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Database: PDB
Entry: 3SKC
LinkDB: 3SKC
Original site: 3SKC 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       22-JUN-11   3SKC              
TITLE     HUMAN B-RAF KINASE IN COMPLEX WITH AN AMIDE LINKED PYRAZOLOPYRIDINE   
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HUMAN B-RAF KINASE UNP RESIDUES 432-726;                   
COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL       
COMPND   6 ONCOGENE HOMOLOG B1;                                                 
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI5                                        
KEYWDS    KINASE, ATP-COMPETITIVE INHIBITOR, TRANSFERASE, RAS, MEK, C-RAF,      
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.C.VOEGTLI,H.L.STURGIS                                               
REVDAT   2   14-DEC-11 3SKC    1       JRNL                                     
REVDAT   1   17-AUG-11 3SKC    0                                                
JRNL        AUTH   S.WENGLOWSKY,K.A.AHRENDT,A.J.BUCKMELTER,B.FENG,S.L.GLOOR,    
JRNL        AUTH 2 S.GRADL,J.GRINA,J.D.HANSEN,E.R.LAIRD,P.LUNGHOFER,S.MATHIEU,  
JRNL        AUTH 3 D.MORENO,B.NEWHOUSE,L.REN,T.RISOM,J.RUDOLPH,J.SEO,           
JRNL        AUTH 4 H.L.STURGIS,W.C.VOEGTLI,Z.WEN                                
JRNL        TITL   PYRAZOLOPYRIDINE INHIBITORS OF B-RAFV600E. PART 2:           
JRNL        TITL 2 STRUCTURE-ACTIVITY RELATIONSHIPS.                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  5533 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21802293                                                     
JRNL        DOI    10.1016/J.BMCL.2011.06.097                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2005                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2139817.240                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15245                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 905                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2390               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2360               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.274                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.900                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 905                  
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0090               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 15245                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2318                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3180                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 143                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4291                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.24000                                             
REMARK   3    B22 (A**2) : -3.24000                                             
REMARK   3    B33 (A**2) : 6.49000                                              
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) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.470 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.680 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.550 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.650 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 24.74                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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.PARA                               
REMARK   3  PARAMETER FILE  2  : AR00461060.PAR                                 
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : AR00461060.TOP                                 
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3SKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066308.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC CONFOCAL                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15245                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.86000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, 100 MM TRIS PH 9.0, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       75.73500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       53.95000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       53.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.86750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       53.95000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       53.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      113.60250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       53.95000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.95000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.86750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       53.95000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.95000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      113.60250            
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       75.73500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     LEU A   597                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     VAL A   600                                                      
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     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                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG B   662     NH2  ARG B   662     7645     2.17            
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      145.36    -34.26                                   
REMARK 500    ASP A 454      153.98    -46.36                                   
REMARK 500    ILE A 463      -45.24   -135.57                                   
REMARK 500    SER A 465     -167.47   -109.88                                   
REMARK 500    PHE A 468        7.27     40.83                                   
REMARK 500    ASN A 486       65.31     27.74                                   
REMARK 500    THR A 488       51.39     36.92                                   
REMARK 500    ALA A 489       99.69     63.01                                   
REMARK 500    THR A 491       40.70     90.48                                   
REMARK 500    GLN A 493       66.41   -101.36                                   
REMARK 500    ARG A 509       88.96   -151.96                                   
REMARK 500    LYS A 522      -86.18    -54.85                                   
REMARK 500    GLN A 530      150.99    -44.59                                   
REMARK 500    ASP A 576       41.25   -161.15                                   
REMARK 500    LYS A 578      166.62    172.84                                   
REMARK 500    ASP A 587       16.94     52.95                                   
REMARK 500    ASP A 594       74.85     94.82                                   
REMARK 500    PHE A 595     -134.09    -82.48                                   
REMARK 500    SER A 614      -26.66   -166.13                                   
REMARK 500    SER A 616       40.44   -157.77                                   
REMARK 500    MET A 627       86.94    -50.62                                   
REMARK 500    ASP B 449      146.10    -36.24                                   
REMARK 500    ASP B 454      152.02    -46.32                                   
REMARK 500    ILE B 463      -45.99   -134.59                                   
REMARK 500    SER B 467      -63.93    -90.32                                   
REMARK 500    ASN B 486       64.19     26.14                                   
REMARK 500    THR B 488       49.66     37.70                                   
REMARK 500    ALA B 489      100.75     63.81                                   
REMARK 500    THR B 491       41.90     90.01                                   
REMARK 500    GLN B 493       66.48   -101.14                                   
REMARK 500    LYS B 522      -84.51    -56.20                                   
REMARK 500    GLN B 530      151.23    -46.79                                   
REMARK 500    ASP B 576       41.90   -163.68                                   
REMARK 500    LYS B 578      165.70    172.40                                   
REMARK 500    GLU B 586       32.23     39.73                                   
REMARK 500    ASP B 587       15.33     53.73                                   
REMARK 500    ASP B 594       39.50     86.44                                   
REMARK 500    LYS B 601      -57.13   -163.72                                   
REMARK 500    SER B 602       17.33    -66.98                                   
REMARK 500    ARG B 603       -6.14   -150.80                                   
REMARK 500    LEU B 613       49.48    -63.29                                   
REMARK 500    SER B 614      -26.01   -168.63                                   
REMARK 500    SER B 616       39.42   -156.00                                   
REMARK 500    MET B 627       85.42    -48.96                                   
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 GLN A  493     GLN A  494                  149.80                    
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 BR2 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR2 B 801                 
DBREF  3SKC A  432   726  UNP    P15056   BRAF_HUMAN     432    726             
DBREF  3SKC B  432   726  UNP    P15056   BRAF_HUMAN     432    726             
SEQADV 3SKC MET A  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC ASP A  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC ARG A  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC GLY A  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC SER A  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS A  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC GLY A  431  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC MET B  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC ASP B  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC ARG B  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC GLY B  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC SER B  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC HIS B  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3SKC GLY B  431  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    BR2  A 801      32                                                       
HET    BR2  B 801      32                                                       
HETNAM     BR2 2,6-DIFLUORO-N-[(5S)-3-METHOXY-5H-PYRAZOLO[3,4-                  
HETNAM   2 BR2  B]PYRIDIN-5-YL]-3-[(PHENYLSULFONYL)AMINO]BENZAMIDE              
FORMUL   3  BR2    2(C20 H15 F2 N5 O4 S)                                        
HELIX    1   1 GLN A  494  ARG A  506  1                                  13    
HELIX    2   2 LEU A  537  ILE A  543  1                                   7    
HELIX    3   3 GLU A  549  LYS A  570  1                                  22    
HELIX    4   4 LYS A  578  ASN A  580  5                                   3    
HELIX    5   5 SER A  616  MET A  620  5                                   5    
HELIX    6   6 ALA A  621  ARG A  626  1                                   6    
HELIX    7   7 SER A  634  GLY A  652  1                                  19    
HELIX    8   8 ASN A  661  ARG A  671  1                                  11    
HELIX    9   9 ASP A  677  VAL A  681  5                                   5    
HELIX   10  10 PRO A  686  LEU A  697  1                                  12    
HELIX   11  11 LYS A  700  ARG A  704  5                                   5    
HELIX   12  12 LEU A  706  SER A  720  1                                  15    
HELIX   13  13 GLN B  494  ARG B  506  1                                  13    
HELIX   14  14 LEU B  537  ILE B  543  1                                   7    
HELIX   15  15 GLU B  549  LYS B  570  1                                  22    
HELIX   16  16 LYS B  578  ASN B  580  5                                   3    
HELIX   17  17 SER B  607  LEU B  613  1                                   7    
HELIX   18  18 SER B  616  MET B  620  5                                   5    
HELIX   19  19 ALA B  621  ARG B  626  1                                   6    
HELIX   20  20 SER B  634  GLY B  652  1                                  19    
HELIX   21  21 ASN B  661  ARG B  671  1                                  11    
HELIX   22  22 ASP B  677  VAL B  681  5                                   5    
HELIX   23  23 PRO B  686  LEU B  697  1                                  12    
HELIX   24  24 LYS B  700  ARG B  704  5                                   5    
HELIX   25  25 LEU B  706  SER B  720  1                                  15    
SHEET    1   A 5 THR A 458  ARG A 462  0                                        
SHEET    2   A 5 THR A 470  LYS A 475 -1  O  LYS A 473   N  GLN A 461           
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  THR A 529   N  ALA A 481           
SHEET    5   A 5 PHE A 516  SER A 520 -1  N  GLY A 518   O  VAL A 528           
SHEET    1   B 3 GLY A 534  SER A 536  0                                        
SHEET    2   B 3 ILE A 582  HIS A 585 -1  O  LEU A 584   N  SER A 535           
SHEET    3   B 3 THR A 589  ILE A 592 -1  O  LYS A 591   N  PHE A 583           
SHEET    1   C 5 THR B 458  ARG B 462  0                                        
SHEET    2   C 5 THR B 470  LYS B 475 -1  O  LYS B 473   N  GLN B 461           
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  THR B 529   N  ALA B 481           
SHEET    5   C 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
SHEET    1   D 3 GLY B 534  SER B 536  0                                        
SHEET    2   D 3 ILE B 582  HIS B 585 -1  O  LEU B 584   N  SER B 535           
SHEET    3   D 3 THR B 589  ILE B 592 -1  O  LYS B 591   N  PHE B 583           
CISPEP   1 PRO A  490    THR A  491          0         5.53                     
CISPEP   2 PRO A  492    GLN A  493          0        -8.21                     
CISPEP   3 PRO B  490    THR B  491          0         5.48                     
CISPEP   4 PRO B  492    GLN B  493          0        -7.97                     
SITE     1 AC1 12 ALA A 481  LYS A 483  LEU A 505  LEU A 514                    
SITE     2 AC1 12 PHE A 516  ILE A 527  THR A 529  GLN A 530                    
SITE     3 AC1 12 TRP A 531  CYS A 532  ASP A 594  PHE A 595                    
SITE     1 AC2 12 ALA B 481  LYS B 483  LEU B 505  LEU B 514                    
SITE     2 AC2 12 THR B 529  GLN B 530  TRP B 531  CYS B 532                    
SITE     3 AC2 12 PHE B 583  ASP B 594  PHE B 595  GLY B 596                    
CRYST1  107.900  107.900  151.470  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      0.009268  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009268  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006602        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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