HEADER TRANSFERASE 27-JUL-07 2V7A
TITLE CRYSTAL STRUCTURE OF THE T315I ABL MUTANT IN COMPLEX WITH THE
TITLE 2 INHIBITOR PHA-739358
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 229-512;
COMPND 5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1, P150, C-
COMPND 6 ABL;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: AUTOGRAPHA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 254361;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS KINASE, NUCLEUS, MYRISTATE, CYTOPLASM, MANGANESE, CELL ADHESION,
KEYWDS 2 METAL-BINDING, PROTO-ONCOGENE, TYROSINE-PROTEIN KINASE, CHROMOSOMAL
KEYWDS 3 REARRANGEMENT, TRANSFERASE, LIPOPROTEIN, POLYMORPHISM, CYTOSKELETON,
KEYWDS 4 MAGNESIUM, SH2 DOMAIN, SH3 DOMAIN, ATP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 5 ALTERNATIVE SPLICING, PHOSPHORYLATION, KINASE INHIBITOR, T315I ABL
KEYWDS 6 MUTANT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MODUGNO,E.CASALE,C.SONCINI,P.ROSETTANI,R.COLOMBO,R.LUPI,L.RUSCONI,
AUTHOR 2 D.FANCELLI,P.CARPINELLI,A.D.CAMERON,A.ISACCHI,J.MOLL
REVDAT 6 13-DEC-23 2V7A 1 REMARK LINK
REVDAT 5 16-OCT-19 2V7A 1 REMARK
REVDAT 4 03-APR-19 2V7A 1 SOURCE LINK
REVDAT 3 29-JUL-15 2V7A 1 REMARK VERSN HETSYN FORMUL
REVDAT 2 24-FEB-09 2V7A 1 VERSN
REVDAT 1 18-SEP-07 2V7A 0
JRNL AUTH M.MODUGNO,E.CASALE,C.SONCINI,P.ROSETTANI,R.COLOMBO,R.LUPI,
JRNL AUTH 2 L.RUSCONI,D.FANCELLI,P.CARPINELLI,A.D.CAMERON,A.ISACCHI,
JRNL AUTH 3 J.MOLL
JRNL TITL CRYSTAL STRUCTURE OF THE T315I ABL MUTANT IN COMPLEX WITH
JRNL TITL 2 THE AURORA KINASES INHIBITOR PHA-739358.
JRNL REF CANCER RES. V. 67 7987 2007
JRNL REFN ISSN 0008-5472
JRNL PMID 17804707
JRNL DOI 10.1158/0008-5472.CAN-07-1825
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27517
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1476
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2007
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4400
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59000
REMARK 3 B22 (A**2) : 0.59000
REMARK 3 B33 (A**2) : -0.88000
REMARK 3 B12 (A**2) : 0.29000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.378
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.257
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.168
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4590 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6219 ; 1.580 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 537 ; 6.596 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;39.781 ;24.218
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 803 ;16.241 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;14.912 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 653 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3480 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2113 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3118 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 228 ; 0.153 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 50 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.116 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2V7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1290033293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29049
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1FPU
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000 ,1M HEPES PH 7.0, 0.1 M
REMARK 280 MGCL2,
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.95400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.97700
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.95400
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 18.97700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 315 TO ILE
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 315 TO ILE
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 227
REMARK 465 PRO A 228
REMARK 465 SER A 229
REMARK 465 PRO A 230
REMARK 465 ASN A 231
REMARK 465 TYR A 232
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 GLY B 227
REMARK 465 PRO B 228
REMARK 465 SER B 229
REMARK 465 PRO B 230
REMARK 465 ASN B 231
REMARK 465 TYR B 232
REMARK 465 ASP B 233
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 503 CA C O CB OG
REMARK 470 SER B 503 CA C O CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 363 O HOH A 2050 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 239 -38.58 -36.18
REMARK 500 GLU A 275 -32.18 -39.39
REMARK 500 THR A 306 37.29 -142.36
REMARK 500 GLU A 308 158.64 166.54
REMARK 500 ASN A 336 -169.34 -104.96
REMARK 500 ARG A 362 8.16 83.27
REMARK 500 ASP A 363 32.62 -153.59
REMARK 500 ASP A 381 66.73 64.01
REMARK 500 TYR A 440 61.50 39.37
REMARK 500 ILE A 502 -71.29 -123.46
REMARK 500 LYS B 245 -145.90 -106.07
REMARK 500 LYS B 274 154.90 -46.83
REMARK 500 LEU B 302 -62.60 -105.96
REMARK 500 CYS B 330 160.82 -49.51
REMARK 500 ARG B 362 -18.98 77.78
REMARK 500 ALA B 380 -166.43 -120.25
REMARK 500 HIS B 396 155.52 -46.19
REMARK 500 PRO B 402 88.08 -64.58
REMARK 500 ASP B 455 5.76 85.39
REMARK 500 ILE B 502 -83.05 -117.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 368 OD1
REMARK 620 2 ASP A 381 OD1 77.0
REMARK 620 3 HOH A2054 O 70.9 91.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 627 A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 627 B 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AB2 RELATED DB: PDB
REMARK 900 PROTO-ONCOGENE TYROSINE KINASE (SRC HOMOLOGY 2 DOMAIN) ("ABELSON",
REMARK 900 SH2 ABL) (NMR, 20 STRUCTURES)
REMARK 900 RELATED ID: 1JU5 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF AN CRK SH2 DOMAIN, CRK -DERIVEDPHOPHOPEPTIDE,
REMARK 900 AND ABL SH3 DOMAIN BY NMR SPECTROSCOPY
REMARK 900 RELATED ID: 2F4J RELATED DB: PDB
REMARK 900 STRUCTURE OF THE KINASE DOMAIN OF AN IMATINIB-RESISTANT ABLMUTANT
REMARK 900 IN COMPLEX WITH THE AURORA KINASE INHIBITOR VX-680
REMARK 900 RELATED ID: 2G2F RELATED DB: PDB
REMARK 900 A SRC-LIKE INACTIVE CONFORMATION IN THE ABL TYROSINE KINASEDOMAIN
REMARK 900 RELATED ID: 2GQG RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DASATINIB (BMS- 354825) BOUND
REMARK 900 TOACTIVATED ABL KINASE DOMAIN
REMARK 900 RELATED ID: 1ABL RELATED DB: PDB
REMARK 900 PROTO-ONCOGENE TYROSINE KINASE (SH3 ABL DOMAIN) (THEORETICAL MODEL)
REMARK 900 RELATED ID: 1AWO RELATED DB: PDB
REMARK 900 THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2
REMARK 900 IN THE SH(32) CONSTRUCT, 20 STRUCTURES
REMARK 900 RELATED ID: 1BBZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED
REMARK 900 HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND
REMARK 900 INTERACTIONS
REMARK 900 RELATED ID: 1OPL RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE AUTO-INHIBITION OF C-ABL TYROSINEKINASE
REMARK 900 RELATED ID: 1ZZP RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE F-ACTIN BINDING DOMAIN OF BCR-ABL/C-ABL
REMARK 900 RELATED ID: 2ABL RELATED DB: PDB
REMARK 900 SH3-SH2 DOMAIN FRAGMENT OF HUMAN BCR-ABL TYROSINE KINASE
REMARK 900 RELATED ID: 2FO0 RELATED DB: PDB
REMARK 900 ORGANIZATION OF THE SH3-SH2 UNIT IN ACTIVE AND INACTIVEFORMS OF THE
REMARK 900 C-ABL TYROSINE KINASE
REMARK 900 RELATED ID: 2G2H RELATED DB: PDB
REMARK 900 A SRC-LIKE INACTIVE CONFORMATION IN THE ABL TYROSINE KINASEDOMAIN
DBREF 2V7A A 227 228 PDB 2V7A 2V7A 227 228
DBREF 2V7A A 229 512 UNP P00519 ABL1_HUMAN 229 512
DBREF 2V7A B 227 228 PDB 2V7A 2V7A 227 228
DBREF 2V7A B 229 512 UNP P00519 ABL1_HUMAN 229 512
SEQADV 2V7A ILE A 315 UNP P00519 THR 315 ENGINEERED MUTATION
SEQADV 2V7A ILE B 315 UNP P00519 THR 315 ENGINEERED MUTATION
SEQRES 1 A 286 GLY PRO SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG
SEQRES 2 A 286 THR ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN
SEQRES 3 A 286 TYR GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER
SEQRES 4 A 286 LEU THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET
SEQRES 5 A 286 GLU VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS
SEQRES 6 A 286 GLU ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL
SEQRES 7 A 286 CYS THR ARG GLU PRO PRO PHE TYR ILE ILE ILE GLU PHE
SEQRES 8 A 286 MET THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS
SEQRES 9 A 286 ASN ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET
SEQRES 10 A 286 ALA THR GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS
SEQRES 11 A 286 LYS ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN CYS
SEQRES 12 A 286 LEU VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE
SEQRES 13 A 286 GLY LEU SER ARG LEU MET THR GLY ASP THR PTR THR ALA
SEQRES 14 A 286 HIS ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO
SEQRES 15 A 286 GLU SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP
SEQRES 16 A 286 VAL TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR
SEQRES 17 A 286 TYR GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN
SEQRES 18 A 286 VAL TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG
SEQRES 19 A 286 PRO GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG
SEQRES 20 A 286 ALA CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE
SEQRES 21 A 286 ALA GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU
SEQRES 22 A 286 SER SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS
SEQRES 1 B 286 GLY PRO SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG
SEQRES 2 B 286 THR ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN
SEQRES 3 B 286 TYR GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER
SEQRES 4 B 286 LEU THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET
SEQRES 5 B 286 GLU VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS
SEQRES 6 B 286 GLU ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL
SEQRES 7 B 286 CYS THR ARG GLU PRO PRO PHE TYR ILE ILE ILE GLU PHE
SEQRES 8 B 286 MET THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS
SEQRES 9 B 286 ASN ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET
SEQRES 10 B 286 ALA THR GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS
SEQRES 11 B 286 LYS ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN CYS
SEQRES 12 B 286 LEU VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE
SEQRES 13 B 286 GLY LEU SER ARG LEU MET THR GLY ASP THR PTR THR ALA
SEQRES 14 B 286 HIS ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO
SEQRES 15 B 286 GLU SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP
SEQRES 16 B 286 VAL TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR
SEQRES 17 B 286 TYR GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN
SEQRES 18 B 286 VAL TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG
SEQRES 19 B 286 PRO GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG
SEQRES 20 B 286 ALA CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE
SEQRES 21 B 286 ALA GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU
SEQRES 22 B 286 SER SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS
MODRES 2V7A PTR A 393 TYR O-PHOSPHOTYROSINE
MODRES 2V7A PTR B 393 TYR O-PHOSPHOTYROSINE
HET PTR A 393 16
HET PTR B 393 16
HET 627 A1504 35
HET MG A1505 1
HET 627 B1504 35
HET MG B1505 1
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 627 N-[(3E)-5-[(2R)-2-METHOXY-2-PHENYLACETYL]PYRROLO[3,4-
HETNAM 2 627 C]PYRAZOL-3(5H)-YLIDENE]-4-(4-METHYLPIPERAZIN-1-YL)
HETNAM 3 627 BENZAMIDE
HETNAM MG MAGNESIUM ION
HETSYN PTR PHOSPHONOTYROSINE
HETSYN 627 DANUSERTIB; PHA-739358
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 3 627 2(C26 H30 N6 O3)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *166(H2 O)
HELIX 1 1 GLU A 238 THR A 240 5 3
HELIX 2 2 LYS A 263 SER A 265 5 3
HELIX 3 3 GLU A 279 LYS A 291 1 13
HELIX 4 4 ASN A 322 CYS A 330 1 9
HELIX 5 5 ASN A 336 LYS A 357 1 22
HELIX 6 6 ALA A 365 ARG A 367 5 3
HELIX 7 7 ASP A 381 SER A 385 5 5
HELIX 8 8 PRO A 402 THR A 406 5 5
HELIX 9 9 ALA A 407 ASN A 414 1 8
HELIX 10 10 SER A 417 THR A 434 1 18
HELIX 11 11 ASP A 444 SER A 446 5 3
HELIX 12 12 GLN A 447 LYS A 454 1 8
HELIX 13 13 PRO A 465 TRP A 476 1 12
HELIX 14 14 ASN A 479 ARG A 483 5 5
HELIX 15 15 SER A 485 SER A 501 1 17
HELIX 16 16 GLU B 238 THR B 240 5 3
HELIX 17 17 LYS B 263 SER B 265 5 3
HELIX 18 18 GLU B 279 LYS B 291 1 13
HELIX 19 19 ASN B 322 CYS B 330 1 9
HELIX 20 20 ASN B 336 LYS B 357 1 22
HELIX 21 21 ALA B 365 ARG B 367 5 3
HELIX 22 22 GLU B 373 HIS B 375 5 3
HELIX 23 23 PRO B 402 THR B 406 5 5
HELIX 24 24 ALA B 407 ASN B 414 1 8
HELIX 25 25 SER B 417 TYR B 435 1 19
HELIX 26 26 GLN B 447 LYS B 454 1 8
HELIX 27 27 PRO B 465 TRP B 476 1 12
HELIX 28 28 ASN B 479 ARG B 483 5 5
HELIX 29 29 SER B 485 SER B 501 1 17
SHEET 1 AA 5 ILE A 242 LYS A 247 0
SHEET 2 AA 5 VAL A 256 TRP A 261 -1 O GLU A 258 N LYS A 245
SHEET 3 AA 5 LEU A 266 THR A 272 -1 O LEU A 266 N TRP A 261
SHEET 4 AA 5 TYR A 312 GLU A 316 -1 O ILE A 313 N LYS A 271
SHEET 5 AA 5 LEU A 301 CYS A 305 -1 N LEU A 302 O ILE A 314
SHEET 1 AB 2 PHE A 359 ILE A 360 0
SHEET 2 AB 2 ARG A 386 LEU A 387 -1 O ARG A 386 N ILE A 360
SHEET 1 AC 2 CYS A 369 VAL A 371 0
SHEET 2 AC 2 VAL A 377 VAL A 379 -1 O LYS A 378 N LEU A 370
SHEET 1 AD 2 PTR A 393 THR A 394 0
SHEET 2 AD 2 LYS A 415 PHE A 416 -1 O PHE A 416 N PTR A 393
SHEET 1 BA 5 ILE B 242 LYS B 247 0
SHEET 2 BA 5 VAL B 256 TRP B 261 -1 O GLU B 258 N LYS B 245
SHEET 3 BA 5 LEU B 266 LEU B 273 -1 O LEU B 266 N TRP B 261
SHEET 4 BA 5 PHE B 311 GLU B 316 -1 O PHE B 311 N LEU B 273
SHEET 5 BA 5 LEU B 301 CYS B 305 -1 N LEU B 302 O ILE B 314
SHEET 1 BB 2 PHE B 359 ILE B 360 0
SHEET 2 BB 2 ARG B 386 LEU B 387 -1 O ARG B 386 N ILE B 360
SHEET 1 BC 2 CYS B 369 VAL B 371 0
SHEET 2 BC 2 VAL B 377 VAL B 379 -1 O LYS B 378 N LEU B 370
SHEET 1 BD 2 PTR B 393 THR B 394 0
SHEET 2 BD 2 LYS B 415 PHE B 416 -1 O PHE B 416 N PTR B 393
LINK C THR A 392 N PTR A 393 1555 1555 1.33
LINK C PTR A 393 N THR A 394 1555 1555 1.32
LINK C THR B 392 N PTR B 393 1555 1555 1.34
LINK C PTR B 393 N THR B 394 1555 1555 1.33
LINK OD1 ASN A 368 MG MG A1505 1555 1555 2.44
LINK OD1 ASP A 381 MG MG A1505 1555 1555 2.06
LINK MG MG A1505 O HOH A2054 1555 1555 2.40
LINK OD1 ASP B 381 MG MG B1505 1555 1555 2.21
CISPEP 1 PRO A 309 PRO A 310 0 -22.73
CISPEP 2 PRO B 309 PRO B 310 0 -8.77
SITE 1 AC1 13 LEU A 248 GLY A 250 ALA A 269 LYS A 271
SITE 2 AC1 13 GLU A 316 PHE A 317 MET A 318 THR A 319
SITE 3 AC1 13 GLY A 321 ARG A 367 LEU A 370 HOH A2006
SITE 4 AC1 13 HOH A2104
SITE 1 AC2 13 LEU B 248 GLY B 250 ALA B 269 LYS B 271
SITE 2 AC2 13 GLU B 316 PHE B 317 MET B 318 THR B 319
SITE 3 AC2 13 GLY B 321 ARG B 367 LEU B 370 ASP B 381
SITE 4 AC2 13 HOH B2062
SITE 1 AC3 3 ASN A 368 ASP A 381 HOH A2054
SITE 1 AC4 2 ASN B 368 ASP B 381
CRYST1 159.757 159.757 56.931 90.00 90.00 120.00 P 62 12
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 0.006260 0.003614 0.000000 0.00000
SCALE2 0.000000 0.007228 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017565 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
