HEADER TRANSFERASE 10-APR-01 1IEP
TITLE CRYSTAL STRUCTURE OF THE C-ABL KINASE DOMAIN IN COMPLEX 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, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NAGAR,W.BORNMANN,T.SCHINDLER,B.CLARKSON,J.KURIYAN
REVDAT 4 09-AUG-23 1IEP 1 REMARK SEQADV HETSYN
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,D.R.VEACH,
JRNL AUTH 2 W.T.MILLER,B.CLARKSON,J.KURIYAN
JRNL TITL CRYSTAL STRUCTURES OF THE KINASE DOMAIN OF C-ABL IN COMPLEX
JRNL TITL 2 WITH THE SMALL MOLECULE INHIBITORS PD173955 AND IMATINIB
JRNL TITL 3 (STI-571)
JRNL REF CANCER RES. V. 62 4236 2002
JRNL REFN ISSN 0008-5472
JRNL PMID 12154025
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.690
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 : 0.35
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. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013215.
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, PH
REMARK 280 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
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI A 201
REMARK 800
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 A 4 1
HET CL A 5 1
HET STI A 201 37
HET CL B 3 1
HET CL B 6 1
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 7 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 LINES ARE NOT SHOWN.)
END
