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Database: PDB
Entry: 3HMI
LinkDB: 3HMI
Original site: 3HMI 
HEADER    TRANSFERASE                             29-MAY-09   3HMI              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN ABL2 IN COMPLEX WITH 5-AMINO-3-{[4-    
TITLE    2 (AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-        
TITLE    3 TRIAZOLE-1-CARBOTHIOAMIDE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ABL2;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEIN KINASE;                                            
COMPND   5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 2, ABELSON-  
COMPND   6 RELATED GENE PROTEIN, TYROSINE KINASE ARG;                           
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ABL2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH 5 INSECT CELLS;                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE                               
KEYWDS    TYROSINE KINASE, ABL, ABL2, ABELSON MURINE LEUKEMIA VIRAL ONCOGENE,   
KEYWDS   2 ATP-BINDING, CELL ADHESION, CYTOSKELETON, KINASE, LIPOPROTEIN,       
KEYWDS   3 MAGNESIUM, MANGANESE, METAL-BINDING, MYRISTATE, NUCLEOTIDE-BINDING,  
KEYWDS   4 PHOSPHOPROTEIN, SH2 DOMAIN, SH3 DOMAIN, TRANSFERASE, TYROSINE-       
KEYWDS   5 PROTEIN KINASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, 
KEYWDS   6 SGC                                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,E.SALAH,A.BARR,P.MAHAJAN,B.SHRESTHA,P.SAVITSKY,           
AUTHOR   2 A.CHAIKUAD,C.ALLERSTON,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,         
AUTHOR   3 J.WEIGELT,A.EDWARDS,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)     
REVDAT   3   01-NOV-17 3HMI    1       REMARK                                   
REVDAT   2   13-JUL-11 3HMI    1       VERSN                                    
REVDAT   1   07-JUL-09 3HMI    0                                                
JRNL        AUTH   E.UGOCHUKWU,E.SALAH,A.BARR,P.MAHAJAN,B.SHRESTHA,P.SAVITSKY,  
JRNL        AUTH 2 A.CHAIKUAD,C.ALLERSTON,F.VON DELFT,S.KNAPP                   
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN ABL2 IN COMPLEX WITH          
JRNL        TITL 2 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,             
JRNL        TITL 3 6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 27347                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1462                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2216                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 111                          
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2126                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 235                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.95                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28000                                             
REMARK   3    B22 (A**2) : 1.62000                                              
REMARK   3    B33 (A**2) : -1.27000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.40000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.091         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.828         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2260 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1495 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3089 ; 1.465 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3648 ; 0.889 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   282 ; 6.222 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    96 ;37.560 ;24.063       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   374 ;12.655 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;17.297 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   336 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2514 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   461 ; 0.001 ; 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):  1361 ; 0.810 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   546 ; 0.237 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2202 ; 1.353 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   899 ; 1.877 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   879 ; 2.852 ; 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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   279        A   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.2659   6.8628  -3.7654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1134 T22:   0.1806                                     
REMARK   3      T33:   0.1409 T12:  -0.0223                                     
REMARK   3      T13:   0.0101 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4018 L22:   1.9523                                     
REMARK   3      L33:   3.2343 L12:  -0.2087                                     
REMARK   3      L13:  -0.8860 L23:   0.3092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0703 S12:   0.0183 S13:  -0.1289                       
REMARK   3      S21:   0.0704 S22:  -0.0720 S23:   0.1349                       
REMARK   3      S31:   0.2139 S32:  -0.5782 S33:   0.1423                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   295        A   319                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.1567   5.9182  -9.6184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0786 T22:   0.0393                                     
REMARK   3      T33:   0.0720 T12:  -0.0423                                     
REMARK   3      T13:   0.0043 T23:  -0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5322 L22:   4.1056                                     
REMARK   3      L33:   3.8801 L12:  -1.3105                                     
REMARK   3      L13:  -1.4442 L23:   0.9616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0689 S12:   0.1917 S13:  -0.2812                       
REMARK   3      S21:   0.1112 S22:  -0.2136 S23:   0.1282                       
REMARK   3      S31:   0.1782 S32:  -0.2485 S33:   0.2825                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   326        A   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3099  14.2316 -10.0469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0651 T22:   0.0498                                     
REMARK   3      T33:   0.0574 T12:  -0.0140                                     
REMARK   3      T13:  -0.0189 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3338 L22:   0.5448                                     
REMARK   3      L33:   2.5086 L12:   0.2853                                     
REMARK   3      L13:  -0.8883 L23:  -0.0266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0017 S12:  -0.0039 S13:   0.0009                       
REMARK   3      S21:  -0.0277 S22:   0.0034 S23:   0.0281                       
REMARK   3      S31:  -0.1326 S32:   0.1225 S33:  -0.0017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   433        A   490                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2902   8.3094 -13.8369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0399 T22:   0.2169                                     
REMARK   3      T33:   0.0664 T12:  -0.0296                                     
REMARK   3      T13:   0.0096 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6207 L22:   2.0046                                     
REMARK   3      L33:   3.4381 L12:  -0.5744                                     
REMARK   3      L13:   0.0354 L23:   0.6998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0202 S12:  -0.2045 S13:  -0.1346                       
REMARK   3      S21:   0.0623 S22:   0.0389 S23:  -0.0517                       
REMARK   3      S31:   0.2484 S32:   0.3457 S33:  -0.0186                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   491        A   517                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4878  11.2027 -19.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0288 T22:   0.3698                                     
REMARK   3      T33:   0.0392 T12:  -0.0612                                     
REMARK   3      T13:   0.0076 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5303 L22:   4.9375                                     
REMARK   3      L33:   3.6524 L12:  -1.6862                                     
REMARK   3      L13:   0.4927 L23:   0.2675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0986 S12:   0.0663 S13:   0.0079                       
REMARK   3      S21:  -0.2297 S22:  -0.1197 S23:   0.1396                       
REMARK   3      S31:  -0.1452 S32:   0.4889 S33:   0.0211                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   518        A   544                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8097  21.3946 -11.6138              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0862 T22:   0.3021                                     
REMARK   3      T33:   0.0810 T12:  -0.1016                                     
REMARK   3      T13:   0.0070 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1655 L22:   3.1901                                     
REMARK   3      L33:   2.3575 L12:  -0.5369                                     
REMARK   3      L13:   0.6022 L23:  -0.2178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0674 S12:  -0.1685 S13:   0.3618                       
REMARK   3      S21:  -0.0874 S22:   0.0849 S23:  -0.1494                       
REMARK   3      S31:  -0.2771 S32:   0.3794 S33:  -0.0175                       
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 3HMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053315.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-09                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97630                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR225                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28844                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.80200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3GVU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M LITHIUM SULFATE, 0.05M DI-SODIUM    
REMARK 280  HYDROGEN PHOSPHATE, 0.05M CITRIC ACID, 19%(W/V) PEG 1000, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       82.96000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       82.96000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       19.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: PISA                                                  
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 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     MET A   255                                                      
REMARK 465     GLY A   256                                                      
REMARK 465     HIS A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     HIS A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLY A   265                                                      
REMARK 465     VAL A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     THR A   270                                                      
REMARK 465     GLU A   271                                                      
REMARK 465     ASN A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     TYR A   274                                                      
REMARK 465     PHE A   275                                                      
REMARK 465     GLN A   276                                                      
REMARK 465     SER A   277                                                      
REMARK 465     MET A   278                                                      
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     LYS A 309    CE   NZ                                             
REMARK 470     LYS A 320    CG   CD   CE   NZ                                   
REMARK 470     THR A 323    OG1  CG2                                            
REMARK 470     MET A 324    CG   SD   CE                                        
REMARK 470     GLU A 325    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 327    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 331    CE   NZ                                             
REMARK 470     LYS A 402    CE   NZ                                             
REMARK 470     ILE A 406    CD1                                                 
REMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 493    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 508    CG   CD   OE1  OE2                                  
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 291     -136.08   -112.78                                   
REMARK 500    LYS A 320     -149.82   -116.45                                   
REMARK 500    GLU A 325       66.47   -114.57                                   
REMARK 500    ARG A 408       -2.59     76.23                                   
REMARK 500    ASP A 409       51.16   -150.47                                   
REMARK 500    LEU A 433      107.54   -175.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DKI A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GVU   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN ABL2 IN COMPLEX WITH GLEEVEC          
DBREF  3HMI A  279   546  UNP    P42684   ABL2_HUMAN     279    546             
SEQADV 3HMI MET A  255  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI GLY A  256  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  257  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  258  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  259  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  260  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  261  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI HIS A  262  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI SER A  263  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI SER A  264  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI GLY A  265  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI VAL A  266  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI ASP A  267  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI LEU A  268  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI GLY A  269  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI THR A  270  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI GLU A  271  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI ASN A  272  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI LEU A  273  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI TYR A  274  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI PHE A  275  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI GLN A  276  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI SER A  277  UNP  P42684              EXPRESSION TAG                 
SEQADV 3HMI MET A  278  UNP  P42684              EXPRESSION TAG                 
SEQRES   1 A  292  MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP          
SEQRES   2 A  292  LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LYS          
SEQRES   3 A  292  TRP GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS          
SEQRES   4 A  292  LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR VAL GLY VAL          
SEQRES   5 A  292  TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU          
SEQRES   6 A  292  LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU          
SEQRES   7 A  292  ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL          
SEQRES   8 A  292  GLN LEU LEU GLY VAL CYS THR LEU GLU PRO PRO PHE TYR          
SEQRES   9 A  292  ILE VAL THR GLU TYR MET PRO TYR GLY ASN LEU LEU ASP          
SEQRES  10 A  292  TYR LEU ARG GLU CYS ASN ARG GLU GLU VAL THR ALA VAL          
SEQRES  11 A  292  VAL LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET          
SEQRES  12 A  292  GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU          
SEQRES  13 A  292  ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS VAL VAL          
SEQRES  14 A  292  LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY          
SEQRES  15 A  292  ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE          
SEQRES  16 A  292  LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN THR PHE          
SEQRES  17 A  292  SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU          
SEQRES  18 A  292  TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY          
SEQRES  19 A  292  ILE ASP LEU SER GLN VAL TYR ASP LEU LEU GLU LYS GLY          
SEQRES  20 A  292  TYR ARG MET GLU GLN PRO GLU GLY CYS PRO PRO LYS VAL          
SEQRES  21 A  292  TYR GLU LEU MET ARG ALA CYS TRP LYS TRP SER PRO ALA          
SEQRES  22 A  292  ASP ARG PRO SER PHE ALA GLU THR HIS GLN ALA PHE GLU          
SEQRES  23 A  292  THR MET PHE HIS ASP SER                                      
HET    DKI  A   1      28                                                       
HETNAM     DKI 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-               
HETNAM   2 DKI  DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE              
HETSYN     DKI CDK 1/2 INHIBITOR                                                
FORMUL   2  DKI    C15 H13 F2 N7 O2 S2                                          
FORMUL   3  HOH   *235(H2 O)                                                    
HELIX    1   1 GLU A  284  THR A  286  5                                   3    
HELIX    2   2 GLY A  295  GLN A  298  5                                   4    
HELIX    3   3 LYS A  309  SER A  311  5                                   3    
HELIX    4   4 GLU A  325  GLU A  338  1                                  14    
HELIX    5   5 ASN A  368  CYS A  376  1                                   9    
HELIX    6   6 THR A  382  LYS A  403  1                                  22    
HELIX    7   7 ALA A  411  ARG A  413  5                                   3    
HELIX    8   8 GLU A  419  HIS A  421  5                                   3    
HELIX    9   9 PRO A  448  THR A  452  5                                   5    
HELIX   10  10 ALA A  453  ASN A  460  1                                   8    
HELIX   11  11 SER A  463  THR A  480  1                                  18    
HELIX   12  12 ASP A  490  SER A  492  5                                   3    
HELIX   13  13 GLN A  493  LYS A  500  1                                   8    
HELIX   14  14 PRO A  511  TRP A  522  1                                  12    
HELIX   15  15 SER A  525  ARG A  529  5                                   5    
HELIX   16  16 SER A  531  SER A  546  1                                  16    
SHEET    1   A 5 ILE A 288  LYS A 293  0                                        
SHEET    2   A 5 VAL A 302  TRP A 307 -1  O  VAL A 304   N  HIS A 292           
SHEET    3   A 5 LEU A 312  THR A 318 -1  O  LEU A 312   N  TRP A 307           
SHEET    4   A 5 TYR A 358  GLU A 362 -1  O  ILE A 359   N  LYS A 317           
SHEET    5   A 5 LEU A 347  CYS A 351 -1  N  GLY A 349   O  VAL A 360           
SHEET    1   B 2 PHE A 405  ILE A 406  0                                        
SHEET    2   B 2 SER A 431  ARG A 432 -1  O  SER A 431   N  ILE A 406           
SHEET    1   C 2 CYS A 415  VAL A 417  0                                        
SHEET    2   C 2 VAL A 423  VAL A 425 -1  O  LYS A 424   N  LEU A 416           
SHEET    1   D 2 TYR A 439  THR A 440  0                                        
SHEET    2   D 2 THR A 461  PHE A 462 -1  O  PHE A 462   N  TYR A 439           
CISPEP   1 PRO A  355    PRO A  356          0       -12.44                     
SITE     1 AC1 16 HOH A  54  HOH A 207  LEU A 294  GLY A 295                    
SITE     2 AC1 16 GLN A 298  TYR A 299  VAL A 302  GLU A 362                    
SITE     3 AC1 16 TYR A 363  MET A 364  GLY A 367  ARG A 413                    
SITE     4 AC1 16 ASN A 414  LEU A 416  ALA A 426  PHE A 428                    
CRYST1  165.920   39.800   43.130  90.00  95.69  90.00 C 1 2 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      0.006027  0.000000  0.000601        0.00000                         
SCALE2      0.000000  0.025126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023301        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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