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Database: PDB
Entry: 2G2F
LinkDB: 2G2F
Original site: 2G2F 
HEADER    TRANSFERASE                             15-FEB-06   2G2F              
TITLE     A SRC-LIKE INACTIVE CONFORMATION IN THE ABL TYROSINE KINASE DOMAIN    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ABL KINASE;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ABL KINASE DOMAIN;                                         
COMPND   5 SYNONYM: P150, C- ABL, ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG
COMPND   6 1;                                                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ATP-PEPTIDE CONJUGATE;                                     
COMPND  11 CHAIN: C;                                                            
COMPND  12 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: ABL1, ABL, JTK7;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS                         
KEYWDS    PROTEIN KINASE, TRANSFERASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.LEVINSON,O.KUCHMENT                                               
REVDAT   3   07-MAR-12 2G2F    1       HET    HETATM HETNAM VERSN               
REVDAT   2   24-FEB-09 2G2F    1       VERSN                                    
REVDAT   1   23-MAY-06 2G2F    0                                                
JRNL        AUTH   N.M.LEVINSON,O.KUCHMENT,K.SHEN,M.A.YOUNG,M.KOLDOBSKIY,       
JRNL        AUTH 2 M.KARPLUS,P.A.COLE,J.KURIYAN                                 
JRNL        TITL   A SRC-LIKE INACTIVE CONFORMATION IN THE ABL TYROSINE KINASE  
JRNL        TITL 2 DOMAIN.                                                      
JRNL        REF    PLOS BIOL.                    V.   4   753 2006              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   16640460                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.0040144                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 22582                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1115                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4435                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 85                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.37                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2G2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036603.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.115879                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22582                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.050                              
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: PDB ENTRY 1M52                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 5.5, 25% PEG 3350,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       52.83450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.83450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.66100            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     MET A   228                                                      
REMARK 465     SER A   229                                                      
REMARK 465     PRO A   230                                                      
REMARK 465     ASN A   231                                                      
REMARK 465     GLU A   507                                                      
REMARK 465     LYS A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     LEU A   510                                                      
REMARK 465     GLY A   511                                                      
REMARK 465     LYS A   512                                                      
REMARK 465     GLY B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     MET B   228                                                      
REMARK 465     SER B   229                                                      
REMARK 465     PRO B   230                                                      
REMARK 465     ASN B   231                                                      
REMARK 465     TYR B   232                                                      
REMARK 465     ASP B   233                                                      
REMARK 465     GLY B   249                                                      
REMARK 465     GLY B   250                                                      
REMARK 465     GLY B   251                                                      
REMARK 465     GLN B   252                                                      
REMARK 465     TYR B   253                                                      
REMARK 465     SER B   503                                                      
REMARK 465     ASP B   504                                                      
REMARK 465     GLU B   505                                                      
REMARK 465     VAL B   506                                                      
REMARK 465     GLU B   507                                                      
REMARK 465     LYS B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     LEU B   510                                                      
REMARK 465     GLY B   511                                                      
REMARK 465     LYS B   512                                                      
REMARK 465     ALA C   112                                                      
REMARK 465     LYS C   113                                                      
REMARK 465     LYS C   114                                                      
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     ASP A 504    CG   OD1  OD2                                       
REMARK 470     GLU A 505    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 506    CG1  CG2                                            
REMARK 470     GLU B 255    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 104    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    ASP A 233      131.60   -172.75                                   
REMARK 500    LYS A 245      -67.95   -100.56                                   
REMARK 500    GLN A 252       19.07    -65.61                                   
REMARK 500    TYR A 253        9.49   -151.64                                   
REMARK 500    LYS A 262      -63.48    -29.42                                   
REMARK 500    LEU A 273      117.59   -164.18                                   
REMARK 500    LYS A 274     -148.53    -97.26                                   
REMARK 500    GLU A 275       34.25    -78.94                                   
REMARK 500    ASP A 276     -132.02    -57.71                                   
REMARK 500    VAL A 280      -61.84    -26.86                                   
REMARK 500    LYS A 357       16.91    -64.82                                   
REMARK 500    LEU A 387      113.11   -170.82                                   
REMARK 500    TYR A 440       61.43     35.31                                   
REMARK 500    SER A 481        2.62    -67.40                                   
REMARK 500    ASP A 504      -74.91    -70.42                                   
REMARK 500    GLU A 505       -8.53    -53.36                                   
REMARK 500    GLU B 236      135.00    -35.85                                   
REMARK 500    MET B 237     -155.46   -130.00                                   
REMARK 500    ARG B 239       22.07    -77.15                                   
REMARK 500    LYS B 245      -33.63   -144.05                                   
REMARK 500    TYR B 264       -9.98     70.38                                   
REMARK 500    SER B 265       66.83     36.88                                   
REMARK 500    GLU B 316      157.45    -46.12                                   
REMARK 500    ASP B 363       64.12   -156.40                                   
REMARK 500    PHE B 382      -74.15     -2.81                                   
REMARK 500    THR B 389      -53.85   -131.33                                   
REMARK 500    PRO B 396      151.15    -47.47                                   
REMARK 500    ALA B 397      -95.69      3.62                                   
REMARK 500    ALA B 399      119.30    -27.19                                   
REMARK 500    PRO B 402      104.92    -59.22                                   
REMARK 500    ASP B 455       28.70     80.95                                   
REMARK 500    SER B 501     -137.10    -93.33                                   
REMARK 500    ALA C 105      100.69    113.37                                   
REMARK 500    PRO C 110      155.58    -41.19                                   
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 AGS B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 112 C 201                 
DBREF  2G2F A  229   512  UNP    P00519   ABL1_HUMAN     229    512             
DBREF  2G2F B  229   512  UNP    P00519   ABL1_HUMAN     229    512             
DBREF  2G2F C  104   114  PDB    2G2F     2G2F           104    114             
SEQADV 2G2F GLY A  226  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F HIS A  227  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F MET A  228  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F PRO A  396  UNP  P00519    HIS   396 ENGINEERED                     
SEQADV 2G2F GLY B  226  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F HIS B  227  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F MET B  228  UNP  P00519              CLONING ARTIFACT               
SEQADV 2G2F PRO B  396  UNP  P00519    HIS   396 ENGINEERED                     
SEQRES   1 A  287  GLY HIS MET SER PRO ASN TYR ASP LYS TRP GLU MET GLU          
SEQRES   2 A  287  ARG THR ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY          
SEQRES   3 A  287  GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR          
SEQRES   4 A  287  SER LEU THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR          
SEQRES   5 A  287  MET GLU VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET          
SEQRES   6 A  287  LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY          
SEQRES   7 A  287  VAL CYS THR ARG GLU PRO PRO PHE TYR ILE ILE THR GLU          
SEQRES   8 A  287  PHE MET THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU          
SEQRES   9 A  287  CYS ASN ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR          
SEQRES  10 A  287  MET ALA THR GLN ILE SER SER ALA MET GLU TYR LEU GLU          
SEQRES  11 A  287  LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  12 A  287  CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP          
SEQRES  13 A  287  PHE GLY LEU SER ARG LEU MET THR GLY ASP THR TYR THR          
SEQRES  14 A  287  ALA PRO ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA          
SEQRES  15 A  287  PRO GLU SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER          
SEQRES  16 A  287  ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA          
SEQRES  17 A  287  THR TYR GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER          
SEQRES  18 A  287  GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU          
SEQRES  19 A  287  ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET          
SEQRES  20 A  287  ARG ALA CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER          
SEQRES  21 A  287  PHE ALA GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN          
SEQRES  22 A  287  GLU SER SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY          
SEQRES  23 A  287  LYS                                                          
SEQRES   1 B  287  GLY HIS MET SER PRO ASN TYR ASP LYS TRP GLU MET GLU          
SEQRES   2 B  287  ARG THR ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY          
SEQRES   3 B  287  GLN TYR GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR          
SEQRES   4 B  287  SER LEU THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR          
SEQRES   5 B  287  MET GLU VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET          
SEQRES   6 B  287  LYS GLU ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY          
SEQRES   7 B  287  VAL CYS THR ARG GLU PRO PRO PHE TYR ILE ILE THR GLU          
SEQRES   8 B  287  PHE MET THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU          
SEQRES   9 B  287  CYS ASN ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR          
SEQRES  10 B  287  MET ALA THR GLN ILE SER SER ALA MET GLU TYR LEU GLU          
SEQRES  11 B  287  LYS LYS ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  12 B  287  CYS LEU VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP          
SEQRES  13 B  287  PHE GLY LEU SER ARG LEU MET THR GLY ASP THR TYR THR          
SEQRES  14 B  287  ALA PRO ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA          
SEQRES  15 B  287  PRO GLU SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER          
SEQRES  16 B  287  ASP VAL TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA          
SEQRES  17 B  287  THR TYR GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER          
SEQRES  18 B  287  GLN VAL TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU          
SEQRES  19 B  287  ARG PRO GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET          
SEQRES  20 B  287  ARG ALA CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER          
SEQRES  21 B  287  PHE ALA GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN          
SEQRES  22 B  287  GLU SER SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY          
SEQRES  23 B  287  LYS                                                          
SEQRES   1 C   11  GLU ALA ILE PHE ALA ALA PRO PHE ALA LYS LYS                  
HET    AGS  B 601      31                                                       
HET    112  C 201      35                                                       
HETNAM     AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER                       
HETNAM     112 THIOPHOSPHORIC ACID O-((ADENOSYL-PHOSPHO)PHOSPHO)-S-             
HETNAM   2 112  ACETAMIDYL-DIESTER                                              
HETSYN     AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);                  
HETSYN   2 AGS  ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-            
HETSYN   3 AGS  DIPHOSPHATE MONOTHIOPHOSPHATE                                   
FORMUL   4  AGS    C10 H16 N5 O12 P3 S                                          
FORMUL   5  112    C12 H19 N6 O13 P3 S                                          
FORMUL   6  HOH   *85(H2 O)                                                     
HELIX    1   1 GLU A  238  THR A  240  5                                   3    
HELIX    2   2 LYS A  263  SER A  265  5                                   3    
HELIX    3   3 GLU A  279  LYS A  291  1                                  13    
HELIX    4   4 ASN A  322  CYS A  330  1                                   9    
HELIX    5   5 ASN A  336  LYS A  357  1                                  22    
HELIX    6   6 ALA A  365  ARG A  367  5                                   3    
HELIX    7   7 GLU A  373  HIS A  375  5                                   3    
HELIX    8   8 LYS A  404  THR A  406  5                                   3    
HELIX    9   9 ALA A  407  ASN A  414  1                                   8    
HELIX   10  10 SER A  417  THR A  434  1                                  18    
HELIX   11  11 ASP A  444  SER A  446  5                                   3    
HELIX   12  12 GLN A  447  LYS A  454  1                                   8    
HELIX   13  13 PRO A  465  TRP A  476  1                                  12    
HELIX   14  14 ASN A  479  ARG A  483  5                                   5    
HELIX   15  15 SER A  485  VAL A  506  1                                  22    
HELIX   16  16 LYS B  263  SER B  265  5                                   3    
HELIX   17  17 GLU B  279  LYS B  291  1                                  13    
HELIX   18  18 ASN B  322  CYS B  330  1                                   9    
HELIX   19  19 ASN B  336  ASN B  358  1                                  23    
HELIX   20  20 ALA B  365  ARG B  367  5                                   3    
HELIX   21  21 PRO B  402  THR B  406  5                                   5    
HELIX   22  22 ALA B  407  ASN B  414  1                                   8    
HELIX   23  23 ILE B  418  ALA B  433  1                                  16    
HELIX   24  24 ASP B  444  SER B  446  5                                   3    
HELIX   25  25 GLN B  447  LYS B  454  1                                   8    
HELIX   26  26 PRO B  465  TRP B  476  1                                  12    
HELIX   27  27 ASN B  479  ARG B  483  5                                   5    
HELIX   28  28 SER B  485  GLU B  499  1                                  15    
SHEET    1   A 5 ILE A 242  GLY A 249  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  LEU A 273 -1  O  VAL A 270   N  TYR A 257           
SHEET    4   A 5 PHE A 311  GLU A 316 -1  O  THR A 315   N  ALA A 269           
SHEET    5   A 5 LEU A 301  CYS A 305 -1  N  LEU A 302   O  ILE A 314           
SHEET    1   B 2 PHE A 359  HIS A 361  0                                        
SHEET    2   B 2 LEU A 384  ARG A 386 -1  O  SER A 385   N  ILE A 360           
SHEET    1   C 2 CYS A 369  GLY A 372  0                                        
SHEET    2   C 2 LEU A 376  VAL A 379 -1  O  LEU A 376   N  GLY A 372           
SHEET    1   D 2 TYR A 393  THR A 394  0                                        
SHEET    2   D 2 LYS A 415  PHE A 416 -1  O  PHE A 416   N  TYR A 393           
SHEET    1   E 2 PHE A 401  PRO A 402  0                                        
SHEET    2   E 2 PHE C 107  ALA C 108 -1  O  ALA C 108   N  PHE A 401           
SHEET    1   F 5 ILE B 242  LYS B 247  0                                        
SHEET    2   F 5 GLU B 255  TRP B 261 -1  O  GLU B 258   N  HIS B 246           
SHEET    3   F 5 LEU B 266  LEU B 273 -1  O  VAL B 270   N  TYR B 257           
SHEET    4   F 5 PHE B 311  GLU B 316 -1  O  THR B 315   N  ALA B 269           
SHEET    5   F 5 LEU B 301  CYS B 305 -1  N  GLY B 303   O  ILE B 314           
SHEET    1   G 2 PHE B 359  HIS B 361  0                                        
SHEET    2   G 2 LEU B 384  ARG B 386 -1  O  SER B 385   N  ILE B 360           
SHEET    1   H 2 CYS B 369  VAL B 371  0                                        
SHEET    2   H 2 VAL B 377  VAL B 379 -1  O  LYS B 378   N  LEU B 370           
SHEET    1   I 2 THR B 392  THR B 394  0                                        
SHEET    2   I 2 LYS B 415  SER B 417 -1  O  PHE B 416   N  TYR B 393           
LINK         CZ  PHE C 107                 NS  112 C 201     1555   1555  1.47  
CISPEP   1 PRO A  309    PRO A  310          0        -0.09                     
CISPEP   2 PRO B  309    PRO B  310          0        -0.17                     
SITE     1 AC1 10 LEU B 248  VAL B 256  ALA B 269  THR B 315                    
SITE     2 AC1 10 GLU B 316  PHE B 317  MET B 318  GLY B 321                    
SITE     3 AC1 10 ASN B 322  ARG B 367                                          
SITE     1 AC2 15 LEU A 248  GLY A 250  GLY A 251  GLN A 252                    
SITE     2 AC2 15 VAL A 256  ALA A 269  LYS A 271  THR A 315                    
SITE     3 AC2 15 GLU A 316  PHE A 317  MET A 318  ASN A 322                    
SITE     4 AC2 15 ASP A 363  HOH A 635  PHE C 107                               
CRYST1  105.669  133.322   56.576  90.00  90.00  90.00 P 21 21 2     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      0.009464  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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