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Database: PDB
Entry: 3UA7
LinkDB: 3UA7
Original site: 3UA7 
HEADER    TRANSFERASE/VIRAL PROTEIN               21-OCT-11   3UA7              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN FYN SH3 DOMAIN IN COMPLEX WITH A       
TITLE    2 PEPTIDE FROM THE HEPATITIS C VIRUS NS5A-PROTEIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE FYN;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SH3 DOMAIN (UNP RESIDUES 81-143);                          
COMPND   5 SYNONYM: PROTO-ONCOGENE SYN, PROTO-ONCOGENE C-FYN, SRC-LIKE KINASE,  
COMPND   6 SLK, P59-FYN;                                                        
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NON-STRUCTURAL PROTEIN 5A;                                 
COMPND  11 CHAIN: E, F;                                                         
COMPND  12 FRAGMENT: PROLINE-RICH REGION (UNP RESIDUES 350-360);                
COMPND  13 SYNONYM: NS5A;                                                       
COMPND  14 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: FYN;                                                           
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: PET3D;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;                              
SOURCE  14 ORGANISM_COMMON: HCV;                                                
SOURCE  15 ORGANISM_TAXID: 11103                                                
KEYWDS    BETA BARREL, KINASE, POLY PROLINE RICH MOTIF, TRANSFERASE-VIRAL       
KEYWDS   2 PROTEIN COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.MARTIN-GARCIA,J.RUIZ-SANZ,I.LUQUE,A.CAMARA-ARTIGAS                
REVDAT   2   23-JAN-13 3UA7    1       JRNL                                     
REVDAT   1   25-JUL-12 3UA7    0                                                
JRNL        AUTH   J.M.MARTIN-GARCIA,I.LUQUE,J.RUIZ-SANZ,A.CAMARA-ARTIGAS       
JRNL        TITL   THE PROMISCUOUS BINDING OF THE FYN SH3 DOMAIN TO A PEPTIDE   
JRNL        TITL 2 FROM THE NS5A PROTEIN.                                       
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68  1030 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22868769                                                     
JRNL        DOI    10.1107/S0907444912019798                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 40262                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4012                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2687                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 262                          
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2077                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 173                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96000                                              
REMARK   3    B22 (A**2) : 0.96000                                              
REMARK   3    B33 (A**2) : -1.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.154         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2146 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2924 ; 1.877 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 7.485 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;32.177 ;24.286       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   306 ;12.813 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;20.483 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   308 ; 0.153 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1682 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1307 ; 3.322 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2100 ; 4.559 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   839 ; 5.818 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   824 ; 7.904 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2146 ; 3.554 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     85       A     114      2                      
REMARK   3           1     B     85       B     114      2                      
REMARK   3           1     C     85       C     114      2                      
REMARK   3           1     D     85       D     114      2                      
REMARK   3           2     A    118       A     140      5                      
REMARK   3           2     B    118       B     140      5                      
REMARK   3           2     C    118       C     140      5                      
REMARK   3           2     D    118       D     140      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    120 ; 0.230 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    120 ; 0.220 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    120 ; 0.230 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    120 ; 0.240 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    223 ; 0.510 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    223 ; 0.850 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    223 ; 0.640 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    223 ; 0.760 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    A    (A):     93 ; 0.630 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):     93 ; 0.500 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    C    (A):     93 ; 0.460 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    D    (A):     93 ; 0.490 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):    120 ; 3.150 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):    120 ; 3.680 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):    120 ; 3.470 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):    120 ; 3.340 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    223 ; 3.380 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    223 ; 3.630 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    223 ; 3.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    223 ; 3.280 ; 2.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):     93 ; 3.360 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):     93 ; 3.980 ;10.000           
REMARK   3   LOOSE THERMAL      1    C (A**2):     93 ; 3.710 ;10.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):     93 ; 3.350 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 3UA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068500.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
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                  : DIAMOND(001)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44446                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.526                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.45400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SHF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4 M SODIUM FORMATE, 10 MM ZINC           
REMARK 280  CHLORIDE, 0.1 M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.79500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       25.69500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       25.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.39750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       25.69500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       25.69500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      139.19250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       25.69500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       25.69500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.39750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       25.69500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       25.69500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      139.19250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       92.79500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 F  40  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    80                                                      
REMARK 465     MET B    80                                                      
REMARK 465     MET C    80                                                      
REMARK 465     GLY C    81                                                      
REMARK 465     THR C    82                                                      
REMARK 465     ASP C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     MET D    80                                                      
REMARK 465     GLY D    81                                                      
REMARK 465     THR D    82                                                      
REMARK 465     ARG E     9                                                      
REMARK 465     LYS E    10                                                      
REMARK 465     ARG E    11                                                      
REMARK 465     ACE F     0                                                      
REMARK 465     ARG F     9                                                      
REMARK 465     LYS F    10                                                      
REMARK 465     ARG F    11                                                      
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    GLU A 116       53.38   -107.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN C   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT C 144   O2                                                     
REMARK 620 2 GLU C 107   OE2 111.8                                              
REMARK 620 3 HIS C 104   ND1 119.4 107.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT D   1   O1                                                     
REMARK 620 2 GLU D 107   OE2 116.2                                              
REMARK 620 3 HIS D 104   ND1 115.8 102.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 145  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  83   O                                                      
REMARK 620 2 GLY B  83   O   167.0                                              
REMARK 620 3 HOH A 167   O    85.1  82.5                                        
REMARK 620 4 HOH D  66   O   107.3  78.6 131.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 144                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 144                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 145                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SHF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UA6   RELATED DB: PDB                                   
DBREF  3UA7 A   81   143  UNP    P06241   FYN_HUMAN       81    143             
DBREF  3UA7 B   81   143  UNP    P06241   FYN_HUMAN       81    143             
DBREF  3UA7 C   81   143  UNP    P06241   FYN_HUMAN       81    143             
DBREF  3UA7 D   81   143  UNP    P06241   FYN_HUMAN       81    143             
DBREF  3UA7 E    1    11  UNP    Q9YKI6   Q9YKI6_9HEPC   350    360             
DBREF  3UA7 F    1    11  UNP    Q9YKI6   Q9YKI6_9HEPC   350    360             
SEQADV 3UA7 MET A   80  UNP  P06241              INITIATING METHIONINE          
SEQADV 3UA7 MET B   80  UNP  P06241              INITIATING METHIONINE          
SEQADV 3UA7 MET C   80  UNP  P06241              INITIATING METHIONINE          
SEQADV 3UA7 MET D   80  UNP  P06241              INITIATING METHIONINE          
SEQADV 3UA7 ACE E    0  UNP  Q9YKI6              ACETYLATION                    
SEQADV 3UA7 ACE F    0  UNP  Q9YKI6              ACETYLATION                    
SEQRES   1 A   64  MET GLY THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 A   64  TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS          
SEQRES   3 A   64  GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP          
SEQRES   4 A   64  TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY          
SEQRES   5 A   64  TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER              
SEQRES   1 B   64  MET GLY THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 B   64  TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS          
SEQRES   3 B   64  GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP          
SEQRES   4 B   64  TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY          
SEQRES   5 B   64  TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER              
SEQRES   1 C   64  MET GLY THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 C   64  TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS          
SEQRES   3 C   64  GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP          
SEQRES   4 C   64  TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY          
SEQRES   5 C   64  TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER              
SEQRES   1 D   64  MET GLY THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP          
SEQRES   2 D   64  TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS          
SEQRES   3 D   64  GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP          
SEQRES   4 D   64  TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY          
SEQRES   5 D   64  TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER              
SEQRES   1 E   12  ACE ALA PRO PRO ILE PRO PRO PRO ARG ARG LYS ARG              
SEQRES   1 F   12  ACE ALA PRO PRO ILE PRO PRO PRO ARG ARG LYS ARG              
HET    ACE  E   0       3                                                       
HET    GOL  A   1       6                                                       
HET     CL  A 144       1                                                       
HET     NA  A 145       1                                                       
HET     ZN  C   1       1                                                       
HET    FMT  C 144       3                                                       
HET     ZN  D   2       1                                                       
HET    FMT  D   1       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     FMT FORMIC ACID                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  ACE    C2 H4 O                                                      
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8   CL    CL 1-                                                        
FORMUL   9   NA    NA 1+                                                        
FORMUL  10   ZN    2(ZN 2+)                                                     
FORMUL  11  FMT    2(C H2 O2)                                                   
FORMUL  14  HOH   *173(H2 O)                                                    
SHEET    1   A 5 THR A 130  PRO A 134  0                                        
SHEET    2   A 5 TRP A 119  SER A 124 -1  N  ALA A 122   O  GLY A 131           
SHEET    3   A 5 LYS A 108  ASN A 113 -1  N  LEU A 112   O  GLU A 121           
SHEET    4   A 5 PHE A  87  ALA A  89 -1  N  PHE A  87   O  PHE A 109           
SHEET    5   A 5 VAL A 138  PRO A 140 -1  O  ALA A 139   N  VAL A  88           
SHEET    1   B 5 THR B 130  PRO B 134  0                                        
SHEET    2   B 5 TRP B 119  SER B 124 -1  N  ALA B 122   O  GLY B 131           
SHEET    3   B 5 LYS B 108  ASN B 113 -1  N  GLN B 110   O  ARG B 123           
SHEET    4   B 5 PHE B  87  ALA B  89 -1  N  PHE B  87   O  PHE B 109           
SHEET    5   B 5 VAL B 138  PRO B 140 -1  O  ALA B 139   N  VAL B  88           
SHEET    1   C 5 THR C 130  PRO C 134  0                                        
SHEET    2   C 5 TRP C 119  SER C 124 -1  N  ALA C 122   O  GLY C 131           
SHEET    3   C 5 LYS C 108  ASN C 113 -1  N  LEU C 112   O  GLU C 121           
SHEET    4   C 5 PHE C  87  ALA C  89 -1  N  PHE C  87   O  PHE C 109           
SHEET    5   C 5 VAL C 138  PRO C 140 -1  O  ALA C 139   N  VAL C  88           
SHEET    1   D 5 THR D 130  PRO D 134  0                                        
SHEET    2   D 5 TRP D 119  SER D 124 -1  N  ALA D 122   O  GLY D 131           
SHEET    3   D 5 LYS D 108  ASN D 113 -1  N  LEU D 112   O  GLU D 121           
SHEET    4   D 5 LEU D  86  ALA D  89 -1  N  PHE D  87   O  PHE D 109           
SHEET    5   D 5 VAL D 138  PRO D 140 -1  O  ALA D 139   N  VAL D  88           
LINK         C   ACE E   0                 N   ALA E   1     1555   1555  1.33  
LINK        ZN    ZN C   1                 O2  FMT C 144     1555   1555  1.86  
LINK        ZN    ZN D   2                 O1  FMT D   1     1555   1555  1.95  
LINK         OE2 GLU C 107                ZN    ZN C   1     1555   1555  1.99  
LINK         OE2 GLU D 107                ZN    ZN D   2     1555   1555  2.00  
LINK         ND1 HIS D 104                ZN    ZN D   2     1555   1555  2.06  
LINK         ND1 HIS C 104                ZN    ZN C   1     1555   1555  2.09  
LINK         O   GLY A  83                NA    NA A 145     1555   1555  2.16  
LINK         O   GLY B  83                NA    NA A 145     1555   1555  2.37  
LINK        NA    NA A 145                 O   HOH A 167     1555   1555  2.50  
LINK        NA    NA A 145                 O   HOH D  66     1555   1555  2.63  
SITE     1 AC1  4 HIS B 104  HIS C 104  GLU C 107  FMT C 144                    
SITE     1 AC2  4 HIS A 104  FMT D   1  HIS D 104  GLU D 107                    
SITE     1 AC3  4 THR A  97  ASP A 100  TRP A 119  TYR A 132                    
SITE     1 AC4  8 HIS A 104   ZN D   2  HOH D  75  SER D 102                    
SITE     2 AC4  8 PHE D 103  HIS D 104  GLU D 107  HOH D 158                    
SITE     1 AC5  7 HIS B 104   ZN C   1  SER C 102  PHE C 103                    
SITE     2 AC5  7 HIS C 104  GLU C 107  HOH C 154                               
SITE     1 AC6  4 THR A 127  VAL D  88  GLY D 106  LYS D 108                    
SITE     1 AC7  4 GLY A  83  HOH A 167  GLY B  83  HOH D  66                    
CRYST1   51.390   51.390  185.590  90.00  90.00  90.00 P 41 21 2    32          
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      0.019459  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019459  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005388        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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