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Database: PDB
Entry: 4J9C
LinkDB: 4J9C
Original site: 4J9C 
HEADER    TRANSFERASE/UNKNOWN FUNCTION            16-FEB-13   4J9C              
TITLE     CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN H59Q-N96T MUTANT COMPLEXED    
TITLE    2 WITH THE DESIGNED HIGH-AFFINITY PEPTIDE LIGAND P17                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;                              
COMPND   3 CHAIN: A;                                                            
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 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: P17;                                                       
COMPND  12 CHAIN: B;                                                            
COMPND  13 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: ABL, ABL1, JTK7;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    BETA SHANDWICH, SH3 DOMAIN, KINASE, POLY PROLINE RICH MOTIFS,         
KEYWDS   2 TRANSFERASE-UNKNOWN FUNCTION COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CAMARA-ARTIGAS                                                      
REVDAT   2   15-OCT-14 4J9C    1       AUTHOR                                   
REVDAT   1   29-JAN-14 4J9C    0                                                
JRNL        AUTH   A.CAMARA-ARTIGAS                                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN H59Q-N96T MUTANT     
JRNL        TITL 2 COMPLEXED WITH THE DESIGNED HIGH-AFFINITY PEPTIDE LIGAND P17 
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.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 29561                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1500                            
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 16.7558 -  2.8950    0.77     2074    66  0.1948 0.2325        
REMARK   3     2  2.8950 -  2.2997    1.00     2647   128  0.1631 0.1569        
REMARK   3     3  2.2997 -  2.0096    1.00     2643   136  0.1370 0.1246        
REMARK   3     4  2.0096 -  1.8261    1.00     2611   136  0.1250 0.1367        
REMARK   3     5  1.8261 -  1.6953    1.00     2680   123  0.1212 0.1741        
REMARK   3     6  1.6953 -  1.5955    1.00     2592   154  0.1175 0.1232        
REMARK   3     7  1.5955 -  1.5156    1.00     2621   180  0.1239 0.1704        
REMARK   3     8  1.5156 -  1.4497    1.00     2655   133  0.1163 0.1416        
REMARK   3     9  1.4497 -  1.3939    1.00     2624   158  0.1170 0.1460        
REMARK   3    10  1.3939 -  1.3458    1.00     2584   133  0.1165 0.1421        
REMARK   3    11  1.3458 -  1.3038    1.00     2693   134  0.1262 0.1526        
REMARK   3    12  1.3038 -  1.2665    1.00     2601   152  0.1283 0.1899        
REMARK   3    13  1.2665 -  1.2332    1.00     2635   170  0.1319 0.1904        
REMARK   3    14  1.2332 -  1.2031    1.00     2606   127  0.1332 0.1545        
REMARK   3    15  1.2031 -  1.1758    1.00     2623   147  0.1309 0.1337        
REMARK   3    16  1.1758 -  1.1507    1.00     2616   176  0.1319 0.1849        
REMARK   3    17  1.1507 -  1.1277    1.00     2633   119  0.1412 0.2199        
REMARK   3    18  1.1277 -  1.1065    1.00     2614   140  0.1564 0.1502        
REMARK   3    19  1.1065 -  1.0867    1.00     2632   152  0.1730 0.1802        
REMARK   3    20  1.0867 -  1.0683    0.99     2612   130  0.1920 0.2439        
REMARK   3    21  1.0683 -  1.0510    0.98     2575   125  0.2298 0.2666        
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)     : 0.080            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.30                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.95                          
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      :  0.008            569                                  
REMARK   3   ANGLE     :  1.237            772                                  
REMARK   3   CHIRALITY :  0.070             83                                  
REMARK   3   PLANARITY :  0.008             99                                  
REMARK   3   DIHEDRAL  : 14.422            209                                  
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 4J9C 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 RCSB077759.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT ESRF MONOCHROMATOR     
REMARK 200                                   AND TORODIAL FOCUSING MIRROR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29561                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.051                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.995                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : 0.04000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.610                              
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   (%): 38.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMS, 5% PEG 200, 20 MM LICL, 0.1   
REMARK 280  M ACONA , PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2                         
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+1/3                                            
REMARK 290       5555   -X+Y,Y,-Z+2/3                                           
REMARK 290       6555   X,X-Y,-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 -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       30.27333            
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       15.13667            
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       15.13667            
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       30.27333            
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        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 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 303  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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASN A   78   OD1                                                 
REMARK 480     ARG A   89   NH1                                                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF P17                    
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: 4J9B   RELATED DB: PDB                                   
DBREF  4J9C A   60   121  UNP    P00519   ABL1_HUMAN      60    121             
DBREF  4J9C B    0    10  PDB    4J9C     4J9C             0     10             
SEQADV 4J9C MET A   59  UNP  P00519              INITIATING METHIONINE          
SEQADV 4J9C GLN A   95  UNP  P00519    HIS    95 ENGINEERED MUTATION            
SEQADV 4J9C THR A   96  UNP  P00519    ASN    96 ENGINEERED MUTATION            
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 GLN THR 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 SER PRO PRO LEU PRO PRO                  
HET    ACE  B   0       3                                                       
HET    PGE  A 201      24                                                       
HET    PEG  A 202      17                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   3  PGE    C6 H14 O4                                                    
FORMUL   4  PEG    C4 H10 O3                                                    
FORMUL   5  HOH   *80(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           
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.33  
SITE     1 AC1  7 TYR A  70  SER A 113  ASN A 114  ILE A 116                    
SITE     2 AC1  7 HOH A 330  PRO B   9  PRO B  10                               
SITE     1 AC2  4 LEU A  91  GLU A 101  ASN A 106  HOH A 332                    
SITE     1 AC3 32 TYR A  70  SER A  75  ASP A  77  LYS A  84                    
SITE     2 AC3 32 ASN A  94  GLU A  98  TRP A  99  LYS A 105                    
SITE     3 AC3 32 ASN A 106  TRP A 110  PRO A 112  ASN A 114                    
SITE     4 AC3 32 TYR A 115  PGE A 201  HOH A 308  HOH A 312                    
SITE     5 AC3 32 HOH A 316  HOH A 354  HOH A 364  HOH B 101                    
SITE     6 AC3 32 HOH B 102  HOH B 103  HOH B 104  HOH B 105                    
SITE     7 AC3 32 HOH B 106  HOH B 107  HOH B 108  HOH B 109                    
SITE     8 AC3 32 HOH B 111  HOH B 113  HOH B 115  HOH B 116                    
CRYST1   49.646   49.646   45.410  90.00  90.00 120.00 P 32 1 2      6          
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      0.020143  0.011629  0.000000        0.00000                         
SCALE2      0.000000  0.023259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022022        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system