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Database: PDB
Entry: 3D4Q
LinkDB: 3D4Q
Original site: 3D4Q 
HEADER    TRANSFERASE                             14-MAY-08   3D4Q              
TITLE     PYRAZOLE-BASED INHIBITORS OF B-RAF KINASE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: B-RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE;      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 432-726;                                          
COMPND   5 SYNONYM: P94, V-RAF MURINE SARCOMA VIRAL ONCOGENE HOMOLOG B1;        
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 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: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HI-5;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, ATP-BINDING, CARDIOMYOPATHY, DISEASE MUTATION, METAL-BINDING, 
KEYWDS   2 NUCLEOTIDE-BINDING, PHORBOL-ESTER BINDING, PHOSPHOPROTEIN, PROTO-    
KEYWDS   3 ONCOGENE, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, ZINC-FINGER  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MORALES,G.P.A.VIGERS,B.J.BRANDHUBER                                 
REVDAT   4   24-JAN-18 3D4Q    1       AUTHOR                                   
REVDAT   3   08-SEP-10 3D4Q    1       SOURCE                                   
REVDAT   2   24-FEB-09 3D4Q    1       VERSN                                    
REVDAT   1   19-AUG-08 3D4Q    0                                                
JRNL        AUTH   J.D.HANSEN,J.GRINA,B.NEWHOUSE,M.WELCH,G.TOPALOV,N.LITTMAN,   
JRNL        AUTH 2 M.CALLEJO,S.GLOOR,M.MARTINSON,E.LAIRD,B.J.BRANDHUBER,        
JRNL        AUTH 3 G.VIGERS,T.MORALES,R.WOESSNER,N.RANDOLPH,J.LYSSIKATOS,       
JRNL        AUTH 4 A.OLIVERO                                                    
JRNL        TITL   POTENT AND SELECTIVE PYRAZOLE-BASED INHIBITORS OF B-RAF      
JRNL        TITL 2 KINASE.                                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  4692 2008              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   18676143                                                     
JRNL        DOI    10.1016/J.BMCL.2008.07.002                                   
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) : 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)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20642                          
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) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1002                            
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            : 4214                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18900                                             
REMARK   3    B22 (A**2) : -0.18900                                             
REMARK   3    B33 (A**2) : 0.37800                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED 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) : 0.020                           
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : AR00384000.PAR                                 
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047589.                                   
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                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20661                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.07400                            
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 3350 0.1M TRIS 10% TACSIMATE,     
REMARK 280  PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.26800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.17150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.17150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.63400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.17150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.17150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.90200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.17150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.17150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.63400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.17150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.17150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      121.90200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       81.26800            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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   420                                                      
REMARK 465     ASP A   421                                                      
REMARK 465     ARG A   422                                                      
REMARK 465     GLY A   423                                                      
REMARK 465     SER A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     HIS A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     ASP A   434                                                      
REMARK 465     ARG A   435                                                      
REMARK 465     ASN A   436                                                      
REMARK 465     ARG A   437                                                      
REMARK 465     MET A   438                                                      
REMARK 465     LYS A   439                                                      
REMARK 465     THR A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     ARG A   443                                                      
REMARK 465     ARG A   444                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     SER A   447                                                      
REMARK 465     LYS A   601                                                      
REMARK 465     SER A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     TRP A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 465     GLN A   609                                                      
REMARK 465     PHE A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     GLN A   612                                                      
REMARK 465     ILE A   724                                                      
REMARK 465     HIS A   725                                                      
REMARK 465     ARG A   726                                                      
REMARK 465     MET B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     ARG B   422                                                      
REMARK 465     GLY B   423                                                      
REMARK 465     SER B   424                                                      
REMARK 465     HIS B   425                                                      
REMARK 465     HIS B   426                                                      
REMARK 465     HIS B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     HIS B   429                                                      
REMARK 465     HIS B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     SER B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     ASP B   434                                                      
REMARK 465     ARG B   435                                                      
REMARK 465     ASN B   436                                                      
REMARK 465     ARG B   437                                                      
REMARK 465     MET B   438                                                      
REMARK 465     LYS B   439                                                      
REMARK 465     THR B   440                                                      
REMARK 465     LEU B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     ARG B   443                                                      
REMARK 465     ARG B   444                                                      
REMARK 465     ASP B   445                                                      
REMARK 465     SER B   446                                                      
REMARK 465     SER B   447                                                      
REMARK 465     LYS B   601                                                      
REMARK 465     SER B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     TRP B   604                                                      
REMARK 465     SER B   605                                                      
REMARK 465     GLY B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     HIS B   608                                                      
REMARK 465     GLN B   609                                                      
REMARK 465     PHE B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     GLN B   612                                                      
REMARK 465     ILE B   724                                                      
REMARK 465     HIS B   725                                                      
REMARK 465     ARG B   726                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   501     O28  SM5 A     1              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO A 523   C   -  N   -  CA  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    PRO B 523   C   -  N   -  CA  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    PRO B 632   C   -  N   -  CA  ANGL. DEV. =   9.3 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    ASP A 449      160.31    -43.33                                   
REMARK 500    THR A 488      -29.24     61.85                                   
REMARK 500    ALA A 489      132.11    137.11                                   
REMARK 500    THR A 491      156.43    -45.62                                   
REMARK 500    LEU A 514      130.06    -36.16                                   
REMARK 500    GLN A 530      156.02    -49.12                                   
REMARK 500    ASP A 576       33.96   -155.27                                   
REMARK 500    LYS A 578      163.71    178.49                                   
REMARK 500    GLU A 586       23.31     48.90                                   
REMARK 500    ASP A 587       -4.02     59.92                                   
REMARK 500    ASP A 594       95.94     67.73                                   
REMARK 500    SER A 614      137.47   -176.28                                   
REMARK 500    SER A 616      -69.99    -92.13                                   
REMARK 500    ILE A 617      -39.44     81.10                                   
REMARK 500    MET A 627       81.23    -43.35                                   
REMARK 500    ASP A 629     -158.72   -153.82                                   
REMARK 500    TYR A 656       31.92     73.45                                   
REMARK 500    PRO A 722       -6.23    -55.60                                   
REMARK 500    ASP B 449      164.86    -40.55                                   
REMARK 500    GLN B 461      125.63    -36.56                                   
REMARK 500    THR B 488      -32.53     61.73                                   
REMARK 500    ALA B 489      133.89    142.37                                   
REMARK 500    THR B 491      157.29    -48.18                                   
REMARK 500    HIS B 510      131.18   -171.48                                   
REMARK 500    GLN B 530      154.70    -49.95                                   
REMARK 500    ASP B 576       33.86   -152.40                                   
REMARK 500    LYS B 578      159.70    176.42                                   
REMARK 500    ASP B 587       -5.45     60.20                                   
REMARK 500    ASP B 594       97.83     64.55                                   
REMARK 500    SER B 614      137.66   -176.80                                   
REMARK 500    SER B 616      -67.47    -95.43                                   
REMARK 500    ILE B 617      -41.16     80.91                                   
REMARK 500    MET B 627       83.62    -43.40                                   
REMARK 500    ASP B 629     -158.31   -155.21                                   
REMARK 500    PRO B 722       -6.54    -56.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  485     ASN A  486                 -142.46                    
REMARK 500 ASN A  486     VAL A  487                  133.98                    
REMARK 500 LEU B  485     ASN B  486                 -139.78                    
REMARK 500 ASN B  486     VAL B  487                  134.31                    
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 SM5 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM5 B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PSB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PSD   RELATED DB: PDB                                   
DBREF  3D4Q A  433   726  UNP    P15056   BRAF1_HUMAN    433    726             
DBREF  3D4Q B  433   726  UNP    P15056   BRAF1_HUMAN    433    726             
SEQADV 3D4Q MET A  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q ASP A  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q ARG A  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q GLY A  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q SER A  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS A  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q GLY A  431  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q SER A  432  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q MET B  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q ASP B  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q ARG B  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q GLY B  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q SER B  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q HIS B  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q GLY B  431  UNP  P15056              EXPRESSION TAG                 
SEQADV 3D4Q SER B  432  UNP  P15056              EXPRESSION TAG                 
SEQRES   1 A  307  MET ASP ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER          
SEQRES   2 A  307  GLU ASP ARG ASN ARG MET LYS THR LEU GLY ARG ARG ASP          
SEQRES   3 A  307  SER SER ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR          
SEQRES   4 A  307  VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL          
SEQRES   5 A  307  TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET          
SEQRES   6 A  307  LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA          
SEQRES   7 A  307  PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS          
SEQRES   8 A  307  VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO          
SEQRES   9 A  307  GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER          
SEQRES  10 A  307  LEU TYR HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU          
SEQRES  11 A  307  MET ILE LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN          
SEQRES  12 A  307  GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG          
SEQRES  13 A  307  ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU          
SEQRES  14 A  307  THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS          
SEQRES  15 A  307  SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER          
SEQRES  16 A  307  GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET          
SEQRES  17 A  307  GLN ASP LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR          
SEQRES  18 A  307  ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN          
SEQRES  19 A  307  LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE          
SEQRES  20 A  307  PHE MET VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER          
SEQRES  21 A  307  LYS VAL ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU          
SEQRES  22 A  307  MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO          
SEQRES  23 A  307  LEU PHE PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA          
SEQRES  24 A  307  ARG SER LEU PRO LYS ILE HIS ARG                              
SEQRES   1 B  307  MET ASP ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER          
SEQRES   2 B  307  GLU ASP ARG ASN ARG MET LYS THR LEU GLY ARG ARG ASP          
SEQRES   3 B  307  SER SER ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR          
SEQRES   4 B  307  VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL          
SEQRES   5 B  307  TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET          
SEQRES   6 B  307  LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA          
SEQRES   7 B  307  PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS          
SEQRES   8 B  307  VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO          
SEQRES   9 B  307  GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER          
SEQRES  10 B  307  LEU TYR HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU          
SEQRES  11 B  307  MET ILE LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN          
SEQRES  12 B  307  GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG          
SEQRES  13 B  307  ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU          
SEQRES  14 B  307  THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS          
SEQRES  15 B  307  SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER          
SEQRES  16 B  307  GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET          
SEQRES  17 B  307  GLN ASP LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR          
SEQRES  18 B  307  ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN          
SEQRES  19 B  307  LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE          
SEQRES  20 B  307  PHE MET VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER          
SEQRES  21 B  307  LYS VAL ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU          
SEQRES  22 B  307  MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO          
SEQRES  23 B  307  LEU PHE PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA          
SEQRES  24 B  307  ARG SER LEU PRO LYS ILE HIS ARG                              
HET    SM5  A   1      28                                                       
HET    SM5  B   1      28                                                       
HETNAM     SM5 (1E)-5-(1-PIPERIDIN-4-YL-3-PYRIDIN-4-YL-1H-PYRAZOL-4-            
HETNAM   2 SM5  YL)-2,3-DIHYDRO-1H-INDEN-1-ONE OXIME                            
FORMUL   3  SM5    2(C22 H23 N5 O)                                              
FORMUL   5  HOH   *23(H2 O)                                                     
HELIX    1   1 THR A  491  ARG A  506  1                                  16    
HELIX    2   2 SER A  536  ILE A  543  1                                   8    
HELIX    3   3 GLU A  549  LYS A  570  1                                  22    
HELIX    4   4 GLU A  586  LEU A  588  5                                   3    
HELIX    5   5 ALA A  621  ARG A  626  1                                   6    
HELIX    6   6 SER A  634  GLY A  652  1                                  19    
HELIX    7   7 ASN A  661  ARG A  671  1                                  11    
HELIX    8   8 ASP A  677  VAL A  681  5                                   5    
HELIX    9   9 PRO A  686  LEU A  697  1                                  12    
HELIX   10  10 LYS A  700  ARG A  704  5                                   5    
HELIX   11  11 LEU A  706  SER A  720  1                                  15    
HELIX   12  12 THR B  491  ARG B  506  1                                  16    
HELIX   13  13 SER B  536  ILE B  543  1                                   8    
HELIX   14  14 GLU B  549  LYS B  570  1                                  22    
HELIX   15  15 GLU B  586  LEU B  588  5                                   3    
HELIX   16  16 ALA B  621  ARG B  626  1                                   6    
HELIX   17  17 SER B  634  GLY B  652  1                                  19    
HELIX   18  18 ASN B  661  GLY B  672  1                                  12    
HELIX   19  19 ASP B  677  VAL B  681  5                                   5    
HELIX   20  20 PRO B  686  LEU B  697  1                                  12    
HELIX   21  21 LYS B  700  ARG B  704  5                                   5    
HELIX   22  22 LEU B  706  SER B  720  1                                  15    
SHEET    1   A 5 THR A 458  GLY A 466  0                                        
SHEET    2   A 5 GLY A 469  LYS A 475 -1  O  VAL A 471   N  GLY A 464           
SHEET    3   A 5 ASP A 479  MET A 484 -1  O  VAL A 482   N  TYR A 472           
SHEET    4   A 5 ALA A 526  GLN A 530 -1  O  ILE A 527   N  LYS A 483           
SHEET    5   A 5 PHE A 516  SER A 520 -1  N  MET A 517   O  VAL A 528           
SHEET    1   B 2 ILE A 582  HIS A 585  0                                        
SHEET    2   B 2 THR A 589  ILE A 592 -1  O  LYS A 591   N  PHE A 583           
SHEET    1   C 5 THR B 458  GLY B 466  0                                        
SHEET    2   C 5 GLY B 469  LYS B 475 -1  O  VAL B 471   N  GLY B 464           
SHEET    3   C 5 ASP B 479  MET B 484 -1  O  VAL B 482   N  TYR B 472           
SHEET    4   C 5 ALA B 526  GLN B 530 -1  O  ILE B 527   N  LYS B 483           
SHEET    5   C 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
SHEET    1   D 2 ILE B 582  HIS B 585  0                                        
SHEET    2   D 2 THR B 589  ILE B 592 -1  O  LYS B 591   N  PHE B 583           
SITE     1 AC1 11 ILE A 463  GLY A 464  SER A 465  ALA A 481                    
SITE     2 AC1 11 LYS A 483  GLU A 501  TRP A 531  CYS A 532                    
SITE     3 AC1 11 PHE A 583  ASP A 594  TYR B 673                               
SITE     1 AC2 11 ILE B 463  GLY B 464  SER B 465  ALA B 481                    
SITE     2 AC2 11 LYS B 483  GLU B 501  GLN B 530  TRP B 531                    
SITE     3 AC2 11 CYS B 532  PHE B 583  ASP B 594                               
CRYST1  100.343  100.343  162.536  90.00  90.00  90.00 P 41 21 2    16          
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      0.009966  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009966  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006152        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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