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1iep.pdb
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HEADER TRANSFERASE 10-APR-01 1IEP
TITLE CRYSTAL STRUCTURE OF THE C-ABL KINASE DOMAIN IN COMPLEX
TITLE 2 WITH STI-571.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: P150, C-ABL;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS KINASE, KINASE INHIBITOR, STI-571, ACTIVATION LOOP,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NAGAR,W.BORNMANN,T.SCHINDLER,B.CLARKSON,J.KURIYAN
REVDAT 3 24-FEB-09 1IEP 1 VERSN
REVDAT 2 01-JUL-03 1IEP 1 JRNL
REVDAT 1 18-APR-01 1IEP 0
JRNL AUTH B.NAGAR,W.BORNMANN,P.PELLICENA,T.SCHINDLER,
JRNL AUTH 2 D.R.VEACH,W.T.MILLER,B.CLARKSON,J.KURIYAN
JRNL TITL CRYSTAL STRUCTURES OF THE KINASE DOMAIN OF C-ABL
JRNL TITL 2 IN COMPLEX WITH THE SMALL MOLECULE INHIBITORS
JRNL TITL 3 PD173955 AND IMATINIB (STI-571)
JRNL REF CANCER RES. V. 62 4236 2002
JRNL REFN ISSN 0008-5472
JRNL PMID 12154025
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 565920.720
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 35704
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 SET) : 0.231
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2917
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4978
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 452
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4458
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 172
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 20.66000
REMARK 3 B22 (A**2) : -6.98000
REMARK 3 B33 (A**2) : -13.67000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.69
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.530 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.230 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.690 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 49.07
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : STIPIPFLIP.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : STIPIPFLIP.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IEP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-01.
REMARK 100 THE RCSB ID CODE IS RCSB013215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.949
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37004
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1FPU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, MES,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.68550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 76.72100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.68550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.72100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 73.68550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.72100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 73.68550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 76.72100
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 76.72100
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 76.72100
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 76.72100
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 76.72100
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 73.68550
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 73.68550
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 73.68550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 56.44250
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 73.68550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 223
REMARK 465 ALA A 224
REMARK 465 GLU A 499
REMARK 465 SER A 500
REMARK 465 SER A 501
REMARK 465 ILE A 502
REMARK 465 SER A 503
REMARK 465 ASP A 504
REMARK 465 GLU A 505
REMARK 465 VAL A 506
REMARK 465 GLU A 507
REMARK 465 LYS A 508
REMARK 465 GLU A 509
REMARK 465 LEU A 510
REMARK 465 GLY A 511
REMARK 465 LYS A 512
REMARK 465 ARG A 513
REMARK 465 GLY A 514
REMARK 465 THR A 515
REMARK 465 GLY B 223
REMARK 465 ALA B 224
REMARK 465 GLU B 499
REMARK 465 SER B 500
REMARK 465 SER B 501
REMARK 465 ILE B 502
REMARK 465 SER B 503
REMARK 465 ASP B 504
REMARK 465 GLU B 505
REMARK 465 VAL B 506
REMARK 465 GLU B 507
REMARK 465 LYS B 508
REMARK 465 GLU B 509
REMARK 465 LEU B 510
REMARK 465 GLY B 511
REMARK 465 LYS B 512
REMARK 465 ARG B 513
REMARK 465 GLY B 514
REMARK 465 THR B 515
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 LYS A 245 -143.51 -126.27
REMARK 500 LYS A 262 -63.58 -29.05
REMARK 500 LYS A 263 -18.69 -42.64
REMARK 500 LYS A 274 169.47 -49.52
REMARK 500 GLU A 275 78.74 -52.31
REMARK 500 ASP A 276 82.34 54.59
REMARK 500 MET A 278 37.61 -70.50
REMARK 500 ARG A 362 -16.49 87.76
REMARK 500 ASP A 363 54.49 -150.99
REMARK 500 HIS A 396 99.09 -174.66
REMARK 500 TYR A 440 61.19 38.04
REMARK 500 SER B 229 140.99 -39.16
REMARK 500 LYS B 245 -129.10 -93.00
REMARK 500 LYS B 262 -72.14 -26.96
REMARK 500 LYS B 263 -34.93 -38.82
REMARK 500 MET B 278 13.82 -150.89
REMARK 500 ARG B 362 -19.72 87.89
REMARK 500 ASP B 363 55.43 -146.51
REMARK 500 LEU B 387 -38.40 -163.21
REMARK 500 THR B 389 -176.15 -68.60
REMARK 500 ASP B 391 -9.78 -58.19
REMARK 500 HIS B 396 129.65 -170.86
REMARK 500 MET B 496 20.35 -69.59
REMARK 500 PHE B 497 -97.19 -142.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 6
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI A 201
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FPU RELATED DB: PDB
DBREF 1IEP A 229 515 UNP P00520 ABL1_MOUSE 229 515
DBREF 1IEP B 229 515 UNP P00520 ABL1_MOUSE 229 515
SEQADV 1IEP GLY A 223 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP ALA A 224 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP MET A 225 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP ASP A 226 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP PRO A 227 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP SER A 228 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP GLY B 223 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP ALA B 224 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP MET B 225 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP ASP B 226 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP PRO B 227 UNP P00520 CLONING ARTIFACT
SEQADV 1IEP SER B 228 UNP P00520 CLONING ARTIFACT
SEQRES 1 A 293 GLY ALA MET ASP PRO SER SER PRO ASN TYR ASP LYS TRP
SEQRES 2 A 293 GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS LEU
SEQRES 3 A 293 GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP
SEQRES 4 A 293 LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU LYS
SEQRES 5 A 293 GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU ALA
SEQRES 6 A 293 ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN
SEQRES 7 A 293 LEU LEU GLY VAL CYS THR ARG GLU PRO PRO PHE TYR ILE
SEQRES 8 A 293 ILE THR GLU PHE MET THR TYR GLY ASN LEU LEU ASP TYR
SEQRES 9 A 293 LEU ARG GLU CYS ASN ARG GLN GLU VAL SER ALA VAL VAL
SEQRES 10 A 293 LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET GLU
SEQRES 11 A 293 TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA
SEQRES 12 A 293 ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS
SEQRES 13 A 293 VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY ASP
SEQRES 14 A 293 THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE LYS
SEQRES 15 A 293 TRP THR ALA PRO GLU SER LEU ALA TYR ASN LYS PHE SER
SEQRES 16 A 293 ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP
SEQRES 17 A 293 GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY ILE
SEQRES 18 A 293 ASP LEU SER GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR
SEQRES 19 A 293 ARG MET GLU ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR
SEQRES 20 A 293 GLU LEU MET ARG ALA CYS TRP GLN TRP ASN PRO SER ASP
SEQRES 21 A 293 ARG PRO SER PHE ALA GLU ILE HIS GLN ALA PHE GLU THR
SEQRES 22 A 293 MET PHE GLN GLU SER SER ILE SER ASP GLU VAL GLU LYS
SEQRES 23 A 293 GLU LEU GLY LYS ARG GLY THR
SEQRES 1 B 293 GLY ALA MET ASP PRO SER SER PRO ASN TYR ASP LYS TRP
SEQRES 2 B 293 GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS LEU
SEQRES 3 B 293 GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP
SEQRES 4 B 293 LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU LYS
SEQRES 5 B 293 GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU ALA
SEQRES 6 B 293 ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN
SEQRES 7 B 293 LEU LEU GLY VAL CYS THR ARG GLU PRO PRO PHE TYR ILE
SEQRES 8 B 293 ILE THR GLU PHE MET THR TYR GLY ASN LEU LEU ASP TYR
SEQRES 9 B 293 LEU ARG GLU CYS ASN ARG GLN GLU VAL SER ALA VAL VAL
SEQRES 10 B 293 LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET GLU
SEQRES 11 B 293 TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA
SEQRES 12 B 293 ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS
SEQRES 13 B 293 VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY ASP
SEQRES 14 B 293 THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE LYS
SEQRES 15 B 293 TRP THR ALA PRO GLU SER LEU ALA TYR ASN LYS PHE SER
SEQRES 16 B 293 ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP
SEQRES 17 B 293 GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY ILE
SEQRES 18 B 293 ASP LEU SER GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR
SEQRES 19 B 293 ARG MET GLU ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR
SEQRES 20 B 293 GLU LEU MET ARG ALA CYS TRP GLN TRP ASN PRO SER ASP
SEQRES 21 B 293 ARG PRO SER PHE ALA GLU ILE HIS GLN ALA PHE GLU THR
SEQRES 22 B 293 MET PHE GLN GLU SER SER ILE SER ASP GLU VAL GLU LYS
SEQRES 23 B 293 GLU LEU GLY LYS ARG GLY THR
HET CL A 1 1
HET CL A 2 1
HET CL B 3 1
HET CL A 4 1
HET CL A 5 1
HET CL B 6 1
HET STI A 201 37
HET STI B 202 37
HETNAM CL CHLORIDE ION
HETNAM STI 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-
HETNAM 2 STI PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE
HETSYN STI STI-571;IMATINIB
FORMUL 3 CL 6(CL 1-)
FORMUL 9 STI 2(C29 H31 N7 O)
FORMUL 11 HOH *172(H2 O)
HELIX 1 1 GLU A 238 THR A 240 5 3
HELIX 2 2 GLY A 249 GLN A 252 5 4
HELIX 3 3 LYS A 263 SER A 265 5 3
HELIX 4 4 GLU A 279 LYS A 291 1 13
HELIX 5 5 ASN A 322 CYS A 330 1 9
HELIX 6 6 SER A 336 LYS A 357 1 22
HELIX 7 7 ALA A 365 ARG A 367 5 3
HELIX 8 8 GLU A 373 HIS A 375 5 3
HELIX 9 9 PRO A 402 THR A 406 5 5
HELIX 10 10 ALA A 407 ASN A 414 1 8
HELIX 11 11 SER A 417 THR A 434 1 18
HELIX 12 12 ASP A 444 SER A 446 5 3
HELIX 13 13 GLN A 447 LYS A 454 1 8
HELIX 14 14 PRO A 465 TRP A 476 1 12
HELIX 15 15 ASN A 479 ARG A 483 5 5
HELIX 16 16 SER A 485 GLN A 498 1 14
HELIX 17 17 GLU B 238 THR B 240 5 3
HELIX 18 18 GLY B 249 GLN B 252 5 4
HELIX 19 19 LYS B 263 SER B 265 5 3
HELIX 20 20 GLU B 279 LYS B 291 1 13
HELIX 21 21 ASN B 322 CYS B 330 1 9
HELIX 22 22 SER B 336 LYS B 357 1 22
HELIX 23 23 ALA B 365 ARG B 367 5 3
HELIX 24 24 GLU B 373 HIS B 375 5 3
HELIX 25 25 GLY B 383 LEU B 387 5 5
HELIX 26 26 PRO B 402 THR B 406 5 5
HELIX 27 27 ALA B 407 ASN B 414 1 8
HELIX 28 28 SER B 417 THR B 434 1 18
HELIX 29 29 ASP B 444 SER B 446 5 3
HELIX 30 30 GLN B 447 LYS B 454 1 8
HELIX 31 31 PRO B 465 TRP B 476 1 12
HELIX 32 32 ASN B 479 ARG B 483 5 5
HELIX 33 33 SER B 485 MET B 496 1 12
SHEET 1 A 5 ILE A 242 LYS A 247 0
SHEET 2 A 5 VAL A 256 TRP A 261 -1 N GLU A 258 O HIS A 246
SHEET 3 A 5 LEU A 266 THR A 272 -1 O LEU A 266 N TRP A 261
SHEET 4 A 5 TYR A 312 GLU A 316 -1 O ILE A 313 N LYS A 271
SHEET 5 A 5 LEU A 301 CYS A 305 -1 N LEU A 302 O ILE A 314
SHEET 1 B 2 CYS A 369 VAL A 371 0
SHEET 2 B 2 VAL A 377 VAL A 379 -1 O LYS A 378 N LEU A 370
SHEET 1 C 2 THR A 394 HIS A 396 0
SHEET 2 C 2 ALA A 399 PHE A 401 -1 O ALA A 399 N HIS A 396
SHEET 1 D 5 ILE B 242 LYS B 247 0
SHEET 2 D 5 VAL B 256 TRP B 261 -1 N GLU B 258 O HIS B 246
SHEET 3 D 5 LEU B 266 THR B 272 -1 O LEU B 266 N TRP B 261
SHEET 4 D 5 TYR B 312 GLU B 316 -1 O ILE B 313 N LYS B 271
SHEET 5 D 5 LEU B 301 CYS B 305 -1 N LEU B 302 O ILE B 314
SHEET 1 E 2 CYS B 369 VAL B 371 0
SHEET 2 E 2 VAL B 377 VAL B 379 -1 O LYS B 378 N LEU B 370
SHEET 1 F 2 THR B 394 HIS B 396 0
SHEET 2 F 2 ALA B 399 PHE B 401 -1 O ALA B 399 N HIS B 396
CISPEP 1 PRO A 309 PRO A 310 0 0.03
CISPEP 2 PRO B 309 PRO B 310 0 0.04
SITE 1 AC1 1 HOH A 60
SITE 1 AC2 2 STI A 201 ILE A 360
SITE 1 AC3 3 HOH B 151 STI B 202 ILE B 360
SITE 1 AC4 2 THR A 319 GLY A 372
SITE 1 AC5 4 STI A 201 TYR A 253 GLY A 321 ASN A 322
SITE 1 AC6 4 STI B 202 TYR B 253 GLY B 321 ASN B 322
SITE 1 AC7 20 CL A 2 CL A 5 HOH A 75 LEU A 248
SITE 2 AC7 20 TYR A 253 ALA A 269 LYS A 271 GLU A 286
SITE 3 AC7 20 MET A 290 VAL A 299 ILE A 313 THR A 315
SITE 4 AC7 20 PHE A 317 MET A 318 ILE A 360 HIS A 361
SITE 5 AC7 20 ARG A 362 ALA A 380 ASP A 381 PHE A 382
SITE 1 AC8 19 CL B 3 CL B 6 HOH B 165 LEU B 248
SITE 2 AC8 19 TYR B 253 VAL B 256 ALA B 269 LYS B 271
SITE 3 AC8 19 GLU B 286 MET B 290 VAL B 299 ILE B 313
SITE 4 AC8 19 THR B 315 MET B 318 ILE B 360 HIS B 361
SITE 5 AC8 19 ALA B 380 ASP B 381 PHE B 382
CRYST1 112.885 147.371 153.442 90.00 90.00 90.00 F 2 2 2 32
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 0.008859 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006786 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006517 0.00000
ATOM 1 N MET A 225 19.353 41.547 -3.887 1.00 72.26 N
ATOM 2 CA MET A 225 20.513 40.939 -4.592 1.00 70.80 C
ATOM 3 C MET A 225 20.150 39.658 -5.355 1.00 69.53 C
ATOM 4 O MET A 225 19.053 39.551 -5.903 1.00 68.86 O
ATOM 5 CB MET A 225 21.642 40.678 -3.592 1.00 71.61 C
ATOM 6 CG MET A 225 21.233 39.903 -2.360 1.00 72.49 C
ATOM 7 SD MET A 225 22.533 39.928 -1.113 1.00 76.72 S
ATOM 8 CE MET A 225 23.771 38.881 -1.885 1.00 71.61 C
ATOM 9 N ASP A 226 21.068 38.694 -5.390 1.00 67.35 N
ATOM 10 CA ASP A 226 20.856 37.440 -6.117 1.00 64.67 C
ATOM 11 C ASP A 226 20.124 36.371 -5.299 1.00 60.64 C
ATOM 12 O ASP A 226 20.680 35.818 -4.351 1.00 61.28 O
ATOM 13 CB ASP A 226 22.208 36.890 -6.586 1.00 68.19 C
ATOM 14 CG ASP A 226 22.073 35.863 -7.699 1.00 72.67 C
ATOM 15 OD1 ASP A 226 21.305 34.890 -7.529 1.00 73.52 O
ATOM 16 OD2 ASP A 226 22.740 36.029 -8.744 1.00 72.20 O
ATOM 17 N PRO A 227 18.872 36.052 -5.675 1.00 58.29 N
ATOM 18 CA PRO A 227 18.030 35.054 -4.999 1.00 56.77 C
ATOM 19 C PRO A 227 18.675 33.677 -4.831 1.00 58.61 C
ATOM 20 O PRO A 227 18.457 32.997 -3.824 1.00 57.58 O
ATOM 21 CB PRO A 227 16.788 34.997 -5.884 1.00 55.32 C
ATOM 22 CG PRO A 227 16.706 36.383 -6.436 1.00 57.16 C
ATOM 23 CD PRO A 227 18.142 36.670 -6.796 1.00 56.73 C
ATOM 24 N SER A 228 19.458 33.264 -5.821 1.00 59.84 N
ATOM 25 CA SER A 228 20.130 31.969 -5.773 1.00 62.95 C
ATOM 26 C SER A 228 21.464 32.040 -5.031 1.00 65.13 C
ATOM 27 O SER A 228 22.045 31.008 -4.688 1.00 66.16 O
ATOM 28 CB SER A 228 20.364 31.447 -7.191 1.00 62.28 C
ATOM 29 OG SER A 228 21.180 32.341 -7.928 1.00 62.06 O
ATOM 30 N SER A 229 21.950 33.253 -4.788 1.00 64.53 N
ATOM 31 CA SER A 229 23.216 33.437 -4.085 1.00 65.76 C
ATOM 32 C SER A 229 23.144 32.931 -2.643 1.00 66.52 C
ATOM 33 O SER A 229 22.121 33.077 -1.970 1.00 64.82 O
ATOM 34 CB SER A 229 23.619 34.914 -4.089 1.00 66.77 C
ATOM 35 OG SER A 229 24.716 35.143 -3.220 1.00 65.78 O
ATOM 36 N PRO A 230 24.239 32.327 -2.153 1.00 66.91 N
ATOM 37 CA PRO A 230 24.317 31.793 -0.789 1.00 67.68 C
ATOM 38 C PRO A 230 24.165 32.880 0.276 1.00 67.83 C
ATOM 39 O PRO A 230 23.752 32.609 1.406 1.00 68.00 O
ATOM 40 CB PRO A 230 25.702 31.145 -0.751 1.00 67.73 C
ATOM 41 CG PRO A 230 25.937 30.756 -2.179 1.00 67.84 C
ATOM 42 CD PRO A 230 25.446 31.972 -2.919 1.00 66.34 C
ATOM 43 N ASN A 231 24.500 34.111 -0.097 1.00 66.49 N
ATOM 44 CA ASN A 231 24.419 35.239 0.819 1.00 66.05 C
ATOM 45 C ASN A 231 23.237 36.164 0.516 1.00 61.13 C
ATOM 46 O ASN A 231 23.340 37.382 0.668 1.00 58.71 O
ATOM 47 CB ASN A 231 25.726 36.040 0.765 1.00 70.48 C
ATOM 48 CG ASN A 231 26.937 35.211 1.171 1.00 74.28 C
ATOM 49 OD1 ASN A 231 26.811 34.220 1.891 1.00 78.33 O
ATOM 50 ND2 ASN A 231 28.117 35.619 0.716 1.00 74.69 N
ATOM 51 N TYR A 232 22.114 35.591 0.092 1.00 55.17 N
ATOM 52 CA TYR A 232 20.945 36.405 -0.222 1.00 50.20 C
ATOM 53 C TYR A 232 20.279 36.969 1.023 1.00 48.25 C
ATOM 54 O TYR A 232 19.972 36.238 1.966 1.00 52.46 O
ATOM 55 CB TYR A 232 19.891 35.609 -0.999 1.00 46.52 C
ATOM 56 CG TYR A 232 18.676 36.451 -1.350 1.00 43.11 C
ATOM 57 CD1 TYR A 232 18.715 37.355 -2.411 1.00 40.63 C
ATOM 58 CD2 TYR A 232 17.508 36.387 -0.583 1.00 41.66 C
ATOM 59 CE1 TYR A 232 17.625 38.180 -2.700 1.00 42.95 C
ATOM 60 CE2 TYR A 232 16.408 37.210 -0.866 1.00 37.96 C
ATOM 61 CZ TYR A 232 16.478 38.102 -1.921 1.00 39.57 C
ATOM 62 OH TYR A 232 15.420 38.937 -2.194 1.00 40.75 O
ATOM 63 N ASP A 233 20.052 38.274 1.014 1.00 47.94 N
ATOM 64 CA ASP A 233 19.381 38.942 2.122 1.00 46.79 C
ATOM 65 C ASP A 233 18.290 39.792 1.493 1.00 43.90 C
ATOM 66 O ASP A 233 18.582 40.735 0.758 1.00 40.31 O
ATOM 67 CB ASP A 233 20.348 39.842 2.890 1.00 45.63 C
ATOM 68 CG ASP A 233 19.691 40.506 4.088 1.00 51.78 C
ATOM 69 OD1 ASP A 233 18.531 40.963 3.964 1.00 51.54 O
ATOM 70 OD2 ASP A 233 20.334 40.578 5.154 1.00 53.30 O
ATOM 71 N LYS A 234 17.035 39.457 1.771 1.00 43.11 N
ATOM 72 CA LYS A 234 15.920 40.207 1.200 1.00 42.42 C
ATOM 73 C LYS A 234 15.946 41.692 1.557 1.00 41.40 C
ATOM 74 O LYS A 234 15.401 42.516 0.827 1.00 39.09 O
ATOM 75 CB LYS A 234 14.591 39.605 1.655 1.00 44.79 C
ATOM 76 CG LYS A 234 14.361 39.636 3.156 1.00 47.10 C
ATOM 77 CD LYS A 234 13.049 38.955 3.503 1.00 49.82 C
ATOM 78 CE LYS A 234 12.810 38.914 5.001 1.00 51.10 C
ATOM 79 NZ LYS A 234 11.495 38.291 5.325 1.00 49.81 N
ATOM 80 N TRP A 235 16.592 42.034 2.667 1.00 41.10 N
ATOM 81 CA TRP A 235 16.640 43.427 3.107 1.00 40.69 C
ATOM 82 C TRP A 235 17.655 44.315 2.389 1.00 42.11 C
ATOM 83 O TRP A 235 17.481 45.535 2.351 1.00 37.17 O
ATOM 84 CB TRP A 235 16.880 43.493 4.619 1.00 37.95 C
ATOM 85 CG TRP A 235 15.806 42.843 5.431 1.00 34.37 C
ATOM 86 CD1 TRP A 235 15.874 41.639 6.063 1.00 35.72 C
ATOM 87 CD2 TRP A 235 14.500 43.373 5.715 1.00 36.45 C
ATOM 88 NE1 TRP A 235 14.695 41.384 6.729 1.00 38.24 N
ATOM 89 CE2 TRP A 235 13.837 42.433 6.532 1.00 36.83 C
ATOM 90 CE3 TRP A 235 13.830 44.552 5.359 1.00 36.90 C
ATOM 91 CZ2 TRP A 235 12.532 42.634 7.002 1.00 41.62 C
ATOM 92 CZ3 TRP A 235 12.530 44.753 5.827 1.00 40.27 C
ATOM 93 CH2 TRP A 235 11.899 43.798 6.639 1.00 39.51 C
ATOM 94 N GLU A 236 18.707 43.717 1.823 1.00 42.48 N
ATOM 95 CA GLU A 236 19.727 44.490 1.105 1.00 43.64 C
ATOM 96 C GLU A 236 19.069 45.163 -0.085 1.00 46.41 C
ATOM 97 O GLU A 236 18.358 44.515 -0.850 1.00 48.57 O
ATOM 98 CB GLU A 236 20.851 43.584 0.591 1.00 43.17 C
ATOM 99 CG GLU A 236 21.694 42.896 1.661 1.00 45.14 C
ATOM 100 CD GLU A 236 22.663 43.840 2.360 1.00 49.61 C
ATOM 101 OE1 GLU A 236 22.934 44.935 1.822 1.00 47.60 O
ATOM 102 OE2 GLU A 236 23.164 43.475 3.444 1.00 51.07 O
ATOM 103 N MET A 237 19.307 46.457 -0.256 1.00 47.75 N
ATOM 104 CA MET A 237 18.703 47.170 -1.371 1.00 52.18 C
ATOM 105 C MET A 237 19.714 48.004 -2.134 1.00 54.03 C
ATOM 106 O MET A 237 20.879 48.088 -1.750 1.00 53.01 O
ATOM 107 CB MET A 237 17.558 48.059 -0.878 1.00 54.76 C
ATOM 108 CG MET A 237 17.972 49.157 0.078 1.00 62.51 C
ATOM 109 SD MET A 237 16.541 50.098 0.656 1.00 74.54 S
ATOM 110 CE MET A 237 16.249 51.167 -0.758 1.00 74.99 C
ATOM 111 N GLU A 238 19.253 48.628 -3.212 1.00 56.90 N
ATOM 112 CA GLU A 238 20.119 49.442 -4.044 1.00 61.36 C
ATOM 113 C GLU A 238 20.302 50.859 -3.518 1.00 62.92 C
ATOM 114 O GLU A 238 19.362 51.655 -3.466 1.00 61.45 O
ATOM 115 CB GLU A 238 19.585 49.482 -5.478 1.00 66.85 C
ATOM 116 CG GLU A 238 20.532 50.153 -6.466 1.00 75.99 C
ATOM 117 CD GLU A 238 21.924 49.537 -6.452 1.00 80.91 C
ATOM 118 OE1 GLU A 238 22.046 48.327 -6.750 1.00 83.02 O
ATOM 119 OE2 GLU A 238 22.896 50.262 -6.140 1.00 81.87 O
ATOM 120 N ARG A 239 21.535 51.153 -3.127 1.00 62.34 N
ATOM 121 CA ARG A 239 21.921 52.456 -2.608 1.00 65.10 C
ATOM 122 C ARG A 239 21.474 53.576 -3.548 1.00 64.58 C
ATOM 123 O ARG A 239 21.137 54.671 -3.108 1.00 65.28 O
ATOM 124 CB ARG A 239 23.441 52.481 -2.451 1.00 66.01 C
ATOM 125 CG ARG A 239 24.041 53.792 -1.995 1.00 70.00 C
ATOM 126 CD ARG A 239 25.554 53.725 -2.155 1.00 69.64 C
ATOM 127 NE ARG A 239 26.097 52.511 -1.550 1.00 67.44 N
ATOM 128 CZ ARG A 239 26.127 52.277 -0.243 1.00 65.26 C
ATOM 129 NH1 ARG A 239 25.647 53.179 0.601 1.00 65.80 N
ATOM 130 NH2 ARG A 239 26.621 51.138 0.220 1.00 60.60 N
ATOM 131 N THR A 240 21.471 53.281 -4.844 1.00 66.16 N
ATOM 132 CA THR A 240 21.093 54.241 -5.880 1.00 67.57 C
ATOM 133 C THR A 240 19.599 54.568 -5.913 1.00 68.41 C
ATOM 134 O THR A 240 19.195 55.617 -6.420 1.00 66.88 O
ATOM 135 CB THR A 240 21.515 53.719 -7.273 1.00 68.91 C
ATOM 136 OG1 THR A 240 22.941 53.584 -7.319 1.00 70.67 O
ATOM 137 CG2 THR A 240 21.063 54.672 -8.368 1.00 68.90 C
ATOM 138 N ASP A 241 18.786 53.664 -5.376 1.00 69.49 N
ATOM 139 CA ASP A 241 17.336 53.846 -5.339 1.00 70.98 C
ATOM 140 C ASP A 241 16.904 54.991 -4.426 1.00 69.74 C
ATOM 141 O ASP A 241 15.808 55.536 -4.578 1.00 67.19 O
ATOM 142 CB ASP A 241 16.661 52.554 -4.868 1.00 73.87 C
ATOM 143 CG ASP A 241 16.602 51.496 -5.950 1.00 76.31 C
ATOM 144 OD1 ASP A 241 17.617 51.293 -6.649 1.00 77.15 O
ATOM 145 OD2 ASP A 241 15.537 50.859 -6.093 1.00 78.66 O
ATOM 146 N ILE A 242 17.769 55.355 -3.484 1.00 68.06 N
ATOM 147 CA ILE A 242 17.455 56.411 -2.528 1.00 66.29 C
ATOM 148 C ILE A 242 18.124 57.754 -2.799 1.00 66.55 C
ATOM 149 O ILE A 242 19.335 57.833 -2.996 1.00 66.04 O
ATOM 150 CB ILE A 242 17.825 55.972 -1.100 1.00 64.69 C
ATOM 151 CG1 ILE A 242 17.131 54.648 -0.771 1.00 64.66 C
ATOM 152 CG2 ILE A 242 17.426 57.053 -0.106 1.00 63.57 C
ATOM 153 CD1 ILE A 242 17.619 53.992 0.502 1.00 64.35 C
ATOM 154 N THR A 243 17.317 58.810 -2.800 1.00 67.08 N
ATOM 155 CA THR A 243 17.809 60.165 -3.014 1.00 69.10 C
ATOM 156 C THR A 243 18.158 60.736 -1.640 1.00 67.42 C
ATOM 157 O THR A 243 17.268 61.072 -0.861 1.00 65.86 O
ATOM 158 CB THR A 243 16.723 61.058 -3.663 1.00 71.41 C
ATOM 159 OG1 THR A 243 16.308 60.484 -4.907 1.00 74.68 O
ATOM 160 CG2 THR A 243 17.256 62.463 -3.912 1.00 70.63 C
ATOM 161 N MET A 244 19.450 60.829 -1.339 1.00 65.51 N
ATOM 162 CA MET A 244 19.892 61.352 -0.052 1.00 64.75 C
ATOM 163 C MET A 244 19.727 62.859 0.027 1.00 67.28 C
ATOM 164 O MET A 244 19.970 63.570 -0.948 1.00 69.88 O
ATOM 165 CB MET A 244 21.354 60.987 0.193 1.00 63.74 C
ATOM 166 CG MET A 244 21.583 59.509 0.383 1.00 61.24 C
ATOM 167 SD MET A 244 20.719 58.905 1.832 1.00 60.02 S
ATOM 168 CE MET A 244 21.935 59.234 3.098 1.00 55.60 C
ATOM 169 N LYS A 245 19.315 63.343 1.194 1.00 67.03 N
ATOM 170 CA LYS A 245 19.118 64.771 1.391 1.00 66.74 C
ATOM 171 C LYS A 245 19.884 65.301 2.594 1.00 67.96 C
ATOM 172 O LYS A 245 20.999 64.863 2.881 1.00 70.43 O
ATOM 173 CB LYS A 245 17.628 65.083 1.547 1.00 66.80 C
ATOM 174 CG LYS A 245 16.826 64.930 0.268 1.00 68.53 C
ATOM 175 CD LYS A 245 15.367 65.268 0.504 1.00 69.73 C
ATOM 176 CE LYS A 245 14.579 65.259 -0.793 1.00 72.27 C
ATOM 177 NZ LYS A 245 13.135 65.564 -0.567 1.00 71.73 N
ATOM 178 N HIS A 246 19.272 66.250 3.293 1.00 67.70 N
ATOM 179 CA HIS A 246 19.872 66.876 4.463 1.00 68.02 C
ATOM 180 C HIS A 246 19.775 65.984 5.697 1.00 65.33 C
ATOM 181 O HIS A 246 19.018 65.011 5.713 1.00 63.74 O
ATOM 182 CB HIS A 246 19.161 68.198 4.740 1.00 71.81 C
ATOM 183 CG HIS A 246 17.680 68.052 4.906 1.00 75.53 C
ATOM 184 ND1 HIS A 246 17.115 67.376 5.966 1.00 77.95 N
ATOM 185 CD2 HIS A 246 16.651 68.455 4.124 1.00 78.35 C
ATOM 186 CE1 HIS A 246 15.800 67.369 5.829 1.00 78.87 C
ATOM 187 NE2 HIS A 246 15.493 68.016 4.720 1.00 79.65 N
ATOM 188 N LYS A 247 20.543 66.322 6.729 1.00 61.87 N
ATOM 189 CA LYS A 247 20.520 65.560 7.967 1.00 61.27 C
ATOM 190 C LYS A 247 19.179 65.815 8.632 1.00 60.24 C
ATOM 191 O LYS A 247 18.655 66.930 8.591 1.00 59.45 O
ATOM 192 CB LYS A 247 21.648 65.995 8.900 1.00 60.33 C
ATOM 193 CG LYS A 247 23.024 65.863 8.293 1.00 62.87 C
ATOM 194 CD LYS A 247 24.113 66.062 9.330 1.00 65.68 C
ATOM 195 CE LYS A 247 24.133 64.927 10.338 1.00 63.92 C
ATOM 196 NZ LYS A 247 25.293 65.045 11.268 1.00 66.62 N
ATOM 197 N LEU A 248 18.630 64.773 9.241 1.00 58.44 N
ATOM 198 CA LEU A 248 17.339 64.855 9.904 1.00 59.05 C
ATOM 199 C LEU A 248 17.397 65.620 11.223 1.00 59.56 C
ATOM 200 O LEU A 248 18.366 65.514 11.977 1.00 57.75 O
ATOM 201 CB LEU A 248 16.810 63.440 10.144 1.00 57.98 C
ATOM 202 CG LEU A 248 15.358 63.175 9.766 1.00 55.91 C
ATOM 203 CD1 LEU A 248 15.080 63.715 8.372 1.00 58.37 C
ATOM 204 CD2 LEU A 248 15.095 61.687 9.832 1.00 56.69 C
ATOM 205 N GLY A 249 16.350 66.397 11.488 1.00 62.66 N
ATOM 206 CA GLY A 249 16.273 67.164 12.720 1.00 66.14 C
ATOM 207 C GLY A 249 17.475 68.037 13.027 1.00 67.59 C
ATOM 208 O GLY A 249 17.993 68.019 14.144 1.00 68.56 O
ATOM 209 N GLY A 250 17.921 68.803 12.039 1.00 68.57 N
ATOM 210 CA GLY A 250 19.059 69.681 12.244 1.00 70.68 C
ATOM 211 C GLY A 250 20.260 69.044 12.920 1.00 69.94 C
ATOM 212 O GLY A 250 21.095 69.747 13.487 1.00 71.58 O
ATOM 213 N GLY A 251 20.346 67.717 12.877 1.00 69.04 N
ATOM 214 CA GLY A 251 21.479 67.032 13.477 1.00 63.27 C
ATOM 215 C GLY A 251 21.268 66.389 14.837 1.00 61.05 C
ATOM 216 O GLY A 251 22.176 65.729 15.346 1.00 58.23 O
ATOM 217 N GLN A 252 20.087 66.561 15.426 1.00 59.44 N
ATOM 218 CA GLN A 252 19.812 65.988 16.744 1.00 57.04 C
ATOM 219 C GLN A 252 19.933 64.465 16.802 1.00 56.80 C
ATOM 220 O GLN A 252 20.284 63.907 17.844 1.00 56.74 O
ATOM 221 CB GLN A 252 18.423 66.423 17.243 1.00 60.05 C
ATOM 222 CG GLN A 252 17.242 65.992 16.376 1.00 62.36 C
ATOM 223 CD GLN A 252 15.912 66.572 16.857 1.00 64.34 C
ATOM 224 OE1 GLN A 252 15.520 66.394 18.011 1.00 66.78 O
ATOM 225 NE2 GLN A 252 15.213 67.266 15.966 1.00 61.51 N
ATOM 226 N TYR A 253 19.661 63.788 15.690 1.00 53.49 N
ATOM 227 CA TYR A 253 19.748 62.330 15.674 1.00 51.78 C
ATOM 228 C TYR A 253 21.114 61.802 15.262 1.00 51.62 C
ATOM 229 O TYR A 253 21.383 60.608 15.365 1.00 51.47 O
ATOM 230 CB TYR A 253 18.684 61.745 14.751 1.00 48.86 C
ATOM 231 CG TYR A 253 17.281 62.111 15.155 1.00 43.94 C
ATOM 232 CD1 TYR A 253 16.601 63.148 14.524 1.00 40.72 C
ATOM 233 CD2 TYR A 253 16.635 61.427 16.183 1.00 47.98 C
ATOM 234 CE1 TYR A 253 15.306 63.495 14.905 1.00 43.42 C
ATOM 235 CE2 TYR A 253 15.344 61.767 16.574 1.00 46.35 C
ATOM 236 CZ TYR A 253 14.687 62.799 15.932 1.00 42.81 C
ATOM 237 OH TYR A 253 13.413 63.123 16.323 1.00 48.55 O
ATOM 238 N GLY A 254 21.979 62.693 14.799 1.00 53.67 N
ATOM 239 CA GLY A 254 23.299 62.270 14.381 1.00 51.94 C
ATOM 240 C GLY A 254 23.345 62.070 12.881 1.00 52.22 C
ATOM 241 O GLY A 254 22.706 62.813 12.134 1.00 51.39 O
ATOM 242 N GLU A 255 24.092 61.061 12.442 1.00 49.22 N
ATOM 243 CA GLU A 255 24.235 60.763 11.023 1.00 49.63 C
ATOM 244 C GLU A 255 22.998 60.105 10.418 1.00 48.16 C
ATOM 245 O GLU A 255 23.084 59.029 9.822 1.00 46.17 O
ATOM 246 CB GLU A 255 25.452 59.864 10.795 1.00 53.08 C
ATOM 247 CG GLU A 255 26.788 60.532 11.102 1.00 61.51 C
ATOM 248 CD GLU A 255 27.021 61.787 10.274 1.00 66.06 C
ATOM 249 OE1 GLU A 255 26.880 61.719 9.033 1.00 66.28 O
ATOM 250 OE2 GLU A 255 27.350 62.840 10.863 1.00 69.86 O
ATOM 251 N VAL A 256 21.848 60.752 10.578 1.00 43.76 N
ATOM 252 CA VAL A 256 20.605 60.238 10.024 1.00 41.44 C
ATOM 253 C VAL A 256 20.060 61.267 9.052 1.00 42.09 C
ATOM 254 O VAL A 256 19.820 62.413 9.423 1.00 43.44 O
ATOM 255 CB VAL A 256 19.565 59.973 11.120 1.00 40.49 C
ATOM 256 CG1 VAL A 256 18.282 59.446 10.489 1.00 36.23 C
ATOM 257 CG2 VAL A 256 20.120 58.966 12.128 1.00 35.69 C
ATOM 258 N TYR A 257 19.860 60.853 7.807 1.00 42.35 N
ATOM 259 CA TYR A 257 19.384 61.766 6.779 1.00 44.91 C
ATOM 260 C TYR A 257 17.996 61.465 6.244 1.00 45.99 C
ATOM 261 O TYR A 257 17.520 60.329 6.295 1.00 45.15 O
ATOM 262 CB TYR A 257 20.361 61.774 5.592 1.00 43.74 C
ATOM 263 CG TYR A 257 21.788 62.118 5.956 1.00 44.36 C
ATOM 264 CD1 TYR A 257 22.560 61.253 6.733 1.00 44.33 C
ATOM 265 CD2 TYR A 257 22.361 63.316 5.539 1.00 46.49 C
ATOM 266 CE1 TYR A 257 23.862 61.575 7.091 1.00 49.80 C
ATOM 267 CE2 TYR A 257 23.667 63.652 5.891 1.00 49.96 C
ATOM 268 CZ TYR A 257 24.410 62.780 6.670 1.00 53.56 C
ATOM 269 OH TYR A 257 25.687 63.126 7.056 1.00 56.22 O
ATOM 270 N GLU A 258 17.349 62.505 5.735 1.00 45.89 N
ATOM 271 CA GLU A 258 16.044 62.345 5.124 1.00 50.20 C
ATOM 272 C GLU A 258 16.372 61.849 3.723 1.00 49.54 C
ATOM 273 O GLU A 258 17.372 62.259 3.133 1.00 48.75 O
ATOM 274 CB GLU A 258 15.304 63.681 5.030 1.00 51.89 C
ATOM 275 CG GLU A 258 13.954 63.575 4.327 1.00 57.93 C
ATOM 276 CD GLU A 258 13.162 64.871 4.364 1.00 64.20 C
ATOM 277 OE1 GLU A 258 13.608 65.863 3.751 1.00 67.16 O
ATOM 278 OE2 GLU A 258 12.091 64.895 5.011 1.00 66.36 O
ATOM 279 N GLY A 259 15.542 60.964 3.194 1.00 50.84 N
ATOM 280 CA GLY A 259 15.795 60.449 1.867 1.00 53.70 C
ATOM 281 C GLY A 259 14.512 60.212 1.109 1.00 55.83 C
ATOM 282 O GLY A 259 13.420 60.274 1.676 1.00 56.23 O
ATOM 283 N VAL A 260 14.643 59.947 -0.184 1.00 57.31 N
ATOM 284 CA VAL A 260 13.485 59.689 -1.020 1.00 58.97 C
ATOM 285 C VAL A 260 13.676 58.371 -1.750 1.00 60.14 C
ATOM 286 O VAL A 260 14.567 58.242 -2.588 1.00 59.15 O
ATOM 287 CB VAL A 260 13.285 60.802 -2.064 1.00 59.26 C
ATOM 288 CG1 VAL A 260 11.971 60.590 -2.798 1.00 59.57 C
ATOM 289 CG2 VAL A 260 13.308 62.162 -1.385 1.00 60.54 C
ATOM 290 N TRP A 261 12.853 57.384 -1.419 1.00 60.87 N
ATOM 291 CA TRP A 261 12.949 56.099 -2.085 1.00 62.33 C
ATOM 292 C TRP A 261 12.224 56.267 -3.418 1.00 64.33 C
ATOM 293 O TRP A 261 11.043 55.944 -3.544 1.00 62.30 O
ATOM 294 CB TRP A 261 12.292 55.003 -1.243 1.00 62.64 C
ATOM 295 CG TRP A 261 12.711 53.618 -1.644 1.00 64.19 C
ATOM 296 CD1 TRP A 261 13.631 53.284 -2.598 1.00 64.54 C
ATOM 297 CD2 TRP A 261 12.244 52.382 -1.088 1.00 66.16 C
ATOM 298 NE1 TRP A 261 13.766 51.920 -2.670 1.00 65.70 N
ATOM 299 CE2 TRP A 261 12.927 51.340 -1.756 1.00 67.43 C
ATOM 300 CE3 TRP A 261 11.315 52.053 -0.093 1.00 66.69 C
ATOM 301 CZ2 TRP A 261 12.712 49.991 -1.458 1.00 67.72 C
ATOM 302 CZ3 TRP A 261 11.099 50.711 0.204 1.00 67.55 C
ATOM 303 CH2 TRP A 261 11.795 49.697 -0.479 1.00 68.98 C
ATOM 304 N LYS A 262 12.953 56.799 -4.396 1.00 67.46 N
ATOM 305 CA LYS A 262 12.450 57.065 -5.743 1.00 70.51 C
ATOM 306 C LYS A 262 11.337 56.135 -6.213 1.00 71.37 C
ATOM 307 O LYS A 262 10.214 56.571 -6.470 1.00 70.06 O
ATOM 308 CB LYS A 262 13.600 56.991 -6.748 1.00 72.64 C
ATOM 309 CG LYS A 262 14.771 57.914 -6.458 1.00 74.62 C
ATOM 310 CD LYS A 262 15.854 57.726 -7.509 1.00 76.61 C
ATOM 311 CE LYS A 262 17.029 58.656 -7.290 1.00 79.97 C
ATOM 312 NZ LYS A 262 18.071 58.461 -8.339 1.00 81.88 N
ATOM 313 N LYS A 263 11.672 54.855 -6.330 1.00 73.06 N
ATOM 314 CA LYS A 263 10.748 53.823 -6.789 1.00 75.17 C
ATOM 315 C LYS A 263 9.336 53.918 -6.208 1.00 75.34 C
ATOM 316 O LYS A 263 8.398 53.340 -6.755 1.00 75.96 O
ATOM 317 CB LYS A 263 11.337 52.444 -6.481 1.00 76.94 C
ATOM 318 CG LYS A 263 10.609 51.282 -7.132 1.00 78.96 C
ATOM 319 CD LYS A 263 11.225 49.950 -6.724 1.00 81.00 C
ATOM 320 CE LYS A 263 12.696 49.868 -7.100 1.00 82.63 C
ATOM 321 NZ LYS A 263 13.313 48.592 -6.636 1.00 83.28 N
ATOM 322 N TYR A 264 9.178 54.639 -5.102 1.00 74.56 N
ATOM 323 CA TYR A 264 7.865 54.775 -4.486 1.00 72.45 C
ATOM 324 C TYR A 264 7.554 56.210 -4.067 1.00 70.42 C
ATOM 325 O TYR A 264 6.547 56.465 -3.403 1.00 67.50 O
ATOM 326 CB TYR A 264 7.758 53.846 -3.274 1.00 76.26 C
ATOM 327 CG TYR A 264 8.166 52.418 -3.566 1.00 79.90 C
ATOM 328 CD1 TYR A 264 9.509 52.042 -3.564 1.00 82.83 C
ATOM 329 CD2 TYR A 264 7.214 51.450 -3.881 1.00 81.18 C
ATOM 330 CE1 TYR A 264 9.895 50.738 -3.870 1.00 83.07 C
ATOM 331 CE2 TYR A 264 7.588 50.143 -4.191 1.00 82.35 C
ATOM 332 CZ TYR A 264 8.930 49.794 -4.184 1.00 83.29 C
ATOM 333 OH TYR A 264 9.310 48.507 -4.499 1.00 84.17 O
ATOM 334 N SER A 265 8.411 57.146 -4.466 1.00 68.74 N
ATOM 335 CA SER A 265 8.224 58.553 -4.118 1.00 67.51 C
ATOM 336 C SER A 265 7.960 58.633 -2.618 1.00 64.13 C
ATOM 337 O SER A 265 7.168 59.452 -2.153 1.00 65.76 O
ATOM 338 CB SER A 265 7.032 59.133 -4.882 1.00 69.42 C
ATOM 339 OG SER A 265 7.171 58.920 -6.275 1.00 72.47 O
ATOM 340 N LEU A 266 8.639 57.770 -1.872 1.00 58.48 N
ATOM 341 CA LEU A 266 8.480 57.695 -0.429 1.00 53.91 C
ATOM 342 C LEU A 266 9.614 58.376 0.328 1.00 51.41 C
ATOM 343 O LEU A 266 10.793 58.124 0.062 1.00 50.02 O
ATOM 344 CB LEU A 266 8.401 56.228 -0.006 1.00 51.74 C
ATOM 345 CG LEU A 266 8.126 55.926 1.468 1.00 53.35 C
ATOM 346 CD1 LEU A 266 6.696 56.323 1.812 1.00 50.66 C
ATOM 347 CD2 LEU A 266 8.340 54.444 1.732 1.00 48.73 C
ATOM 348 N THR A 267 9.252 59.247 1.266 1.00 47.07 N
ATOM 349 CA THR A 267 10.247 59.930 2.081 1.00 44.50 C
ATOM 350 C THR A 267 10.635 58.958 3.188 1.00 41.84 C
ATOM 351 O THR A 267 9.771 58.382 3.848 1.00 40.72 O
ATOM 352 CB THR A 267 9.691 61.212 2.708 1.00 45.02 C
ATOM 353 OG1 THR A 267 9.328 62.129 1.672 1.00 46.49 O
ATOM 354 CG2 THR A 267 10.736 61.856 3.606 1.00 40.98 C
ATOM 355 N VAL A 268 11.935 58.779 3.386 1.00 37.58 N
ATOM 356 CA VAL A 268 12.429 57.849 4.387 1.00 36.97 C
ATOM 357 C VAL A 268 13.546 58.467 5.214 1.00 39.82 C
ATOM 358 O VAL A 268 14.052 59.543 4.891 1.00 39.44 O
ATOM 359 CB VAL A 268 12.996 56.566 3.717 1.00 36.94 C
ATOM 360 CG1 VAL A 268 11.950 55.938 2.803 1.00 39.02 C
ATOM 361 CG2 VAL A 268 14.248 56.907 2.925 1.00 33.41 C
ATOM 362 N ALA A 269 13.915 57.776 6.289 1.00 36.76 N
ATOM 363 CA ALA A 269 15.004 58.208 7.156 1.00 35.79 C
ATOM 364 C ALA A 269 16.121 57.206 6.899 1.00 36.85 C
ATOM 365 O ALA A 269 15.887 56.000 6.889 1.00 36.10 O
ATOM 366 CB ALA A 269 14.583 58.157 8.619 1.00 28.49 C
ATOM 367 N VAL A 270 17.332 57.702 6.686 1.00 38.68 N
ATOM 368 CA VAL A 270 18.457 56.827 6.414 1.00 39.33 C
ATOM 369 C VAL A 270 19.606 57.048 7.389 1.00 41.20 C
ATOM 370 O VAL A 270 20.265 58.088 7.367 1.00 39.20 O
ATOM 371 CB VAL A 270 18.978 57.033 4.967 1.00 41.50 C
ATOM 372 CG1 VAL A 270 20.112 56.061 4.671 1.00 44.19 C
ATOM 373 CG2 VAL A 270 17.843 56.838 3.971 1.00 40.59 C
ATOM 374 N LYS A 271 19.832 56.072 8.262 1.00 41.77 N
ATOM 375 CA LYS A 271 20.934 56.165 9.198 1.00 42.80 C
ATOM 376 C LYS A 271 22.155 55.632 8.458 1.00 48.02 C
ATOM 377 O LYS A 271 22.061 54.651 7.716 1.00 44.88 O
ATOM 378 CB LYS A 271 20.684 55.319 10.447 1.00 41.74 C
ATOM 379 CG LYS A 271 21.824 55.414 11.465 1.00 40.61 C
ATOM 380 CD LYS A 271 21.542 54.654 12.745 1.00 39.04 C
ATOM 381 CE LYS A 271 22.647 54.906 13.769 1.00 43.13 C
ATOM 382 NZ LYS A 271 22.429 54.229 15.083 1.00 41.62 N
ATOM 383 N THR A 272 23.292 56.289 8.642 1.00 50.52 N
ATOM 384 CA THR A 272 24.514 55.857 7.990 1.00 57.69 C
ATOM 385 C THR A 272 25.669 55.875 8.981 1.00 61.64 C
ATOM 386 O THR A 272 25.496 56.238 10.146 1.00 57.70 O
ATOM 387 CB THR A 272 24.858 56.749 6.786 1.00 57.28 C
ATOM 388 OG1 THR A 272 26.062 56.271 6.175 1.00 61.89 O
ATOM 389 CG2 THR A 272 25.048 58.195 7.223 1.00 59.11 C
ATOM 390 N LEU A 273 26.848 55.476 8.520 1.00 66.84 N
ATOM 391 CA LEU A 273 28.011 55.436 9.391 1.00 73.77 C
ATOM 392 C LEU A 273 29.035 56.489 8.986 1.00 78.92 C
ATOM 393 O LEU A 273 29.333 56.657 7.801 1.00 78.87 O
ATOM 394 CB LEU A 273 28.630 54.040 9.344 1.00 72.50 C
ATOM 395 CG LEU A 273 29.473 53.616 10.542 1.00 73.48 C
ATOM 396 CD1 LEU A 273 28.739 53.933 11.834 1.00 71.62 C
ATOM 397 CD2 LEU A 273 29.764 52.126 10.441 1.00 74.69 C
ATOM 398 N LYS A 274 29.566 57.202 9.976 1.00 85.21 N
ATOM 399 CA LYS A 274 30.554 58.245 9.722 1.00 91.78 C
ATOM 400 C LYS A 274 31.666 57.720 8.818 1.00 95.68 C
ATOM 401 O LYS A 274 31.762 56.518 8.568 1.00 96.61 O
ATOM 402 CB LYS A 274 31.163 58.753 11.035 1.00 91.97 C
ATOM 403 CG LYS A 274 30.158 59.196 12.091 1.00 92.15 C
ATOM 404 CD LYS A 274 29.666 58.017 12.918 1.00 92.01 C
ATOM 405 CE LYS A 274 28.856 58.484 14.115 1.00 93.16 C
ATOM 406 NZ LYS A 274 28.526 57.359 15.036 1.00 94.89 N
ATOM 407 N GLU A 275 32.507 58.630 8.339 1.00 99.49 N
ATOM 408 CA GLU A 275 33.609 58.280 7.451 1.00103.37 C
ATOM 409 C GLU A 275 34.483 57.161 8.014 1.00104.67 C
ATOM 410 O GLU A 275 35.564 57.412 8.545 1.00104.96 O
ATOM 411 CB GLU A 275 34.466 59.518 7.180 1.00105.54 C
ATOM 412 CG GLU A 275 33.665 60.798 6.942 1.00109.06 C
ATOM 413 CD GLU A 275 32.617 60.658 5.849 1.00110.66 C
ATOM 414 OE1 GLU A 275 31.646 59.893 6.041 1.00112.02 O
ATOM 415 OE2 GLU A 275 32.763 61.316 4.797 1.00111.60 O
ATOM 416 N ASP A 276 34.004 55.927 7.891 1.00106.84 N
ATOM 417 CA ASP A 276 34.727 54.755 8.374 1.00108.62 C
ATOM 418 C ASP A 276 35.102 54.870 9.850 1.00108.52 C
ATOM 419 O ASP A 276 36.228 55.235 10.189 1.00108.58 O
ATOM 420 CB ASP A 276 35.985 54.545 7.529 1.00110.36 C
ATOM 421 CG ASP A 276 35.673 54.388 6.052 1.00112.32 C
ATOM 422 OD1 ASP A 276 36.624 54.333 5.244 1.00114.19 O
ATOM 423 OD2 ASP A 276 34.476 54.318 5.699 1.00112.05 O
ATOM 424 N THR A 277 34.150 54.548 10.721 1.00108.10 N
ATOM 425 CA THR A 277 34.370 54.612 12.161 1.00107.87 C
ATOM 426 C THR A 277 34.409 53.212 12.772 1.00107.13 C
ATOM 427 O THR A 277 33.844 52.268 12.221 1.00108.80 O
ATOM 428 CB THR A 277 33.265 55.442 12.851 1.00108.53 C