2.175 18.377 -12.775 1.00141.24 C
ANISOU 2172 CE LYS A1083 14137 21695 17832 1060 1397 3455 C
ATOM 2173 NZ LYS A1083 3.287 17.596 -13.376 1.00149.60 N1+
ANISOU 2173 NZ LYS A1083 15215 22783 18843 1195 1546 3554 N1+
ATOM 2174 N VAL A1084 -3.838 17.770 -8.455 1.00108.29 N
ANISOU 2174 N VAL A1084 10184 17348 13612 440 675 2584 N
ATOM 2175 CA VAL A1084 -4.801 17.055 -7.602 1.00107.58 C
ANISOU 2175 CA VAL A1084 10153 17236 13489 351 568 2422 C
ATOM 2176 C VAL A1084 -5.154 15.709 -8.255 1.00112.23 C
ANISOU 2176 C VAL A1084 10874 17886 13882 381 554 2316 C
ATOM 2177 O VAL A1084 -5.215 14.692 -7.564 1.00111.11 O
ANISOU 2177 O VAL A1084 10780 17703 13734 331 513 2204 O
ATOM 2178 CB VAL A1084 -6.083 17.902 -7.320 1.00111.37 C
ANISOU 2178 CB VAL A1084 10602 17727 13987 301 488 2409 C
ATOM 2179 CG1 VAL A1084 -6.986 17.229 -6.287 1.00110.17 C
ANISOU 2179 CG1 VAL A1084 10489 17548 13822 215 388 2268 C
ATOM 2180 CG2 VAL A1084 -5.734 19.320 -6.870 1.00111.23 C
ANISOU 2180 CG2 VAL A1084 10477 17640 14146 287 499 2516 C
ATOM 2181 N LYS A1085 -5.382 15.719 -9.583 1.00110.30 N
ANISOU 2181 N LYS A1085 10696 17734 13478 462 582 2353 N
ATOM 2182 CA LYS A1085 -5.759 14.554 -10.389 1.00110.94 C
ANISOU 2182 CA LYS A1085 10930 17869 13352 502 554 2260 C
ATOM 2183 C LYS A1085 -4.639 13.502 -10.404 1.00115.49 C
ANISOU 2183 C LYS A1085 11574 18413 13895 559 631 2233 C
ATOM 2184 O LYS A1085 -4.933 12.306 -10.345 1.00115.02 O
ANISOU 2184 O LYS A1085 11631 18342 13728 541 575 2108 O
ATOM 2185 CB LYS A1085 -6.115 14.986 -11.821 1.00114.71 C
ANISOU 2185 CB LYS A1085 11468 18445 13672 597 581 2331 C
ATOM 2186 CG LYS A1085 -7.339 15.906 -11.877 1.00129.38 C
ANISOU 2186 CG LYS A1085 13278 20349 15533 546 498 2354 C
ATOM 2187 CD LYS A1085 -7.632 16.439 -13.269 1.00140.99 C
ANISOU 2187 CD LYS A1085 14767 21910 16895 651 555 2469 C
ATOM 2188 CE LYS A1085 -8.489 15.529 -14.116 1.00152.77 C
ANISOU 2188 CE LYS A1085 16426 23471 18148 696 492 2403 C
ATOM 2189 NZ LYS A1085 -9.932 15.753 -13.863 1.00160.91 N1+
ANISOU 2189 NZ LYS A1085 17457 24539 19143 609 350 2364 N1+
ATOM 2190 N GLU A1086 -3.369 13.946 -10.445 1.00112.69 N
ANISOU 2190 N GLU A1086 11140 18038 13637 629 756 2362 N
ATOM 2191 CA GLU A1086 -2.198 13.065 -10.431 1.00113.02 C
ANISOU 2191 CA GLU A1086 11220 18052 13673 696 850 2373 C
ATOM 2192 C GLU A1086 -1.972 12.493 -9.028 1.00115.72 C
ANISOU 2192 C GLU A1086 11525 18300 14142 588 795 2278 C
ATOM 2193 O GLU A1086 -1.494 11.363 -8.905 1.00115.41 O
ANISOU 2193 O GLU A1086 11569 18239 14042 612 818 2209 O
ATOM 2194 CB GLU A1086 -0.945 13.811 -10.921 1.00115.35 C
ANISOU 2194 CB GLU A1086 11410 18356 14061 796 997 2571 C
ATOM 2195 CG GLU A1086 -0.835 13.931 -12.437 1.00128.93 C
ANISOU 2195 CG GLU A1086 13210 20172 15607 958 1101 2665 C
ATOM 2196 CD GLU A1086 -1.933 14.679 -13.177 1.00154.32 C
ANISOU 2196 CD GLU A1086 16438 23461 18735 970 1056 2690 C
ATOM 2197 OE1 GLU A1086 -2.467 15.670 -12.626 1.00150.35 O
ANISOU 2197 OE1 GLU A1086 15807 22940 18379 888 1009 2742 O
ATOM 2198 OE2 GLU A1086 -2.252 14.275 -14.319 1.00151.27 O1-
ANISOU 2198 OE2 GLU A1086 16197 23147 18130 1069 1071 2665 O1-
ATOM 2199 N ALA A1087 -2.329 13.268 -7.980 1.00111.11 N
ANISOU 2199 N ALA A1087 10827 17660 13729 476 724 2276 N
ATOM 2200 CA ALA A1087 -2.206 12.868 -6.575 1.00109.70 C
ANISOU 2200 CA ALA A1087 10614 17392 13674 372 662 2190 C
ATOM 2201 C ALA A1087 -3.220 11.776 -6.221 1.00112.89 C
ANISOU 2201 C ALA A1087 11122 17801 13969 308 557 2018 C
ATOM 2202 O ALA A1087 -2.901 10.886 -5.430 1.00112.01 O
ANISOU 2202 O ALA A1087 11034 17636 13888 264 536 1934 O
ATOM 2203 CB ALA A1087 -2.396 14.074 -5.668 1.00109.71 C
ANISOU 2203 CB ALA A1087 10494 17331 13860 292 612 2238 C
ATOM 2204 N GLN A1088 -4.434 11.842 -6.811 1.00109.45 N
ANISOU 2204 N GLN A1088 10742 17429 13413 302 489 1978 N
ATOM 2205 CA GLN A1088 -5.510 10.865 -6.607 1.00108.75 C
ANISOU 2205 CA GLN A1088 10743 17352 13226 238 374 1840 C
ATOM 2206 C GLN A1088 -5.181 9.546 -7.317 1.00113.29 C
ANISOU 2206 C GLN A1088 11469 17940 13637 297 388 1769 C
ATOM 2207 O GLN A1088 -5.488 8.477 -6.784 1.00112.52 O
ANISOU 2207 O GLN A1088 11435 17808 13509 239 314 1653 O
ATOM 2208 CB GLN A1088 -6.857 11.419 -7.100 1.00110.22 C
ANISOU 2208 CB GLN A1088 10930 17602 13345 214 294 1849 C
ATOM 2209 CG GLN A1088 -7.412 12.544 -6.233 1.00121.57 C
ANISOU 2209 CG GLN A1088 12242 19019 14932 152 263 1894 C
ATOM 2210 CD GLN A1088 -8.688 13.122 -6.788 1.00138.85 C
ANISOU 2210 CD GLN A1088 14424 21277 17053 141 197 1922 C
ATOM 2211 OE1 GLN A1088 -8.702 13.778 -7.836 1.00135.35 O
ANISOU 2211 OE1 GLN A1088 13982 20895 16550 206 236 2008 O
ATOM 2212 NE2 GLN A1088 -9.787 12.929 -6.077 1.00129.42 N
ANISOU 2212 NE2 GLN A1088 13217 20081 15873 61 97 1862 N
ATOM 2213 N ALA A1089 -4.551 9.629 -8.511 1.00110.82 N
ANISOU 2213 N ALA A1089 11217 17673 13217 422 486 1844 N
ATOM 2214 CA ALA A1089 -4.137 8.482 -9.324 1.00111.51 C
ANISOU 2214 CA ALA A1089 11471 17770 13129 514 520 1791 C
ATOM 2215 C ALA A1089 -2.972 7.736 -8.670 1.00114.83 C
ANISOU 2215 C ALA A1089 11886 18125 13621 535 601 1779 C
ATOM 2216 O ALA A1089 -2.929 6.508 -8.732 1.00114.55 O
ANISOU 2216 O ALA A1089 11984 18063 13476 554 579 1678 O
ATOM 2217 CB ALA A1089 -3.746 8.940 -10.719 1.00113.68 C
ANISOU 2217 CB ALA A1089 11806 18116 13273 660 618 1896 C
ATOM 2218 N ALA A1090 -2.038 8.481 -8.040 1.00111.10 N
ANISOU 2218 N ALA A1090 11259 17619 13332 529 686 1886 N
ATOM 2219 CA ALA A1090 -0.878 7.928 -7.333 1.00110.76 C
ANISOU 2219 CA ALA A1090 11180 17515 13390 539 761 1902 C
ATOM 2220 C ALA A1090 -1.308 7.238 -6.035 1.00113.79 C
ANISOU 2220 C ALA A1090 11556 17832 13849 410 655 1768 C
ATOM 2221 O ALA A1090 -0.663 6.278 -5.613 1.00113.31 O
ANISOU 2221 O ALA A1090 11540 17728 13787 422 685 1720 O
ATOM 2222 CB ALA A1090 0.127 9.027 -7.034 1.00111.41 C
ANISOU 2222 CB ALA A1090 11093 17578 13661 552 849 2068 C
ATOM 2223 N ALA A1091 -2.399 7.729 -5.410 1.00109.70 N
ANISOU 2223 N ALA A1091 10981 17307 13394 297 539 1716 N
ATOM 2224 CA ALA A1091 -2.972 7.164 -4.188 1.00108.44 C
ANISOU 2224 CA ALA A1091 10809 17093 13302 180 437 1601 C
ATOM 2225 C ALA A1091 -3.757 5.887 -4.502 1.00112.74 C
ANISOU 2225 C ALA A1091 11497 17650 13690 163 351 1470 C
ATOM 2226 O ALA A1091 -3.901 5.029 -3.630 1.00111.69 O
ANISOU 2226 O ALA A1091 11376 17469 13591 90 289 1376 O
ATOM 2227 CB ALA A1091 -3.868 8.181 -3.508 1.00108.35 C
ANISOU 2227 CB ALA A1091 10695 17077 13398 93 360 1612 C
ATOM 2228 N GLU A1092 -4.253 5.757 -5.753 1.00110.50 N
ANISOU 2228 N GLU A1092 11324 17424 13235 228 337 1467 N
ATOM 2229 CA GLU A1092 -4.970 4.573 -6.234 1.00111.04 C
ANISOU 2229 CA GLU A1092 11551 17495 13142 216 237 1353 C
ATOM 2230 C GLU A1092 -3.989 3.405 -6.405 1.00115.95 C
ANISOU 2230 C GLU A1092 12299 18074 13683 293 301 1302 C
ATOM 2231 O GLU A1092 -4.388 2.247 -6.286 1.00115.63 O
ANISOU 2231 O GLU A1092 12371 17997 13565 253 209 1189 O
ATOM 2232 CB GLU A1092 -5.698 4.873 -7.550 1.00113.53 C
ANISOU 2232 CB GLU A1092 11956 17881 13300 266 193 1375 C
ATOM 2233 N GLN A1093 -2.701 3.727 -6.672 1.00113.34 N
ANISOU 2233 N GLN A1093 11942 17744 13378 403 459 1398 N
ATOM 2234 CA GLN A1093 -1.593 2.778 -6.816 1.00113.98 C
ANISOU 2234 CA GLN A1093 12122 17787 13397 499 556 1383 C
ATOM 2235 C GLN A1093 -1.188 2.197 -5.454 1.00117.24 C
ANISOU 2235 C GLN A1093 12458 18129 13958 411 543 1332 C
ATOM 2236 O GLN A1093 -0.659 1.086 -5.400 1.00117.25 O
ANISOU 2236 O GLN A1093 12562 18086 13901 449 568 1270 O
ATOM 2237 CB GLN A1093 -0.384 3.455 -7.480 1.00116.20 C
ANISOU 2237 CB GLN A1093 12369 18103 13678 649 736 1538 C
ATOM 2238 CG GLN A1093 -0.457 3.527 -9.006 1.00132.88 C
ANISOU 2238 CG GLN A1093 14623 20281 15585 788 779 1575 C
ATOM 2239 CD GLN A1093 0.077 2.300 -9.722 1.00154.14 C
ANISOU 2239 CD GLN A1093 17520 22960 18088 942 859 1542 C
ATOM 2240 OE1 GLN A1093 0.429 1.274 -9.122 1.00149.33 O
ANISOU 2240 OE1 GLN A1093 16969 22288 17482 941 870 1472 O
ATOM 2241 NE2 GLN A1093 0.170 2.390 -11.041 1.00148.28 N
ANISOU 2241 NE2 GLN A1093 16900 22274 17166 1089 922 1596 N
ATOM 2242 N LEU A1094 -1.430 2.956 -4.361 1.00112.80 N
ANISOU 2242 N LEU A1094 11728 17551 13580 298 503 1357 N
ATOM 2243 CA LEU A1094 -1.141 2.559 -2.978 1.00111.61 C
ANISOU 2243 CA LEU A1094 11495 17335 13576 204 476 1313 C
ATOM 2244 C LEU A1094 -2.110 1.447 -2.535 1.00115.45 C
ANISOU 2244 C LEU A1094 12067 17794 14004 117 342 1165 C
ATOM 2245 O LEU A1094 -1.740 0.604 -1.714 1.00114.45 O
ANISOU 2245 O LEU A1094 11945 17613 13929 80 335 1106 O
ATOM 2246 CB LEU A1094 -1.243 3.795 -2.047 1.00110.63 C
ANISOU 2246 CB LEU A1094 11199 17202 13636 122 455 1379 C
ATOM 2247 CG LEU A1094 -0.542 3.792 -0.661 1.00114.39 C
ANISOU 2247 CG LEU A1094 11565 17608 14291 57 465 1391 C
ATOM 2248 CD1 LEU A1094 -1.387 3.150 0.429 1.00113.49 C
ANISOU 2248 CD1 LEU A1094 11454 17457 14210 -53 353 1269 C
ATOM 2249 CD2 LEU A1094 0.895 3.280 -0.715 1.00117.55 C
ANISOU 2249 CD2 LEU A1094 11962 17979 14724 132 585 1457 C
ATOM 2250 N LYS A1095 -3.336 1.442 -3.104 1.00112.66 N
ANISOU 2250 N LYS A1095 11777 17479 13551 83 232 1118 N
ATOM 2251 CA LYS A1095 -4.389 0.459 -2.837 1.00112.49 C
ANISOU 2251 CA LYS A1095 11829 17436 13475 -5 85 1003 C
ATOM 2252 C LYS A1095 -3.988 -0.919 -3.383 1.00118.35 C
ANISOU 2252 C LYS A1095 12754 18135 14077 54 84 920 C
ATOM 2253 O LYS A1095 -4.193 -1.923 -2.704 1.00117.51 O
ANISOU 2253 O LYS A1095 12680 17977 13989 -16 6 832 O
ATOM 2254 CB LYS A1095 -5.715 0.929 -3.461 1.00115.04 C
ANISOU 2254 CB LYS A1095 12165 17814 13729 -45 -27 1007 C
ATOM 2255 CG LYS A1095 -6.950 0.193 -2.954 1.00126.37 C
ANISOU 2255 CG LYS A1095 13609 19234 15173 -165 -191 930 C
ATOM 2256 CD LYS A1095 -8.210 0.766 -3.577 1.00134.67 C
ANISOU 2256 CD LYS A1095 14643 20347 16179 -206 -295 965 C
ATOM 2257 CE LYS A1095 -9.461 0.151 -3.014 1.00143.61 C
ANISOU 2257 CE LYS A1095 15786 21465 17313 -318 -464 911 C
ATOM 2258 NZ LYS A1095 -10.681 0.765 -3.606 1.00152.89 N1+
ANISOU 2258 NZ LYS A1095 16935 22702 18453 -357 -567 965 N1+
ATOM 2259 N THR A1096 -3.392 -0.960 -4.591 1.00117.16 N
ANISOU 2259 N THR A1096 12725 18004 13788 192 176 953 N
ATOM 2260 CA THR A1096 -2.941 -2.199 -5.241 1.00118.62 C
ANISOU 2260 CA THR A1096 13110 18142 13818 280 191 880 C
ATOM 2261 C THR A1096 -1.667 -2.749 -4.566 1.00123.49 C
ANISOU 2261 C THR A1096 13691 18707 14522 320 314 892 C
ATOM 2262 O THR A1096 -1.370 -3.938 -4.708 1.00123.53 O
ANISOU 2262 O THR A1096 13838 18654 14444 356 305 811 O
ATOM 2263 CB THR A1096 -2.701 -1.970 -6.743 1.00127.75 C
ANISOU 2263 CB THR A1096 14418 19339 14782 436 261 922 C
ATOM 2264 OG1 THR A1096 -1.786 -0.888 -6.919 1.00127.25 O
ANISOU 2264 OG1 THR A1096 14236 19326 14790 527 429 1065 O
ATOM 2265 CG2 THR A1096 -3.989 -1.695 -7.512 1.00126.78 C
ANISOU 2265 CG2 THR A1096 14374 19256 14539 399 117 892 C
ATOM 2266 N THR A1097 -0.930 -1.888 -3.834 1.00120.44 N
ANISOU 2266 N THR A1097 13119 18336 14308 312 417 996 N
ATOM 2267 CA THR A1097 0.305 -2.233 -3.122 1.00120.51 C
ANISOU 2267 CA THR A1097 13061 18301 14426 339 529 1035 C
ATOM 2268 C THR A1097 -0.034 -2.982 -1.811 1.00124.79 C
ANISOU 2268 C THR A1097 13555 18785 15076 206 431 939 C
ATOM 2269 O THR A1097 0.602 -3.999 -1.523 1.00124.52 O
ANISOU 2269 O THR A1097 13574 18698 15041 231 470 900 O
ATOM 2270 CB THR A1097 1.148 -0.962 -2.863 1.00127.68 C
ANISOU 2270 CB THR A1097 13787 19238 15488 360 641 1188 C
ATOM 2271 OG1 THR A1097 1.310 -0.237 -4.083 1.00127.50 O
ANISOU 2271 OG1 THR A1097 13794 19276 15373 472 717 1284 O
ATOM 2272 CG2 THR A1097 2.523 -1.268 -2.276 1.00126.35 C
ANISOU 2272 CG2 THR A1097 13553 19029 15427 404 762 1257 C
ATOM 2273 N ARG A1098 -1.019 -2.482 -1.025 1.00121.40 N
ANISOU 2273 N ARG A1098 13025 18367 14737 74 312 911 N
ATOM 2274 CA ARG A1098 -1.434 -3.102 0.241 1.00120.67 C
ANISOU 2274 CA ARG A1098 12874 18228 14745 -47 220 834 C
ATOM 2275 C ARG A1098 -2.227 -4.402 -0.012 1.00126.68 C
ANISOU 2275 C ARG A1098 13786 18956 15390 -80 103 713 C
ATOM 2276 O ARG A1098 -2.146 -5.321 0.804 1.00125.53 O
ANISOU 2276 O ARG A1098 13632 18760 15304 -145 58 651 O
ATOM 2277 CB ARG A1098 -2.242 -2.126 1.134 1.00119.56 C
ANISOU 2277 CB ARG A1098 12585 18113 14728 -153 147 859 C
ATOM 2278 CG ARG A1098 -3.521 -1.522 0.532 1.00129.79 C
ANISOU 2278 CG ARG A1098 13896 19465 15952 -179 56 861 C
ATOM 2279 CD ARG A1098 -4.788 -2.241 0.976 1.00138.63 C
ANISOU 2279 CD ARG A1098 15033 20575 17063 -282 -95 780 C
ATOM 2280 NE ARG A1098 -5.989 -1.648 0.380 1.00145.81 N
ANISOU 2280 NE ARG A1098 15945 21541 17915 -309 -183 801 N
ATOM 2281 CZ ARG A1098 -7.233 -2.051 0.623 1.00157.19 C
ANISOU 2281 CZ ARG A1098 17388 22989 19349 -396 -322 765 C
ATOM 2282 NH1 ARG A1098 -7.464 -3.057 1.456 1.00142.58 N
ANISOU 2282 NH1 ARG A1098 15536 21092 17547 -467 -389 704 N
ATOM 2283 NH2 ARG A1098 -8.257 -1.448 0.034 1.00143.51 N1+
ANISOU 2283 NH2 ARG A1098 15647 21311 17568 -415 -396 803 N1+
ATOM 2284 N ASN A1099 -2.962 -4.481 -1.147 1.00125.90 N
ANISOU 2284 N ASN A1099 13830 18880 15127 -37 45 685 N
ATOM 2285 CA ASN A1099 -3.766 -5.646 -1.538 1.00127.29 C
ANISOU 2285 CA ASN A1099 14171 19012 15181 -69 -91 577 C
ATOM 2286 C ASN A1099 -2.888 -6.853 -1.929 1.00133.85 C
ANISOU 2286 C ASN A1099 15178 19779 15901 38 -22 524 C
ATOM 2287 O ASN A1099 -3.409 -7.962 -2.060 1.00134.25 O
ANISOU 2287 O ASN A1099 15396 19774 15841 24 -134 428 O
ATOM 2288 CB ASN A1099 -4.710 -5.294 -2.697 1.00129.56 C
ANISOU 2288 CB ASN A1099 14550 19340 15335 -68 -196 572 C
ATOM 2289 CG ASN A1099 -6.068 -4.769 -2.272 1.00155.02 C
ANISOU 2289 CG ASN A1099 17634 22614 18652 -190 -308 603 C
ATOM 2290 OD1 ASN A1099 -6.484 -3.671 -2.654 1.00149.84 O
ANISOU 2290 OD1 ASN A1099 16897 22023 18012 -171 -271 681 O
ATOM 2291 ND2 ASN A1099 -6.817 -5.563 -1.518 1.00147.43 N
ANISOU 2291 ND2 ASN A1099 16653 21623 17741 -310 -454 550 N
ATOM 2292 N ALA A1100 -1.568 -6.638 -2.101 1.00131.84 N
ANISOU 2292 N ALA A1100 14886 19526 15682 144 157 594 N
ATOM 2293 CA ALA A1100 -0.599 -7.673 -2.470 1.00133.37 C
ANISOU 2293 CA ALA A1100 15226 19665 15784 267 256 570 C
ATOM 2294 C ALA A1100 -0.012 -8.393 -1.238 1.00138.15 C
ANISOU 2294 C ALA A1100 15752 20211 16526 204 274 541 C
ATOM 2295 O ALA A1100 0.519 -9.499 -1.382 1.00138.49 O
ANISOU 2295 O ALA A1100 15938 20186 16494 252 279 472 O
ATOM 2296 CB ALA A1100 0.528 -7.055 -3.286 1.00134.82 C
ANISOU 2296 CB ALA A1100 15402 19892 15931 430 451 693 C
ATOM 2297 N TYR A1101 -0.102 -7.774 -0.041 1.00134.58 N
ANISOU 2297 N TYR A1101 15086 19782 16268 101 277 591 N
ATOM 2298 CA TYR A1101 0.453 -8.327 1.200 1.00134.04 C
ANISOU 2298 CA TYR A1101 14922 19666 16342 35 289 574 C
ATOM 2299 C TYR A1101 -0.628 -8.853 2.172 1.00137.80 C
ANISOU 2299 C TYR A1101 15353 20120 16883 -121 121 489 C
ATOM 2300 O TYR A1101 -0.281 -9.579 3.111 1.00136.47 O
ANISOU 2300 O TYR A1101 15118 19912 16822 -183 112 464 O
ATOM 2301 CB TYR A1101 1.313 -7.272 1.913 1.00134.54 C
ANISOU 2301 CB TYR A1101 14789 19757 16573 33 400 694 C
ATOM 2302 CG TYR A1101 2.595 -6.938 1.181 1.00137.43 C
ANISOU 2302 CG TYR A1101 15162 20142 16912 180 573 809 C
ATOM 2303 CD1 TYR A1101 3.753 -7.682 1.385 1.00139.93 C
ANISOU 2303 CD1 TYR A1101 15500 20418 17248 259 689 841 C
ATOM 2304 CD2 TYR A1101 2.658 -5.861 0.301 1.00138.69 C
ANISOU 2304 CD2 TYR A1101 15295 20362 17037 244 627 902 C
ATOM 2305 CE1 TYR A1101 4.938 -7.375 0.719 1.00141.78 C
ANISOU 2305 CE1 TYR A1101 15728 20676 17467 405 859 973 C
ATOM 2306 CE2 TYR A1101 3.837 -5.544 -0.371 1.00140.53 C
ANISOU 2306 CE2 TYR A1101 15522 20619 17256 386 793 1030 C
ATOM 2307 CZ TYR A1101 4.976 -6.304 -0.158 1.00148.60 C
ANISOU 2307 CZ TYR A1101 16562 21602 18297 469 911 1071 C
ATOM 2308 OH TYR A1101 6.145 -5.999 -0.812 1.00150.65 O
ANISOU 2308 OH TYR A1101 16798 21889 18552 617 1084 1223 O
ATOM 2309 N ILE A1102 -1.921 -8.522 1.939 1.00135.25 N
ANISOU 2309 N ILE A1102 15063 19826 16499 -180 -10 457 N
ATOM 2310 CA ILE A1102 -3.044 -8.972 2.783 1.00134.67 C
ANISOU 2310 CA ILE A1102 14933 19741 16496 -320 -164 404 C
ATOM 2311 C ILE A1102 -3.309 -10.487 2.578 1.00139.83 C
ANISOU 2311 C ILE A1102 15742 20316 17070 -345 -269 302 C
ATOM 2312 O ILE A1102 -3.961 -11.115 3.413 1.00138.81 O
ANISOU 2312 O ILE A1102 15565 20164 17011 -458 -390 266 O
ATOM 2313 CB ILE A1102 -4.349 -8.142 2.574 1.00137.68 C
ANISOU 2313 CB ILE A1102 15248 20185 16880 -388 -268 434 C
ATOM 2314 CG1 ILE A1102 -4.852 -8.174 1.110 1.00139.46 C
ANISOU 2314 CG1 ILE A1102 15625 20427 16936 -350 -345 414 C
ATOM 2315 CG2 ILE A1102 -4.177 -6.710 3.103 1.00137.33 C
ANISOU 2315 CG2 ILE A1102 15022 20196 16960 -399 -193 524 C
ATOM 2316 CD1 ILE A1102 -6.372 -7.979 0.930 1.00146.18 C
ANISOU 2316 CD1 ILE A1102 16407 21329 17805 -452 -494 438 C
ATOM 2317 N GLN A1103 -2.801 -11.059 1.472 1.00138.20 N
ANISOU 2317 N GLN A1103 15721 20064 16726 -234 -216 263 N
ATOM 2318 CA GLN A1103 -2.932 -12.484 1.154 1.00139.25 C
ANISOU 2318 CA GLN A1103 16034 20104 16771 -238 -307 162 C
ATOM 2319 C GLN A1103 -1.735 -13.281 1.728 1.00143.01 C
ANISOU 2319 C GLN A1103 16503 20524 17309 -192 -192 151 C
ATOM 2320 O GLN A1103 -1.710 -14.512 1.634 1.00143.07 O
ANISOU 2320 O GLN A1103 16607 20451 17303 -226 -269 73 O
ATOM 2321 CB GLN A1103 -3.064 -12.697 -0.374 1.00142.49 C
ANISOU 2321 CB GLN A1103 16693 20487 16961 -132 -340 116 C
ATOM 2322 CG GLN A1103 -1.914 -12.136 -1.218 1.00159.63 C
ANISOU 2322 CG GLN A1103 18918 22702 19033 42 -155 183 C
ATOM 2323 CD GLN A1103 -2.184 -12.218 -2.702 1.00181.28 C
ANISOU 2323 CD GLN A1103 21886 25439 21554 136 -207 150 C
ATOM 2324 OE1 GLN A1103 -2.330 -13.300 -3.280 1.00178.38 O
ANISOU 2324 OE1 GLN A1103 21748 24985 21041 164 -308 53 O
ATOM 2325 NE2 GLN A1103 -2.213 -11.067 -3.359 1.00173.47 N
ANISOU 2325 NE2 GLN A1103 20846 24535 20529 195 -138 231 N
ATOM 2326 N LYS A1104 -0.765 -12.570 2.344 1.00138.79 N
ANISOU 2326 N LYS A1104 15847 20031 16855 -124 -17 238 N
ATOM 2327 CA LYS A1104 0.444 -13.157 2.924 1.00138.22 C
ANISOU 2327 CA LYS A1104 15741 19920 16857 -75 109 258 C
ATOM 2328 C LYS A1104 0.503 -13.027 4.455 1.00140.31 C
ANISOU 2328 C LYS A1104 15803 20189 17319 -199 86 276 C
ATOM 2329 O LYS A1104 1.233 -13.796 5.086 1.00139.68 O
ANISOU 2329 O LYS A1104 15716 20058 17297 -200 126 258 O
ATOM 2330 CB LYS A1104 1.688 -12.489 2.318 1.00141.06 C
ANISOU 2330 CB LYS A1104 16072 20320 17204 67 305 367 C
ATOM 2331 N TYR A1105 -0.242 -12.070 5.050 1.00135.66 N
ANISOU 2331 N TYR A1105 15061 19660 16826 -294 27 313 N
ATOM 2332 CA TYR A1105 -0.191 -11.841 6.496 1.00133.95 C
ANISOU 2332 CA TYR A1105 14669 19447 16778 -391 13 334 C
ATOM 2333 C TYR A1105 -1.569 -11.796 7.169 1.00136.37 C
ANISOU 2333 C TYR A1105 14912 19771 17131 -517 -141 302 C
ATOM 2334 O TYR A1105 -1.694 -12.312 8.282 1.00135.26 O
ANISOU 2334 O TYR A1105 14690 19610 17094 -591 -179 287 O
ATOM 2335 CB TYR A1105 0.548 -10.529 6.803 1.00134.51 C
ANISOU 2335 CB TYR A1105 14590 19567 16949 -369 117 438 C
ATOM 2336 CG TYR A1105 2.012 -10.551 6.417 1.00136.90 C
ANISOU 2336 CG TYR A1105 14907 19859 17251 -255 274 508 C
ATOM 2337 CD1 TYR A1105 2.978 -11.024 7.303 1.00138.59 C
ANISOU 2337 CD1 TYR A1105 15067 20031 17559 -252 342 528 C
ATOM 2338 CD2 TYR A1105 2.435 -10.088 5.175 1.00138.58 C
ANISOU 2338 CD2 TYR A1105 15175 20105 17374 -147 360 569 C
ATOM 2339 CE1 TYR A1105 4.328 -11.047 6.955 1.00140.08 C
ANISOU 2339 CE1 TYR A1105 15255 20212 17756 -144 491 614 C
ATOM 2340 CE2 TYR A1105 3.782 -10.106 4.816 1.00140.11 C
ANISOU 2340 CE2 TYR A1105 15367 20294 17575 -33 515 659 C
ATOM 2341 CZ TYR A1105 4.726 -10.585 5.711 1.00147.26 C
ANISOU 2341 CZ TYR A1105 16214 21157 18579 -32 580 685 C
ATOM 2342 OH TYR A1105 6.056 -10.605 5.369 1.00148.88 O
ANISOU 2342 OH TYR A1105 16404 21362 18803 84 737 796 O
ATOM 2343 N LEU A1106 -2.576 -11.156 6.540 1.00132.45 N
ANISOU 2343 N LEU A1106 14434 19320 16571 -535 -218 310 N
ATOM 2344 CA LEU A1106 -3.915 -11.004 7.127 1.00131.52 C
ANISOU 2344 CA LEU A1106 14240 19231 16502 -641 -352 309 C
ATOM 2345 C LEU A1106 -4.649 -12.342 7.284 1.00135.19 C
ANISOU 2345 C LEU A1106 14778 19640 16949 -715 -491 242 C
ATOM 2346 O LEU A1106 -5.397 -12.489 8.252 1.00134.22 O
ANISOU 2346 O LEU A1106 14552 19533 16915 -808 -580 260 O
ATOM 2347 CB LEU A1106 -4.774 -10.052 6.291 1.00131.96 C
ANISOU 2347 CB LEU A1106 14301 19348 16490 -635 -395 346 C
ATOM 2348 N ARG A 248 -4.436 -13.306 6.368 1.00132.32 N1+
ANISOU 2348 N ARG A 248 14591 19207 16479 -671 -509 174 N1+
ATOM 2349 CA ARG A 248 -5.096 -14.617 6.438 1.00132.56 C
ANISOU 2349 CA ARG A 248 14701 19165 16500 -747 -656 111 C
ATOM 2350 C ARG A 248 -4.487 -15.501 7.527 1.00134.93 C
ANISOU 2350 C ARG A 248 14940 19418 16909 -776 -618 93 C
ATOM 2351 O ARG A 248 -5.164 -16.403 8.016 1.00134.59 O
ANISOU 2351 O ARG A 248 14887 19332 16919 -865 -739 69 O
ATOM 2352 CB ARG A 248 -5.022 -15.382 5.099 1.00134.62 C
ANISOU 2352 CB ARG A 248 15207 19352 16590 -685 -711 34 C
ATOM 2353 CG ARG A 248 -5.588 -14.718 3.853 1.00146.89 C
ANISOU 2353 CG ARG A 248 16879 20934 17998 -641 -762 34 C
ATOM 2354 CD ARG A 248 -5.524 -15.666 2.657 1.00160.11 C
ANISOU 2354 CD ARG A 248 18824 22510 19499 -580 -833 -56 C
ATOM 2355 NE ARG A 248 -4.156 -16.073 2.313 1.00169.60 N
ANISOU 2355 NE ARG A 248 20143 23674 20623 -432 -663 -82 N
ATOM 2356 CZ ARG A 248 -3.839 -16.912 1.328 1.00185.20 C
ANISOU 2356 CZ ARG A 248 22373 25574 22421 -325 -669 -150 C
ATOM 2357 NH1 ARG A 248 -4.787 -17.447 0.567 1.00174.20 N
ANISOU 2357 NH1 ARG A 248 21158 24128 20903 -357 -853 -210 N
ATOM 2358 NH2 ARG A 248 -2.570 -17.219 1.095 1.00171.64 N1+
ANISOU 2358 NH2 ARG A 248 20737 23832 20645 -178 -490 -150 N1+
ATOM 2359 N ASN A 249 -3.200 -15.275 7.869 1.00130.23 N
ANISOU 2359 N ASN A 249 14307 18826 16348 -699 -455 112 N
ATOM 2360 CA ASN A 249 -2.442 -16.062 8.843 1.00129.10 C
ANISOU 2360 CA ASN A 249 14114 18638 16299 -709 -398 101 C
ATOM 2361 C ASN A 249 -2.500 -15.470 10.263 1.00130.47 C
ANISOU 2361 C ASN A 249 14083 18863 16628 -772 -373 159 C
ATOM 2362 O ASN A 249 -2.243 -16.204 11.221 1.00129.52 O
ANISOU 2362 O ASN A 249 13909 18709 16594 -810 -371 149 O
ATOM 2363 CB ASN A 249 -0.988 -16.188 8.390 1.00130.36 C
ANISOU 2363 CB ASN A 249 14346 18772 16414 -586 -237 106 C
ATOM 2364 CG ASN A 249 -0.822 -17.070 7.175 1.00155.40 C
ANISOU 2364 CG ASN A 249 17744 21871 19429 -504 -249 39 C
ATOM 2365 OD1 ASN A 249 -0.749 -18.298 7.278 1.00150.47 O
ANISOU 2365 OD1 ASN A 249 17214 21164 18792 -513 -290 -23 O
ATOM 2366 ND2 ASN A 249 -0.783 -16.467 5.990 1.00148.04 N
ANISOU 2366 ND2 ASN A 249 16916 20965 18367 -419 -217 48 N
ATOM 2367 N ARG A 250 -2.836 -14.168 10.403 1.00125.58 N
ANISOU 2367 N ARG A 250 13361 18317 16037 -777 -354 218 N
ATOM 2368 CA ARG A 250 -2.931 -13.469 11.693 1.00123.68 C
ANISOU 2368 CA ARG A 250 12954 18118 15922 -819 -331 271 C
ATOM 2369 C ARG A 250 -4.177 -13.905 12.486 1.00125.12 C
ANISOU 2369 C ARG A 250 13062 18309 16167 -912 -449 275 C
ATOM 2370 O ARG A 250 -4.164 -13.892 13.723 1.00123.81 O
ANISOU 2370 O ARG A 250 12788 18153 16102 -941 -433 300 O
ATOM 2371 CB ARG A 250 -2.983 -11.959 11.425 1.00124.36 C
ANISOU 2371 CB ARG A 250 12981 18267 16002 -787 -287 330 C
ATOM 2372 CG ARG A 250 -2.509 -11.059 12.548 1.00135.45 C
ANISOU 2372 CG ARG A 250 14260 19694 17511 -787 -224 384 C
ATOM 2373 CD ARG A 250 -2.670 -9.594 12.161 1.00146.68 C
ANISOU 2373 CD ARG A 250 15654 21166 18912 -754 -198 437 C
ATOM 2374 NE ARG A 250 -1.747 -9.186 11.096 1.00156.91 N
ANISOU 2374 NE ARG A 250 17006 22456 20157 -677 -106 459 N
ATOM 2375 CZ ARG A 250 -1.690 -7.968 10.564 1.00171.36 C
ANISOU 2375 CZ ARG A 250 18814 24322 21974 -638 -66 516 C
ATOM 2376 NH1 ARG A 250 -2.506 -7.011 10.990 1.00158.63 N
ANISOU 2376 NH1 ARG A 250 17135 22749 20388 -667 -111 545 N
ATOM 2377 NH2 ARG A 250 -0.819 -7.697 9.603 1.00158.18 N1+
ANISOU 2377 NH2 ARG A 250 17187 22649 20265 -561 26 552 N1+
ATOM 2378 N ASP A 251 -5.249 -14.293 11.763 1.00120.88 N
ANISOU 2378 N ASP A 251 12585 17771 15572 -955 -571 260 N
ATOM 2379 CA ASP A 251 -6.522 -14.738 12.340 1.00120.05 C
ANISOU 2379 CA ASP A 251 12405 17677 15530 -1045 -695 287 C
ATOM 2380 C ASP A 251 -6.360 -16.066 13.077 1.00121.52 C
ANISOU 2380 C ASP A 251 12587 17801 15783 -1089 -726 258 C
ATOM 2381 O ASP A 251 -6.982 -16.256 14.123 1.00120.62 O
ANISOU 2381 O ASP A 251 12354 17709 15769 -1140 -759 305 O
ATOM 2382 CB ASP A 251 -7.605 -14.868 11.254 1.00123.17 C
ANISOU 2382 CB ASP A 251 12879 18071 15848 -1085 -833 286 C
ATOM 2383 CG ASP A 251 -7.994 -13.557 10.595 1.00134.76 C
ANISOU 2383 CG ASP A 251 14335 19608 17259 -1054 -821 328 C
ATOM 2384 OD1 ASP A 251 -8.386 -12.614 11.325 1.00134.85 O
ANISOU 2384 OD1 ASP A 251 14213 19687 17336 -1057 -789 398 O
ATOM 2385 OD2 ASP A 251 -7.937 -13.482 9.348 1.00141.99 O1-
ANISOU 2385 OD2 ASP A 251 15382 20509 18058 -1022 -849 293 O1-
ATOM 2386 N THR A 252 -5.521 -16.976 12.534 1.00116.66 N
ANISOU 2386 N THR A 252 12105 17110 15112 -1058 -707 187 N
ATOM 2387 CA THR A 252 -5.224 -18.280 13.134 1.00115.55 C
ANISOU 2387 CA THR A 252 11981 16898 15026 -1089 -728 152 C
ATOM 2388 C THR A 252 -4.309 -18.092 14.344 1.00116.01 C
ANISOU 2388 C THR A 252 11932 16972 15175 -1061 -601 174 C
ATOM 2389 O THR A 252 -4.389 -18.877 15.286 1.00115.04 O
ANISOU 2389 O THR A 252 11748 16825 15138 -1105 -622 179 O
ATOM 2390 CB THR A 252 -4.600 -19.241 12.114 1.00123.93 C
ANISOU 2390 CB THR A 252 13240 17868 15982 -1047 -741 69 C
ATOM 2391 OG1 THR A 252 -3.433 -18.643 11.544 1.00123.55 O
ANISOU 2391 OG1 THR A 252 13256 17830 15859 -938 -598 57 O
ATOM 2392 CG2 THR A 252 -5.579 -19.659 11.021 1.00123.64 C
ANISOU 2392 CG2 THR A 252 13329 17792 15857 -1091 -905 39 C
ATOM 2393 N MET A 253 -3.446 -17.049 14.312 1.00110.54 N
ANISOU 2393 N MET A 253 11215 16318 14469 -992 -479 195 N
ATOM 2394 CA MET A 253 -2.515 -16.695 15.387 1.00108.65 C
ANISOU 2394 CA MET A 253 10880 16089 14313 -967 -373 225 C
ATOM 2395 C MET A 253 -3.269 -16.107 16.590 1.00110.31 C
ANISOU 2395 C MET A 253 10948 16354 14611 -1010 -399 279 C
ATOM 2396 O MET A 253 -3.012 -16.518 17.724 1.00109.29 O
ANISOU 2396 O MET A 253 10748 16215 14563 -1027 -378 291 O
ATOM 2397 CB MET A 253 -1.445 -15.698 14.886 1.00110.70 C
ANISOU 2397 CB MET A 253 11159 16364 14536 -887 -257 246 C
ATOM 2398 CG MET A 253 -0.256 -16.349 14.203 1.00114.78 C
ANISOU 2398 CG MET A 253 11780 16824 15006 -819 -175 218 C
ATOM 2399 SD MET A 253 0.873 -17.132 15.367 1.00118.21 S
ANISOU 2399 SD MET A 253 12138 17223 15554 -817 -92 238 S
ATOM 2400 CE MET A 253 2.208 -17.544 14.252 1.00115.90 C
ANISOU 2400 CE MET A 253 11985 16869 15184 -715 13 219 C
ATOM 2401 N MET A 254 -4.201 -15.160 16.341 1.00105.78 N
ANISOU 2401 N MET A 254 10338 15838 14014 -1018 -441 316 N
ATOM 2402 CA MET A 254 -4.993 -14.488 17.380 1.00104.50 C
ANISOU 2402 CA MET A 254 10058 15732 13917 -1036 -457 377 C
ATOM 2403 C MET A 254 -6.018 -15.445 18.028 1.00106.65 C
ANISOU 2403 C MET A 254 10270 16004 14248 -1099 -544 401 C
ATOM 2404 O MET A 254 -6.350 -15.270 19.207 1.00105.79 O
ANISOU 2404 O MET A 254 10064 15926 14206 -1099 -530 449 O
ATOM 2405 CB MET A 254 -5.700 -13.248 16.807 1.00107.09 C
ANISOU 2405 CB MET A 254 10372 16117 14198 -1018 -472 416 C
ATOM 2406 CG MET A 254 -4.752 -12.075 16.573 1.00110.66 C
ANISOU 2406 CG MET A 254 10841 16578 14627 -957 -381 421 C
ATOM 2407 SD MET A 254 -5.563 -10.537 16.055 1.00115.24 S
ANISOU 2407 SD MET A 254 11396 17224 15167 -930 -391 474 S
ATOM 2408 CE MET A 254 -5.964 -10.931 14.323 1.00112.97 C
ANISOU 2408 CE MET A 254 11212 16939 14774 -941 -454 445 C
ATOM 2409 N SER A 255 -6.495 -16.459 17.268 1.00102.30 N
ANISOU 2409 N SER A 255 9784 15415 13672 -1148 -637 373 N
ATOM 2410 CA SER A 255 -7.438 -17.481 17.747 1.00101.66 C
ANISOU 2410 CA SER A 255 9649 15321 13657 -1219 -737 407 C
ATOM 2411 C SER A 255 -6.778 -18.370 18.808 1.00102.95 C
ANISOU 2411 C SER A 255 9779 15444 13894 -1224 -694 391 C
ATOM 2412 O SER A 255 -7.429 -18.749 19.785 1.00102.48 O
ANISOU 2412 O SER A 255 9616 15405 13916 -1256 -725 451 O
ATOM 2413 CB SER A 255 -7.944 -18.336 16.587 1.00106.25 C
ANISOU 2413 CB SER A 255 10334 15848 14188 -1272 -863 373 C
ATOM 2414 OG SER A 255 -8.883 -19.311 17.015 1.00114.99 O
ANISOU 2414 OG SER A 255 11379 16937 15376 -1352 -978 422 O
ATOM 2415 N LEU A 256 -5.484 -18.692 18.605 1.00 97.51 N
ANISOU 2415 N LEU A 256 9171 14703 13177 -1186 -617 323 N
ATOM 2416 CA LEU A 256 -4.672 -19.498 19.514 1.00 95.86 C
ANISOU 2416 CA LEU A 256 8937 14453 13031 -1183 -564 307 C
ATOM 2417 C LEU A 256 -4.161 -18.638 20.668 1.00 96.63 C
ANISOU 2417 C LEU A 256 8940 14597 13177 -1143 -472 346 C
ATOM 2418 O LEU A 256 -4.016 -19.149 21.778 1.00 96.08 O
ANISOU 2418 O LEU A 256 8804 14522 13179 -1154 -455 366 O
ATOM 2419 CB LEU A 256 -3.499 -20.141 18.754 1.00 96.09 C
ANISOU 2419 CB LEU A 256 9092 14408 13008 -1147 -512 234 C
ATOM 2420 CG LEU A 256 -2.746 -21.277 19.449 1.00100.45 C
ANISOU 2420 CG LEU A 256 9640 14904 13622 -1151 -474 215 C
ATOM 2421 CD1 LEU A 256 -3.597 -22.541 19.529 1.00101.20 C
ANISOU 2421 CD1 LEU A 256 9742 14950 13758 -1222 -587 208 C
ATOM 2422 CD2 LEU A 256 -1.458 -21.582 18.719 1.00103.30 C
ANISOU 2422 CD2 LEU A 256 10114 15209 13926 -1087 -387 165 C
ATOM 2423 N LEU A 257 -3.901 -17.336 20.407 1.00 90.88 N
ANISOU 2423 N LEU A 257 8215 13908 12409 -1098 -422 358 N
ATOM 2424 CA LEU A 257 -3.424 -16.367 21.396 1.00 89.01 C
ANISOU 2424 CA LEU A 257 7914 13701 12205 -1059 -356 391 C
ATOM 2425 C LEU A 257 -4.488 -16.140 22.486 1.00 90.18 C
ANISOU 2425 C LEU A 257 7968 13900 12397 -1067 -389 451 C
ATOM 2426 O LEU A 257 -4.146 -16.146 23.671 1.00 89.23 O
ANISOU 2426 O LEU A 257 7800 13781 12325 -1050 -355 469 O
ATOM 2427 CB LEU A 257 -3.057 -15.033 20.706 1.00 89.01 C
ANISOU 2427 CB LEU A 257 7947 13722 12151 -1016 -317 395 C
ATOM 2428 CG LEU A 257 -2.357 -13.972 21.569 1.00 93.31 C
ANISOU 2428 CG LEU A 257 8454 14272 12726 -978 -261 422 C
ATOM 2429 CD1 LEU A 257 -0.853 -14.231 21.668 1.00 93.30 C
ANISOU 2429 CD1 LEU A 257 8472 14220 12757 -965 -197 408 C
ATOM 2430 CD2 LEU A 257 -2.592 -12.584 21.004 1.00 96.19 C
ANISOU 2430 CD2 LEU A 257 8835 14669 13046 -946 -254 444 C
ATOM 2431 N LYS A 258 -5.767 -15.964 22.079 1.00 85.22 N
ANISOU 2431 N LYS A 258 7314 13314 11751 -1086 -455 491 N
ATOM 2432 CA LYS A 258 -6.904 -15.747 22.982 1.00 84.32 C
ANISOU 2432 CA LYS A 258 7104 13256 11676 -1079 -478 573 C
ATOM 2433 C LYS A 258 -7.159 -16.974 23.869 1.00 86.30 C
ANISOU 2433 C LYS A 258 7293 13493 12003 -1113 -503 600 C
ATOM 2434 O LYS A 258 -7.463 -16.808 25.052 1.00 85.32 O
ANISOU 2434 O LYS A 258 7097 13405 11916 -1077 -473 658 O
ATOM 2435 CB LYS A 258 -8.175 -15.398 22.186 1.00 87.48 C
ANISOU 2435 CB LYS A 258 7484 13703 12052 -1098 -547 625 C
ATOM 2436 CG LYS A 258 -8.266 -13.934 21.747 1.00 99.47 C
ANISOU 2436 CG LYS A 258 9023 15260 13510 -1046 -513 637 C
ATOM 2437 CD LYS A 258 -8.778 -13.012 22.866 1.00105.94 C
ANISOU 2437 CD LYS A 258 9777 16132 14344 -978 -465 707 C
ATOM 2438 CE LYS A 258 -8.922 -11.568 22.437 1.00112.20 C
ANISOU 2438 CE LYS A 258 10595 16955 15081 -925 -438 722 C
ATOM 2439 NZ LYS A 258 -10.026 -11.372 21.459 1.00119.36 N1+
ANISOU 2439 NZ LYS A 258 11477 17907 15967 -950 -497 775 N1+
ATOM 2440 N THR A 259 -7.006 -18.193 23.301 1.00 82.12 N
ANISOU 2440 N THR A 259 6803 12909 11491 -1173 -555 560 N
ATOM 2441 CA THR A 259 -7.180 -19.482 23.986 1.00 81.67 C
ANISOU 2441 CA THR A 259 6696 12823 11511 -1216 -588 581 C
ATOM 2442 C THR A 259 -6.176 -19.599 25.153 1.00 84.05 C
ANISOU 2442 C THR A 259 6976 13112 11846 -1178 -503 565 C
ATOM 2443 O THR A 259 -6.557 -20.027 26.246 1.00 83.34 O
ANISOU 2443 O THR A 259 6803 13045 11819 -1174 -499 624 O
ATOM 2444 CB THR A 259 -7.016 -20.636 22.974 1.00 89.21 C
ANISOU 2444 CB THR A 259 7737 13700 12458 -1279 -662 520 C
ATOM 2445 OG1 THR A 259 -7.903 -20.425 21.872 1.00 90.16 O
ANISOU 2445 OG1 THR A 259 7892 13829 12537 -1314 -753 532 O
ATOM 2446 CG2 THR A 259 -7.277 -22.012 23.592 1.00 87.67 C
ANISOU 2446 CG2 THR A 259 7494 13465 12352 -1333 -713 546 C
ATOM 2447 N VAL A 260 -4.912 -19.189 24.910 1.00 79.75 N
ANISOU 2447 N VAL A 260 6502 12535 11263 -1147 -437 498 N
ATOM 2448 CA VAL A 260 -3.796 -19.194 25.859 1.00 78.80 C
ANISOU 2448 CA VAL A 260 6371 12396 11173 -1116 -366 484 C
ATOM 2449 C VAL A 260 -4.106 -18.250 27.052 1.00 81.89 C
ANISOU 2449 C VAL A 260 6705 12841 11569 -1063 -336 539 C
ATOM 2450 O VAL A 260 -3.864 -18.628 28.205 1.00 81.41 O
ANISOU 2450 O VAL A 260 6601 12781 11551 -1048 -314 561 O
ATOM 2451 CB VAL A 260 -2.489 -18.799 25.116 1.00 82.67 C
ANISOU 2451 CB VAL A 260 6942 12844 11624 -1096 -312 426 C
ATOM 2452 CG1 VAL A 260 -1.422 -18.272 26.065 1.00 81.98 C
ANISOU 2452 CG1 VAL A 260 6838 12750 11561 -1060 -251 434 C
ATOM 2453 CG2 VAL A 260 -1.950 -19.968 24.299 1.00 82.94 C
ANISOU 2453 CG2 VAL A 260 7040 12814 11660 -1123 -313 376 C
ATOM 2454 N VAL A 261 -4.654 -17.044 26.768 1.00 77.69 N
ANISOU 2454 N VAL A 261 6182 12351 10987 -1027 -338 560 N
ATOM 2455 CA VAL A 261 -5.009 -16.024 27.766 1.00 76.94 C
ANISOU 2455 CA VAL A 261 6062 12299 10875 -959 -312 608 C
ATOM 2456 C VAL A 261 -6.168 -16.544 28.660 1.00 80.72 C
ANISOU 2456 C VAL A 261 6454 12827 11390 -943 -325 691 C
ATOM 2457 O VAL A 261 -6.192 -16.231 29.851 1.00 79.85 O
ANISOU 2457 O VAL A 261 6326 12737 11278 -881 -291 727 O
ATOM 2458 CB VAL A 261 -5.349 -14.665 27.085 1.00 80.78 C
ANISOU 2458 CB VAL A 261 6586 12811 11298 -924 -311 612 C
ATOM 2459 CG1 VAL A 261 -5.786 -13.613 28.105 1.00 80.57 C
ANISOU 2459 CG1 VAL A 261 6554 12818 11243 -842 -286 660 C
ATOM 2460 CG2 VAL A 261 -4.160 -14.145 26.283 1.00 80.33 C
ANISOU 2460 CG2 VAL A 261 6600 12707 11214 -934 -291 550 C
ATOM 2461 N ILE A 262 -7.086 -17.358 28.101 1.00 78.01 N
ANISOU 2461 N ILE A 262 6060 12500 11082 -997 -380 730 N
ATOM 2462 CA ILE A 262 -8.205 -17.942 28.854 1.00 78.59 C
ANISOU 2462 CA ILE A 262 6030 12621 11211 -991 -398 835 C
ATOM 2463 C ILE A 262 -7.646 -18.995 29.841 1.00 82.02 C
ANISOU 2463 C ILE A 262 6432 13027 11704 -1001 -379 833 C
ATOM 2464 O ILE A 262 -8.096 -19.043 30.991 1.00 81.59 O
ANISOU 2464 O ILE A 262 6312 13015 11671 -945 -346 911 O
ATOM 2465 CB ILE A 262 -9.305 -18.521 27.908 1.00 82.78 C
ANISOU 2465 CB ILE A 262 6513 13163 11776 -1063 -486 888 C
ATOM 2466 CG1 ILE A 262 -9.983 -17.407 27.048 1.00 83.59 C
ANISOU 2466 CG1 ILE A 262 6632 13309 11821 -1040 -501 912 C
ATOM 2467 CG2 ILE A 262 -10.363 -19.358 28.657 1.00 84.28 C
ANISOU 2467 CG2 ILE A 262 6577 13390 12054 -1076 -517 1013 C
ATOM 2468 CD1 ILE A 262 -10.742 -16.214 27.791 1.00 92.72 C
ANISOU 2468 CD1 ILE A 262 7721 14549 12958 -942 -452 1027 C
ATOM 2469 N VAL A 263 -6.641 -19.792 29.404 1.00 78.11 N
ANISOU 2469 N VAL A 263 5987 12463 11229 -1060 -390 749 N
ATOM 2470 CA VAL A 263 -5.966 -20.810 30.229 1.00 77.46 C
ANISOU 2470 CA VAL A 263 5881 12346 11203 -1074 -369 739 C
ATOM 2471 C VAL A 263 -5.225 -20.099 31.386 1.00 79.90 C
ANISOU 2471 C VAL A 263 6206 12668 11485 -999 -301 734 C
ATOM 2472 O VAL A 263 -5.311 -20.540 32.538 1.00 79.38 O
ANISOU 2472 O VAL A 263 6087 12621 11453 -968 -278 784 O
ATOM 2473 CB VAL A 263 -5.014 -21.707 29.384 1.00 81.25 C
ANISOU 2473 CB VAL A 263 6427 12745 11698 -1139 -386 651 C
ATOM 2474 CG1 VAL A 263 -4.186 -22.645 30.263 1.00 80.81 C
ANISOU 2474 CG1 VAL A 263 6350 12654 11700 -1145 -352 642 C
ATOM 2475 CG2 VAL A 263 -5.794 -22.510 28.350 1.00 81.82 C
ANISOU 2475 CG2 VAL A 263 6504 12790 11792 -1212 -473 655 C
ATOM 2476 N LEU A 264 -4.540 -18.979 31.072 1.00 75.55 N
ANISOU 2476 N LEU A 264 5731 12102 10871 -968 -278 681 N
ATOM 2477 CA LEU A 264 -3.796 -18.167 32.038 1.00 74.78 C
ANISOU 2477 CA LEU A 264 5673 11999 10743 -906 -240 670 C
ATOM 2478 C LEU A 264 -4.750 -17.412 32.976 1.00 79.02 C
ANISOU 2478 C LEU A 264 6190 12595 11238 -815 -224 741 C
ATOM 2479 O LEU A 264 -4.465 -17.301 34.169 1.00 78.25 O
ANISOU 2479 O LEU A 264 6103 12500 11130 -758 -200 759 O
ATOM 2480 CB LEU A 264 -2.882 -17.176 31.302 1.00 74.43 C
ANISOU 2480 CB LEU A 264 5709 11916 10656 -909 -236 608 C
ATOM 2481 CG LEU A 264 -1.725 -16.624 32.115 1.00 78.74 C
ANISOU 2481 CG LEU A 264 6300 12421 11198 -882 -223 587 C
ATOM 2482 CD1 LEU A 264 -0.409 -17.183 31.618 1.00 78.77 C
ANISOU 2482 CD1 LEU A 264 6316 12367 11247 -938 -212 545 C
ATOM 2483 CD2 LEU A 264 -1.694 -15.118 32.066 1.00 80.95 C
ANISOU 2483 CD2 LEU A 264 6645 12697 11417 -833 -232 580 C
ATOM 2484 N GLY A 265 -5.855 -16.906 32.421 1.00 76.51 N
ANISOU 2484 N GLY A 265 5852 12325 10894 -797 -235 786 N
ATOM 2485 CA GLY A 265 -6.887 -16.171 33.147 1.00 76.97 C
ANISOU 2485 CA GLY A 265 5891 12445 10910 -697 -207 869 C
ATOM 2486 C GLY A 265 -7.548 -17.006 34.224 1.00 81.66 C
ANISOU 2486 C GLY A 265 6398 13084 11546 -659 -184 963 C
ATOM 2487 O GLY A 265 -7.663 -16.562 35.367 1.00 81.35 O
ANISOU 2487 O GLY A 265 6381 13068 11461 -555 -140 1003 O
ATOM 2488 N ALA A 266 -7.938 -18.248 33.870 1.00 78.65 N
ANISOU 2488 N ALA A 266 5927 12709 11249 -738 -217 1000 N
ATOM 2489 CA ALA A 266 -8.557 -19.213 34.784 1.00 78.85 C
ANISOU 2489 CA ALA A 266 5849 12772 11337 -719 -202 1103 C
ATOM 2490 C ALA A 266 -7.571 -19.649 35.870 1.00 82.64 C
ANISOU 2490 C ALA A 266 6356 13223 11822 -694 -169 1067 C
ATOM 2491 O ALA A 266 -7.993 -19.902 37.000 1.00 82.75 O
ANISOU 2491 O ALA A 266 6320 13281 11841 -617 -127 1154 O
ATOM 2492 CB ALA A 266 -9.054 -20.423 34.012 1.00 79.82 C
ANISOU 2492 CB ALA A 266 5888 12883 11559 -832 -269 1136 C
ATOM 2493 N PHE A 267 -6.261 -19.719 35.527 1.00 78.34 N
ANISOU 2493 N PHE A 267 5887 12606 11272 -752 -183 951 N
ATOM 2494 CA PHE A 267 -5.174 -20.095 36.433 1.00 77.82 C
ANISOU 2494 CA PHE A 267 5850 12503 11215 -743 -163 912 C
ATOM 2495 C PHE A 267 -4.976 -19.032 37.525 1.00 81.54 C
ANISOU 2495 C PHE A 267 6397 12987 11599 -629 -131 917 C
ATOM 2496 O PHE A 267 -4.768 -19.393 38.680 1.00 80.80 O
ANISOU 2496 O PHE A 267 6297 12901 11504 -579 -107 948 O
ATOM 2497 CB PHE A 267 -3.866 -20.302 35.646 1.00 79.18 C
ANISOU 2497 CB PHE A 267 6079 12598 11408 -829 -185 806 C
ATOM 2498 CG PHE A 267 -2.760 -21.015 36.395 1.00 80.49 C
ANISOU 2498 CG PHE A 267 6246 12723 11614 -847 -172 781 C
ATOM 2499 CD1 PHE A 267 -2.633 -22.397 36.330 1.00 83.53 C
ANISOU 2499 CD1 PHE A 267 6566 13088 12082 -910 -176 792 C
ATOM 2500 CD2 PHE A 267 -1.815 -20.301 37.125 1.00 82.49 C
ANISOU 2500 CD2 PHE A 267 6568 12948 11825 -807 -165 750 C
ATOM 2501 CE1 PHE A 267 -1.609 -23.057 37.015 1.00 84.30 C
ANISOU 2501 CE1 PHE A 267 6660 13150 12220 -925 -159 775 C
ATOM 2502 CE2 PHE A 267 -0.788 -20.963 37.808 1.00 84.96 C
ANISOU 2502 CE2 PHE A 267 6876 13225 12182 -829 -160 737 C
ATOM 2503 CZ PHE A 267 -0.689 -22.335 37.744 1.00 83.09 C
ANISOU 2503 CZ PHE A 267 6566 12978 12027 -885 -150 751 C
ATOM 2504 N ILE A 268 -5.050 -17.734 37.162 1.00 78.61 N
ANISOU 2504 N ILE A 268 6107 12611 11150 -585 -135 887 N
ATOM 2505 CA ILE A 268 -4.875 -16.615 38.095 1.00 78.83 C
ANISOU 2505 CA ILE A 268 6237 12632 11083 -474 -121 881 C
ATOM 2506 C ILE A 268 -6.089 -16.534 39.050 1.00 83.95 C
ANISOU 2506 C ILE A 268 6854 13356 11687 -345 -68 992 C
ATOM 2507 O ILE A 268 -5.890 -16.535 40.261 1.00 83.95 O
ANISOU 2507 O ILE A 268 6897 13357 11642 -259 -45 1012 O
ATOM 2508 CB ILE A 268 -4.633 -15.269 37.335 1.00 81.84 C
ANISOU 2508 CB ILE A 268 6714 12978 11404 -470 -147 822 C
ATOM 2509 CG1 ILE A 268 -3.270 -15.299 36.588 1.00 81.86 C
ANISOU 2509 CG1 ILE A 268 6751 12905 11448 -577 -189 731 C
ATOM 2510 CG2 ILE A 268 -4.707 -14.055 38.285 1.00 82.86 C
ANISOU 2510 CG2 ILE A 268 6963 13094 11425 -341 -141 825 C
ATOM 2511 CD1 ILE A 268 -3.049 -14.192 35.523 1.00 89.48 C
ANISOU 2511 CD1 ILE A 268 7776 13841 12383 -598 -213 686 C
ATOM 2512 N ILE A 269 -7.323 -16.513 38.508 1.00 80.93 N
ANISOU 2512 N ILE A 269 6393 13038 11320 -329 -48 1074 N
ATOM 2513 CA ILE A 269 -8.594 -16.374 39.235 1.00 81.74 C
ANISOU 2513 CA ILE A 269 6444 13224 11391 -201 14 1209 C
ATOM 2514 C ILE A 269 -8.762 -17.470 40.334 1.00 86.56 C
ANISOU 2514 C ILE A 269 6971 13871 12045 -163 52 1295 C
ATOM 2515 O ILE A 269 -9.340 -17.169 41.381 1.00 86.96 O
ANISOU 2515 O ILE A 269 7037 13973 12032 -14 117 1384 O
ATOM 2516 CB ILE A 269 -9.777 -16.386 38.206 1.00 85.17 C
ANISOU 2516 CB ILE A 269 6775 13712 11873 -237 7 1289 C
ATOM 2517 CG1 ILE A 269 -9.878 -15.064 37.375 1.00 85.52 C
ANISOU 2517 CG1 ILE A 269 6910 13742 11842 -213 -3 1240 C
ATOM 2518 CG2 ILE A 269 -11.148 -16.652 38.860 1.00 86.64 C
ANISOU 2518 CG2 ILE A 269 6846 13994 12078 -134 69 1471 C
ATOM 2519 CD1 ILE A 269 -8.668 -14.057 37.189 1.00 91.75 C
ANISOU 2519 CD1 ILE A 269 7817 14445 12600 -290 -56 1086 C
ATOM 2520 N CYS A 270 -8.238 -18.695 40.128 1.00 82.98 N
ANISOU 2520 N CYS A 270 6442 13390 11694 -284 17 1270 N
ATOM 2521 CA CYS A 270 -8.406 -19.770 41.112 1.00 83.44 C
ANISOU 2521 CA CYS A 270 6412 13483 11807 -258 50 1357 C
ATOM 2522 C CYS A 270 -7.195 -19.903 42.073 1.00 86.12 C
ANISOU 2522 C CYS A 270 6840 13773 12108 -237 51 1281 C
ATOM 2523 O CYS A 270 -7.397 -20.299 43.223 1.00 86.16 O
ANISOU 2523 O CYS A 270 6821 13818 12099 -145 98 1359 O
ATOM 2524 CB CYS A 270 -8.678 -21.095 40.412 1.00 84.15 C
ANISOU 2524 CB CYS A 270 6364 13571 12038 -394 7 1394 C
ATOM 2525 SG CYS A 270 -7.229 -21.810 39.599 1.00 87.40 S
ANISOU 2525 SG CYS A 270 6820 13880 12509 -557 -60 1237 S
ATOM 2526 N TRP A 271 -5.954 -19.637 41.603 1.00 81.05 N
ANISOU 2526 N TRP A 271 6288 13050 11459 -321 -1 1145 N
ATOM 2527 CA TRP A 271 -4.752 -19.797 42.433 1.00 80.10 C
ANISOU 2527 CA TRP A 271 6238 12877 11319 -321 -16 1084 C
ATOM 2528 C TRP A 271 -4.458 -18.583 43.327 1.00 84.23 C
ANISOU 2528 C TRP A 271 6916 13380 11709 -195 -16 1055 C
ATOM 2529 O TRP A 271 -3.891 -18.780 44.403 1.00 84.14 O
ANISOU 2529 O TRP A 271 6953 13353 11665 -147 -17 1054 O
ATOM 2530 CB TRP A 271 -3.513 -20.090 41.580 1.00 77.79 C
ANISOU 2530 CB TRP A 271 5962 12505 11089 -461 -70 976 C
ATOM 2531 CG TRP A 271 -3.382 -21.530 41.182 1.00 78.37 C
ANISOU 2531 CG TRP A 271 5921 12572 11283 -566 -73 990 C
ATOM 2532 CD1 TRP A 271 -3.698 -22.080 39.976 1.00 81.17 C
ANISOU 2532 CD1 TRP A 271 6214 12919 11710 -662 -93 980 C
ATOM 2533 CD2 TRP A 271 -2.898 -22.604 42.000 1.00 78.12 C
ANISOU 2533 CD2 TRP A 271 5837 12535 11309 -581 -60 1016 C
ATOM 2534 NE1 TRP A 271 -3.438 -23.430 39.988 1.00 80.58 N
ANISOU 2534 NE1 TRP A 271 6060 12826 11732 -735 -97 994 N
ATOM 2535 CE2 TRP A 271 -2.941 -23.779 41.217 1.00 81.94 C
ANISOU 2535 CE2 TRP A 271 6228 13002 11903 -689 -72 1019 C
ATOM 2536 CE3 TRP A 271 -2.426 -22.689 43.322 1.00 79.39 C
ANISOU 2536 CE3 TRP A 271 6029 12701 11436 -512 -44 1037 C
ATOM 2537 CZ2 TRP A 271 -2.533 -25.025 41.711 1.00 81.13 C
ANISOU 2537 CZ2 TRP A 271 6057 12885 11883 -729 -63 1044 C
ATOM 2538 CZ3 TRP A 271 -2.011 -23.920 43.806 1.00 80.71 C
ANISOU 2538 CZ3 TRP A 271 6119 12862 11686 -555 -33 1064 C
ATOM 2539 CH2 TRP A 271 -2.072 -25.071 43.009 1.00 81.17 C
ANISOU 2539 CH2 TRP A 271 6078 12902 11859 -662 -39 1069 C
ATOM 2540 N THR A 272 -4.809 -17.349 42.893 1.00 80.82 N
ANISOU 2540 N THR A 272 6570 12940 11197 -144 -24 1031 N
ATOM 2541 CA THR A 272 -4.564 -16.113 43.655 1.00 81.07 C
ANISOU 2541 CA THR A 272 6774 12934 11095 -24 -39 996 C
ATOM 2542 C THR A 272 -5.279 -16.158 45.042 1.00 85.93 C
ANISOU 2542 C THR A 272 7421 13606 11620 151 27 1088 C
ATOM 2543 O THR A 272 -4.588 -15.862 46.016 1.00 85.80 O
ANISOU 2543 O THR A 272 7532 13542 11526 213 -3 1049 O
ATOM 2544 CB THR A 272 -4.968 -14.858 42.855 1.00 88.49 C
ANISOU 2544 CB THR A 272 7786 13860 11977 1 -51 966 C
ATOM 2545 OG1 THR A 272 -4.302 -14.881 41.592 1.00 87.37 O
ANISOU 2545 OG1 THR A 272 7609 13671 11915 -152 -103 891 O
ATOM 2546 CG2 THR A 272 -4.630 -13.552 43.575 1.00 86.85 C
ANISOU 2546 CG2 THR A 272 7775 13589 11634 113 -85 917 C
ATOM 2547 N PRO A 273 -6.582 -16.553 45.204 1.00 83.26 N
ANISOU 2547 N PRO A 273 6975 13367 11294 236 113 1219 N
ATOM 2548 CA PRO A 273 -7.182 -16.565 46.559 1.00 84.17 C
ANISOU 2548 CA PRO A 273 7129 13537 11315 422 188 1318 C
ATOM 2549 C PRO A 273 -6.471 -17.510 47.528 1.00 87.70 C
ANISOU 2549 C PRO A 273 7563 13975 11785 413 181 1319 C
ATOM 2550 O PRO A 273 -6.413 -17.217 48.720 1.00 88.38 O
ANISOU 2550 O PRO A 273 7765 14062 11754 561 206 1339 O
ATOM 2551 CB PRO A 273 -8.626 -17.024 46.321 1.00 86.44 C
ANISOU 2551 CB PRO A 273 7249 13934 11662 473 275 1479 C
ATOM 2552 CG PRO A 273 -8.609 -17.686 45.002 1.00 90.12 C
ANISOU 2552 CG PRO A 273 7570 14393 12277 278 225 1457 C
ATOM 2553 CD PRO A 273 -7.585 -16.947 44.195 1.00 84.87 C
ANISOU 2553 CD PRO A 273 7021 13634 11590 177 142 1297 C
ATOM 2554 N GLY A 274 -5.922 -18.602 47.005 1.00 82.57 N
ANISOU 2554 N GLY A 274 6784 13312 11277 246 147 1297 N
ATOM 2555 CA GLY A 274 -5.179 -19.575 47.793 1.00 81.84 C
ANISOU 2555 CA GLY A 274 6662 13207 11226 216 137 1297 C
ATOM 2556 C GLY A 274 -3.808 -19.084 48.200 1.00 84.20 C
ANISOU 2556 C GLY A 274 7117 13410 11467 186 54 1175 C
ATOM 2557 O GLY A 274 -3.338 -19.415 49.290 1.00 83.82 O
ANISOU 2557 O GLY A 274 7116 13355 11376 242 50 1186 O
ATOM 2558 N LEU A 275 -3.157 -18.289 47.325 1.00 79.77 N
ANISOU 2558 N LEU A 275 6630 12774 10906 96 -19 1069 N
ATOM 2559 CA LEU A 275 -1.831 -17.712 47.568 1.00 79.03 C
ANISOU 2559 CA LEU A 275 6675 12579 10776 50 -117 966 C
ATOM 2560 C LEU A 275 -1.930 -16.476 48.473 1.00 83.22 C
ANISOU 2560 C LEU A 275 7413 13072 11135 206 -146 945 C
ATOM 2561 O LEU A 275 -1.000 -16.220 49.240 1.00 83.07 O
ANISOU 2561 O LEU A 275 7518 12981 11063 214 -226 895 O
ATOM 2562 CB LEU A 275 -1.122 -17.362 46.251 1.00 78.21 C
ANISOU 2562 CB LEU A 275 6556 12410 10749 -102 -179 883 C
ATOM 2563 CG LEU A 275 -0.607 -18.548 45.425 1.00 82.09 C
ANISOU 2563 CG LEU A 275 6893 12903 11394 -259 -174 877 C
ATOM 2564 CD1 LEU A 275 -0.421 -18.158 43.986 1.00 81.73 C
ANISOU 2564 CD1 LEU A 275 6827 12827 11401 -362 -197 823 C
ATOM 2565 CD2 LEU A 275 0.691 -19.113 45.987 1.00 84.48 C
ANISOU 2565 CD2 LEU A 275 7203 13150 11746 -327 -223 850 C
ATOM 2566 N VAL A 276 -3.059 -15.727 48.401 1.00 79.81 N
ANISOU 2566 N VAL A 276 7025 12685 10614 335 -86 987 N
ATOM 2567 CA VAL A 276 -3.330 -14.557 49.252 1.00 80.40 C
ANISOU 2567 CA VAL A 276 7312 12725 10509 513 -97 975 C
ATOM 2568 C VAL A 276 -3.613 -15.085 50.676 1.00 84.83 C
ANISOU 2568 C VAL A 276 7912 13335 10983 668 -40 1050 C
ATOM 2569 O VAL A 276 -3.207 -14.459 51.659 1.00 84.95 O
ANISOU 2569 O VAL A 276 8129 13287 10859 777 -93 1009 O
ATOM 2570 CB VAL A 276 -4.478 -13.664 48.682 1.00 84.41 C
ANISOU 2570 CB VAL A 276 7842 13272 10958 609 -35 1010 C
ATOM 2571 CG1 VAL A 276 -4.971 -12.636 49.698 1.00 85.45 C
ANISOU 2571 CG1 VAL A 276 8189 13385 10893 835 -13 1024 C
ATOM 2572 CG2 VAL A 276 -4.036 -12.959 47.403 1.00 83.42 C
ANISOU 2572 CG2 VAL A 276 7722 13083 10892 471 -108 923 C
ATOM 2573 N LEU A 277 -4.245 -16.278 50.764 1.00 81.22 N
ANISOU 2573 N LEU A 277 7263 12982 10616 667 58 1159 N
ATOM 2574 CA LEU A 277 -4.562 -16.981 52.009 1.00 81.86 C
ANISOU 2574 CA LEU A 277 7332 13125 10645 800 128 1254 C
ATOM 2575 C LEU A 277 -3.278 -17.354 52.757 1.00 85.79 C
ANISOU 2575 C LEU A 277 7907 13551 11136 740 35 1183 C
ATOM 2576 O LEU A 277 -3.271 -17.322 53.985 1.00 86.30 O
ANISOU 2576 O LEU A 277 8092 13620 11077 888 48 1211 O
ATOM 2577 CB LEU A 277 -5.393 -18.238 51.703 1.00 81.60 C
ANISOU 2577 CB LEU A 277 7046 13205 10755 760 228 1387 C
ATOM 2578 CG LEU A 277 -6.117 -18.914 52.866 1.00 87.13 C
ANISOU 2578 CG LEU A 277 7692 14002 11412 927 338 1537 C
ATOM 2579 CD1 LEU A 277 -7.394 -18.178 53.235 1.00 88.44 C
ANISOU 2579 CD1 LEU A 277 7909 14241 11454 1152 449 1652 C
ATOM 2580 CD2 LEU A 277 -6.473 -20.321 52.503 1.00 89.14 C
ANISOU 2580 CD2 LEU A 277 7691 14327 11851 816 383 1639 C
ATOM 2581 N LEU A 278 -2.198 -17.689 52.015 1.00 81.55 N
ANISOU 2581 N LEU A 278 7309 12947 10728 533 -57 1097 N
ATOM 2582 CA LEU A 278 -0.878 -18.022 52.561 1.00 81.35 C
ANISOU 2582 CA LEU A 278 7338 12847 10724 448 -157 1036 C
ATOM 2583 C LEU A 278 -0.234 -16.781 53.185 1.00 87.33 C
ANISOU 2583 C LEU A 278 8354 13498 11331 518 -273 951 C
ATOM 2584 O LEU A 278 0.424 -16.895 54.217 1.00 87.62 O
ANISOU 2584 O LEU A 278 8496 13493 11303 556 -337 938 O
ATOM 2585 CB LEU A 278 0.038 -18.613 51.472 1.00 79.96 C
ANISOU 2585 CB LEU A 278 7025 12631 10727 222 -210 984 C
ATOM 2586 CG LEU A 278 -0.269 -20.036 50.987 1.00 83.62 C
ANISOU 2586 CG LEU A 278 7256 13169 11348 129 -129 1052 C
ATOM 2587 CD1 LEU A 278 0.342 -20.284 49.626 1.00 82.77 C
ANISOU 2587 CD1 LEU A 278 7050 13018 11380 -56 -165 994 C
ATOM 2588 CD2 LEU A 278 0.220 -21.090 51.977 1.00 85.92 C
ANISOU 2588 CD2 LEU A 278 7496 13478 11673 130 -121 1096 C
ATOM 2589 N LEU A 279 -0.444 -15.599 52.565 1.00 84.93 N
ANISOU 2589 N LEU A 279 8157 13143 10969 535 -310 896 N
ATOM 2590 CA LEU A 279 0.062 -14.309 53.040 1.00 86.06 C
ANISOU 2590 CA LEU A 279 8559 13170 10972 599 -433 814 C
ATOM 2591 C LEU A 279 -0.693 -13.866 54.300 1.00 93.28 C
ANISOU 2591 C LEU A 279 9661 14104 11678 849 -385 851 C
ATOM 2592 O LEU A 279 -0.066 -13.403 55.253 1.00 93.80 O
ANISOU 2592 O LEU A 279 9937 14081 11623 914 -491 802 O
ATOM 2593 CB LEU A 279 -0.051 -13.231 51.942 1.00 85.70 C
ANISOU 2593 CB LEU A 279 8553 13071 10939 545 -472 756 C
ATOM 2594 CG LEU A 279 0.810 -13.403 50.683 1.00 88.94 C
ANISOU 2594 CG LEU A 279 8822 13442 11528 317 -532 713 C
ATOM 2595 CD1 LEU A 279 0.301 -12.529 49.558 1.00 88.65 C
ANISOU 2595 CD1 LEU A 279 8782 13400 11503 297 -516 688 C
ATOM 2596 CD2 LEU A 279 2.273 -13.097 50.956 1.00 91.64 C
ANISOU 2596 CD2 LEU A 279 9263 13658 11900 205 -699 649 C
ATOM 2597 N LEU A 280 -2.032 -14.043 54.317 1.00 91.77 N
ANISOU 2597 N LEU A 280 9394 14028 11447 993 -225 948 N
ATOM 2598 CA LEU A 280 -2.908 -13.694 55.447 1.00 93.88 C
ANISOU 2598 CA LEU A 280 9814 14338 11519 1259 -138 1014 C
ATOM 2599 C LEU A 280 -2.726 -14.661 56.637 1.00100.51 C
ANISOU 2599 C LEU A 280 10639 15226 12326 1332 -104 1078 C
ATOM 2600 O LEU A 280 -3.179 -14.365 57.746 1.00101.53 O
ANISOU 2600 O LEU A 280 10936 15368 12271 1558 -56 1119 O
ATOM 2601 CB LEU A 280 -4.388 -13.686 55.008 1.00 93.97 C
ANISOU 2601 CB LEU A 280 9701 14471 11534 1374 31 1131 C
ATOM 2602 CG LEU A 280 -4.829 -12.609 54.009 1.00 98.39 C
ANISOU 2602 CG LEU A 280 10302 14998 12083 1364 24 1091 C
ATOM 2603 CD1 LEU A 280 -6.137 -12.985 53.358 1.00 98.42 C
ANISOU 2603 CD1 LEU A 280 10093 15136 12166 1400 178 1224 C
ATOM 2604 CD2 LEU A 280 -4.947 -11.241 54.666 1.00102.17 C
ANISOU 2604 CD2 LEU A 280 11092 15389 12340 1562 -15 1037 C
ATOM 2605 N ASP A 281 -2.075 -15.812 56.399 1.00 97.68 N
ANISOU 2605 N ASP A 281 10083 14891 12140 1152 -123 1088 N
ATOM 2606 CA ASP A 281 -1.820 -16.833 57.412 1.00 98.58 C
ANISOU 2606 CA ASP A 281 10149 15052 12255 1190 -95 1151 C
ATOM 2607 C ASP A 281 -0.686 -16.420 58.359 1.00104.70 C
ANISOU 2607 C ASP A 281 11155 15712 12914 1205 -247 1063 C
ATOM 2608 O ASP A 281 -0.751 -16.722 59.549 1.00105.37 O
ANISOU 2608 O ASP A 281 11329 15825 12883 1353 -219 1111 O
ATOM 2609 CB ASP A 281 -1.471 -18.172 56.730 1.00 99.10 C
ANISOU 2609 CB ASP A 281 9933 15169 12553 982 -71 1186 C
ATOM 2610 CG ASP A 281 -1.337 -19.350 57.673 1.00109.37 C
ANISOU 2610 CG ASP A 281 11140 16534 13881 1014 -20 1270 C
ATOM 2611 OD1 ASP A 281 -2.322 -19.673 58.363 1.00111.52 O1-
ANISOU 2611 OD1 ASP A 281 11378 16907 14088 1191 110 1392 O1-
ATOM 2612 OD2 ASP A 281 -0.275 -19.991 57.666 1.00112.78 O
ANISOU 2612 OD2 ASP A 281 11512 16922 14417 860 -100 1230 O
ATOM 2613 N VAL A 282 0.337 -15.737 57.834 1.00101.98 N
ANISOU 2613 N VAL A 282 10904 15239 12604 1054 -413 945 N
ATOM 2614 CA VAL A 282 1.525 -15.348 58.590 1.00103.17 C
ANISOU 2614 CA VAL A 282 11258 15264 12679 1026 -593 866 C
ATOM 2615 C VAL A 282 1.592 -13.821 58.828 1.00110.39 C
ANISOU 2615 C VAL A 282 12484 16051 13407 1136 -712 777 C
ATOM 2616 O VAL A 282 2.205 -13.405 59.811 1.00111.05 O
ANISOU 2616 O VAL A 282 12801 16041 13353 1205 -842 731 O
ATOM 2617 CB VAL A 282 2.790 -15.854 57.849 1.00105.74 C
ANISOU 2617 CB VAL A 282 11439 15529 13209 757 -709 822 C
ATOM 2618 CG1 VAL A 282 2.773 -17.377 57.759 1.00104.54 C
ANISOU 2618 CG1 VAL A 282 11009 15488 13224 666 -596 905 C
ATOM 2619 CG2 VAL A 282 2.864 -15.267 56.446 1.00104.60 C
ANISOU 2619 CG2 VAL A 282 11243 15333 13168 616 -751 765 C
ATOM 2620 N CYS A 283 0.971 -12.999 57.955 1.00108.75 N
ANISOU 2620 N CYS A 283 12290 15836 13195 1150 -676 753 N
ATOM 2621 CA CYS A 283 1.026 -11.536 58.073 1.00110.75 C
ANISOU 2621 CA CYS A 283 12831 15961 13289 1242 -790 667 C
ATOM 2622 C CYS A 283 -0.293 -10.940 58.622 1.00117.70 C
ANISOU 2622 C CYS A 283 13863 16896 13961 1530 -650 714 C
ATOM 2623 O CYS A 283 -0.346 -9.728 58.860 1.00118.40 O
ANISOU 2623 O CYS A 283 14224 16874 13887 1645 -734 645 O
ATOM 2624 CB CYS A 283 1.393 -10.903 56.732 1.00110.29 C
ANISOU 2624 CB CYS A 283 12704 15837 13364 1060 -864 607 C
ATOM 2625 SG CYS A 283 2.984 -11.457 56.057 1.00113.09 S
ANISOU 2625 SG CYS A 283 12888 16123 13957 744 -1015 572 S
ATOM 2626 N CYS A 284 -1.333 -11.770 58.844 1.00115.82 N
ANISOU 2626 N CYS A 284 13460 16819 13729 1650 -446 837 N
ATOM 2627 CA CYS A 284 -2.621 -11.310 59.370 1.00117.79 C
ANISOU 2627 CA CYS A 284 13821 17138 13795 1935 -289 915 C
ATOM 2628 C CYS A 284 -3.080 -12.250 60.529 1.00123.00 C
ANISOU 2628 C CYS A 284 14440 17913 14380 2109 -157 1036 C
ATOM 2629 O CYS A 284 -3.996 -13.060 60.358 1.00122.10 O
ANISOU 2629 O CYS A 284 14089 17949 14355 2146 21 1171 O
ATOM 2630 CB CYS A 284 -3.650 -11.217 58.240 1.00117.68 C
ANISOU 2630 CB CYS A 284 13613 17215 13885 1914 -154 979 C
ATOM 2631 SG CYS A 284 -5.338 -10.757 58.737 1.00123.35 S
ANISOU 2631 SG CYS A 284 14396 18047 14425 2252 69 1120 S
ATOM 2632 N PRO A 285 -2.477 -12.134 61.735 1.00121.25 N
ANISOU 2632 N PRO A 285 14452 17622 13995 2218 -246 997 N
ATOM 2633 CA PRO A 285 -2.904 -12.989 62.851 1.00122.02 C
ANISOU 2633 CA PRO A 285 14517 17832 14012 2395 -114 1118 C
ATOM 2634 C PRO A 285 -3.976 -12.299 63.709 1.00127.94 C
ANISOU 2634 C PRO A 285 15490 18617 14503 2749 22 1189 C
ATOM 2635 O PRO A 285 -3.756 -11.189 64.202 1.00129.04 O
ANISOU 2635 O PRO A 285 15978 18626 14427 2889 -83 1090 O
ATOM 2636 CB PRO A 285 -1.605 -13.214 63.633 1.00124.13 C
ANISOU 2636 CB PRO A 285 14924 17998 14243 2314 -297 1033 C
ATOM 2637 CG PRO A 285 -0.640 -12.111 63.168 1.00128.55 C
ANISOU 2637 CG PRO A 285 15687 18369 14787 2174 -530 869 C
ATOM 2638 CD PRO A 285 -1.349 -11.274 62.138 1.00123.66 C
ANISOU 2638 CD PRO A 285 15056 17740 14188 2178 -481 849 C
ATOM 2639 N GLN A 286 -5.153 -12.959 63.857 1.00124.56 N
ANISOU 2639 N GLN A 286 14868 18364 14096 2902 255 1373 N
ATOM 2640 CA GLN A 286 -6.343 -12.550 64.634 1.00126.10 C
ANISOU 2640 CA GLN A 286 15189 18641 14082 3252 444 1503 C
ATOM 2641 C GLN A 286 -7.275 -11.550 63.887 1.00129.80 C
ANISOU 2641 C GLN A 286 15650 19128 14538 3334 540 1537 C
ATOM 2642 O GLN A 286 -8.320 -11.182 64.445 1.00130.82 O
ANISOU 2642 O GLN A 286 15810 19356 14541 3613 733 1685 O
ATOM 2643 CB GLN A 286 -5.994 -11.975 66.022 1.00129.60 C
ANISOU 2643 CB GLN A 286 16049 18980 14212 3508 375 1434 C
ATOM 2644 CG GLN A 286 -5.440 -13.009 67.001 1.00144.22 C
ANISOU 2644 CG GLN A 286 17914 20861 16024 3536 353 1466 C
ATOM 2645 CD GLN A 286 -5.034 -12.361 68.298 1.00163.59 C
ANISOU 2645 CD GLN A 286 20809 23183 18166 3757 241 1369 C
ATOM 2646 OE1 GLN A 286 -5.869 -11.995 69.130 1.00161.34 O
ANISOU 2646 OE1 GLN A 286 20750 22923 17631 4096 369 1437 O
ATOM 2647 NE2 GLN A 286 -3.736 -12.202 68.491 1.00153.68 N
ANISOU 2647 NE2 GLN A 286 19694 21782 16914 3578 -6 1214 N
ATOM 2648 N CYS A 287 -6.945 -11.156 62.642 1.00124.75 N
ANISOU 2648 N CYS A 287 14965 18406 14027 3109 422 1420 N
ATOM 2649 CA CYS A 287 -7.821 -10.248 61.884 1.00124.53 C
ANISOU 2649 CA CYS A 287 14929 18395 13993 3174 504 1450 C
ATOM 2650 C CYS A 287 -8.976 -11.041 61.238 1.00127.08 C
ANISOU 2650 C CYS A 287 14866 18899 14521 3124 690 1637 C
ATOM 2651 O CYS A 287 -10.109 -10.546 61.218 1.00127.44 O
ANISOU 2651 O CYS A 287 14892 19023 14508 3312 847 1761 O
ATOM 2652 CB CYS A 287 -7.062 -9.419 60.843 1.00123.84 C
ANISOU 2652 CB CYS A 287 14935 18153 13964 2962 311 1267 C
ATOM 2653 SG CYS A 287 -5.323 -9.890 60.586 1.00126.20 S
ANISOU 2653 SG CYS A 287 15211 18325 14413 2623 54 1099 S
ATOM 2654 N ASP A 288 -8.698 -12.271 60.738 1.00121.75 N
ANISOU 2654 N ASP A 288 13897 18280 14082 2874 663 1658 N
ATOM 2655 CA ASP A 288 -9.689 -13.141 60.092 1.00120.38 C
ANISOU 2655 CA ASP A 288 13362 18250 14126 2774 788 1813 C
ATOM 2656 C ASP A 288 -9.299 -14.626 60.211 1.00121.94 C
ANISOU 2656 C ASP A 288 13323 18524 14482 2649 805 1888 C
ATOM 2657 O ASP A 288 -8.111 -14.962 60.167 1.00120.48 O
ANISOU 2657 O ASP A 288 13188 18262 14327 2504 670 1769 O
ATOM 2658 CB ASP A 288 -9.843 -12.756 58.609 1.00120.72 C
ANISOU 2658 CB ASP A 288 13282 18243 14342 2514 692 1716 C
ATOM 2659 CG ASP A 288 -11.058 -13.335 57.938 1.00130.36 C
ANISOU 2659 CG ASP A 288 14186 19594 15750 2443 811 1870 C
ATOM 2660 OD1 ASP A 288 -12.187 -12.952 58.318 1.00131.75 O
ANISOU 2660 OD1 ASP A 288 14352 19851 15858 2642 953 2011 O
ATOM 2661 OD2 ASP A 288 -10.886 -14.133 57.001 1.00134.91 O1-
ANISOU 2661 OD2 ASP A 288 14533 20185 16541 2188 754 1852 O1-
ATOM 2662 N VAL A 289 -10.316 -15.503 60.353 1.00117.72 N
ANISOU 2662 N VAL A 289 12525 18142 14060 2703 967 2098 N
ATOM 2663 CA VAL A 289 -10.164 -16.960 60.468 1.00116.42 C
ANISOU 2663 CA VAL A 289 12114 18064 14056 2609 1007 2207 C
ATOM 2664 C VAL A 289 -9.882 -17.565 59.085 1.00116.78 C
ANISOU 2664 C VAL A 289 11926 18084 14361 2269 901 2133 C
ATOM 2665 O VAL A 289 -10.518 -17.144 58.116 1.00115.74 O
ANISOU 2665 O VAL A 289 11705 17950 14320 2167 890 2120 O
ATOM 2666 CB VAL A 289 -11.409 -17.649 61.104 1.00121.42 C
ANISOU 2666 CB VAL A 289 12554 18864 14718 2805 1217 2482 C
ATOM 2667 CG1 VAL A 289 -11.035 -19.001 61.709 1.00121.20 C
ANISOU 2667 CG1 VAL A 289 12330 18916 14805 2769 1262 2603 C
ATOM 2668 CG2 VAL A 289 -12.120 -16.762 62.123 1.00123.27 C
ANISOU 2668 CG2 VAL A 289 13018 19127 14691 3164 1348 2569 C
ATOM 2669 N LEU A 290 -8.984 -18.577 58.997 1.00111.07 N
ANISOU 2669 N LEU A 290 11110 17339 13752 2101 825 2085 N
ATOM 2670 CA LEU A 290 -8.666 -19.251 57.725 1.00108.46 C
ANISOU 2670 CA LEU A 290 10565 16985 13659 1800 741 2026 C
ATOM 2671 C LEU A 290 -9.521 -20.527 57.591 1.00111.08 C
ANISOU 2671 C LEU A 290 10600 17429 14178 1746 830 2204 C
ATOM 2672 O LEU A 290 -9.000 -21.648 57.505 1.00109.18 O
ANISOU 2672 O LEU A 290 10226 17166 14092 1551 766 2166 O
ATOM 2673 CB LEU A 290 -7.169 -19.564 57.603 1.00107.29 C
ANISOU 2673 CB LEU A 290 10509 16712 13543 1602 573 1830 C
ATOM 2674 CG LEU A 290 -6.251 -18.353 57.551 1.00112.22 C
ANISOU 2674 CG LEU A 290 11415 17214 14009 1632 462 1664 C
ATOM 2675 CD1 LEU A 290 -5.522 -18.162 58.856 1.00113.28 C
ANISOU 2675 CD1 LEU A 290 11765 17283 13993 1721 391 1599 C
ATOM 2676 CD2 LEU A 290 -5.295 -18.456 56.427 1.00113.38 C
ANISOU 2676 CD2 LEU A 290 11527 17271 14279 1387 337 1524 C
ATOM 2677 N ALA A 291 -10.858 -20.336 57.599 1.00108.39 N
ANISOU 2677 N ALA A 291 10150 17205 13828 1920 978 2410 N
ATOM 2678 CA ALA A 291 -11.843 -21.416 57.502 1.00108.07 C
ANISOU 2678 CA ALA A 291 9818 17273 13969 1888 1065 2616 C
ATOM 2679 C ALA A 291 -11.938 -21.936 56.076 1.00109.70 C
ANISOU 2679 C ALA A 291 9810 17475 14396 1651 1009 2619 C
ATOM 2680 O ALA A 291 -11.959 -23.152 55.873 1.00108.73 O
ANISOU 2680 O ALA A 291 9484 17367 14461 1490 982 2670 O
ATOM 2681 CB ALA A 291 -13.208 -20.931 57.974 1.00110.64 C
ANISOU 2681 CB ALA A 291 10107 17724 14207 2169 1242 2854 C
ATOM 2682 N TYR A 292 -11.982 -21.018 55.087 1.00104.95 N
ANISOU 2682 N TYR A 292 9264 16847 13767 1630 984 2561 N
ATOM 2683 CA TYR A 292 -12.052 -21.356 53.669 1.00103.34 C
ANISOU 2683 CA TYR A 292 8891 16630 13742 1418 921 2550 C
ATOM 2684 C TYR A 292 -10.674 -21.812 53.162 1.00103.31 C
ANISOU 2684 C TYR A 292 8942 16504 13808 1167 767 2317 C
ATOM 2685 O TYR A 292 -10.024 -21.129 52.364 1.00102.02 O
ANISOU 2685 O TYR A 292 8896 16263 13606 1084 687 2160 O
ATOM 2686 CB TYR A 292 -12.603 -20.196 52.821 1.00105.43 C
ANISOU 2686 CB TYR A 292 9189 16922 13946 1509 965 2597 C
ATOM 2687 CG TYR A 292 -12.334 -18.816 53.367 1.00107.88 C
ANISOU 2687 CG TYR A 292 9788 17172 14028 1663 964 2467 C
ATOM 2688 CD1 TYR A 292 -11.117 -18.185 53.143 1.00108.76 C
ANISOU 2688 CD1 TYR A 292 10039 17172 14112 1526 842 2253 C
ATOM 2689 CD2 TYR A 292 -13.318 -18.118 54.058 1.00110.40 C
ANISOU 2689 CD2 TYR A 292 10230 17550 14166 1956 1092 2583 C
ATOM 2690 CE1 TYR A 292 -10.874 -16.901 53.620 1.00110.15 C
ANISOU 2690 CE1 TYR A 292 10478 17283 14091 1660 828 2144 C
ATOM 2691 CE2 TYR A 292 -13.093 -16.828 54.525 1.00111.83 C
ANISOU 2691 CE2 TYR A 292 10695 17661 14133 2101 1081 2461 C
ATOM 2692 CZ TYR A 292 -11.866 -16.227 54.310 1.00118.27 C
ANISOU 2692 CZ TYR A 292 11646 18357 14935 1945 942 2242 C
ATOM 2693 OH TYR A 292 -11.632 -14.954 54.752 1.00119.80 O
ANISOU 2693 OH TYR A 292 12117 18472 14929 2081 919 2131 O
ATOM 2694 N GLU A 293 -10.246 -23.002 53.627 1.00 97.75 N
ANISOU 2694 N GLU A 293 8136 15790 13213 1059 737 2318 N
ATOM 2695 CA GLU A 293 -8.973 -23.591 53.229 1.00 95.18 C
ANISOU 2695 CA GLU A 293 7822 15366 12974 839 617 2147 C
ATOM 2696 C GLU A 293 -9.248 -24.796 52.305 1.00 96.42 C
ANISOU 2696 C GLU A 293 7750 15533 13353 648 585 2204 C
ATOM 2697 O GLU A 293 -8.516 -24.972 51.338 1.00 94.80 O
ANISOU 2697 O GLU A 293 7551 15248 13221 465 491 2066 O
ATOM 2698 CB GLU A 293 -8.069 -23.929 54.439 1.00 96.45 C
ANISOU 2698 CB GLU A 293 8072 15495 13081 863 597 2088 C
ATOM 2699 CG GLU A 293 -8.150 -25.293 55.108 1.00107.36 C
ANISOU 2699 CG GLU A 293 9292 16941 14560 880 656 2232 C
ATOM 2700 CD GLU A 293 -6.955 -25.682 55.967 1.00126.63 C
ANISOU 2700 CD GLU A 293 11812 19334 16968 858 612 2150 C
ATOM 2701 OE1 GLU A 293 -6.232 -24.800 56.494 1.00118.38 O
ANISOU 2701 OE1 GLU A 293 10979 18220 15780 895 553 2013 O
ATOM 2702 OE2 GLU A 293 -6.750 -26.908 56.103 1.00120.60 O1-
ANISOU 2702 OE2 GLU A 293 10893 18597 16334 792 629 2228 O1-
ATOM 2703 N LYS A 294 -10.327 -25.565 52.557 1.00 92.35 N
ANISOU 2703 N LYS A 294 7040 15109 12940 694 658 2413 N
ATOM 2704 CA LYS A 294 -10.746 -26.708 51.740 1.00 91.08 C
ANISOU 2704 CA LYS A 294 6663 14951 12993 521 614 2492 C
ATOM 2705 C LYS A 294 -11.356 -26.244 50.402 1.00 92.71 C
ANISOU 2705 C LYS A 294 6838 15145 13242 437 567 2476 C
ATOM 2706 O LYS A 294 -11.202 -26.930 49.389 1.00 91.24 O
ANISOU 2706 O LYS A 294 6567 14905 13195 244 478 2427 O
ATOM 2707 CB LYS A 294 -11.729 -27.623 52.493 1.00 94.65 C
ANISOU 2707 CB LYS A 294 6914 15501 13547 601 697 2741 C
ATOM 2708 CG LYS A 294 -12.826 -26.959 53.343 1.00107.14 C
ANISOU 2708 CG LYS A 294 8478 17198 15032 847 830 2941 C
ATOM 2709 CD LYS A 294 -13.542 -27.975 54.268 1.00117.16 C
ANISOU 2709 CD LYS A 294 9548 18562 16406 931 917 3193 C
ATOM 2710 CE LYS A 294 -12.715 -28.363 55.475 1.00126.29 C
ANISOU 2710 CE LYS A 294 10783 19727 17473 1037 969 3176 C
ATOM 2711 NZ LYS A 294 -13.382 -29.398 56.303 1.00135.44 N1+
ANISOU 2711 NZ LYS A 294 11739 20982 18739 1122 1059 3432 N1+
ATOM 2712 N PHE A 295 -12.023 -25.078 50.404 1.00 88.94 N
ANISOU 2712 N PHE A 295 6441 14712 12640 585 625 2514 N
ATOM 2713 CA PHE A 295 -12.661 -24.475 49.233 1.00 88.37 C
ANISOU 2713 CA PHE A 295 6348 14638 12590 530 591 2511 C
ATOM 2714 C PHE A 295 -11.628 -23.982 48.205 1.00 89.82 C
ANISOU 2714 C PHE A 295 6668 14712 12748 374 482 2270 C
ATOM 2715 O PHE A 295 -11.782 -24.268 47.014 1.00 88.60 O
ANISOU 2715 O PHE A 295 6439 14523 12701 212 404 2238 O
ATOM 2716 CB PHE A 295 -13.566 -23.313 49.650 1.00 91.32 C
ANISOU 2716 CB PHE A 295 6795 15085 12816 758 697 2613 C
ATOM 2717 CG PHE A 295 -14.727 -23.679 50.545 1.00 94.57 C
ANISOU 2717 CG PHE A 295 7052 15617 13262 924 818 2884 C
ATOM 2718 CD1 PHE A 295 -15.953 -24.034 50.005 1.00 98.57 C
ANISOU 2718 CD1 PHE A 295 7353 16191 13908 893 829 3082 C
ATOM 2719 CD2 PHE A 295 -14.613 -23.597 51.928 1.00 97.61 C
ANISOU 2719 CD2 PHE A 295 7503 16051 13535 1122 921 2954 C
ATOM 2720 CE1 PHE A 295 -17.037 -24.337 50.832 1.00101.08 C
ANISOU 2720 CE1 PHE A 295 7514 16625 14268 1053 946 3359 C
ATOM 2721 CE2 PHE A 295 -15.695 -23.910 52.755 1.00102.03 C
ANISOU 2721 CE2 PHE A 295 7917 16729 14122 1294 1048 3223 C
ATOM 2722 CZ PHE A 295 -16.905 -24.257 52.201 1.00100.95 C
ANISOU 2722 CZ PHE A 295 7561 16661 14136 1261 1064 3430 C
ATOM 2723 N PHE A 296 -10.582 -23.252 48.655 1.00 85.45 N
ANISOU 2723 N PHE A 296 6312 14100 12053 424 472 2112 N
ATOM 2724 CA PHE A 296 -9.530 -22.721 47.779 1.00 83.89 C
ANISOU 2724 CA PHE A 296 6243 13803 11829 295 379 1904 C
ATOM 2725 C PHE A 296 -8.633 -23.840 47.230 1.00 86.05 C
ANISOU 2725 C PHE A 296 6450 14008 12238 93 299 1815 C
ATOM 2726 O PHE A 296 -8.044 -23.667 46.162 1.00 84.56 O
ANISOU 2726 O PHE A 296 6301 13749 12077 -40 226 1687 O
ATOM 2727 CB PHE A 296 -8.669 -21.665 48.496 1.00 85.66 C
ANISOU 2727 CB PHE A 296 6689 13979 11879 404 378 1786 C
ATOM 2728 CG PHE A 296 -9.333 -20.345 48.846 1.00 88.06 C
ANISOU 2728 CG PHE A 296 7119 14312 12028 584 432 1815 C
ATOM 2729 CD1 PHE A 296 -10.504 -19.940 48.213 1.00 91.47 C
ANISOU 2729 CD1 PHE A 296 7475 14797 12483 610 467 1906 C
ATOM 2730 CD2 PHE A 296 -8.751 -19.479 49.758 1.00 90.55 C
ANISOU 2730 CD2 PHE A 296 7640 14592 12173 727 440 1749 C
ATOM 2731 CE1 PHE A 296 -11.103 -18.718 48.527 1.00 93.04 C
ANISOU 2731 CE1 PHE A 296 7794 15019 12537 785 524 1936 C
ATOM 2732 CE2 PHE A 296 -9.348 -18.254 50.064 1.00 94.14 C
ANISOU 2732 CE2 PHE A 296 8234 15058 12475 901 486 1767 C
ATOM 2733 CZ PHE A 296 -10.522 -17.886 49.452 1.00 92.53 C
ANISOU 2733 CZ PHE A 296 7946 14913 12298 933 536 1862 C
ATOM 2734 N LEU A 297 -8.542 -24.980 47.951 1.00 82.42 N
ANISOU 2734 N LEU A 297 5890 13569 11859 82 320 1891 N
ATOM 2735 CA LEU A 297 -7.782 -26.169 47.552 1.00 81.30 C
ANISOU 2735 CA LEU A 297 5678 13366 11849 -86 259 1831 C
ATOM 2736 C LEU A 297 -8.456 -26.824 46.341 1.00 85.49 C
ANISOU 2736 C LEU A 297 6077 13885 12521 -225 206 1872 C
ATOM 2737 O LEU A 297 -7.773 -27.126 45.364 1.00 84.29 O
ANISOU 2737 O LEU A 297 5950 13653 12422 -371 134 1749 O
ATOM 2738 CB LEU A 297 -7.688 -27.168 48.734 1.00 81.59 C
ANISOU 2738 CB LEU A 297 5636 13437 11928 -36 306 1929 C
ATOM 2739 CG LEU A 297 -6.467 -28.090 48.885 1.00 85.49 C
ANISOU 2739 CG LEU A 297 6135 13862 12485 -142 266 1839 C
ATOM 2740 CD1 LEU A 297 -6.312 -29.049 47.743 1.00 85.21 C
ANISOU 2740 CD1 LEU A 297 6005 13766 12604 -327 199 1802 C
ATOM 2741 CD2 LEU A 297 -5.215 -27.334 49.161 1.00 87.76 C
ANISOU 2741 CD2 LEU A 297 6598 14090 12658 -130 238 1686 C
ATOM 2742 N LEU A 298 -9.796 -27.021 46.407 1.00 83.19 N
ANISOU 2742 N LEU A 298 5649 13671 12287 -175 238 2051 N
ATOM 2743 CA LEU A 298 -10.611 -27.617 45.344 1.00 83.46 C
ANISOU 2743 CA LEU A 298 5553 13698 12460 -301 171 2119 C
ATOM 2744 C LEU A 298 -10.701 -26.690 44.132 1.00 87.46 C
ANISOU 2744 C LEU A 298 6142 14173 12916 -354 120 2019 C
ATOM 2745 O LEU A 298 -10.734 -27.179 43.003 1.00 86.86 O
ANISOU 2745 O LEU A 298 6034 14040 12928 -503 30 1973 O
ATOM 2746 CB LEU A 298 -12.023 -27.955 45.856 1.00 84.78 C
ANISOU 2746 CB LEU A 298 5545 13963 12704 -219 220 2366 C
ATOM 2747 CG LEU A 298 -12.139 -29.119 46.851 1.00 90.11 C
ANISOU 2747 CG LEU A 298 6090 14671 13475 -193 259 2504 C
ATOM 2748 CD1 LEU A 298 -13.392 -29.003 47.690 1.00 91.65 C
ANISOU 2748 CD1 LEU A 298 6152 14986 13685 -37 352 2754 C
ATOM 2749 CD2 LEU A 298 -12.104 -30.458 46.148 1.00 92.57 C
ANISOU 2749 CD2 LEU A 298 6290 14913 13971 -384 155 2510 C
ATOM 2750 N LEU A 299 -10.715 -25.360 44.367 1.00 84.39 N
ANISOU 2750 N LEU A 299 5870 13813 12380 -228 172 1983 N
ATOM 2751 CA LEU A 299 -10.781 -24.320 43.333 1.00 84.16 C
ANISOU 2751 CA LEU A 299 5930 13761 12288 -255 136 1892 C
ATOM 2752 C LEU A 299 -9.551 -24.381 42.406 1.00 88.39 C
ANISOU 2752 C LEU A 299 6567 14192 12825 -399 59 1692 C
ATOM 2753 O LEU A 299 -9.699 -24.248 41.189 1.00 88.43 O
ANISOU 2753 O LEU A 299 6576 14164 12859 -498 -5 1641 O
ATOM 2754 CB LEU A 299 -10.888 -22.933 43.998 1.00 84.33 C
ANISOU 2754 CB LEU A 299 6075 13822 12144 -77 213 1889 C
ATOM 2755 CG LEU A 299 -11.262 -21.741 43.108 1.00 88.80 C
ANISOU 2755 CG LEU A 299 6712 14385 12641 -66 197 1844 C
ATOM 2756 CD1 LEU A 299 -12.725 -21.796 42.685 1.00 90.08 C
ANISOU 2756 CD1 LEU A 299 6731 14625 12872 -47 211 2021 C
ATOM 2757 CD2 LEU A 299 -11.012 -20.439 43.830 1.00 91.01 C
ANISOU 2757 CD2 LEU A 299 7156 14670 12753 97 256 1798 C
ATOM 2758 N ALA A 300 -8.357 -24.611 42.981 1.00 84.57 N
ANISOU 2758 N ALA A 300 6159 13660 12313 -405 65 1594 N
ATOM 2759 CA ALA A 300 -7.101 -24.734 42.244 1.00 83.76 C
ANISOU 2759 CA ALA A 300 6141 13464 12220 -523 9 1429 C
ATOM 2760 C ALA A 300 -6.974 -26.112 41.588 1.00 88.42 C
ANISOU 2760 C ALA A 300 6643 14007 12948 -665 -45 1426 C
ATOM 2761 O ALA A 300 -6.322 -26.235 40.550 1.00 87.54 O
ANISOU 2761 O ALA A 300 6584 13824 12853 -768 -96 1314 O
ATOM 2762 CB ALA A 300 -5.928 -24.494 43.179 1.00 84.09 C
ANISOU 2762 CB ALA A 300 6282 13475 12192 -472 32 1356 C
ATOM 2763 N GLU A 301 -7.592 -27.141 42.197 1.00 86.43 N
ANISOU 2763 N GLU A 301 6261 13789 12789 -663 -34 1553 N
ATOM 2764 CA GLU A 301 -7.596 -28.526 41.714 1.00 86.90 C
ANISOU 2764 CA GLU A 301 6236 13797 12985 -789 -92 1567 C
ATOM 2765 C GLU A 301 -8.420 -28.653 40.425 1.00 92.16 C
ANISOU 2765 C GLU A 301 6867 14440 13709 -884 -174 1582 C
ATOM 2766 O GLU A 301 -8.022 -29.390 39.521 1.00 91.90 O
ANISOU 2766 O GLU A 301 6855 14324 13737 -1004 -245 1506 O
ATOM 2767 CB GLU A 301 -8.158 -29.468 42.798 1.00 88.98 C
ANISOU 2767 CB GLU A 301 6361 14111 13335 -747 -58 1725 C
ATOM 2768 CG GLU A 301 -7.992 -30.952 42.501 1.00 99.38 C
ANISOU 2768 CG GLU A 301 7599 15363 14797 -870 -117 1740 C
ATOM 2769 CD GLU A 301 -8.664 -31.921 43.457 1.00119.71 C
ANISOU 2769 CD GLU A 301 10017 17986 17481 -844 -96 1917 C
ATOM 2770 OE1 GLU A 301 -9.283 -31.471 44.448 1.00117.53 O
ANISOU 2770 OE1 GLU A 301 9683 17807 17165 -713 -19 2047 O
ATOM 2771 OE2 GLU A 301 -8.580 -33.143 43.205 1.00111.67 O1-
ANISOU 2771 OE2 GLU A 301 8938 16905 16587 -949 -154 1930 O1-
ATOM 2772 N PHE A 302 -9.568 -27.937 40.349 1.00 89.62 N
ANISOU 2772 N PHE A 302 6496 14190 13364 -826 -166 1686 N
ATOM 2773 CA PHE A 302 -10.481 -27.944 39.201 1.00 90.20 C
ANISOU 2773 CA PHE A 302 6526 14255 13492 -908 -251 1727 C
ATOM 2774 C PHE A 302 -9.821 -27.337 37.946 1.00 93.08 C
ANISOU 2774 C PHE A 302 7029 14553 13783 -974 -299 1556 C
ATOM 2775 O PHE A 302 -10.203 -27.704 36.834 1.00 93.63 O
ANISOU 2775 O PHE A 302 7096 14576 13903 -1078 -393 1541 O
ATOM 2776 CB PHE A 302 -11.803 -27.188 39.491 1.00 93.04 C
ANISOU 2776 CB PHE A 302 6795 14718 13840 -812 -215 1896 C
ATOM 2777 CG PHE A 302 -12.766 -27.640 40.576 1.00 95.99 C
ANISOU 2777 CG PHE A 302 7001 15171 14298 -740 -170 2114 C
ATOM 2778 CD1 PHE A 302 -13.137 -28.977 40.698 1.00 99.83 C
ANISOU 2778 CD1 PHE A 302 7365 15627 14937 -834 -232 2204 C
ATOM 2779 CD2 PHE A 302 -13.389 -26.711 41.402 1.00 99.06 C
ANISOU 2779 CD2 PHE A 302 7355 15664 14618 -574 -67 2243 C
ATOM 2780 CE1 PHE A 302 -14.065 -29.377 41.665 1.00101.92 C
ANISOU 2780 CE1 PHE A 302 7463 15971 15292 -765 -186 2425 C
ATOM 2781 CE2 PHE A 302 -14.296 -27.118 42.387 1.00103.05 C
ANISOU 2781 CE2 PHE A 302 7703 16252 15201 -491 -11 2463 C
ATOM 2782 CZ PHE A 302 -14.625 -28.449 42.513 1.00101.67 C
ANISOU 2782 CZ PHE A 302 7392 16052 15186 -591 -71 2559 C
ATOM 2783 N ASN A 303 -8.840 -26.418 38.121 1.00 87.48 N
ANISOU 2783 N ASN A 303 6444 13835 12958 -914 -241 1435 N
ATOM 2784 CA ASN A 303 -8.131 -25.755 37.019 1.00 86.24 C
ANISOU 2784 CA ASN A 303 6414 13622 12732 -960 -269 1287 C
ATOM 2785 C ASN A 303 -7.327 -26.749 36.175 1.00 89.01 C
ANISOU 2785 C ASN A 303 6810 13874 13135 -1077 -327 1184 C
ATOM 2786 O ASN A 303 -7.213 -26.561 34.962 1.00 88.92 O
ANISOU 2786 O ASN A 303 6870 13817 13099 -1137 -378 1105 O
ATOM 2787 CB ASN A 303 -7.206 -24.664 37.542 1.00 86.17 C
ANISOU 2787 CB ASN A 303 6512 13618 12610 -873 -202 1205 C
ATOM 2788 CG ASN A 303 -6.508 -23.840 36.476 1.00104.78 C
ANISOU 2788 CG ASN A 303 8983 15929 14899 -906 -223 1080 C
ATOM 2789 OD1 ASN A 303 -5.299 -23.654 36.543 1.00 98.23 O
ANISOU 2789 OD1 ASN A 303 8222 15034 14067 -954 -227 978 O
ATOM 2790 ND2 ASN A 303 -7.214 -23.372 35.447 1.00 95.89 N
ANISOU 2790 ND2 ASN A 303 7872 14837 13724 -884 -236 1099 N
ATOM 2791 N SER A 304 -6.787 -27.806 36.815 1.00 84.34 N
ANISOU 2791 N SER A 304 6182 13251 12611 -1099 -315 1191 N
ATOM 2792 CA SER A 304 -6.021 -28.871 36.160 1.00 83.50 C
ANISOU 2792 CA SER A 304 6120 13048 12559 -1193 -357 1106 C
ATOM 2793 C SER A 304 -6.913 -29.658 35.180 1.00 86.43 C
ANISOU 2793 C SER A 304 6462 13373 13005 -1290 -466 1139 C
ATOM 2794 O SER A 304 -6.397 -30.293 34.261 1.00 85.79 O
ANISOU 2794 O SER A 304 6462 13201 12935 -1362 -517 1047 O
ATOM 2795 CB SER A 304 -5.411 -29.806 37.200 1.00 86.96 C
ANISOU 2795 CB SER A 304 6509 13472 13059 -1184 -317 1132 C
ATOM 2796 OG SER A 304 -4.521 -29.116 38.061 1.00 94.84 O
ANISOU 2796 OG SER A 304 7549 14499 13988 -1105 -238 1096 O
ATOM 2797 N ALA A 305 -8.249 -29.582 35.372 1.00 82.52 N
ANISOU 2797 N ALA A 305 5857 12940 12558 -1286 -503 1276 N
ATOM 2798 CA ALA A 305 -9.276 -30.203 34.535 1.00 82.84 C
ANISOU 2798 CA ALA A 305 5851 12945 12678 -1381 -627 1339 C
ATOM 2799 C ALA A 305 -9.889 -29.185 33.554 1.00 85.24 C
ANISOU 2799 C ALA A 305 6200 13274 12913 -1385 -669 1325 C
ATOM 2800 O ALA A 305 -10.438 -29.584 32.533 1.00 85.25 O
ANISOU 2800 O ALA A 305 6221 13221 12950 -1476 -787 1324 O
ATOM 2801 CB ALA A 305 -10.365 -30.800 35.412 1.00 84.49 C
ANISOU 2801 CB ALA A 305 5886 13210 13007 -1378 -645 1532 C
ATOM 2802 N MET A 306 -9.791 -27.876 33.872 1.00 80.33 N
ANISOU 2802 N MET A 306 5603 12729 12191 -1286 -579 1314 N
ATOM 2803 CA MET A 306 -10.326 -26.771 33.066 1.00 79.75 C
ANISOU 2803 CA MET A 306 5567 12690 12045 -1271 -599 1307 C
ATOM 2804 C MET A 306 -9.595 -26.594 31.735 1.00 82.50 C
ANISOU 2804 C MET A 306 6063 12959 12323 -1328 -643 1149 C
ATOM 2805 O MET A 306 -10.244 -26.241 30.753 1.00 82.49 O
ANISOU 2805 O MET A 306 6084 12957 12302 -1367 -716 1155 O
ATOM 2806 CB MET A 306 -10.263 -25.444 33.838 1.00 81.51 C
ANISOU 2806 CB MET A 306 5797 13000 12175 -1141 -487 1326 C
ATOM 2807 CG MET A 306 -11.345 -25.291 34.880 1.00 85.85 C
ANISOU 2807 CG MET A 306 6210 13645 12764 -1059 -443 1507 C
ATOM 2808 SD MET A 306 -11.171 -23.764 35.833 1.00 89.68 S
ANISOU 2808 SD MET A 306 6747 14211 13117 -887 -314 1510 S
ATOM 2809 CE MET A 306 -12.124 -22.642 34.826 1.00 86.90 C
ANISOU 2809 CE MET A 306 6409 13894 12715 -885 -349 1535 C
ATOM 2810 N ASN A 307 -8.255 -26.798 31.706 1.00 77.87 N
ANISOU 2810 N ASN A 307 5576 12313 11697 -1323 -594 1022 N
ATOM 2811 CA ASN A 307 -7.419 -26.634 30.508 1.00 77.16 C
ANISOU 2811 CA ASN A 307 5628 12153 11535 -1354 -610 883 C
ATOM 2812 C ASN A 307 -7.932 -27.496 29.314 1.00 80.95 C
ANISOU 2812 C ASN A 307 6156 12555 12046 -1453 -739 862 C
ATOM 2813 O ASN A 307 -8.226 -26.881 28.290 1.00 79.96 O
ANISOU 2813 O ASN A 307 6098 12429 11856 -1465 -782 826 O
ATOM 2814 CB ASN A 307 -5.939 -26.941 30.798 1.00 78.17 C
ANISOU 2814 CB ASN A 307 5826 12230 11644 -1332 -534 787 C
ATOM 2815 CG ASN A 307 -5.242 -25.943 31.699 1.00104.13 C
ANISOU 2815 CG ASN A 307 9111 15572 14881 -1246 -432 780 C
ATOM 2816 OD1 ASN A 307 -5.854 -25.041 32.289 1.00101.52 O
ANISOU 2816 OD1 ASN A 307 8732 15318 14524 -1186 -405 845 O
ATOM 2817 ND2 ASN A 307 -3.928 -26.083 31.823 1.00 94.10 N
ANISOU 2817 ND2 ASN A 307 7898 14257 13597 -1234 -376 706 N
ATOM 2818 N PRO A 308 -8.137 -28.848 29.396 1.00 78.60 N
ANISOU 2818 N PRO A 308 5831 12190 11842 -1524 -815 889 N
ATOM 2819 CA PRO A 308 -8.645 -29.582 28.217 1.00 79.80 C
ANISOU 2819 CA PRO A 308 6056 12252 12011 -1617 -960 862 C
ATOM 2820 C PRO A 308 -10.074 -29.184 27.815 1.00 85.85 C
ANISOU 2820 C PRO A 308 6749 13064 12804 -1660 -1066 970 C
ATOM 2821 O PRO A 308 -10.451 -29.377 26.659 1.00 86.38 O
ANISOU 2821 O PRO A 308 6905 13068 12845 -1725 -1186 931 O
ATOM 2822 CB PRO A 308 -8.599 -31.050 28.665 1.00 82.01 C
ANISOU 2822 CB PRO A 308 6302 12456 12403 -1677 -1015 892 C
ATOM 2823 CG PRO A 308 -7.637 -31.080 29.794 1.00 85.36 C
ANISOU 2823 CG PRO A 308 6685 12912 12835 -1608 -877 881 C
ATOM 2824 CD PRO A 308 -7.862 -29.787 30.503 1.00 80.14 C
ANISOU 2824 CD PRO A 308 5946 12375 12129 -1523 -781 938 C
ATOM 2825 N ILE A 309 -10.853 -28.611 28.750 1.00 82.92 N
ANISOU 2825 N ILE A 309 6223 12803 12481 -1616 -1020 1110 N
ATOM 2826 CA ILE A 309 -12.227 -28.150 28.516 1.00 83.75 C
ANISOU 2826 CA ILE A 309 6229 12970 12624 -1641 -1098 1246 C
ATOM 2827 C ILE A 309 -12.165 -26.859 27.671 1.00 87.70 C
ANISOU 2827 C ILE A 309 6815 13507 12999 -1598 -1069 1178 C
ATOM 2828 O ILE A 309 -12.987 -26.692 26.770 1.00 87.88 O
ANISOU 2828 O ILE A 309 6845 13524 13020 -1655 -1180 1214 O
ATOM 2829 CB ILE A 309 -12.985 -27.971 29.877 1.00 87.05 C
ANISOU 2829 CB ILE A 309 6456 13494 13123 -1578 -1028 1428 C
ATOM 2830 CG1 ILE A 309 -13.306 -29.331 30.586 1.00 88.37 C
ANISOU 2830 CG1 ILE A 309 6515 13624 13437 -1637 -1083 1529 C
ATOM 2831 CG2 ILE A 309 -14.289 -27.165 29.726 1.00 88.25 C
ANISOU 2831 CG2 ILE A 309 6501 13738 13294 -1562 -1058 1580 C
ATOM 2832 CD1 ILE A 309 -12.471 -30.609 30.330 1.00 96.78 C
ANISOU 2832 CD1 ILE A 309 7678 14557 14537 -1718 -1148 1415 C
ATOM 2833 N ILE A 310 -11.161 -25.989 27.929 1.00 84.14 N
ANISOU 2833 N ILE A 310 6434 13087 12449 -1507 -934 1081 N
ATOM 2834 CA ILE A 310 -10.936 -24.730 27.205 1.00 84.16 C
ANISOU 2834 CA ILE A 310 6520 13121 12335 -1458 -891 1013 C
ATOM 2835 C ILE A 310 -10.550 -25.036 25.738 1.00 90.18 C
ANISOU 2835 C ILE A 310 7436 13794 13036 -1522 -977 892 C
ATOM 2836 O ILE A 310 -11.142 -24.452 24.827 1.00 90.04 O
ANISOU 2836 O ILE A 310 7447 13791 12971 -1540 -1038 900 O
ATOM 2837 CB ILE A 310 -9.873 -23.835 27.918 1.00 86.09 C
ANISOU 2837 CB ILE A 310 6801 13403 12507 -1355 -741 947 C
ATOM 2838 CG1 ILE A 310 -10.421 -23.305 29.265 1.00 86.43 C
ANISOU 2838 CG1 ILE A 310 6722 13540 12578 -1272 -663 1068 C
ATOM 2839 CG2 ILE A 310 -9.412 -22.663 27.018 1.00 86.27 C
ANISOU 2839 CG2 ILE A 310 6930 13432 12417 -1320 -708 860 C
ATOM 2840 CD1 ILE A 310 -9.353 -22.849 30.283 1.00 93.98 C
ANISOU 2840 CD1 ILE A 310 7710 14508 13489 -1185 -544 1015 C
ATOM 2841 N TYR A 311 -9.591 -25.962 25.518 1.00 88.22 N
ANISOU 2841 N TYR A 311 7286 13451 12783 -1547 -980 789 N
ATOM 2842 CA TYR A 311 -9.136 -26.352 24.178 1.00 89.21 C
ANISOU 2842 CA TYR A 311 7579 13482 12835 -1584 -1046 671 C
ATOM 2843 C TYR A 311 -10.238 -27.073 23.373 1.00 95.76 C
ANISOU 2843 C TYR A 311 8426 14254 13705 -1685 -1232 713 C
ATOM 2844 O TYR A 311 -10.160 -27.106 22.145 1.00 95.83 O
ANISOU 2844 O TYR A 311 8579 14201 13630 -1708 -1305 631 O
ATOM 2845 CB TYR A 311 -7.890 -27.262 24.253 1.00 90.36 C
ANISOU 2845 CB TYR A 311 7819 13539 12975 -1573 -996 571 C
ATOM 2846 CG TYR A 311 -6.690 -26.691 24.980 1.00 91.18 C
ANISOU 2846 CG TYR A 311 7914 13681 13049 -1487 -833 531 C
ATOM 2847 CD1 TYR A 311 -6.057 -25.536 24.525 1.00 92.60 C
ANISOU 2847 CD1 TYR A 311 8154 13897 13134 -1422 -750 479 C
ATOM 2848 CD2 TYR A 311 -6.105 -27.375 26.042 1.00 91.50 C
ANISOU 2848 CD2 TYR A 311 7897 13710 13160 -1475 -773 546 C
ATOM 2849 CE1 TYR A 311 -4.932 -25.024 25.172 1.00 92.46 C
ANISOU 2849 CE1 TYR A 311 8128 13902 13100 -1356 -623 453 C
ATOM 2850 CE2 TYR A 311 -4.980 -26.874 26.697 1.00 91.33 C
ANISOU 2850 CE2 TYR A 311 7870 13716 13115 -1406 -642 516 C
ATOM 2851 CZ TYR A 311 -4.394 -25.700 26.255 1.00 98.26 C
ANISOU 2851 CZ TYR A 311 8803 14626 13906 -1350 -574 471 C
ATOM 2852 OH TYR A 311 -3.283 -25.209 26.898 1.00 98.55 O
ANISOU 2852 OH TYR A 311 8832 14679 13933 -1293 -466 454 O
ATOM 2853 N SER A 312 -11.249 -27.644 24.060 1.00 94.14 N
ANISOU 2853 N SER A 312 8076 14066 13626 -1744 -1312 848 N
ATOM 2854 CA SER A 312 -12.345 -28.391 23.440 1.00 96.04 C
ANISOU 2854 CA SER A 312 8309 14247 13935 -1856 -1509 916 C
ATOM 2855 C SER A 312 -13.346 -27.482 22.702 1.00101.49 C
ANISOU 2855 C SER A 312 8973 14997 14593 -1875 -1584 984 C
ATOM 2856 O SER A 312 -13.834 -27.881 21.641 1.00101.88 O
ANISOU 2856 O SER A 312 9114 14971 14626 -1957 -1749 965 O
ATOM 2857 CB SER A 312 -13.086 -29.216 24.486 1.00100.28 C
ANISOU 2857 CB SER A 312 8673 14794 14636 -1909 -1560 1068 C
ATOM 2858 OG SER A 312 -14.017 -30.101 23.886 1.00111.10 O
ANISOU 2858 OG SER A 312 10043 16080 16089 -2032 -1771 1133 O
ATOM 2859 N TYR A 313 -13.663 -26.285 23.249 1.00 98.44 N
ANISOU 2859 N TYR A 313 8471 14739 14193 -1798 -1470 1063 N
ATOM 2860 CA TYR A 313 -14.631 -25.387 22.615 1.00 99.30 C
ANISOU 2860 CA TYR A 313 8540 14912 14276 -1807 -1527 1141 C
ATOM 2861 C TYR A 313 -13.944 -24.241 21.827 1.00104.27 C
ANISOU 2861 C TYR A 313 9297 15567 14753 -1734 -1439 1020 C
ATOM 2862 O TYR A 313 -14.612 -23.608 21.005 1.00104.34 O
ANISOU 2862 O TYR A 313 9318 15606 14722 -1751 -1505 1052 O
ATOM 2863 CB TYR A 313 -15.627 -24.812 23.650 1.00100.45 C
ANISOU 2863 CB TYR A 313 8473 15180 14512 -1766 -1473 1336 C
ATOM 2864 CG TYR A 313 -15.118 -23.679 24.517 1.00101.13 C
ANISOU 2864 CG TYR A 313 8521 15364 14538 -1630 -1273 1329 C
ATOM 2865 CD1 TYR A 313 -14.451 -23.935 25.713 1.00102.32 C
ANISOU 2865 CD1 TYR A 313 8631 15529 14717 -1569 -1156 1322 C
ATOM 2866 CD2 TYR A 313 -15.390 -22.351 24.196 1.00101.72 C
ANISOU 2866 CD2 TYR A 313 8596 15517 14534 -1562 -1213 1345 C
ATOM 2867 CE1 TYR A 313 -14.016 -22.895 26.538 1.00102.06 C
ANISOU 2867 CE1 TYR A 313 8578 15573 14625 -1446 -995 1318 C
ATOM 2868 CE2 TYR A 313 -14.945 -21.302 25.003 1.00101.64 C
ANISOU 2868 CE2 TYR A 313 8568 15582 14469 -1438 -1047 1339 C
ATOM 2869 CZ TYR A 313 -14.263 -21.580 26.178 1.00107.97 C
ANISOU 2869 CZ TYR A 313 9344 16386 15292 -1381 -945 1324 C
ATOM 2870 OH TYR A 313 -13.839 -20.553 26.985 1.00107.63 O
ANISOU 2870 OH TYR A 313 9302 16403 15189 -1260 -802 1315 O
ATOM 2871 N ARG A 314 -12.639 -23.974 22.070 1.00101.16 N
ANISOU 2871 N ARG A 314 8990 15164 14285 -1655 -1296 895 N
ATOM 2872 CA ARG A 314 -11.913 -22.903 21.378 1.00100.99 C
ANISOU 2872 CA ARG A 314 9075 15163 14133 -1585 -1209 796 C
ATOM 2873 C ARG A 314 -11.211 -23.411 20.116 1.00106.76 C
ANISOU 2873 C ARG A 314 10002 15792 14771 -1609 -1265 656 C
ATOM 2874 O ARG A 314 -11.430 -22.839 19.044 1.00106.90 O
ANISOU 2874 O ARG A 314 10101 15813 14703 -1609 -1309 626 O
ATOM 2875 CB ARG A 314 -10.893 -22.217 22.304 1.00100.15 C
ANISOU 2875 CB ARG A 314 8948 15102 14001 -1486 -1032 759 C
ATOM 2876 CG ARG A 314 -11.497 -21.121 23.178 1.00111.92 C
ANISOU 2876 CG ARG A 314 10308 16702 15514 -1421 -956 868 C
ATOM 2877 CD ARG A 314 -11.768 -19.817 22.420 1.00127.03 C
ANISOU 2877 CD ARG A 314 12248 18672 17346 -1379 -935 871 C
ATOM 2878 NE ARG A 314 -12.478 -18.845 23.263 1.00141.09 N
ANISOU 2878 NE ARG A 314 13917 20547 19144 -1301 -853 975 N
ATOM 2879 CZ ARG A 314 -13.652 -18.274 22.982 1.00159.37 C
ANISOU 2879 CZ ARG A 314 16150 22932 21472 -1289 -881 1091 C
ATOM 2880 NH1 ARG A 314 -14.285 -18.562 21.852 1.00149.74 N
ANISOU 2880 NH1 ARG A 314 14937 21703 20253 -1362 -1002 1123 N
ATOM 2881 NH2 ARG A 314 -14.195 -17.412 23.831 1.00146.38 N1+
ANISOU 2881 NH2 ARG A 314 14424 21364 19830 -1195 -788 1178 N1+
ATOM 2882 N ASP A 315 -10.370 -24.463 20.235 1.00104.18 N
ANISOU 2882 N ASP A 315 9754 15375 14454 -1620 -1259 576 N
ATOM 2883 CA ASP A 315 -9.637 -25.016 19.093 1.00105.01 C
ANISOU 2883 CA ASP A 315 10062 15377 14461 -1618 -1294 446 C
ATOM 2884 C ASP A 315 -10.558 -25.895 18.254 1.00111.13 C
ANISOU 2884 C ASP A 315 10913 16066 15246 -1717 -1500 453 C
ATOM 2885 O ASP A 315 -11.185 -26.818 18.780 1.00111.33 O
ANISOU 2885 O ASP A 315 10865 16051 15383 -1796 -1604 520 O
ATOM 2886 CB ASP A 315 -8.386 -25.792 19.541 1.00106.52 C
ANISOU 2886 CB ASP A 315 10312 15504 14657 -1578 -1198 366 C
ATOM 2887 CG ASP A 315 -7.089 -25.012 19.380 1.00116.76 C
ANISOU 2887 CG ASP A 315 11635 16842 15887 -1476 -1018 311 C
ATOM 2888 OD1 ASP A 315 -6.946 -23.945 20.031 1.00116.81 O
ANISOU 2888 OD1 ASP A 315 11601 16931 15852 -1434 -961 336 O
ATOM 2889 OD2 ASP A 315 -6.215 -25.469 18.612 1.00123.27 O1-
ANISOU 2889 OD2 ASP A 315 12516 17614 16708 -1439 -939 252 O1-
ATOM 2890 N LYS A 316 -10.655 -25.578 16.951 1.00108.94 N
ANISOU 2890 N LYS A 316 10784 15757 14850 -1712 -1565 390 N
ATOM 2891 CA LYS A 316 -11.518 -26.267 15.985 1.00110.67 C
ANISOU 2891 CA LYS A 316 11113 15888 15050 -1802 -1780 385 C
ATOM 2892 C LYS A 316 -10.940 -27.626 15.575 1.00116.21 C
ANISOU 2892 C LYS A 316 11998 16436 15720 -1820 -1854 279 C
ATOM 2893 O LYS A 316 -11.685 -28.606 15.525 1.00116.95 O
ANISOU 2893 O LYS A 316 12104 16442 15888 -1924 -2040 315 O
ATOM 2894 CB LYS A 316 -11.739 -25.402 14.727 1.00113.58 C
ANISOU 2894 CB LYS A 316 11593 16280 15281 -1773 -1810 346 C
ATOM 2895 CG LYS A 316 -12.368 -24.037 14.988 1.00125.69 C
ANISOU 2895 CG LYS A 316 12961 17954 16843 -1760 -1761 455 C
ATOM 2896 CD LYS A 316 -12.441 -23.202 13.714 1.00134.49 C
ANISOU 2896 CD LYS A 316 14192 19091 17818 -1723 -1775 410 C
ATOM 2897 CE LYS A 316 -12.893 -21.780 13.964 1.00143.39 C
ANISOU 2897 CE LYS A 316 15164 20353 18966 -1697 -1709 512 C
ATOM 2898 NZ LYS A 316 -14.302 -21.700 14.439 1.00153.19 N1+
ANISOU 2898 NZ LYS A 316 16250 21634 20322 -1792 -1852 664 N1+
ATOM 2899 N GLU A 317 -9.627 -27.676 15.266 1.00113.00 N
ANISOU 2899 N GLU A 317 11734 15992 15208 -1717 -1713 159 N
ATOM 2900 CA GLU A 317 -8.914 -28.878 14.823 1.00114.05 C
ANISOU 2900 CA GLU A 317 12066 15980 15288 -1701 -1749 51 C
ATOM 2901 C GLU A 317 -8.776 -29.907 15.958 1.00117.91 C
ANISOU 2901 C GLU A 317 12456 16425 15919 -1747 -1748 87 C
ATOM 2902 O GLU A 317 -8.886 -31.106 15.699 1.00118.74 O
ANISOU 2902 O GLU A 317 12682 16396 16039 -1799 -1881 46 O
ATOM 2903 CB GLU A 317 -7.520 -28.494 14.281 1.00115.06 C
ANISOU 2903 CB GLU A 317 12341 16103 15273 -1559 -1566 -54 C
ATOM 2904 CG GLU A 317 -6.772 -29.601 13.543 1.00127.65 C
ANISOU 2904 CG GLU A 317 14185 17547 16771 -1509 -1590 -171 C
ATOM 2905 CD GLU A 317 -7.300 -29.979 12.170 1.00150.62 C
ANISOU 2905 CD GLU A 317 17333 20348 19548 -1527 -1772 -241 C
ATOM 2906 OE1 GLU A 317 -7.486 -29.069 11.330 1.00145.70 O
ANISOU 2906 OE1 GLU A 317 16764 19778 18816 -1489 -1770 -250 O
ATOM 2907 OE2 GLU A 317 -7.472 -31.193 11.915 1.00145.61 O1-
ANISOU 2907 OE2 GLU A 317 16849 19567 18910 -1569 -1915 -294 O1-
ATOM 2908 N MET A 318 -8.534 -29.442 17.196 1.00113.22 N
ANISOU 2908 N MET A 318 11656 15938 15424 -1725 -1605 161 N
ATOM 2909 CA MET A 318 -8.336 -30.289 18.375 1.00112.85 C
ANISOU 2909 CA MET A 318 11499 15869 15509 -1754 -1578 203 C
ATOM 2910 C MET A 318 -9.639 -30.981 18.811 1.00118.20 C
ANISOU 2910 C MET A 318 12060 16520 16329 -1884 -1765 315 C
ATOM 2911 O MET A 318 -9.586 -32.134 19.242 1.00118.18 O
ANISOU 2911 O MET A 318 12064 16427 16411 -1932 -1827 319 O
ATOM 2912 CB MET A 318 -7.768 -29.450 19.531 1.00113.43 C
ANISOU 2912 CB MET A 318 11397 16068 15631 -1688 -1382 254 C
ATOM 2913 CG MET A 318 -6.840 -30.220 20.469 1.00116.41 C
ANISOU 2913 CG MET A 318 11744 16410 16077 -1662 -1285 238 C
ATOM 2914 SD MET A 318 -5.035 -29.965 20.440 1.00119.46 S
ANISOU 2914 SD MET A 318 12219 16789 16381 -1535 -1071 143 S
ATOM 2915 CE MET A 318 -4.906 -28.195 20.555 1.00114.84 C
ANISOU 2915 CE MET A 318 11544 16347 15742 -1469 -946 176 C
ATOM 2916 N SER A 319 -10.797 -30.289 18.677 1.00115.63 N
ANISOU 2916 N SER A 319 11627 16270 16037 -1939 -1857 417 N
ATOM 2917 CA SER A 319 -12.133 -30.786 19.044 1.00116.72 C
ANISOU 2917 CA SER A 319 11627 16400 16321 -2061 -2037 560 C
ATOM 2918 C SER A 319 -12.505 -32.064 18.275 1.00123.03 C
ANISOU 2918 C SER A 319 12587 17026 17133 -2163 -2267 518 C
ATOM 2919 O SER A 319 -13.143 -32.951 18.844 1.00123.53 O
ANISOU 2919 O SER A 319 12552 17039 17344 -2258 -2390 615 O
ATOM 2920 CB SER A 319 -13.188 -29.711 18.790 1.00120.14 C
ANISOU 2920 CB SER A 319 11947 16942 16759 -2084 -2082 669 C
ATOM 2921 OG SER A 319 -14.474 -30.109 19.239 1.00129.13 O
ANISOU 2921 OG SER A 319 12915 18093 18056 -2191 -2233 841 O
ATOM 2922 N ALA A 320 -12.106 -32.152 16.991 1.00120.49 N
ANISOU 2922 N ALA A 320 12518 16610 16653 -2136 -2326 378 N
ATOM 2923 CA ALA A 320 -12.362 -33.305 16.128 1.00122.22 C
ANISOU 2923 CA ALA A 320 12947 16647 16846 -2214 -2549 311 C
ATOM 2924 C ALA A 320 -11.359 -34.441 16.397 1.00125.99 C
ANISOU 2924 C ALA A 320 13549 17000 17320 -2176 -2499 210 C
ATOM 2925 O ALA A 320 -11.685 -35.604 16.151 1.00127.04 O
ANISOU 2925 O ALA A 320 13791 16978 17500 -2261 -2689 195 O
ATOM 2926 CB ALA A 320 -12.296 -32.884 14.668 1.00123.78 C
ANISOU 2926 CB ALA A 320 13380 16797 16853 -2175 -2614 200 C
ATOM 2927 N THR A 321 -10.154 -34.106 16.903 1.00120.89 N
ANISOU 2927 N THR A 321 12889 16419 16626 -2052 -2250 150 N
ATOM 2928 CA THR A 321 -9.081 -35.066 17.192 1.00120.65 C
ANISOU 2928 CA THR A 321 12962 16291 16587 -1995 -2164 63 C
ATOM 2929 C THR A 321 -9.423 -35.921 18.440 1.00124.52 C
ANISOU 2929 C THR A 321 13270 16769 17274 -2077 -2201 168 C
ATOM 2930 O THR A 321 -9.084 -37.109 18.467 1.00124.81 O
ANISOU 2930 O THR A 321 13419 16665 17337 -2097 -2264 117 O
ATOM 2931 CB THR A 321 -7.734 -34.331 17.367 1.00125.92 C
ANISOU 2931 CB THR A 321 13636 17047 17162 -1845 -1891 -2 C
ATOM 2932 OG1 THR A 321 -7.588 -33.357 16.333 1.00125.00 O
ANISOU 2932 OG1 THR A 321 13631 16975 16890 -1776 -1851 -59 O
ATOM 2933 CG2 THR A 321 -6.534 -35.275 17.331 1.00124.23 C
ANISOU 2933 CG2 THR A 321 13577 16721 16902 -1765 -1798 -103 C
ATOM 2934 N PHE A 322 -10.098 -35.323 19.454 1.00120.33 N
ANISOU 2934 N PHE A 322 12465 16381 16874 -2116 -2159 317 N
ATOM 2935 CA PHE A 322 -10.486 -36.010 20.696 1.00120.17 C
ANISOU 2935 CA PHE A 322 12245 16372 17041 -2181 -2177 441 C
ATOM 2936 C PHE A 322 -11.433 -37.194 20.429 1.00126.32 C
ANISOU 2936 C PHE A 322 13057 17008 17931 -2322 -2440 497 C
ATOM 2937 O PHE A 322 -11.322 -38.229 21.092 1.00126.02 O
ANISOU 2937 O PHE A 322 12976 16899 18006 -2360 -2465 528 O
ATOM 2938 CB PHE A 322 -11.160 -35.037 21.689 1.00120.87 C
ANISOU 2938 CB PHE A 322 12057 16642 17226 -2182 -2094 601 C
ATOM 2939 CG PHE A 322 -10.340 -33.862 22.168 1.00120.53 C
ANISOU 2939 CG PHE A 322 11949 16741 17106 -2056 -1852 573 C
ATOM 2940 CD1 PHE A 322 -9.113 -34.057 22.789 1.00122.53 C
ANISOU 2940 CD1 PHE A 322 12215 16999 17342 -1973 -1678 508 C
ATOM 2941 CD2 PHE A 322 -10.848 -32.571 22.104 1.00122.12 C
ANISOU 2941 CD2 PHE A 322 12059 17073 17270 -2028 -1806 632 C
ATOM 2942 CE1 PHE A 322 -8.367 -32.973 23.259 1.00121.88 C
ANISOU 2942 CE1 PHE A 322 12073 17036 17200 -1870 -1479 492 C
ATOM 2943 CE2 PHE A 322 -10.104 -31.487 22.575 1.00123.37 C
ANISOU 2943 CE2 PHE A 322 12165 17348 17363 -1918 -1601 609 C
ATOM 2944 CZ PHE A 322 -8.869 -31.696 23.153 1.00120.45 C
ANISOU 2944 CZ PHE A 322 11816 16971 16976 -1845 -1446 541 C
ATOM 2945 N ARG A 323 -12.366 -37.024 19.473 1.00124.65 N
ANISOU 2945 N ARG A 323 12918 16751 17692 -2404 -2644 517 N
ATOM 2946 CA ARG A 323 -13.347 -38.034 19.074 1.00126.67 C
ANISOU 2946 CA ARG A 323 13215 16860 18055 -2555 -2935 580 C
ATOM 2947 C ARG A 323 -12.700 -39.190 18.298 1.00132.45 C
ANISOU 2947 C ARG A 323 14243 17378 18705 -2555 -3039 419 C
ATOM 2948 O ARG A 323 -13.223 -40.305 18.334 1.00133.63 O
ANISOU 2948 O ARG A 323 14410 17386 18975 -2668 -3238 466 O
ATOM 2949 CB ARG A 323 -14.451 -37.403 18.214 1.00127.66 C
ANISOU 2949 CB ARG A 323 13348 17000 18157 -2636 -3122 643 C
ATOM 2950 CG ARG A 323 -15.349 -36.400 18.934 1.00136.43 C
ANISOU 2950 CG ARG A 323 14162 18303 19371 -2652 -3062 834 C
ATOM 2951 CD ARG A 323 -16.568 -36.025 18.093 1.00146.65 C
ANISOU 2951 CD ARG A 323 15456 19588 20676 -2755 -3287 921 C
ATOM 2952 NE ARG A 323 -16.209 -35.264 16.892 1.00153.93 N
ANISOU 2952 NE ARG A 323 16590 20508 21388 -2690 -3273 776 N
ATOM 2953 CZ ARG A 323 -17.008 -35.079 15.840 1.00169.06 C
ANISOU 2953 CZ ARG A 323 18703 22303 23229 -2765 -3508 724 C
ATOM 2954 NH1 ARG A 323 -18.225 -35.614 15.816 1.00156.84 N
ANISOU 2954 NH1 ARG A 323 17187 20606 21798 -2917 -3793 794 N
ATOM 2955 NH2 ARG A 323 -16.588 -34.379 14.797 1.00156.49 N1+
ANISOU 2955 NH2 ARG A 323 17294 20727 21439 -2688 -3467 599 N1+
ATOM 2956 N GLN A 324 -11.593 -38.914 17.582 1.00128.93 N
ANISOU 2956 N GLN A 324 14030 16902 18055 -2425 -2907 239 N
ATOM 2957 CA GLN A 324 -10.853 -39.893 16.792 1.00130.17 C
ANISOU 2957 CA GLN A 324 14501 16862 18095 -2383 -2967 74 C
ATOM 2958 C GLN A 324 -10.166 -40.941 17.685 1.00133.89 C
ANISOU 2958 C GLN A 324 14939 17272 18660 -2357 -2870 64 C
ATOM 2959 O GLN A 324 -10.093 -42.116 17.299 1.00134.79 O
ANISOU 2959 O GLN A 324 15240 17194 18781 -2395 -3017 0 O
ATOM 2960 CB GLN A 324 -9.809 -39.204 15.899 1.00131.05 C
ANISOU 2960 CB GLN A 324 14830 16995 17970 -2224 -2806 -82 C
ATOM 2961 N ILE A 325 -9.684 -40.518 18.875 1.00128.89 N
ANISOU 2961 N ILE A 325 14075 16799 18099 -2295 -2633 130 N
ATOM 2962 CA ILE A 325 -8.981 -41.376 19.840 1.00128.28 C
ANISOU 2962 CA ILE A 325 13925 16702 18113 -2261 -2507 139 C
ATOM 2963 C ILE A 325 -9.971 -42.336 20.521 1.00133.64 C
ANISOU 2963 C ILE A 325 14448 17320 19010 -2406 -2685 277 C
ATOM 2964 O ILE A 325 -9.684 -43.532 20.627 1.00134.00 O
ANISOU 2964 O ILE A 325 14575 17231 19108 -2418 -2721 242 O
ATOM 2965 CB ILE A 325 -8.228 -40.502 20.872 1.00129.08 C
ANISOU 2965 CB ILE A 325 13826 16997 18222 -2158 -2223 178 C
ATOM 2966 N LEU A 326 -11.150 -41.829 20.922 1.00130.70 N
ANISOU 2966 N LEU A 326 13854 17034 18770 -2515 -2800 444 N
ATOM 2967 CA LEU A 326 -12.220 -42.589 21.594 1.00131.55 C
ANISOU 2967 CA LEU A 326 13773 17102 19108 -2644 -2944 610 C
ATOM 2968 C LEU A 326 -12.798 -43.713 20.711 1.00137.79 C
ANISOU 2968 C LEU A 326 14668 17689 19996 -2805 -3280 649 C
ATOM 2969 O LEU A 326 -13.101 -44.800 21.211 1.00138.28 O
ANISOU 2969 O LEU A 326 14759 17619 20162 -2854 -3358 656 O
ATOM 2970 CB LEU A 326 -13.369 -41.632 22.010 1.00130.68 C
ANISOU 2970 CB LEU A 326 13331 17196 19127 -2667 -2873 812 C
ATOM 2971 CG LEU A 326 -13.065 -40.561 23.051 1.00133.12 C
ANISOU 2971 CG LEU A 326 13503 17695 19383 -2528 -2569 807 C
ATOM 2972 CD1 LEU A 326 -14.050 -39.425 22.972 1.00132.54 C
ANISOU 2972 CD1 LEU A 326 13375 17771 19214 -2481 -2500 826 C
ATOM 2973 CD2 LEU A 326 -13.026 -41.132 24.472 1.00134.85 C
ANISOU 2973 CD2 LEU A 326 13450 18007 19782 -2539 -2488 976 C
ATOM 2974 N GLY A 327 -12.965 -43.416 19.423 1.00135.26 N
ANISOU 2974 N GLY A 327 14409 17337 19646 -2888 -3484 674 N
ATOM 2975 CA GLY A 327 -13.520 -44.336 18.435 1.00161.32 C
ANISOU 2975 CA GLY A 327 17902 20419 22974 -3021 -3813 654 C
ATOM 2976 C GLY A 327 -12.490 -45.315 17.909 1.00178.14 C
ANISOU 2976 C GLY A 327 20428 22360 24898 -2946 -3849 415 C
ATOM 2977 O GLY A 327 -12.461 -46.476 18.313 1.00136.83 O
ANISOU 2977 O GLY A 327 15368 16917 19704 -3008 -4028 365 O
TER 2978 GLY A 327
HETATM 2979 C30 ON9 A2001 1.461 -24.928 46.339 1.00 56.66 C
ANISOU 2979 C30 ON9 A2001 3154 9708 8668 -579 -78 1013 C
HETATM 2980 C31 ON9 A2001 2.795 -24.553 50.198 1.00 59.61 C
ANISOU 2980 C31 ON9 A2001 3751 10075 8824 -352 -146 1064 C
HETATM 2981 C28 ON9 A2001 -2.932 -26.050 46.634 1.00 59.11 C
ANISOU 2981 C28 ON9 A2001 3194 10253 9013 -400 74 1313 C
HETATM 2982 C27 ON9 A2001 -7.385 -30.995 50.927 1.00 83.15 C
ANISOU 2982 C27 ON9 A2001 5465 13697 12431 -71 378 2229 C
HETATM 2983 C29 ON9 A2001 0.704 -24.102 47.344 1.00 57.72 C
ANISOU 2983 C29 ON9 A2001 3364 9892 8675 -435 -65 1055 C
HETATM 2984 C23 ON9 A2001 -5.227 -31.341 53.761 1.00 81.13 C
ANISOU 2984 C23 ON9 A2001 5370 13435 12019 86 444 2162 C
HETATM 2985 C24 ON9 A2001 -4.345 -31.825 54.926 1.00 82.69 C
ANISOU 2985 C24 ON9 A2001 5599 13635 12186 133 463 2164 C
HETATM 2986 C25 ON9 A2001 -4.796 -31.267 56.265 1.00 85.43 C
ANISOU 2986 C25 ON9 A2001 6015 14068 12376 357 545 2265 C
HETATM 2987 C26 ON9 A2001 -7.782 -29.596 52.962 1.00 82.99 C
ANISOU 2987 C26 ON9 A2001 5593 13799 12141 285 526 2332 C
HETATM 2988 C21 ON9 A2001 -5.253 -29.857 53.562 1.00 79.53 C
ANISOU 2988 C21 ON9 A2001 5340 13227 11651 168 435 2071 C
HETATM 2989 C1 ON9 A2001 0.020 -24.853 48.454 1.00 59.74 C
ANISOU 2989 C1 ON9 A2001 3558 10218 8923 -342 -9 1157 C
HETATM 2990 O6 ON9 A2001 0.658 -22.884 47.272 1.00 56.76 O
ANISOU 2990 O6 ON9 A2001 3355 9752 8458 -386 -95 1014 O
HETATM 2991 O5 ON9 A2001 -1.546 -25.897 46.884 1.00 60.07 O
ANISOU 2991 O5 ON9 A2001 3381 10311 9131 -444 42 1232 O
HETATM 2992 C2 ON9 A2001 -1.102 -25.700 48.200 1.00 60.94 C
ANISOU 2992 C2 ON9 A2001 3566 10433 9157 -346 49 1248 C
HETATM 2993 C20 ON9 A2001 -6.405 -29.079 53.171 1.00 80.29 C
ANISOU 2993 C20 ON9 A2001 5433 13376 11697 254 472 2140 C
HETATM 2994 C22 ON9 A2001 -4.205 -28.960 53.735 1.00 77.54 C
ANISOU 2994 C22 ON9 A2001 5278 12912 11270 180 386 1919 C
HETATM 2995 C3 ON9 A2001 -1.770 -26.355 49.261 1.00 62.59 C
ANISOU 2995 C3 ON9 A2001 3705 10712 9366 -252 107 1363 C
HETATM 2996 O3 ON9 A2001 -8.209 -30.462 51.949 1.00 84.00 O
ANISOU 2996 O3 ON9 A2001 5564 13906 12445 129 476 2375 O
HETATM 2997 C6 ON9 A2001 -2.232 -26.808 51.674 1.00 66.09 C
ANISOU 2997 C6 ON9 A2001 4157 11255 9701 -18 192 1522 C
HETATM 2998 O2 ON9 A2001 -8.719 -29.282 53.686 1.00 84.03 O
ANISOU 2998 O2 ON9 A2001 5696 14023 12210 461 618 2487 O
HETATM 2999 C5 ON9 A2001 -0.248 -25.356 50.878 1.00 61.97 C
ANISOU 2999 C5 ON9 A2001 3873 10577 9097 -137 46 1281 C
HETATM 3000 C8 ON9 A2001 -4.219 -25.115 51.525 1.00 70.73 C
ANISOU 3000 C8 ON9 A2001 4805 11939 10131 194 271 1619 C
HETATM 3001 C7 ON9 A2001 -3.176 -25.785 52.445 1.00 70.30 C
ANISOU 3001 C7 ON9 A2001 4780 11855 10076 184 249 1594 C
HETATM 3002 C11 ON9 A2001 -3.272 -22.754 49.327 1.00 70.13 C
ANISOU 3002 C11 ON9 A2001 4978 11710 9957 55 124 1336 C
HETATM 3003 C4 ON9 A2001 -1.364 -26.168 50.592 1.00 63.56 C
ANISOU 3003 C4 ON9 A2001 3915 10846 9388 -140 114 1381 C
HETATM 3004 O1 ON9 A2001 -5.558 -32.029 57.088 1.00 87.64 O
ANISOU 3004 O1 ON9 A2001 6160 14432 12706 450 627 2448 O
HETATM 3005 C9 ON9 A2001 -4.247 -23.570 51.376 1.00 71.07 C
ANISOU 3005 C9 ON9 A2001 5023 11957 10024 281 251 1547 C
HETATM 3006 C13 ON9 A2001 -5.356 -23.221 50.354 1.00 71.55 C
ANISOU 3006 C13 ON9 A2001 5000 12056 10132 259 276 1593 C
HETATM 3007 C10 ON9 A2001 -2.961 -22.923 50.776 1.00 70.10 C
ANISOU 3007 C10 ON9 A2001 5036 11726 9874 175 147 1379 C
HETATM 3008 C12 ON9 A2001 -4.616 -23.053 49.073 1.00 70.59 C
ANISOU 3008 C12 ON9 A2001 4908 11850 10065 91 191 1453 C
HETATM 3009 C17 ON9 A2001 -2.404 -22.428 48.278 1.00 69.88 C
ANISOU 3009 C17 ON9 A2001 4993 11596 9961 -78 49 1214 C
HETATM 3010 O4 ON9 A2001 -1.389 -27.515 52.540 1.00 65.42 O
ANISOU 3010 O4 ON9 A2001 4079 11152 9626 -23 180 1522 O
HETATM 3011 C16 ON9 A2001 -2.901 -22.443 46.950 1.00 68.96 C
ANISOU 3011 C16 ON9 A2001 4805 11480 9917 -172 43 1197 C
HETATM 3012 C15 ON9 A2001 -4.240 -22.789 46.692 1.00 69.17 C
ANISOU 3012 C15 ON9 A2001 4713 11582 9988 -144 97 1302 C
HETATM 3013 C14 ON9 A2001 -5.118 -23.099 47.762 1.00 70.41 C
ANISOU 3013 C14 ON9 A2001 4807 11821 10124 -16 170 1438 C
HETATM 3014 C18 ON9 A2001 -3.863 -26.448 53.696 1.00 74.23 C
ANISOU 3014 C18 ON9 A2001 5200 12443 10561 323 338 1751 C
HETATM 3015 C19 ON9 A2001 -6.005 -27.740 53.116 1.00 78.28 C
ANISOU 3015 C19 ON9 A2001 5374 13086 11281 316 448 2017 C
HETATM 3016 O7 ON9 A2001 1.534 -23.898 50.103 1.00 60.05 O
ANISOU 3016 O7 ON9 A2001 3828 10188 8801 -249 -98 1095 O
HETATM 3017 C ON9 A2001 0.440 -24.710 49.819 1.00 60.44 C
ANISOU 3017 C ON9 A2001 3733 10310 8921 -243 -18 1175 C
HETATM 3018 N ON9 A2001 -4.672 -27.669 53.477 1.00 76.45 N
ANISOU 3018 N ON9 A2001 5261 12784 11003 271 390 1885 N
HETATM 3019 O ON9 A2001 -4.526 -30.161 56.698 1.00 85.65 O1-
ANISOU 3019 O ON9 A2001 6223 14092 12227 472 543 2198 O1-
HETATM 3020 C10 1WV A2002 10.442 -38.057 41.831 1.00 88.43 C
ANISOU 3020 C10 1WV A2002 6674 13102 13823 -1219 308 1032 C
HETATM 3021 C13 1WV A2002 9.217 -35.890 43.927 1.00 86.98 C
ANISOU 3021 C13 1WV A2002 6443 13093 13511 -1183 192 1087 C
HETATM 3022 C17 1WV A2002 9.368 -34.556 47.103 1.00 85.36 C
ANISOU 3022 C17 1WV A2002 6228 13039 13167 -1088 89 1170 C
HETATM 3023 C20 1WV A2002 10.080 -35.039 49.479 1.00 84.70 C
ANISOU 3023 C20 1WV A2002 6073 13008 13103 -1039 76 1288 C
HETATM 3024 C07 1WV A2002 10.071 -40.902 39.129 1.00 91.74 C
ANISOU 3024 C07 1WV A2002 7292 13271 14292 -1224 364 901 C
HETATM 3025 C08 1WV A2002 10.287 -39.490 39.717 1.00 90.63 C
ANISOU 3025 C08 1WV A2002 7093 13233 14108 -1221 348 933 C
HETATM 3026 C09 1WV A2002 10.169 -39.462 41.259 1.00 89.61 C
ANISOU 3026 C09 1WV A2002 6847 13173 14029 -1231 331 1009 C
HETATM 3027 C11 1WV A2002 9.271 -37.066 41.661 1.00 87.66 C
ANISOU 3027 C11 1WV A2002 6583 13069 13655 -1220 238 1009 C
HETATM 3028 C12 1WV A2002 9.497 -35.738 42.410 1.00 87.02 C
ANISOU 3028 C12 1WV A2002 6512 13046 13504 -1200 209 1018 C
HETATM 3029 C14 1WV A2002 9.379 -34.582 44.679 1.00 86.69 C
ANISOU 3029 C14 1WV A2002 6444 13118 13379 -1153 133 1079 C
HETATM 3030 O15 1WV A2002 8.972 -33.477 44.333 1.00 87.01 O
ANISOU 3030 O15 1WV A2002 6532 13177 13350 -1142 107 1035 O
HETATM 3031 O16 1WV A2002 10.062 -34.744 45.867 1.00 85.90 O
ANISOU 3031 O16 1WV A2002 6326 13046 13267 -1133 107 1128 O
HETATM 3032 C18 1WV A2002 10.431 -34.231 48.187 1.00 84.76 C
ANISOU 3032 C18 1WV A2002 6152 12971 13081 -1073 55 1218 C
HETATM 3033 O19 1WV A2002 10.343 -32.884 48.580 1.00 84.51 O
ANISOU 3033 O19 1WV A2002 6204 12965 12938 -1030 -11 1200 O
HETATM 3034 O21 1WV A2002 10.970 -34.760 50.516 1.00 84.64 O
ANISOU 3034 O21 1WV A2002 6074 13005 13078 -1026 36 1332 O
HETATM 3035 C1 1WV A2002 11.260 -41.815 39.340 1.00 92.03 C
ANISOU 3035 C1 1WV A2002 7299 13261 14409 -1199 446 953 C
HETATM 3036 C2 1WV A2002 12.277 -42.024 38.481 1.00 92.39 C
ANISOU 3036 C2 1WV A2002 7411 13240 14455 -1150 534 951 C
HETATM 3037 C3 1WV A2002 12.447 -41.390 37.135 1.00 92.86 C
ANISOU 3037 C3 1WV A2002 7594 13257 14429 -1104 572 894 C
HETATM 3038 O HOH A2101 -3.642 -26.611 38.415 1.00 41.70 O
ANISOU 3038 O HOH A2101 984 7815 7044 -963 -164 1011 O
HETATM 3039 O HOH A2102 -1.409 -28.720 55.705 1.00 83.94 O
ANISOU 3039 O HOH A2102 6401 13612 11882 225 281 1726 O
HETATM 3040 O HOH A2103 7.370 -20.246 39.934 1.00 16.78 O
ANISOU 3040 O HOH A2103 467 3252 2656 -491 -202 724 O
CONECT 11 1302
CONECT 1288 1341
CONECT 1302 11
CONECT 1341 1288
CONECT 2631 2653
CONECT 2653 2631
CONECT 2979 2983
CONECT 2980 3016
CONECT 2981 2991
CONECT 2982 2996
CONECT 2983 2979 2989 2990
CONECT 2984 2985 2988
CONECT 2985 2984 2986
CONECT 2986 2985 3004 3019
CONECT 2987 2993 2996 2998
CONECT 2988 2984 2993 2994
CONECT 2989 2983 2992 3017
CONECT 2990 2983
CONECT 2991 2981 2992
CONECT 2992 2989 2991 2995
CONECT 2993 2987 2988 3015
CONECT 2994 2988 3018
CONECT 2995 2992 3003
CONECT 2996 2982 2987
CONECT 2997 3001 3003 3010
CONECT 2998 2987
CONECT 2999 3003 3017
CONECT 3000 3001 3005
CONECT 3001 2997 3000 3014
CONECT 3002 3007 3008 3009
CONECT 3003 2995 2997 2999
CONECT 3004 2986
CONECT 3005 3000 3006 3007
CONECT 3006 3005 3008
CONECT 3007 3002 3005
CONECT 3008 3002 3006 3013
CONECT 3009 3002 3011
CONECT 3010 2997
CONECT 3011 3009 3012
CONECT 3012 3011 3013
CONECT 3013 3008 3012
CONECT 3014 3001 3018
CONECT 3015 2993 3018
CONECT 3016 2980 3017
CONECT 3017 2989 2999 3016
CONECT 3018 2994 3014 3015
CONECT 3019 2986
CONECT 3020 3026 3027
CONECT 3021 3028 3029
CONECT 3022 3031 3032
CONECT 3023 3032 3034
CONECT 3024 3025 3035
CONECT 3025 3024 3026
CONECT 3026 3020 3025
CONECT 3027 3020 3028
CONECT 3028 3021 3027
CONECT 3029 3021 3030 3031
CONECT 3030 3029
CONECT 3031 3022 3029
CONECT 3032 3022 3023 3033
CONECT 3033 3032
CONECT 3034 3023
CONECT 3035 3024 3036
CONECT 3036 3035 3037
CONECT 3037 3036
MASTER 385 0 2 17 0 0 5 6 3039 1 65 36
END