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Database: PDB
Entry: 3UA6
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HEADER    TRANSFERASE                             21-OCT-11   3UA6              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN FYN SH3 DOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE FYN;                               
COMPND   3 CHAIN: A, B;                                                         
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                                                      
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                                     
KEYWDS    BETA BARREL, TRANSFERASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CAMARA-ARTIGAS,J.M.MARTIN-GARCIA                                    
REVDAT   2   23-JAN-13 3UA6    1       JRNL                                     
REVDAT   1   25-JUL-12 3UA6    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.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 11447                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 544                             
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 454                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 25                           
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 943                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.92                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : 0.53000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.06000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.137         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.052         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1018 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1377 ; 1.978 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   121 ; 7.304 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    54 ;39.365 ;24.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   151 ;13.380 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;11.186 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   142 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   795 ; 0.008 ; 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):   603 ; 2.006 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   953 ; 2.933 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   415 ; 4.354 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   422 ; 6.731 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
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                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     85       A     113      2                      
REMARK   3           1     B     85       B     113      2                      
REMARK   3           2     A    118       A     140      4                      
REMARK   3           2     B    118       B     140      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    114 ; 0.500 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    293 ; 0.760 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    114 ; 1.790 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    293 ; 2.190 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    85        A   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6560  -0.4100 -10.4940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0148 T22:   0.0245                                     
REMARK   3      T33:   0.0284 T12:   0.0120                                     
REMARK   3      T13:  -0.0027 T23:  -0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8237 L22:   1.5698                                     
REMARK   3      L33:   3.7608 L12:  -0.6960                                     
REMARK   3      L13:   0.2198 L23:  -0.4340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:   0.0857 S13:   0.0476                       
REMARK   3      S21:   0.0151 S22:   0.0271 S23:  -0.0215                       
REMARK   3      S31:   0.0178 S32:   0.1312 S33:  -0.0247                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    83        B   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.8320  15.5020  -9.7950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0451 T22:   0.0207                                     
REMARK   3      T33:   0.0285 T12:   0.0169                                     
REMARK   3      T13:  -0.0076 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2479 L22:   2.0904                                     
REMARK   3      L33:   3.3265 L12:  -1.4578                                     
REMARK   3      L13:  -0.1825 L23:   0.5776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0664 S12:  -0.0052 S13:   0.0465                       
REMARK   3      S21:  -0.0101 S22:  -0.0552 S23:   0.1065                       
REMARK   3      S31:  -0.2014 S32:   0.0214 S33:   0.1217                       
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      : RESIDUAL ONLY                                       
REMARK   4                                                                      
REMARK   4 3UA6 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 RCSB068499.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER MICROFOCUS (MONTEL OPTICS)  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11459                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.998                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 2.490                              
REMARK 200  R MERGE                    (I) : 0.02740                            
REMARK 200  R SYM                      (I) : 0.02740                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 0.87                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15110                            
REMARK 200  R SYM FOR SHELL            (I) : 0.15110                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.780                              
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   (%): 50.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.5 M SODIUM FORMATE, 0.1 M MES, PH      
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.14650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.53700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.14650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.53700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 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 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     GLY A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLY A    83                                                      
REMARK 465     VAL A    84                                                      
REMARK 465     ASP A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     MET B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     SER B   143                                                      
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    SER B 114       65.92   -110.26                                   
REMARK 500    SER B 115      -96.56   -107.53                                   
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                              NA A 146  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 138   O                                                      
REMARK 620 2 HOH A  14   O   168.4                                              
REMARK 620 3 HOH A  17   O    91.1  94.0                                        
REMARK 620 4 HOH B  41   O    87.8 102.4  91.8                                  
REMARK 620 5 SER A 135   O    85.9  83.0 132.5 135.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 147  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 100   O                                                      
REMARK 620 2 HOH A  40   O    90.4                                              
REMARK 620 3 THR A  97   O    90.4 127.3                                        
REMARK 620 4 HOH A  21   O    98.9  79.3 151.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B   2  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B  44   O                                                      
REMARK 620 2 SER B 135   O   137.5                                              
REMARK 620 3 HOH B   5   O   104.1 114.6                                        
REMARK 620 4 VAL B 138   O    82.4  90.4  75.7                                  
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 GOL A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 144                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 145                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 146                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 147                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 149                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SHF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UA7   RELATED DB: PDB                                   
DBREF  3UA6 A   81   143  UNP    P06241   FYN_HUMAN       81    143             
DBREF  3UA6 B   81   143  UNP    P06241   FYN_HUMAN       81    143             
SEQADV 3UA6 MET A   80  UNP  P06241              INITIATING METHIONINE          
SEQADV 3UA6 MET B   80  UNP  P06241              INITIATING METHIONINE          
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              
HET    GOL  A   1       6                                                       
HET    GOL  A   2       6                                                       
HET    FMT  A 144       3                                                       
HET    FMT  A 145       3                                                       
HET    FMT  A   3       3                                                       
HET     NA  A 146       1                                                       
HET     NA  A 147       1                                                       
HET    FMT  A 148       3                                                       
HET    FMT  A 149       3                                                       
HET    FMT  B   4       3                                                       
HET     NA  B   2       1                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     FMT FORMIC ACID                                                      
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  FMT    6(C H2 O2)                                                   
FORMUL   8   NA    3(NA 1+)                                                     
FORMUL  14  HOH   *75(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  TRP A 120   O  ILE A 133           
SHEET    3   A 5 LYS A 108  ASN A 113 -1  N  LEU A 112   O  GLU A 121           
SHEET    4   A 5 LEU A  86  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  GLN B 110 -1  N  GLN B 110   O  ARG B 123           
SHEET    4   B 5 LEU B  86  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           
LINK         O   VAL A 138                NA    NA A 146     1555   1555  2.14  
LINK         O   ASP A 100                NA    NA A 147     1555   1555  2.16  
LINK        NA    NA B   2                 O   HOH B  44     1555   1555  2.20  
LINK         O   SER B 135                NA    NA B   2     1555   1555  2.29  
LINK        NA    NA A 146                 O   HOH A  14     1555   1555  2.32  
LINK        NA    NA A 147                 O   HOH A  40     1555   1555  2.33  
LINK        NA    NA A 146                 O   HOH A  17     1555   1555  2.36  
LINK        NA    NA A 146                 O   HOH B  41     1555   1555  2.44  
LINK        NA    NA B   2                 O   HOH B   5     1555   1555  2.46  
LINK         O   VAL B 138                NA    NA B   2     1555   1555  2.52  
LINK         O   THR A  97                NA    NA A 147     1555   1555  2.62  
LINK        NA    NA A 147                 O   HOH A  21     1555   1555  2.66  
LINK         O   SER A 135                NA    NA A 146     1555   1555  2.75  
CISPEP   1 GLU B  116    GLY B  117          0        -1.62                     
SITE     1 AC1  4 HOH A  43  ASN A 136  FMT A 148  GLY B  83                    
SITE     1 AC2  7 GLU A 107  LYS A 108  THR A 126  ASP B 118                    
SITE     2 AC2  7 PRO B 134  SER B 135  ASN B 136                               
SITE     1 AC3  3 TYR A  91  ASP A  92  HIS B 104                               
SITE     1 AC4  3 FMT A   3  VAL A  88  PRO A 140                               
SITE     1 AC5  7 HOH A   8  ALA A  89  LEU A  90  LYS A 105                    
SITE     2 AC5  7 FMT A 145  HIS B 104  LYS B 105                               
SITE     1 AC6  6 HOH A  49  ASP B  92  TYR B  93  GLU B  94                    
SITE     2 AC6  6 ARG B  96  TYR B 137                                          
SITE     1 AC7  5 HOH A  14  HOH A  17  SER A 135  VAL A 138                    
SITE     2 AC7  5 HOH B  41                                                     
SITE     1 AC8  4 HOH B   5  HOH B  44  SER B 135  VAL B 138                    
SITE     1 AC9  5 HOH A  21  HOH A  40  ALA A  95  THR A  97                    
SITE     2 AC9  5 ASP A 100                                                     
SITE     1 BC1  4 GOL A   1  ARG A  96  THR B  85  GLN B 110                    
SITE     1 BC2  4 LYS A 105  GLY A 106  HOH B   5  ASN B 136                    
CRYST1   72.293   47.074   42.467  90.00  98.52  90.00 C 1 2 1       8          
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      0.013833  0.000000  0.002072        0.00000                         
SCALE2      0.000000  0.021243  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023810        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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