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Database: PDB
Entry: 3GVU
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Original site: 3GVU 
HEADER    TRANSFERASE                             31-MAR-09   3GVU              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN ABL2 IN COMPLEX WITH GLEEVEC           
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: HIGH5 INSECT CELL;                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE                               
KEYWDS    TYROSINE KINASE, ABL, ABELSON MURINE LEUKEMIA VIRAL ONCOGENE, ATP-    
KEYWDS   2 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,P.FILIPPAKOPOULOS,A.ROOS,A.C.W.PIKE,F.VON DELFT,          
AUTHOR   3 C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,S.KNAPP,STRUCTURAL      
AUTHOR   4 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   3   01-NOV-17 3GVU    1       REMARK                                   
REVDAT   2   13-JUL-11 3GVU    1       VERSN                                    
REVDAT   1   21-APR-09 3GVU    0                                                
JRNL        AUTH   E.SALAH,E.UGOCHUKWU,A.BARR,P.MAHAJAN,B.SHRESTHA,P.SAVITSKY,  
JRNL        AUTH 2 S.KNAPP                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN ABL2 IN COMPLEX WITH GLEEVEC  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23225                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1244                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1602                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2167                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 149                                     
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) : 16.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.79000                                              
REMARK   3    B22 (A**2) : -1.50000                                             
REMARK   3    B33 (A**2) : -2.29000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.168         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.080         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2355 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1571 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3205 ; 1.474 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3770 ; 1.034 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   280 ; 6.819 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;37.158 ;24.314       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   380 ;14.708 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;12.788 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   334 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2598 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   471 ; 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):  1377 ; 4.535 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   554 ; 1.836 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2220 ; 5.869 ; 7.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   978 ; 7.789 ; 9.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   981 ; 8.238 ;11.000       
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  : 2                                          
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   269        A   367                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6308   4.1759  11.5276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0100 T22:   0.0280                                     
REMARK   3      T33:   0.0338 T12:  -0.0102                                     
REMARK   3      T13:   0.0173 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9376 L22:   2.0734                                     
REMARK   3      L33:   5.3233 L12:   0.0999                                     
REMARK   3      L13:  -0.8965 L23:   1.0574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0402 S12:   0.2513 S13:  -0.0040                       
REMARK   3      S21:   0.0246 S22:   0.0136 S23:   0.0428                       
REMARK   3      S31:  -0.0063 S32:   0.0258 S33:   0.0266                       
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   368        A   546                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9764  17.5564  34.8369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0850 T22:   0.0251                                     
REMARK   3      T33:   0.0157 T12:  -0.0105                                     
REMARK   3      T13:  -0.0245 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4224 L22:   5.5806                                     
REMARK   3      L33:   4.3277 L12:   1.5066                                     
REMARK   3      L13:   0.3709 L23:   3.0241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0462 S12:  -0.0123 S13:   0.1278                       
REMARK   3      S21:   0.4846 S22:   0.0238 S23:  -0.0663                       
REMARK   3      S31:   0.2021 S32:   0.1331 S33:  -0.0700                       
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 3GVU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052370.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.88000                            
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   : 24490                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: 1FPU.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1M CITRATE, PH 5.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       43.90500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.90500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.23000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.72000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.23000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.72000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.90500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.23000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.72000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.90500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.23000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.72000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 249  LIES ON A SPECIAL POSITION.                          
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     LEU A   433                                                      
REMARK 465     MET A   434                                                      
REMARK 465     THR A   435                                                      
REMARK 465     HIS A   442                                                      
REMARK 465     ALA A   443                                                      
REMARK 465     GLY A   444                                                      
REMARK 465     ALA A   445                                                      
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     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 322    CG   OD1  OD2                                       
REMARK 470     ASN A 377    CG   OD1  ND2                                       
REMARK 470     GLU A 379    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 402    CE   NZ                                             
REMARK 470     ARG A 432    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 446    CG   CD   CE   NZ                                   
REMARK 470     ASP A 545    CG   OD1  OD2                                       
REMARK 470     SER A 546    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A    54     O    HOH A   239              2.08            
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    MET A 278   CB  -  CG  -  SD  ANGL. DEV. =  18.8 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    SER A 277     -107.25    -89.92                                   
REMARK 500    SER A 277      138.79   -174.83                                   
REMARK 500    MET A 278      -24.10   -157.48                                   
REMARK 500    MET A 278     -166.80     76.47                                   
REMARK 500    LYS A 280       33.26    -83.64                                   
REMARK 500    LYS A 291      -66.69   -109.40                                   
REMARK 500    ARG A 408       -8.66     84.44                                   
REMARK 500    ASP A 409       46.19   -152.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  276     SER A  277                 -145.70                    
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 STI A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI A 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FPU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL       
REMARK 900 MOLECULE INHIBITOR                                                   
DBREF  3GVU A  279   546  UNP    P42684   ABL2_HUMAN     279    546             
SEQADV 3GVU MET A  255  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU GLY A  256  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  257  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  258  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  259  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  260  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  261  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU HIS A  262  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU SER A  263  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU SER A  264  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU GLY A  265  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU VAL A  266  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU ASP A  267  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU LEU A  268  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU GLY A  269  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU THR A  270  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU GLU A  271  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU ASN A  272  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU LEU A  273  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU TYR A  274  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU PHE A  275  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU GLN A  276  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU SER A  277  UNP  P42684              EXPRESSION TAG                 
SEQADV 3GVU 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    STI  A1001      37                                                       
HET    STI  A1002      37                                                       
HETNAM     STI 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-              
HETNAM   2 STI  PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE             
HETSYN     STI STI-571;IMATINIB                                                 
FORMUL   2  STI    2(C29 H31 N7 O)                                              
FORMUL   4  HOH   *149(H2 O)                                                    
HELIX    1   1 GLY A  269  PHE A  275  1                                   7    
HELIX    2   2 GLU A  284  THR A  286  5                                   3    
HELIX    3   3 GLY A  295  GLN A  298  5                                   4    
HELIX    4   4 LYS A  309  SER A  311  5                                   3    
HELIX    5   5 GLU A  325  LYS A  337  1                                  13    
HELIX    6   6 ASN A  368  CYS A  376  1                                   9    
HELIX    7   7 THR A  382  LYS A  403  1                                  22    
HELIX    8   8 ALA A  411  ARG A  413  5                                   3    
HELIX    9   9 GLU A  419  HIS A  421  5                                   3    
HELIX   10  10 PRO A  448  THR A  452  5                                   5    
HELIX   11  11 ALA A  453  ASN A  460  1                                   8    
HELIX   12  12 SER A  463  THR A  480  1                                  18    
HELIX   13  13 ASP A  490  SER A  492  5                                   3    
HELIX   14  14 GLN A  493  GLY A  501  1                                   9    
HELIX   15  15 PRO A  511  TRP A  522  1                                  12    
HELIX   16  16 SER A  525  ARG A  529  5                                   5    
HELIX   17  17 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  LYS A 291           
SHEET    3   A 5 LEU A 312  LEU A 319 -1  O  LEU A 312   N  TRP A 307           
SHEET    4   A 5 PHE A 357  GLU A 362 -1  O  THR A 361   N  ALA A 315           
SHEET    5   A 5 LEU A 347  CYS A 351 -1  N  LEU A 348   O  VAL A 360           
SHEET    1   B 2 CYS A 415  VAL A 417  0                                        
SHEET    2   B 2 VAL A 423  VAL A 425 -1  O  LYS A 424   N  LEU A 416           
CISPEP   1 PRO A  355    PRO A  356          0         1.87                     
SITE     1 AC1 16 HOH A  73  VAL A 302  ALA A 315  LYS A 317                    
SITE     2 AC1 16 GLU A 332  MET A 336  VAL A 345  ILE A 359                    
SITE     3 AC1 16 THR A 361  TYR A 363  MET A 364  ILE A 406                    
SITE     4 AC1 16 HIS A 407  ALA A 426  ASP A 427  PHE A 428                    
SITE     1 AC2 11 HOH A  30  HOH A  53  ALA A 383  VAL A 384                    
SITE     2 AC2 11 LEU A 387  TYR A 388  GLU A 508  GLY A 509                    
SITE     3 AC2 11 PRO A 511  VAL A 514  HOH A 549                               
CRYST1   88.460   99.440   87.810  90.00  90.00  90.00 C 2 2 21      8          
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      0.011305  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010056  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011388        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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