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Database: PDB
Entry: 3QRJ
LinkDB: 3QRJ
Original site: 3QRJ 
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   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,VAGIN,DODSON                               
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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1745 ; 2.248 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1737 ; 3.351 ; 4.500       
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. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064012.                                      
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                     
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    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                                                                             
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