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Database: PDB
Entry: 1AZG
LinkDB: 1AZG
Original site: 1AZG 
HEADER    COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE)    18-NOV-97   1AZG              
TITLE     NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE                   
TITLE    2 TYROSINE KINASE KINASE COMPLEXED WITH THE SYNTHETIC                  
TITLE    3 PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85              
TITLE    4 SUBUNIT OF PI3-KINASE, MINIMIZED AVERAGE (PROBMAP)                   
TITLE    5 STRUCTURE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRO-PRO-ARG-PRO-LEU-PRO-VAL-ALA-PRO-GLY-SER-SER-           
COMPND   3 LYS-THR;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: P85 SUBUNIT OF PI3-KINASE, RESIDUES 91 - 104;              
COMPND   6 SYNONYM: P2L;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FYN;                                                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: SH3 DOMAIN, RESIDUES 82 - 148;                             
COMPND  12 EC: 2.7.1.112;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 MOL_ID: 2;                                                           
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606;                                                
SOURCE   6 CELL_LINE: BL21;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE), SH3 DOMAIN,                     
KEYWDS   2 POLYPROLINE-BINDING, PHOSPHOTRANSFERASE                              
EXPDTA    SOLUTION NMR                                                          
AUTHOR    D.A.RENZONI,D.J.R.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,C.ROSSI,          
AUTHOR   2 M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY                              
REVDAT   2   24-FEB-09 1AZG    1       VERSN                                    
REVDAT   1   25-FEB-98 1AZG    0                                                
JRNL        AUTH   D.A.RENZONI,D.J.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,           
JRNL        AUTH 2 C.ROSSI,M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY              
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF             
JRNL        TITL 2 THE INTERACTION OF THE SH3 DOMAIN FROM FYN WITH              
JRNL        TITL 3 THE PROLINE-RICH BINDING SITE ON THE P85 SUBUNIT             
JRNL        TITL 4 OF PI3-KINASE.                                               
JRNL        REF    BIOCHEMISTRY                  V.  35 15646 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8961927                                                      
JRNL        DOI    10.1021/BI9620969                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.J.MORTON,D.J.PUGH,E.L.BROWN,J.D.KAHMANN,                   
REMARK   1  AUTH 2 D.A.RENZONI,I.D.CAMPBELL                                     
REMARK   1  TITL   SOLUTION STRUCTURE AND PEPTIDE BINDING OF THE SH3            
REMARK   1  TITL 2 DOMAIN FROM HUMAN FYN                                        
REMARK   1  REF    STRUCTURE                     V.   4   705 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN        
REMARK   3  THE JRNL CITATION ABOVE.                                            
REMARK   4                                                                      
REMARK   4 1AZG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     THR B    82                                                      
REMARK 465     GLY B    83                                                      
REMARK 465     ASP B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     ILE B   144                                                      
REMARK 465     GLN B   145                                                      
REMARK 465     ALA B   146                                                      
REMARK 465     GLU B   147                                                      
REMARK 465     GLU B   148                                                      
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    LEU A  95       98.40     67.31                                   
REMARK 500    PRO A  96       98.10    -61.17                                   
REMARK 500    ALA A  98      173.05    -47.51                                   
REMARK 500    PRO A  99       83.30    -60.78                                   
REMARK 500    THR B  85       71.58   -152.64                                   
REMARK 500    ALA B  95      106.10    -56.28                                   
REMARK 500    ASP B 100     -176.51    -64.57                                   
REMARK 500    PHE B 103     -172.34   -174.58                                   
REMARK 500    GLU B 116     -153.36    -57.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  93         0.29    SIDE_CHAIN                              
REMARK 500    ARG B 123         0.13    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AZG A   91   104  UNP    P27986   P85A_HUMAN      91    104             
DBREF  1AZG B   82   148  UNP    P06241   FYN_HUMAN       81    147             
SEQRES   1 A   14  PRO PRO ARG PRO LEU PRO VAL ALA PRO GLY SER SER LYS          
SEQRES   2 A   14  THR                                                          
SEQRES   1 B   67  THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP TYR GLU          
SEQRES   2 B   67  ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS GLY GLU          
SEQRES   3 B   67  LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP TRP TRP          
SEQRES   4 B   67  GLU ALA ARG SER LEU THR THR GLY GLU THR GLY TYR ILE          
SEQRES   5 B   67  PRO SER ASN TYR VAL ALA PRO VAL ASP SER ILE GLN ALA          
SEQRES   6 B   67  GLU GLU                                                      
HELIX    1  HA PRO B  134  TYR B  137  5                                   4    
SHEET    1  S1 3 LYS B 108  LEU B 112  0                                        
SHEET    2  S1 3 LEU B  86  ALA B  89 -1  N  PHE B  87   O  PHE B 109           
SHEET    3  S1 3 VAL B 138  PRO B 140 -1  O  ALA B 139   N  VAL B  88           
SHEET    1  S2 3 ASN B 113  SER B 114  0                                        
SHEET    2  S2 3 TRP B 119  SER B 124 -1  N  GLU B 121   O  ASN B 113           
SHEET    3  S2 3 THR B 130  ILE B 133 -1  O  ILE B 133   N  TRP B 120           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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