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Database: PDB
Entry: 2DQ7
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Original site: 2DQ7 
HEADER    TRANSFERASE                             23-MAY-06   2DQ7              
TITLE     CRYSTAL STRUCTURE OF FYN KINASE DOMAIN COMPLEXED WITH STAUROSPORINE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FYN;                
COMPND   3 CHAIN: X;                                                            
COMPND   4 FRAGMENT: FYN, PROTEIN KINASE;                                       
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    SRC FAMILY, KINASE DOMAIN, STAUROSPORINE, TRANSFERASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KINOSHITA,T.TADA                                                    
REVDAT   4   22-APR-15 2DQ7    1       DBREF  VERSN                             
REVDAT   3   24-FEB-09 2DQ7    1       VERSN                                    
REVDAT   2   11-JUL-06 2DQ7    1       JRNL                                     
REVDAT   1   04-JUL-06 2DQ7    0                                                
JRNL        AUTH   T.KINOSHITA,M.MATSUBARA,H.ISHIGURO,K.OKITA,T.TADA            
JRNL        TITL   STRUCTURE OF HUMAN FYN KINASE DOMAIN COMPLEXED WITH          
JRNL        TITL 2 STAUROSPORINE.                                               
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 346   840 2006              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   16782058                                                     
JRNL        DOI    10.1016/J.BBRC.2006.05.212                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 8817                           
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) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 464                             
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            : 2121                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 2DQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025712.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-06                          
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9281                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1QPC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.15M AMMONIUM SULFATE, 0.2M NACL,       
REMARK 280  0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      140.65933            
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       70.32967            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.32967            
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      140.65933            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 X1019  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH X 989  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     PHE X   264                                                      
REMARK 465     THR X   265                                                      
REMARK 465     ALA X   266                                                      
REMARK 465     THR X   267                                                      
REMARK 465     GLU X   268                                                      
REMARK 465     PRO X   269                                                      
REMARK 465     GLN X   270                                                      
REMARK 465     TYR X   271                                                      
REMARK 465     GLN X   272                                                      
REMARK 465     PRO X   273                                                      
REMARK 465     GLY X   274                                                      
REMARK 465     GLU X   275                                                      
REMARK 465     ASN X   276                                                      
REMARK 465     LEU X   277                                                      
REMARK 465     HIS X   278                                                      
REMARK 465     HIS X   279                                                      
REMARK 465     HIS X   280                                                      
REMARK 465     HIS X   281                                                      
REMARK 465     HIS X   282                                                      
REMARK 465     HIS X   283                                                      
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    ARG X   8       -8.36    -56.46                                   
REMARK 500    ASN X  33       -1.97   -140.94                                   
REMARK 500    PRO X  43      -71.54    -37.26                                   
REMARK 500    THR X  45      -77.61    -84.03                                   
REMARK 500    LYS X  95       22.49    -73.60                                   
REMARK 500    ASP X  96     -124.31   -136.52                                   
REMARK 500    LEU X 104      -70.56    -23.18                                   
REMARK 500    ASP X 130       49.96   -152.08                                   
REMARK 500    ARG X 132      159.88    174.65                                   
REMARK 500    ASP X 148       82.83     69.46                                   
REMARK 500    PHE X 149       30.24    -98.97                                   
REMARK 500    GLU X 156     -106.88    -71.10                                   
REMARK 500    ASN X 158      -14.15    177.50                                   
REMARK 500    ALA X 162      170.32    -52.41                                   
REMARK 500    ARG X 163        4.56    -60.65                                   
REMARK 500    ALA X 166      139.33    -39.85                                   
REMARK 500    PRO X 169       79.81    -55.65                                   
REMARK 500    PRO X 208      -84.92    -23.45                                   
REMARK 500    ASN X 212      -31.86    -37.07                                   
REMARK 500    ARG X 221       -5.75    -55.08                                   
REMARK 500    ASP X 230       43.28     29.38                                   
REMARK 500    PRO X 232      150.64    -47.03                                   
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 X 905        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH X 924        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH X 950        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH X 955        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH X 958        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH X 959        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH X 960        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH X 963        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH X 970        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH X 972        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH X 981        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH X 987        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH X 989        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH X 990        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH X1003        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH X1004        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH X1005        DISTANCE =  7.56 ANGSTROMS                       
REMARK 525    HOH X1007        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH X1009        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH X1012        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH X1013        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH X1014        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH X1015        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH X1019        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH X1023        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH X1024        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH X1027        DISTANCE =  9.06 ANGSTROMS                       
REMARK 525    HOH X1029        DISTANCE =  6.76 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STU X 902                 
DBREF  2DQ7 X    1   277  UNP    P06241   FYN_HUMAN      261    537             
SEQADV 2DQ7 HIS X  278  UNP  P06241              EXPRESSION TAG                 
SEQADV 2DQ7 HIS X  279  UNP  P06241              EXPRESSION TAG                 
SEQADV 2DQ7 HIS X  280  UNP  P06241              EXPRESSION TAG                 
SEQADV 2DQ7 HIS X  281  UNP  P06241              EXPRESSION TAG                 
SEQADV 2DQ7 HIS X  282  UNP  P06241              EXPRESSION TAG                 
SEQADV 2DQ7 HIS X  283  UNP  P06241              EXPRESSION TAG                 
SEQRES   1 X  283  LYS ASP VAL TRP GLU ILE PRO ARG GLU SER LEU GLN LEU          
SEQRES   2 X  283  ILE LYS ARG LEU GLY ASN GLY GLN PHE GLY GLU VAL TRP          
SEQRES   3 X  283  MET GLY THR TRP ASN GLY ASN THR LYS VAL ALA ILE LYS          
SEQRES   4 X  283  THR LEU LYS PRO GLY THR MET SER PRO GLU SER PHE LEU          
SEQRES   5 X  283  GLU GLU ALA GLN ILE MET LYS LYS LEU LYS HIS ASP LYS          
SEQRES   6 X  283  LEU VAL GLN LEU TYR ALA VAL VAL SER GLU GLU PRO ILE          
SEQRES   7 X  283  TYR ILE VAL THR GLU TYR MET ASN LYS GLY SER LEU LEU          
SEQRES   8 X  283  ASP PHE LEU LYS ASP GLY GLU GLY ARG ALA LEU LYS LEU          
SEQRES   9 X  283  PRO ASN LEU VAL ASP MET ALA ALA GLN VAL ALA ALA GLY          
SEQRES  10 X  283  MET ALA TYR ILE GLU ARG MET ASN TYR ILE HIS ARG ASP          
SEQRES  11 X  283  LEU ARG SER ALA ASN ILE LEU VAL GLY ASN GLY LEU ILE          
SEQRES  12 X  283  CYS LYS ILE ALA ASP PHE GLY LEU ALA ARG LEU ILE GLU          
SEQRES  13 X  283  ASP ASN GLU PTR THR ALA ARG GLN GLY ALA LYS PHE PRO          
SEQRES  14 X  283  ILE LYS TRP THR ALA PRO GLU ALA ALA LEU TYR GLY ARG          
SEQRES  15 X  283  PHE THR ILE LYS SER ASP VAL TRP SER PHE GLY ILE LEU          
SEQRES  16 X  283  LEU THR GLU LEU VAL THR LYS GLY ARG VAL PRO TYR PRO          
SEQRES  17 X  283  GLY MET ASN ASN ARG GLU VAL LEU GLU GLN VAL GLU ARG          
SEQRES  18 X  283  GLY TYR ARG MET PRO CYS PRO GLN ASP CYS PRO ILE SER          
SEQRES  19 X  283  LEU HIS GLU LEU MET ILE HIS CYS TRP LYS LYS ASP PRO          
SEQRES  20 X  283  GLU GLU ARG PRO THR PHE GLU TYR LEU GLN SER PHE LEU          
SEQRES  21 X  283  GLU ASP TYR PHE THR ALA THR GLU PRO GLN TYR GLN PRO          
SEQRES  22 X  283  GLY GLU ASN LEU HIS HIS HIS HIS HIS HIS                      
MODRES 2DQ7 PTR X  160  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  X 160      16                                                       
HET    STU  X 902      35                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     STU STAUROSPORINE                                                    
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  STU    C28 H26 N4 O3                                                
FORMUL   3  HOH   *130(H2 O)                                                    
HELIX    1   1 PRO X    7  GLU X    9  5                                   3    
HELIX    2   2 SER X   47  LYS X   59  1                                  13    
HELIX    3   3 LEU X   90  LYS X   95  1                                   6    
HELIX    4   4 LYS X  103  MET X  124  1                                  22    
HELIX    5   5 ARG X  132  ALA X  134  5                                   3    
HELIX    6   6 ALA X  174  LEU X  179  1                                   6    
HELIX    7   7 THR X  184  THR X  201  1                                  18    
HELIX    8   8 ASN X  211  GLY X  222  1                                  12    
HELIX    9   9 LEU X  235  TRP X  243  1                                   9    
HELIX   10  10 ASP X  246  ARG X  250  5                                   5    
HELIX   11  11 THR X  252  ASP X  262  1                                  11    
SHEET    1   A 5 LEU X  11  GLY X  18  0                                        
SHEET    2   A 5 VAL X  25  TRP X  30 -1  O  MET X  27   N  ILE X  14           
SHEET    3   A 5 THR X  34  LYS X  39 -1  O  ILE X  38   N  TRP X  26           
SHEET    4   A 5 TYR X  79  GLU X  83 -1  O  THR X  82   N  ALA X  37           
SHEET    5   A 5 LEU X  69  VAL X  73 -1  N  TYR X  70   O  VAL X  81           
SHEET    1   B 3 GLY X  88  SER X  89  0                                        
SHEET    2   B 3 ILE X 136  GLY X 139 -1  O  VAL X 138   N  GLY X  88           
SHEET    3   B 3 ILE X 143  ILE X 146 -1  O  LYS X 145   N  LEU X 137           
SHEET    1   C 2 TYR X 126  ILE X 127  0                                        
SHEET    2   C 2 ARG X 153  LEU X 154 -1  O  ARG X 153   N  ILE X 127           
SHEET    1   D 2 PTR X 160  THR X 161  0                                        
SHEET    2   D 2 ARG X 182  PHE X 183 -1  O  PHE X 183   N  PTR X 160           
LINK         C   GLU X 159                 N   PTR X 160     1555   1555  1.33  
LINK         C   PTR X 160                 N   THR X 161     1555   1555  1.33  
CISPEP   1 GLU X   76    PRO X   77          0        -0.34                     
SITE     1 AC1 12 LEU X  17  ASN X  19  ALA X  37  LYS X  39                    
SITE     2 AC1 12 THR X  82  GLU X  83  TYR X  84  MET X  85                    
SITE     3 AC1 12 GLY X  88  ALA X 134  LEU X 137  ASP X 148                    
CRYST1   52.962   52.962  210.989  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018881  0.010901  0.000000        0.00000                         
SCALE2      0.000000  0.021802  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004740        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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