HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-FEB-11 3QRJ
TITLE THE CRYSTAL STRUCTURE OF HUMAN ABL1 KINASE DOMAIN T315I MUTANT IN
TITLE 2 COMPLEX WITH DCC-2036
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 229-499;
COMPND 5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1, PROTO-
COMPND 6 ONCOGENE C-ABL, P150;
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 GENE: ABL1, ABL, JTK7;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS ABL1, KINASE, KINASE DOMAIN, T315I, GATEKEEPER MUTATION, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.W.CHAN,S.C.WISE,M.D.KAUFMAN,Y.M.AHN,C.L.ENSINGER,T.HAACK,M.M.HOOD,
AUTHOR 2 J.JONES,J.W.LORD,W.P.LU,D.MILLER,W.C.PATT,B.D.SMITH,P.A.PETILLO,
AUTHOR 3 T.J.RUTKOSKI,H.TELIKEPALLI,L.VOGETI,T.YAO,L.CHUN,R.CLARK,
AUTHOR 4 P.EVANGELISTA,L.C.GAVRILESCU,K.LAZARIDES,V.M.ZALESKAS,L.J.STEWART,
AUTHOR 5 R.A.VAN ETTEN,D.L.FLYNN
REVDAT 3 03-APR-24 3QRJ 1 REMARK
REVDAT 2 21-FEB-24 3QRJ 1 REMARK SEQADV
REVDAT 1 01-JUN-11 3QRJ 0
JRNL AUTH W.W.CHAN,S.C.WISE,M.D.KAUFMAN,Y.M.AHN,C.L.ENSINGER,T.HAACK,
JRNL AUTH 2 M.M.HOOD,J.JONES,J.W.LORD,W.P.LU,D.MILLER,W.C.PATT,
JRNL AUTH 3 B.D.SMITH,P.A.PETILLO,T.J.RUTKOSKI,H.TELIKEPALLI,L.VOGETI,
JRNL AUTH 4 T.YAO,L.CHUN,R.CLARK,P.EVANGELISTA,L.C.GAVRILESCU,
JRNL AUTH 5 K.LAZARIDES,V.M.ZALESKAS,L.J.STEWART,R.A.VAN ETTEN,D.L.FLYNN
JRNL TITL CONFORMATIONAL CONTROL INHIBITION OF THE BCR-ABL1 TYROSINE
JRNL TITL 2 KINASE, INCLUDING THE GATEKEEPER T315I MUTANT, BY THE
JRNL TITL 3 SWITCH-CONTROL INHIBITOR DCC-2036.
JRNL REF CANCER CELL V. 19 556 2011
JRNL REFN ISSN 1535-6108
JRNL PMID 21481795
JRNL DOI 10.1016/J.CCR.2011.03.003
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 40360
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2035
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2268
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.447
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4373 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2898 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5955 ; 1.724 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7045 ; 0.978 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 534 ; 7.022 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;39.157 ;23.641
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 712 ;15.626 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.169 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 635 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4867 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 940 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2628 ; 0.864 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1060 ; 0.233 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4212 ; 1.463 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1745 ; 2.248 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1737 ; 3.351 ; 4.500
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
REMARK 4
REMARK 4 3QRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000064012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41838
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: ABL KINASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% PEG 3350, 100MM BISTRIS PH 7.1,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K, PH 7.10
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 29.71750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -59.43500
REMARK 350 BIOMT3 2 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 THR A 223
REMARK 465 SER A 224
REMARK 465 MET A 225
REMARK 465 ASP A 226
REMARK 465 PRO A 227
REMARK 465 SER 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 233
REMARK 465 LYS A 274
REMARK 465 GLU A 275
REMARK 465 ASP A 276
REMARK 465 THR A 277
REMARK 465 MET A 278
REMARK 465 PHE A 497
REMARK 465 GLN A 498
REMARK 465 GLU A 499
REMARK 465 THR B 223
REMARK 465 SER B 224
REMARK 465 MET B 225
REMARK 465 ASP B 226
REMARK 465 PRO B 227
REMARK 465 SER B 228
REMARK 465 SER B 229
REMARK 465 PRO B 230
REMARK 465 ASN B 231
REMARK 465 TYR B 232
REMARK 465 GLN B 498
REMARK 465 GLU B 499
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 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 GLU A 292 CG CD OE1 OE2
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 LYS A 415 CG CD CE NZ
REMARK 470 ILE A 418 CG1 CG2 CD1
REMARK 470 GLN A 447 CG CD OE1 NE2
REMARK 470 GLU A 450 CG CD OE1 OE2
REMARK 470 GLU A 459 CG CD OE1 OE2
REMARK 470 GLU A 462 CG CD OE1 OE2
REMARK 470 GLU A 494 CG CD OE1 OE2
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 LYS B 245 CG CD CE NZ
REMARK 470 HIS B 246 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 258 CG CD OE1 OE2
REMARK 470 LYS B 262 CG CD CE NZ
REMARK 470 LYS B 263 CG CD CE NZ
REMARK 470 GLU B 275 CG CD OE1 OE2
REMARK 470 ASP B 276 CG OD1 OD2
REMARK 470 MET B 278 CG SD CE
REMARK 470 GLU B 279 CG CD OE1 OE2
REMARK 470 GLU B 281 CG CD OE1 OE2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 ARG B 307 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 415 CG CD CE NZ
REMARK 470 ILE B 418 CG1 CG2 CD1
REMARK 470 ASP B 444 CG OD1 OD2
REMARK 470 GLN B 447 CG CD OE1 NE2
REMARK 470 GLU B 450 CG CD OE1 OE2
REMARK 470 LYS B 467 CG CD CE NZ
REMARK 470 PHE B 497 CG CD1 CD2 CE1 CE2 CZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET B 437 CA CB CG SD CE
REMARK 480 GLU B 453 CA CB CG CD OE1 OE2
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 O PHE A 486 O HOH A 186 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 457 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
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 LYS A 245 -122.23 -131.48
REMARK 500 ARG A 307 43.75 -2.29
REMARK 500 ARG A 362 -14.09 80.26
REMARK 500 ASP A 363 43.72 -143.58
REMARK 500 ALA A 365 158.37 176.65
REMARK 500 LYS B 245 -148.34 -115.36
REMARK 500 SER B 265 39.81 31.05
REMARK 500 LYS B 274 -48.79 68.08
REMARK 500 ASP B 276 53.60 -99.29
REMARK 500 ARG B 362 -6.52 82.44
REMARK 500 ARG B 362 -12.55 86.92
REMARK 500 ASP B 363 44.85 -150.92
REMARK 500 THR B 389 75.81 -102.44
REMARK 500 SER B 446 -31.21 -39.15
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 919 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 919 B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QRI RELATED DB: PDB
REMARK 900 HUMAN ABL KINASE DOMAIN IN COMPLEX WITH DCC-2036
REMARK 900 RELATED ID: 3QRK RELATED DB: PDB
REMARK 900 HUMAN ABL2 KINASE DOMAIN IN COMPLEX WITH DP-987
DBREF 3QRJ A 229 499 UNP P00519 ABL1_HUMAN 229 499
DBREF 3QRJ B 229 499 UNP P00519 ABL1_HUMAN 229 499
SEQADV 3QRJ THR A 223 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ SER A 224 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ MET A 225 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ ASP A 226 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ PRO A 227 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ SER A 228 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ ILE A 315 UNP P00519 THR 315 ENGINEERED MUTATION
SEQADV 3QRJ THR B 223 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ SER B 224 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ MET B 225 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ ASP B 226 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ PRO B 227 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ SER B 228 UNP P00519 EXPRESSION TAG
SEQADV 3QRJ ILE B 315 UNP P00519 THR 315 ENGINEERED MUTATION
SEQRES 1 A 277 THR SER MET ASP PRO SER SER PRO ASN TYR ASP LYS TRP
SEQRES 2 A 277 GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS LEU
SEQRES 3 A 277 GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP
SEQRES 4 A 277 LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU LYS
SEQRES 5 A 277 GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU ALA
SEQRES 6 A 277 ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN
SEQRES 7 A 277 LEU LEU GLY VAL CYS THR ARG GLU PRO PRO PHE TYR ILE
SEQRES 8 A 277 ILE ILE GLU PHE MET THR TYR GLY ASN LEU LEU ASP TYR
SEQRES 9 A 277 LEU ARG GLU CYS ASN ARG GLN GLU VAL ASN ALA VAL VAL
SEQRES 10 A 277 LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET GLU
SEQRES 11 A 277 TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA
SEQRES 12 A 277 ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS
SEQRES 13 A 277 VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY ASP
SEQRES 14 A 277 THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE LYS
SEQRES 15 A 277 TRP THR ALA PRO GLU SER LEU ALA TYR ASN LYS PHE SER
SEQRES 16 A 277 ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP
SEQRES 17 A 277 GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY ILE
SEQRES 18 A 277 ASP LEU SER GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR
SEQRES 19 A 277 ARG MET GLU ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR
SEQRES 20 A 277 GLU LEU MET ARG ALA CYS TRP GLN TRP ASN PRO SER ASP
SEQRES 21 A 277 ARG PRO SER PHE ALA GLU ILE HIS GLN ALA PHE GLU THR
SEQRES 22 A 277 MET PHE GLN GLU
SEQRES 1 B 277 THR SER MET ASP PRO SER SER PRO ASN TYR ASP LYS TRP
SEQRES 2 B 277 GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS LEU
SEQRES 3 B 277 GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP
SEQRES 4 B 277 LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU LYS
SEQRES 5 B 277 GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU ALA
SEQRES 6 B 277 ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN
SEQRES 7 B 277 LEU LEU GLY VAL CYS THR ARG GLU PRO PRO PHE TYR ILE
SEQRES 8 B 277 ILE ILE GLU PHE MET THR TYR GLY ASN LEU LEU ASP TYR
SEQRES 9 B 277 LEU ARG GLU CYS ASN ARG GLN GLU VAL ASN ALA VAL VAL
SEQRES 10 B 277 LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET GLU
SEQRES 11 B 277 TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA
SEQRES 12 B 277 ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS
SEQRES 13 B 277 VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY ASP
SEQRES 14 B 277 THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE LYS
SEQRES 15 B 277 TRP THR ALA PRO GLU SER LEU ALA TYR ASN LYS PHE SER
SEQRES 16 B 277 ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP
SEQRES 17 B 277 GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY ILE
SEQRES 18 B 277 ASP LEU SER GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR
SEQRES 19 B 277 ARG MET GLU ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR
SEQRES 20 B 277 GLU LEU MET ARG ALA CYS TRP GLN TRP ASN PRO SER ASP
SEQRES 21 B 277 ARG PRO SER PHE ALA GLU ILE HIS GLN ALA PHE GLU THR
SEQRES 22 B 277 MET PHE GLN GLU
HET 919 A 2 41
HET 919 B 1 41
HETNAM 919 4-[4-({[3-TERT-BUTYL-1-(QUINOLIN-6-YL)-1H-PYRAZOL-5-
HETNAM 2 919 YL]CARBAMOYL}AMINO)-3-FLUOROPHENOXY]-N-METHYLPYRIDINE-
HETNAM 3 919 2-CARBOXAMIDE
HETSYN 919 DCC-2036
FORMUL 3 919 2(C30 H28 F N7 O3)
FORMUL 5 HOH *243(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 GLU A 279 GLU A 292 1 14
HELIX 4 4 LEU A 323 CYS A 330 1 8
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 GLU A 373 HIS A 375 5 3
HELIX 8 8 GLY A 383 LEU A 387 5 5
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 THR A 495 1 11
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 ILE B 293 1 15
HELIX 21 21 ASN B 322 CYS B 330 1 9
HELIX 22 22 ASN 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 O GLU A 258 N 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 3 GLY A 321 ASN A 322 0
SHEET 2 B 3 CYS A 369 VAL A 371 -1 O VAL A 371 N GLY A 321
SHEET 3 B 3 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 PHE A 401 N THR A 394
SHEET 1 D 5 ILE B 242 LYS B 247 0
SHEET 2 D 5 VAL B 256 TRP B 261 -1 O GLU B 258 N LYS B 245
SHEET 3 D 5 LEU B 266 THR B 272 -1 O VAL B 268 N GLY B 259
SHEET 4 D 5 TYR B 312 GLU B 316 -1 O ILE B 315 N ALA B 269
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 -19.26
CISPEP 2 PRO B 309 PRO B 310 0 -12.80
SITE 1 AC1 17 HOH A 99 LEU A 248 VAL A 256 ALA A 269
SITE 2 AC1 17 LYS A 271 GLU A 282 GLU A 286 MET A 290
SITE 3 AC1 17 VAL A 299 ILE A 315 GLU A 316 PHE A 317
SITE 4 AC1 17 MET A 318 LEU A 370 ALA A 380 ASP A 381
SITE 5 AC1 17 PHE A 382
SITE 1 AC2 17 HOH B 153 LEU B 248 VAL B 256 ALA B 269
SITE 2 AC2 17 LYS B 271 GLU B 282 GLU B 286 MET B 290
SITE 3 AC2 17 VAL B 299 ILE B 315 GLU B 316 PHE B 317
SITE 4 AC2 17 MET B 318 LEU B 370 ALA B 380 ASP B 381
SITE 5 AC2 17 PHE B 382
CRYST1 55.261 59.435 76.285 90.00 109.55 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018096 0.000000 0.006424 0.00000
SCALE2 0.000000 0.016825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
