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Database: PDB
Entry: 1EFN
LinkDB: 1EFN
Original site: 1EFN 
HEADER    COMPLEX (SH3 DOMAIN/VIRAL ENHANCER)     29-JUN-96   1EFN              
TITLE     HIV-1 NEF PROTEIN IN COMPLEX WITH R96I MUTANT FYN SH3 DOMAIN          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FYN TYROSINE KINASE;                                       
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: SH3 DOMAIN, RESIDUES 85-141;                               
COMPND   5 SYNONYM: SRC-HOMOLOGY 3 DOMAIN;                                      
COMPND   6 EC: 2.7.1.112;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HIV-1 NEF PROTEIN;                                         
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: CONSERVED CORE DOMAIN OF NEF, RESIDUES 71-203;             
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HIV-1 NEF;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  10 EXPRESSION_SYSTEM_GENE: FYN TYROSINE KINASE;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  13 ORGANISM_TAXID: 11676;                                               
SOURCE  14 STRAIN: NL4-3;                                                       
SOURCE  15 GENE: HIV-1 NEF;                                                     
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: K12 PR745;                                 
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PGEX-2T(TEV);                             
SOURCE  20 EXPRESSION_SYSTEM_GENE: SYSTEM_GENE: HIV-1 NEF                       
KEYWDS    COMPLEX (SH3 DOMAIN/VIRAL ENHANCER), PROTO-ONCOGENE,                  
KEYWDS   2 TRANSFERASE, TYROSINE-PROTEIN KINASE, PHOSPHORYLATION, AIDS,         
KEYWDS   3 MYRISTYLATION, GTP-BINDING, ATP-BINDING, SH3 DOMAIN, SH2             
KEYWDS   4 DOMAIN, PPII HELIX, PXXP MOTIF                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-H.LEE,J.KURIYAN                                                    
REVDAT   2   24-FEB-09 1EFN    1       VERSN                                    
REVDAT   1   11-JAN-97 1EFN    0                                                
JRNL        AUTH   C.H.LEE,K.SAKSELA,U.A.MIRZA,B.T.CHAIT,J.KURIYAN              
JRNL        TITL   CRYSTAL STRUCTURE OF THE CONSERVED CORE OF HIV-1             
JRNL        TITL 2 NEF COMPLEXED WITH A SRC FAMILY SH3 DOMAIN.                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  85   931 1996              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   8681387                                                      
JRNL        DOI    10.1016/S0092-8674(00)81276-3                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.GRZESIEK,A.BAX,G.M.CLORE,A.M.GRONENBORN,J.S.HU,            
REMARK   1  AUTH 2 J.KAUFMAN,I.PALMER,S.J.STAHL,P.T.WINGFIELD                   
REMARK   1  TITL   THE SOLUTION STRUCTURE OF HIV-1 NEF REVEALS AN               
REMARK   1  TITL 2 UNEXPECTED FOLD AND PERMITS DELINEATION OF THE               
REMARK   1  TITL 3 BINDING SURFACE FOR THE SH3 DOMAIN OF HCK TYROSINE           
REMARK   1  TITL 4 PROTEIN KINASE                                               
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   3   340 1996              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.H.LEE,B.LEUNG,M.A.LEMMON,J.ZHENG,D.COWBURN,                
REMARK   1  AUTH 2 J.KURIYAN,K.SAKSELA                                          
REMARK   1  TITL   A SINGLE AMINO ACID IN THE SH3 DOMAIN OF HCK                 
REMARK   1  TITL 2 DETERMINES ITS HIGH AFFINITY AND SPECIFICITY IN              
REMARK   1  TITL 3 BINDING TO HIV-1 NEF PROTEIN                                 
REMARK   1  REF    EMBO J.                       V.  14  5006 1995              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20684                          
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) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 2635                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 99                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.55                          
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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  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 1EFN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JAN-96                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26464                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      152.73333            
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       76.36667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      114.55000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.18333            
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      190.91667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      152.73333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       76.36667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       38.18333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      114.55000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      190.91667            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     ASP A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     CYS B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     TRP B    57                                                      
REMARK 465     LEU B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ALA B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     VAL B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     PHE B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     GLU B   149                                                      
REMARK 465     PRO B   150                                                      
REMARK 465     ASP B   151                                                      
REMARK 465     LYS B   152                                                      
REMARK 465     VAL B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     ASN B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     ASN B   161                                                      
REMARK 465     THR B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     PRO B   167                                                      
REMARK 465     VAL B   168                                                      
REMARK 465     SER B   169                                                      
REMARK 465     LEU B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     MET B   173                                                      
REMARK 465     ASP B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     PRO B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     ASP C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     CYS D    55                                                      
REMARK 465     ALA D    56                                                      
REMARK 465     TRP D    57                                                      
REMARK 465     LEU D    58                                                      
REMARK 465     GLU D    59                                                      
REMARK 465     ALA D    60                                                      
REMARK 465     GLN D    61                                                      
REMARK 465     GLU D    62                                                      
REMARK 465     GLU D    63                                                      
REMARK 465     GLU D    64                                                      
REMARK 465     GLU D    65                                                      
REMARK 465     VAL D    66                                                      
REMARK 465     GLY D    67                                                      
REMARK 465     PHE D    68                                                      
REMARK 465     PRO D    69                                                      
REMARK 465     VAL D    70                                                      
REMARK 465     GLU D   149                                                      
REMARK 465     PRO D   150                                                      
REMARK 465     ASP D   151                                                      
REMARK 465     LYS D   152                                                      
REMARK 465     VAL D   153                                                      
REMARK 465     GLU D   154                                                      
REMARK 465     GLU D   155                                                      
REMARK 465     ALA D   156                                                      
REMARK 465     ASN D   157                                                      
REMARK 465     LYS D   158                                                      
REMARK 465     GLY D   159                                                      
REMARK 465     GLU D   160                                                      
REMARK 465     ASN D   161                                                      
REMARK 465     THR D   162                                                      
REMARK 465     SER D   163                                                      
REMARK 465     LEU D   164                                                      
REMARK 465     LEU D   165                                                      
REMARK 465     HIS D   166                                                      
REMARK 465     PRO D   167                                                      
REMARK 465     VAL D   168                                                      
REMARK 465     SER D   169                                                      
REMARK 465     LEU D   170                                                      
REMARK 465     HIS D   171                                                      
REMARK 465     GLY D   172                                                      
REMARK 465     MET D   173                                                      
REMARK 465     ASP D   174                                                      
REMARK 465     ASP D   175                                                      
REMARK 465     PRO D   176                                                      
REMARK 465     GLU D   177                                                      
REMARK 465     LYS D   204                                                      
REMARK 465     ASN D   205                                                      
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     LEU A  86    CG   CD1  CD2                                       
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 108    CG   CD   CE   NZ                                   
REMARK 470     LEU A 112    CG   CD1  CD2                                       
REMARK 470     SER A 115    OG                                                  
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 123    CZ   NH1  NH2                                       
REMARK 470     LEU A 125    CG   CD1  CD2                                       
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     ARG B 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  82    CG   CD   CE   NZ                                   
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     VAL D 148    CG1  CG2                                            
REMARK 470     ARG D 178    CG   CD   NE   CZ   NH1  NH2                        
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    PHE A 103     -177.36   -174.05                                   
REMARK 500    ASN A 113      137.34    177.87                                   
REMARK 500    SER A 114       10.86   -144.31                                   
REMARK 500    THR A 127      -29.21   -152.14                                   
REMARK 500    PRO B  72      158.89    -48.46                                   
REMARK 500    VAL B  74      153.64    -48.51                                   
REMARK 500    PRO B 122       74.50    -64.73                                   
REMARK 500    ASP B 123       16.67   -152.17                                   
REMARK 500    CYS B 142       41.76    -91.08                                   
REMARK 500    SER B 187      -36.06    -33.13                                   
REMARK 500    PRO D 122       51.04    -65.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 878        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH B 887        DISTANCE =  5.83 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PBM B 710  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 192   NE2                                                    
REMARK 620 2 ASP D  86   OD1 159.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBM B 710                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBM D 720                 
DBREF  1EFN A   86   143  UNP    P06241   FYN_HUMAN       85    142             
DBREF  1EFN B   54   205  UNP    P03406   NEF_HV1BR       54    205             
DBREF  1EFN C   86   143  UNP    P06241   FYN_HUMAN       85    142             
DBREF  1EFN D   54   205  UNP    P03406   NEF_HV1BR       54    205             
SEQADV 1EFN ILE A   96  UNP  P06241    ARG    95 ENGINEERED                     
SEQADV 1EFN ARG B   71  UNP  P03406    THR    71 ENGINEERED                     
SEQADV 1EFN ILE C   96  UNP  P06241    ARG    95 ENGINEERED                     
SEQADV 1EFN ARG D   71  UNP  P03406    THR    71 ENGINEERED                     
SEQRES   1 A   59  ALA LEU PHE VAL ALA LEU TYR ASP TYR GLU ALA ILE THR          
SEQRES   2 A   59  GLU ASP ASP LEU SER PHE HIS LYS GLY GLU LYS PHE GLN          
SEQRES   3 A   59  ILE LEU ASN SER SER GLU GLY ASP TRP TRP GLU ALA ARG          
SEQRES   4 A   59  SER LEU THR THR GLY GLU THR GLY TYR ILE PRO SER ASN          
SEQRES   5 A   59  TYR VAL ALA PRO VAL ASP SER                                  
SEQRES   1 B  152  ALA CYS ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL          
SEQRES   2 B  152  GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET          
SEQRES   3 B  152  THR TYR LYS ALA ALA VAL ASP LEU SER HIS PHE LEU LYS          
SEQRES   4 B  152  GLU LYS GLY GLY LEU GLU GLY LEU ILE HIS SER GLN ARG          
SEQRES   5 B  152  ARG GLN ASP ILE LEU ASP LEU TRP ILE TYR HIS THR GLN          
SEQRES   6 B  152  GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO          
SEQRES   7 B  152  GLY VAL ARG TYR PRO LEU THR PHE GLY TRP CYS TYR LYS          
SEQRES   8 B  152  LEU VAL PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA ASN          
SEQRES   9 B  152  LYS GLY GLU ASN THR SER LEU LEU HIS PRO VAL SER LEU          
SEQRES  10 B  152  HIS GLY MET ASP ASP PRO GLU ARG GLU VAL LEU GLU TRP          
SEQRES  11 B  152  ARG PHE ASP SER ARG LEU ALA PHE HIS HIS VAL ALA ARG          
SEQRES  12 B  152  GLU LEU HIS PRO GLU TYR PHE LYS ASN                          
SEQRES   1 C   59  ALA LEU PHE VAL ALA LEU TYR ASP TYR GLU ALA ILE THR          
SEQRES   2 C   59  GLU ASP ASP LEU SER PHE HIS LYS GLY GLU LYS PHE GLN          
SEQRES   3 C   59  ILE LEU ASN SER SER GLU GLY ASP TRP TRP GLU ALA ARG          
SEQRES   4 C   59  SER LEU THR THR GLY GLU THR GLY TYR ILE PRO SER ASN          
SEQRES   5 C   59  TYR VAL ALA PRO VAL ASP SER                                  
SEQRES   1 D  152  ALA CYS ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL          
SEQRES   2 D  152  GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET          
SEQRES   3 D  152  THR TYR LYS ALA ALA VAL ASP LEU SER HIS PHE LEU LYS          
SEQRES   4 D  152  GLU LYS GLY GLY LEU GLU GLY LEU ILE HIS SER GLN ARG          
SEQRES   5 D  152  ARG GLN ASP ILE LEU ASP LEU TRP ILE TYR HIS THR GLN          
SEQRES   6 D  152  GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO          
SEQRES   7 D  152  GLY VAL ARG TYR PRO LEU THR PHE GLY TRP CYS TYR LYS          
SEQRES   8 D  152  LEU VAL PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA ASN          
SEQRES   9 D  152  LYS GLY GLU ASN THR SER LEU LEU HIS PRO VAL SER LEU          
SEQRES  10 D  152  HIS GLY MET ASP ASP PRO GLU ARG GLU VAL LEU GLU TRP          
SEQRES  11 D  152  ARG PHE ASP SER ARG LEU ALA PHE HIS HIS VAL ALA ARG          
SEQRES  12 D  152  GLU LEU HIS PRO GLU TYR PHE LYS ASN                          
HET    PBM  B 710       4                                                       
HET    PBM  D 720       4                                                       
HETNAM     PBM TRIMETHYL LEAD ION                                               
FORMUL   5  PBM    2(C3 H9 PB 1+)                                               
FORMUL   7  HOH   *99(H2 O)                                                     
HELIX    1   1 SER A  135  TYR A  137  5                                   3    
HELIX    2   2 TYR B   81  GLU B   93  1                                  13    
HELIX    3   3 GLN B  104  GLN B  118  1                                  15    
HELIX    4   4 SER B  187  ALA B  190  5                                   4    
HELIX    5   5 VAL B  194  LEU B  198  1                                   5    
HELIX    6   6 PRO B  200  TYR B  202  5                                   3    
HELIX    7   7 SER C  135  TYR C  137  5                                   3    
HELIX    8   8 TYR D   81  LYS D   94  1                                  14    
HELIX    9   9 GLN D  104  GLN D  118  1                                  15    
HELIX   10  10 SER D  187  ALA D  190  5                                   4    
HELIX   11  11 VAL D  194  LEU D  198  1                                   5    
SHEET    1   A 5 VAL A 138  PRO A 140  0                                        
SHEET    2   A 5 LEU A  86  ALA A  89 -1  N  VAL A  88   O  ALA A 139           
SHEET    3   A 5 LYS A 108  ASN A 113 -1  N  PHE A 109   O  PHE A  87           
SHEET    4   A 5 TRP A 119  SER A 124 -1  N  ARG A 123   O  GLN A 110           
SHEET    5   A 5 GLU A 129  PRO A 134 -1  N  ILE A 133   O  TRP A 120           
SHEET    1   B 2 TYR B 143  PRO B 147  0                                        
SHEET    2   B 2 LEU B 181  PHE B 185 -1  N  ARG B 184   O  LYS B 144           
SHEET    1   C 5 VAL C 138  PRO C 140  0                                        
SHEET    2   C 5 LEU C  86  ALA C  89 -1  N  VAL C  88   O  ALA C 139           
SHEET    3   C 5 LYS C 108  ASN C 113 -1  N  PHE C 109   O  PHE C  87           
SHEET    4   C 5 TRP C 119  SER C 124 -1  N  ARG C 123   O  GLN C 110           
SHEET    5   C 5 THR C 130  PRO C 134 -1  N  ILE C 133   O  TRP C 120           
SHEET    1   D 2 TYR D 143  PRO D 147  0                                        
SHEET    2   D 2 LEU D 181  PHE D 185 -1  N  ARG D 184   O  LYS D 144           
LINK        PB   PBM B 710                 NE2 HIS B 192     1555   1555  2.98  
LINK        PB   PBM B 710                 OD1 ASP D  86     1555   9655  3.02  
CISPEP   1 GLY B  130    PRO B  131          0        -0.37                     
CISPEP   2 GLY D  130    PRO D  131          0        -0.29                     
SITE     1 AC1  4 HIS B 192  GLU C  98  ASP D  86  HIS D  89                    
SITE     1 AC2  2 PRO B 122  ASP D 108                                          
CRYST1  107.800  107.800  229.100  90.00  90.00 120.00 P 65 2 2     24          
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      0.009276  0.005356  0.000000        0.00000                         
SCALE2      0.000000  0.010712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004365        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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