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Database: PDB
Entry: 3PSD
LinkDB: 3PSD
Original site: 3PSD 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-DEC-10   3PSD              
TITLE     NON-OXIME 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: UNP 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_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, ZINC-FINGER, TRANSFERASE- 
KEYWDS   4 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.MORALES,G.P.A.VIGERS,B.J.BRANDHUBER                                 
REVDAT   3   24-JAN-18 3PSD    1       AUTHOR                                   
REVDAT   2   01-JUN-11 3PSD    1       JRNL                                     
REVDAT   1   18-MAY-11 3PSD    0                                                
JRNL        AUTH   B.J.NEWHOUSE,J.D.HANSEN,J.GRINA,M.WELCH,G.TOPALOV,N.LITTMAN, 
JRNL        AUTH 2 M.CALLEJO,M.MARTINSON,S.GALBRAITH,E.R.LAIRD,B.J.BRANDHUBER,  
JRNL        AUTH 3 G.VIGERS,T.MORALES,R.WOESSNER,N.RANDOLPH,J.LYSSIKATOS,       
JRNL        AUTH 4 A.OLIVERO                                                    
JRNL        TITL   NON-OXIME PYRAZOLE BASED INHIBITORS OF B-RAF KINASE.         
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  3488 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21536432                                                     
JRNL        DOI    10.1016/J.BMCL.2010.12.038                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 8434                           
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) : 0.280                           
REMARK   3   R VALUE            (WORKING SET) : 0.277                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 491                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 587                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.4640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4200                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
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) : 42.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.68000                                              
REMARK   3    B22 (A**2) : 0.68000                                              
REMARK   3    B33 (A**2) : -1.37000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.872         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.645         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.554        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.833                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.772                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4360 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5893 ; 1.061 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   522 ; 4.108 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   186 ;34.967 ;23.871       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   793 ;15.064 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;11.072 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   645 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3324 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2616 ; 0.153 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4236 ; 0.274 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1744 ; 0.088 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1657 ; 0.161 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062758.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
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   : 8936                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 13.90                              
REMARK 200  R MERGE                    (I) : 0.18500                            
REMARK 200  R SYM                      (I) : 0.18000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3D4Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG 3350 100MM TRIS PH8.0 10%       
REMARK 280  TACSIMATE 10% GLYCEROL 1.6MG/ML PROTEIN 500UM INHIBITOR , 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       80.86500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.49000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.43250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.49000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.49000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.29750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.49000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.49000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.43250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.49000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.49000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      121.29750            
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       80.86500            
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     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     LEU A   613                                                      
REMARK 465     SER A   614                                                      
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: 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    ASN A 486       26.10     41.26                                   
REMARK 500    ILE A 543      -60.91   -104.97                                   
REMARK 500    ASP A 576       39.98   -151.92                                   
REMARK 500    ASP A 594       92.45     58.04                                   
REMARK 500    MET A 627       86.06    -65.68                                   
REMARK 500    ASP A 629     -121.98    -92.80                                   
REMARK 500    SER A 720       46.49   -101.45                                   
REMARK 500    PRO B 523      -67.55    -93.86                                   
REMARK 500    ARG B 575       -0.60     68.55                                   
REMARK 500    ASP B 576       36.60   -149.36                                   
REMARK 500    ASP B 587      -29.42     68.44                                   
REMARK 500    ASP B 594       89.79     61.11                                   
REMARK 500    MET B 627       83.20    -64.64                                   
REMARK 500    ASP B 629     -119.44    -92.55                                   
REMARK 500    SER B 720       44.46   -100.17                                   
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 SM7 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SM7 B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D4Q   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE BRAF WITH A PYRAZOLE-BASED INHIBITOR                       
REMARK 900 RELATED ID: 3PSB   RELATED DB: PDB                                   
DBREF  3PSD A  433   726  UNP    P15056   BRAF1_HUMAN    433    726             
DBREF  3PSD B  433   726  UNP    P15056   BRAF1_HUMAN    433    726             
SEQADV 3PSD MET A  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD ASP A  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD ARG A  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD GLY A  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD SER A  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS A  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD GLY A  431  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD SER A  432  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD MET B  420  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD ASP B  421  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD ARG B  422  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD GLY B  423  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD SER B  424  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  425  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  426  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  427  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  428  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  429  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD HIS B  430  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD GLY B  431  UNP  P15056              EXPRESSION TAG                 
SEQADV 3PSD 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    SM7  A   1      29                                                       
HET    SM7  B   2      29                                                       
HETNAM     SM7 6-[1-(PIPERIDIN-4-YL)-3-(PYRIDIN-4-YL)-1H-PYRAZOL-4-             
HETNAM   2 SM7  YL]INDENO[1,2-C]PYRAZOLE                                        
FORMUL   3  SM7    2(C23 H20 N6)                                                
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  ARG B  671  1                                  11    
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  LYS A 473   N  GLN A 461           
SHEET    3   A 5 ASP A 479  MET A 484 -1  O  MET A 484   N  THR A 470           
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 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  LYS B 473   N  GLN B 461           
SHEET    3   C 5 ASP B 479  MET B 484 -1  O  MET B 484   N  THR B 470           
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 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           
CISPEP   1 GLN A  628    ASP A  629          0         2.36                     
CISPEP   2 GLN B  628    ASP B  629          0         2.76                     
SITE     1 AC1 15 ILE A 463  VAL A 471  ALA A 481  LYS A 483                    
SITE     2 AC1 15 GLU A 501  LEU A 514  THR A 529  GLN A 530                    
SITE     3 AC1 15 TRP A 531  CYS A 532  SER A 535  ASN A 580                    
SITE     4 AC1 15 PHE A 583  ASP A 594  TYR B 673                               
SITE     1 AC2 12 ILE B 463  VAL B 471  LYS B 483  GLU B 501                    
SITE     2 AC2 12 LEU B 514  THR B 529  GLN B 530  TRP B 531                    
SITE     3 AC2 12 CYS B 532  SER B 535  PHE B 583  ASP B 594                    
CRYST1   94.980   94.980  161.730  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      0.010529  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006183        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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