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Database: PDB
Entry: 4J9G
LinkDB: 4J9G
Original site: 4J9G 
HEADER    TRANSFERASE/UNKNOWN FUNCTION            16-FEB-13   4J9G              
TITLE     CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH THE DESIGNED   
TITLE    2 HIGH-AFFINITY PEPTIDE LIGAND P7 AT PH7                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;                              
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: SH3 DOMAIN (UNP RESIDUES 60-121);                          
COMPND   5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1, ABELSON   
COMPND   6 TYROSINE-PROTEIN KINASE 1, PROTO-ONCOGENE C-ABL, P150;               
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: P7;                                                        
COMPND  11 CHAIN: B, D, F;                                                      
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 STRAIN: PBAT4;                                                       
SOURCE   6 GENE: ABL, ABL1, JTK7;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    BETA SHANDWICH, SH3 DOMAIN, KINASE, POLY PROLINE RICH MOTIFS,         
KEYWDS   2 TRANSFERASE, TRANSFERASE-UNKNOWN FUNCTION COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CAMARA-ARTIGAS                                                      
REVDAT   1   29-JAN-14 4J9G    0                                                
JRNL        AUTH   A.CAMARA-ARTIGAS                                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH THE   
JRNL        TITL 2 DESIGNED HIGH-AFFINITY PEPTIDE LIGAND P7                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.CAMARA-ARTIGAS,A.PALENCIA,J.C.MARTINEZ,I.LUQUE,J.A.GAVIRA, 
REMARK   1  AUTH 2 J.M.GARCIA-RUIZ                                              
REMARK   1  TITL   CRYSTALLIZATION BY CAPILLARY COUNTER-DIFFUSION AND STRUCTURE 
REMARK   1  TITL 2 DETERMINATION OF THE N114A MUTANT OF THE SH3 DOMAIN OF ABL   
REMARK   1  TITL 3 TYROSINE KINASE COMPLEXED WITH A HIGH-AFFINITY PEPTIDE       
REMARK   1  TITL 4 LIGAND.                                                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   646 2007              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   17452790                                                     
REMARK   1  DOI    10.1107/S0907444907011109                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.PALENCIA,A.CAMARA-ARTIGAS,M.T.PISABARRO,J.C.MARTINEZ,      
REMARK   1  AUTH 2 I.LUQUE                                                      
REMARK   1  TITL   ROLE OF INTERFACIAL WATER MOLECULES IN PROLINE-RICH LIGAND   
REMARK   1  TITL 2 RECOGNITION BY THE SRC HOMOLOGY 3 DOMAIN OF ABL.             
REMARK   1  REF    J.BIOL.CHEM.                  V. 285  2823 2010              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   19906645                                                     
REMARK   1  DOI    10.1074/JBC.M109.048033                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 17945                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 897                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.7094 -  4.1193    0.99     2764   130  0.1870 0.2398        
REMARK   3     2  4.1193 -  3.2702    1.00     2776   140  0.1671 0.1608        
REMARK   3     3  3.2702 -  2.8570    1.00     2750   143  0.1860 0.2049        
REMARK   3     4  2.8570 -  2.5958    1.00     2775   149  0.2064 0.2593        
REMARK   3     5  2.5958 -  2.4098    0.99     2695   174  0.2160 0.2695        
REMARK   3     6  2.4098 -  2.2677    0.99     2730   139  0.2179 0.2703        
REMARK   3     7  2.2677 -  2.1542    0.97     2711   112  0.2704 0.3420        
REMARK   3     8  2.1542 -  2.0604    1.00     2734   173  0.2358 0.3025        
REMARK   3     9  2.0604 -  1.9811    1.00     2798   113  0.2338 0.2940        
REMARK   3    10  1.9811 -  1.9127    0.99     2705   175  0.2891 0.3403        
REMARK   3    11  1.9127 -  1.8529    0.99     2785   143  0.2807 0.3185        
REMARK   3    12  1.8529 -  1.8000    0.69     1854   119  0.2788 0.2694        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.57                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013           1657                                  
REMARK   3   ANGLE     :  1.394           2273                                  
REMARK   3   CHIRALITY :  0.072            237                                  
REMARK   3   PLANARITY :  0.012            300                                  
REMARK   3   DIHEDRAL  : 11.931            593                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4J9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077763.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97951                            
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL-CUT CRYSTAL        
REMARK 200                                   MONOCHROMATOR AND A PAIR OF KB     
REMARK 200                                   MIRRORS                            
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR (VFM)     
REMARK 200                                   AND A HORIZONTAL FOCUSING MIRROR   
REMARK 200                                   (HFM), MANUFACTURED BY IRELEC.     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17945                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.746                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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: 2O88                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, 50 MM LITIUM       
REMARK 280  FORMIATE, 10% GLICEROL, AND 0.1 M MOPS , PH 7, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       30.15733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       15.07867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       15.07867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.15733            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4110 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 3910 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4080 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 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 210  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 202  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    59                                                      
REMARK 465     GLU A    60                                                      
REMARK 465     ASN A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     SER A   121                                                      
REMARK 465     MET C    59                                                      
REMARK 465     GLU C    60                                                      
REMARK 465     ASN C    61                                                      
REMARK 465     ASP C    62                                                      
REMARK 465     ASN C   120                                                      
REMARK 465     SER C   121                                                      
REMARK 465     MET E    59                                                      
REMARK 465     GLU E    60                                                      
REMARK 465     ASN E    61                                                      
REMARK 465     ASP E    62                                                      
REMARK 465     ASN E   120                                                      
REMARK 465     SER E   121                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF P7                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF P7                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF P7                     
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2O88   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND:              
REMARK 900 IMPLICATIONS FOR SH3-LIGAND INTERACTIONS                             
REMARK 900 RELATED ID: 3EG0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114T MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 RELATED ID: 3EG1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114Q MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND:              
REMARK 900 IMPLICATIONS FOR SH3-LIGAND INTERACTIONS                             
REMARK 900 RELATED ID: 3EG2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114Q MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 RELATED ID: 3EG3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 RELATED ID: 3EGU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN              
REMARK 900 RELATED ID: 4J9F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J9H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J9I   RELATED DB: PDB                                   
DBREF  4J9G A   60   121  UNP    P00519   ABL1_HUMAN      60    121             
DBREF  4J9G C   60   121  UNP    P00519   ABL1_HUMAN      60    121             
DBREF  4J9G E   60   121  UNP    P00519   ABL1_HUMAN      60    121             
DBREF  4J9G B    0    10  PDB    4J9G     4J9G             0     10             
DBREF  4J9G D    0    10  PDB    4J9G     4J9G             0     10             
DBREF  4J9G F    0    10  PDB    4J9G     4J9G             0     10             
SEQADV 4J9G MET A   59  UNP  P00519              INITIATING METHIONINE          
SEQADV 4J9G MET C   59  UNP  P00519              INITIATING METHIONINE          
SEQADV 4J9G MET E   59  UNP  P00519              INITIATING METHIONINE          
SEQRES   1 A   63  MET GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 A   63  PHE VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS          
SEQRES   3 A   63  GLY GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY          
SEQRES   4 A   63  GLU TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP          
SEQRES   5 A   63  VAL PRO SER ASN TYR ILE THR PRO VAL ASN SER                  
SEQRES   1 B   11  ACE ALA PRO THR TYR PRO PRO PRO PRO PRO PRO                  
SEQRES   1 C   63  MET GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 C   63  PHE VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS          
SEQRES   3 C   63  GLY GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY          
SEQRES   4 C   63  GLU TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP          
SEQRES   5 C   63  VAL PRO SER ASN TYR ILE THR PRO VAL ASN SER                  
SEQRES   1 D   11  ACE ALA PRO THR TYR PRO PRO PRO PRO PRO PRO                  
SEQRES   1 E   63  MET GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 E   63  PHE VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS          
SEQRES   3 E   63  GLY GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY          
SEQRES   4 E   63  GLU TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP          
SEQRES   5 E   63  VAL PRO SER ASN TYR ILE THR PRO VAL ASN SER                  
SEQRES   1 F   11  ACE ALA PRO THR TYR PRO PRO PRO PRO PRO PRO                  
HET    ACE  B   0       3                                                       
HET    ACE  D   0       3                                                       
HET    ACE  F   0       3                                                       
HET    SO4  E 201       5                                                       
HET    GOL  E 202       9                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  ACE    3(C2 H4 O)                                                   
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *89(H2 O)                                                     
SHEET    1   A 5 GLY A 107  PRO A 112  0                                        
SHEET    2   A 5 TRP A  99  THR A 104 -1  N  CYS A 100   O  VAL A 111           
SHEET    3   A 5 LYS A  87  TYR A  93 -1  N  LEU A  91   O  GLU A 101           
SHEET    4   A 5 LEU A  65  ALA A  68 -1  N  PHE A  66   O  LEU A  88           
SHEET    5   A 5 ILE A 116  PRO A 118 -1  O  THR A 117   N  VAL A  67           
SHEET    1   B 6 GLY C 107  PRO C 112  0                                        
SHEET    2   B 6 TRP C  99  THR C 104 -1  N  THR C 104   O  GLY C 107           
SHEET    3   B 6 LYS C  87  ASN C  94 -1  N  LEU C  91   O  GLU C 101           
SHEET    4   B 6 LYS E  87  ASN E  94 -1  O  TYR E  93   N  TYR C  93           
SHEET    5   B 6 TRP E  99  THR E 104 -1  O  GLU E 101   N  LEU E  91           
SHEET    6   B 6 GLY E 107  PRO E 112 -1  O  VAL E 111   N  CYS E 100           
SHEET    1   C 6 ILE C 116  PRO C 118  0                                        
SHEET    2   C 6 LEU C  65  ALA C  68 -1  N  VAL C  67   O  THR C 117           
SHEET    3   C 6 LYS C  87  ASN C  94 -1  O  LEU C  88   N  PHE C  66           
SHEET    4   C 6 LYS E  87  ASN E  94 -1  O  TYR E  93   N  TYR C  93           
SHEET    5   C 6 LEU E  65  ALA E  68 -1  N  PHE E  66   O  LEU E  88           
SHEET    6   C 6 ILE E 116  PRO E 118 -1  O  THR E 117   N  VAL E  67           
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.33  
LINK         C   ACE D   0                 N   ALA D   1     1555   1555  1.35  
LINK         C   ACE F   0                 N   ALA F   1     1555   1555  1.33  
SITE     1 AC1  4 GLU E  86  LYS E  87  LYS E 105  HOH E 310                    
SITE     1 AC2  8 GLY C  92  GLU C 101  LEU E  91  GLY E  92                    
SITE     2 AC2  8 TYR E  93  GLU E 101  HOH E 303  HOH E 323                    
SITE     1 AC3 16 TYR A  70  SER A  75  GLY A  76  THR A  79                    
SITE     2 AC3 16 LYS A  84  ASN A  94  GLU A  98  TRP A  99                    
SITE     3 AC3 16 LYS A 105  ASN A 106  TRP A 110  TYR A 115                    
SITE     4 AC3 16 HOH A 211  HOH B 101  HOH B 102  HOH B 104                    
SITE     1 AC4 17 TYR C  70  SER C  75  GLY C  76  ASP C  77                    
SITE     2 AC4 17 ASN C  78  THR C  79  ASN C  94  GLU C  98                    
SITE     3 AC4 17 TRP C  99  LYS C 105  ASN C 106  TRP C 110                    
SITE     4 AC4 17 TYR C 115  HOH D 101  TYR E  70  LYS E  84                    
SITE     5 AC4 17 HOH E 304                                                     
SITE     1 AC5 18 TYR C  70  LYS C  84  SER E  75  GLY E  76                    
SITE     2 AC5 18 ASP E  77  ASN E  78  THR E  79  ASN E  94                    
SITE     3 AC5 18 GLU E  98  TRP E  99  LYS E 105  ASN E 106                    
SITE     4 AC5 18 TRP E 110  TYR E 115  HOH E 305  HOH E 319                    
SITE     5 AC5 18 HOH F 101  HOH F 102                                          
CRYST1   86.309   86.309   45.236  90.00  90.00 120.00 P 32 2 1     18          
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      0.011586  0.006689  0.000000        0.00000                         
SCALE2      0.000000  0.013379  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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