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Database: PDB
Entry: 2OFV
LinkDB: 2OFV
Original site: 2OFV 
HEADER    TRANSFERASE                             04-JAN-07   2OFV              
TITLE     CRYSTAL STRUCTURE OF AMINOQUINAZOLINE 1 BOUND TO LCK                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LCK KINASE DOMAIN, RESIDUES 231-497;                       
COMPND   5 SYNONYM: P56-LCK, LYMPHOCYTE CELL-SPECIFIC PROTEIN-                  
COMPND   6 TYROSINE KINASE, LSK, T CELL- SPECIFIC PROTEIN-TYROSINE              
COMPND   7 KINASE;                                                              
COMPND   8 EC: 2.7.10.2;                                                        
COMPND   9 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: LCK;                                                           
SOURCE   6 EXPRESSION_SYSTEM: INSECT CELL;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    LCK, KINASE DOMAIN, TRANSFERASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.HUANG                                                               
REVDAT   2   24-FEB-09 2OFV    1       VERSN                                    
REVDAT   1   27-FEB-07 2OFV    0                                                
JRNL        AUTH   E.F.DIMAURO,J.NEWCOMB,J.J.NUNES,J.E.BEMIS,                   
JRNL        AUTH 2 C.BOUCHER,J.L.BUCHANAN,W.H.BUCKNER,V.J.CEE,L.CHAI,           
JRNL        AUTH 3 H.L.DEAK,L.F.EPSTEIN,T.FAUST,P.GALLANT,                      
JRNL        AUTH 4 S.D.GEUNS-MEYER,A.GORE,Y.GU,B.HENKLE,B.L.HODOUS,             
JRNL        AUTH 5 F.HSIEH,X.HUANG,J.L.KIM,J.H.LEE,M.W.MARTIN,                  
JRNL        AUTH 6 C.E.MASSE,D.C.MCGOWAN,D.METZ,D.MOHN,                         
JRNL        AUTH 7 K.A.MORGENSTERN,A.OLIVEIRA-DOS-SANTOS,V.F.PATEL,             
JRNL        AUTH 8 D.POWERS,P.E.ROSE,S.SCHNEIDER,S.A.TOMLINSON,                 
JRNL        AUTH 9 Y.-Y.TUDOR,S.M.TURCI,A.A.WELCHER,R.D.WHITE,H.ZHAO,           
JRNL        AUTH10 L.ZHU,X.ZHU                                                  
JRNL        TITL   DISCOVERY OF AMINOQUINAZOLINES AS POTENT, ORALLY             
JRNL        TITL 2 BIOAVAILABLE INHIBITORS OF LCK: SYNTHESIS, SAR,              
JRNL        TITL 3 AND IN VIVO ANTI-INFLAMMATORY ACTIVITY                       
JRNL        REF    J.MED.CHEM.                   V.  49  5671 2006              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   16970394                                                     
JRNL        DOI    10.1021/JM0605482                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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             : 41284                          
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) : 0.274                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3878                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 271                                     
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.46                            
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 2OFV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041083.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41290                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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   (%): 54.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M MGACETATE, 5-12.5% PEG8000,        
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
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       71.33000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.44500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.33000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.44500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.                        
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, 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     THR A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     SER A   279                                                      
REMARK 465     MET A   280                                                      
REMARK 465     SER A   281                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     ALA A   284                                                      
REMARK 465     PHE A   285                                                      
REMARK 465     ARG A   387                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     ILE A   389                                                      
REMARK 465     GLU A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     TYR A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     ARG A   397                                                      
REMARK 465     GLU A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     ALA A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     PHE A   402                                                      
REMARK 465     PRO A   403                                                      
REMARK 465     THR A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     THR A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     THR B   226                                                      
REMARK 465     GLN B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     GLN B   230                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     SER B   279                                                      
REMARK 465     MET B   280                                                      
REMARK 465     SER B   281                                                      
REMARK 465     PRO B   282                                                      
REMARK 465     ASP B   283                                                      
REMARK 465     ASN B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     TYR B   394                                                      
REMARK 465     THR B   395                                                      
REMARK 465     ALA B   396                                                      
REMARK 465     ARG B   397                                                      
REMARK 465     GLU B   398                                                      
REMARK 465     GLY B   399                                                      
REMARK 465     ALA B   400                                                      
REMARK 465     LYS B   401                                                      
REMARK 465     PHE B   402                                                      
REMARK 465     GLY B   443                                                      
REMARK 465     MET B   444                                                      
REMARK 465     THR B   445                                                      
REMARK 465     ASN B   446                                                      
REMARK 465     PRO B   447                                                      
REMARK 465     GLU B   448                                                      
REMARK 465     VAL B   449                                                      
REMARK 465     ARG B   455                                                      
REMARK 465     ALA B   500                                                      
REMARK 465     THR B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 231    CG   CD   CE   NZ                                   
REMARK 470     GLN A 277    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 286    CG   CD1  CD2                                       
REMARK 470     THR A 308    OG1  CG2                                            
REMARK 470     GLN A 309    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 374    CG   OD1  OD2                                       
REMARK 470     ILE A 404    CG1  CG2  CD1                                       
REMARK 470     ILE A 450    CG1  CG2  CD1                                       
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 276    CG   CD   CE   NZ                                   
REMARK 470     GLN B 277    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 285    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 298    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 309    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 335    CG   CD   CE   NZ                                   
REMARK 470     ASP B 374    CG   OD1  OD2                                       
REMARK 470     LEU B 376    CG   CD1  CD2                                       
REMARK 470     GLU B 390    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 391    CG   OD1  OD2                                       
REMARK 470     PRO B 403    CG   CD                                             
REMARK 470     ILE B 404    CG1  CG2  CD1                                       
REMARK 470     LYS B 405    CG   CD   CE   NZ                                   
REMARK 470     HIS B 436    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B 450    CG1  CG2  CD1                                       
REMARK 470     ARG B 461    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 463    CG   OD1  OD2                                       
REMARK 470     GLU B 468    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 472    CG   CD1  CD2                                       
REMARK 470     LYS B 478    CG   CD   CE   NZ                                   
REMARK 470     ARG B 491    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 499    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS B 335   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A 363      -17.57     81.39                                   
REMARK 500    ASP A 364       47.95   -141.72                                   
REMARK 500    PHE A 383       29.24   -146.70                                   
REMARK 500    LEU A 385       16.66     54.91                                   
REMARK 500    ASN A 464        2.99     80.08                                   
REMARK 500    TRP B 238        4.24   -152.54                                   
REMARK 500    THR B 330      150.74    -49.00                                   
REMARK 500    ILE B 334        7.63     55.53                                   
REMARK 500    ILE B 338      -38.22    -32.42                                   
REMARK 500    ARG B 363      -17.06     73.02                                   
REMARK 500    SER B 373     -173.73    -65.59                                   
REMARK 500    ASP B 382      105.80   -160.36                                   
REMARK 500    PHE B 383       28.72   -148.26                                   
REMARK 500    ASN B 464       -1.07    105.35                                   
REMARK 500    TRP B 477       36.17    -91.48                                   
REMARK 500    ASP B 496       38.13    -70.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 242 A 503                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 242 B 503                 
DBREF  2OFV A  226   502  UNP    P06239   LCK_HUMAN      226    502             
DBREF  2OFV B  226   502  UNP    P06239   LCK_HUMAN      226    502             
SEQADV 2OFV THR A  226  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLN A  227  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV LYS A  228  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV PRO A  229  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLN A  230  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV LYS A  231  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV THR A  499  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV ALA A  500  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV THR A  501  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLU A  502  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV THR B  226  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLN B  227  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV LYS B  228  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV PRO B  229  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLN B  230  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV LYS B  231  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV THR B  499  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV ALA B  500  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV THR B  501  UNP  P06239              CLONING ARTIFACT               
SEQADV 2OFV GLU B  502  UNP  P06239              CLONING ARTIFACT               
SEQRES   1 A  277  THR GLN LYS PRO GLN LYS PRO TRP TRP GLU ASP GLU TRP          
SEQRES   2 A  277  GLU VAL PRO ARG GLU THR LEU LYS LEU VAL GLU ARG LEU          
SEQRES   3 A  277  GLY ALA GLY GLN PHE GLY GLU VAL TRP MET GLY TYR TYR          
SEQRES   4 A  277  ASN GLY HIS THR LYS VAL ALA VAL LYS SER LEU LYS GLN          
SEQRES   5 A  277  GLY SER MET SER PRO ASP ALA PHE LEU ALA GLU ALA ASN          
SEQRES   6 A  277  LEU MET LYS GLN LEU GLN HIS GLN ARG LEU VAL ARG LEU          
SEQRES   7 A  277  TYR ALA VAL VAL THR GLN GLU PRO ILE TYR ILE ILE THR          
SEQRES   8 A  277  GLU TYR MET GLU ASN GLY SER LEU VAL ASP PHE LEU LYS          
SEQRES   9 A  277  THR PRO SER GLY ILE LYS LEU THR ILE ASN LYS LEU LEU          
SEQRES  10 A  277  ASP MET ALA ALA GLN ILE ALA GLU GLY MET ALA PHE ILE          
SEQRES  11 A  277  GLU GLU ARG ASN TYR ILE HIS ARG ASP LEU ARG ALA ALA          
SEQRES  12 A  277  ASN ILE LEU VAL SER ASP THR LEU SER CYS LYS ILE ALA          
SEQRES  13 A  277  ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR          
SEQRES  14 A  277  THR ALA ARG GLU GLY ALA LYS PHE PRO ILE LYS TRP THR          
SEQRES  15 A  277  ALA PRO GLU ALA ILE ASN TYR GLY THR PHE THR ILE LYS          
SEQRES  16 A  277  SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU ILE          
SEQRES  17 A  277  VAL THR HIS GLY ARG ILE PRO TYR PRO GLY MET THR ASN          
SEQRES  18 A  277  PRO GLU VAL ILE GLN ASN LEU GLU ARG GLY TYR ARG MET          
SEQRES  19 A  277  VAL ARG PRO ASP ASN CYS PRO GLU GLU LEU TYR GLN LEU          
SEQRES  20 A  277  MET ARG LEU CYS TRP LYS GLU ARG PRO GLU ASP ARG PRO          
SEQRES  21 A  277  THR PHE ASP TYR LEU ARG SER VAL LEU GLU ASP PHE PHE          
SEQRES  22 A  277  THR ALA THR GLU                                              
SEQRES   1 B  277  THR GLN LYS PRO GLN LYS PRO TRP TRP GLU ASP GLU TRP          
SEQRES   2 B  277  GLU VAL PRO ARG GLU THR LEU LYS LEU VAL GLU ARG LEU          
SEQRES   3 B  277  GLY ALA GLY GLN PHE GLY GLU VAL TRP MET GLY TYR TYR          
SEQRES   4 B  277  ASN GLY HIS THR LYS VAL ALA VAL LYS SER LEU LYS GLN          
SEQRES   5 B  277  GLY SER MET SER PRO ASP ALA PHE LEU ALA GLU ALA ASN          
SEQRES   6 B  277  LEU MET LYS GLN LEU GLN HIS GLN ARG LEU VAL ARG LEU          
SEQRES   7 B  277  TYR ALA VAL VAL THR GLN GLU PRO ILE TYR ILE ILE THR          
SEQRES   8 B  277  GLU TYR MET GLU ASN GLY SER LEU VAL ASP PHE LEU LYS          
SEQRES   9 B  277  THR PRO SER GLY ILE LYS LEU THR ILE ASN LYS LEU LEU          
SEQRES  10 B  277  ASP MET ALA ALA GLN ILE ALA GLU GLY MET ALA PHE ILE          
SEQRES  11 B  277  GLU GLU ARG ASN TYR ILE HIS ARG ASP LEU ARG ALA ALA          
SEQRES  12 B  277  ASN ILE LEU VAL SER ASP THR LEU SER CYS LYS ILE ALA          
SEQRES  13 B  277  ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR          
SEQRES  14 B  277  THR ALA ARG GLU GLY ALA LYS PHE PRO ILE LYS TRP THR          
SEQRES  15 B  277  ALA PRO GLU ALA ILE ASN TYR GLY THR PHE THR ILE LYS          
SEQRES  16 B  277  SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU ILE          
SEQRES  17 B  277  VAL THR HIS GLY ARG ILE PRO TYR PRO GLY MET THR ASN          
SEQRES  18 B  277  PRO GLU VAL ILE GLN ASN LEU GLU ARG GLY TYR ARG MET          
SEQRES  19 B  277  VAL ARG PRO ASP ASN CYS PRO GLU GLU LEU TYR GLN LEU          
SEQRES  20 B  277  MET ARG LEU CYS TRP LYS GLU ARG PRO GLU ASP ARG PRO          
SEQRES  21 B  277  THR PHE ASP TYR LEU ARG SER VAL LEU GLU ASP PHE PHE          
SEQRES  22 B  277  THR ALA THR GLU                                              
HET    242  A 503      31                                                       
HET    242  B 503      31                                                       
HETNAM     242 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-N-[3-                        
HETNAM   2 242  (TRIFLUOROMETHYL)PHENYL]BENZAMIDE                               
HETSYN     242 AMINOQUINAZOLINE 1                                               
FORMUL   3  242    2(C23 H17 F3 N4 O)                                           
FORMUL   5  HOH   *271(H2 O)                                                    
HELIX    1   1 PRO A  241  GLU A  243  5                                   3    
HELIX    2   2 LEU A  286  LEU A  295  1                                  10    
HELIX    3   3 SER A  323  LYS A  329  1                                   7    
HELIX    4   4 THR A  330  LYS A  335  1                                   6    
HELIX    5   5 THR A  337  ARG A  358  1                                  22    
HELIX    6   6 ARG A  366  ALA A  368  5                                   3    
HELIX    7   7 ALA A  408  GLY A  415  1                                   8    
HELIX    8   8 THR A  418  THR A  435  1                                  18    
HELIX    9   9 THR A  445  GLU A  454  1                                  10    
HELIX   10  10 PRO A  466  TRP A  477  1                                  12    
HELIX   11  11 ARG A  480  ARG A  484  5                                   5    
HELIX   12  12 THR A  486  ASP A  496  1                                  11    
HELIX   13  13 PRO B  241  GLU B  243  5                                   3    
HELIX   14  14 PHE B  285  LEU B  295  1                                  11    
HELIX   15  15 SER B  323  LEU B  328  1                                   6    
HELIX   16  16 THR B  337  ARG B  358  1                                  22    
HELIX   17  17 ARG B  366  ALA B  368  5                                   3    
HELIX   18  18 PRO B  403  THR B  407  5                                   5    
HELIX   19  19 ALA B  408  GLY B  415  1                                   8    
HELIX   20  20 THR B  418  VAL B  434  1                                  17    
HELIX   21  21 PRO B  466  TRP B  477  1                                  12    
HELIX   22  22 ARG B  480  ARG B  484  5                                   5    
HELIX   23  23 THR B  486  ASP B  496  1                                  11    
SHEET    1   A 5 LEU A 245  GLY A 254  0                                        
SHEET    2   A 5 GLY A 257  TYR A 264 -1  O  VAL A 259   N  LEU A 251           
SHEET    3   A 5 THR A 268  LEU A 275 -1  O  VAL A 272   N  TRP A 260           
SHEET    4   A 5 ILE A 312  THR A 316 -1  O  ILE A 312   N  LEU A 275           
SHEET    5   A 5 LEU A 303  VAL A 307 -1  N  TYR A 304   O  ILE A 315           
SHEET    1   B 2 ILE A 370  VAL A 372  0                                        
SHEET    2   B 2 CYS A 378  ILE A 380 -1  O  LYS A 379   N  LEU A 371           
SHEET    1   C 5 LEU B 245  GLY B 254  0                                        
SHEET    2   C 5 GLY B 257  TYR B 264 -1  O  VAL B 259   N  LEU B 251           
SHEET    3   C 5 THR B 268  LEU B 275 -1  O  VAL B 272   N  TRP B 260           
SHEET    4   C 5 ILE B 312  THR B 316 -1  O  ILE B 314   N  LYS B 273           
SHEET    5   C 5 LEU B 303  VAL B 307 -1  N  ALA B 305   O  ILE B 315           
SHEET    1   D 2 ILE B 370  VAL B 372  0                                        
SHEET    2   D 2 CYS B 378  ILE B 380 -1  O  LYS B 379   N  LEU B 371           
CISPEP   1 GLU A  310    PRO A  311          0        -0.92                     
CISPEP   2 GLU B  310    PRO B  311          0         0.31                     
SITE     1 AC1 20 VAL A 259  ALA A 271  VAL A 272  LYS A 273                    
SITE     2 AC1 20 GLU A 288  MET A 292  LEU A 295  LEU A 300                    
SITE     3 AC1 20 VAL A 301  ILE A 314  THR A 316  GLU A 317                    
SITE     4 AC1 20 TYR A 318  MET A 319  HIS A 362  ILE A 380                    
SITE     5 AC1 20 ALA A 381  ASP A 382  PHE A 383  HOH A 630                    
SITE     1 AC2 21 VAL B 259  ALA B 271  LYS B 273  GLU B 288                    
SITE     2 AC2 21 MET B 292  LEU B 300  VAL B 301  ILE B 314                    
SITE     3 AC2 21 THR B 316  GLU B 317  TYR B 318  MET B 319                    
SITE     4 AC2 21 GLY B 322  TYR B 360  LEU B 371  ILE B 380                    
SITE     5 AC2 21 ALA B 381  ASP B 382  PHE B 383  ILE B 389                    
SITE     6 AC2 21 HOH B 518                                                     
CRYST1  142.660   66.890   78.510  90.00 112.00  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      0.007010  0.000000  0.002832        0.00000                         
SCALE2      0.000000  0.014950  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013738        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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