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Database: PDB
Entry: 4DBN
LinkDB: 4DBN
Original site: 4DBN 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       16-JAN-12   4DBN              
TITLE     CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF HUMAN B-RAF WITH A [1,      
TITLE    2 3]THIAZOLO[5,4-B]PYRIDINE DERIVATIVE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 445-726);                      
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, P94, RAFB1;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    KINASE DRUG COMPLEX, SER/THR KINASE, ATP BINDING, PHOSPHORYLATION,    
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.YANO,K.AERTGEERTS                                                 
REVDAT   2   13-JUN-12 4DBN    1       JRNL                                     
REVDAT   1   11-APR-12 4DBN    0                                                
JRNL        AUTH   M.OKANIWA,M.HIROSE,T.IMADA,T.OHASHI,Y.HAYASHI,T.MIYAZAKI,    
JRNL        AUTH 2 T.ARITA,M.YABUKI,K.KAKOI,J.KATO,T.TAKAGI,T.KAWAMOTO,S.YAO,   
JRNL        AUTH 3 A.SUMITA,S.TSUTSUMI,T.TOTTORI,H.OKI,B.C.SANG,J.YANO,         
JRNL        AUTH 4 K.AERTGEERTS,S.YOSHIDA,T.ISHIKAWA                            
JRNL        TITL   DESIGN AND SYNTHESIS OF NOVEL DFG-OUT RAF/VASCULAR           
JRNL        TITL 2 ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (VEGFR2) INHIBITORS. 1. 
JRNL        TITL 3 EXPLORATION OF [5,6]-FUSED BICYCLIC SCAFFOLDS.               
JRNL        REF    J.MED.CHEM.                   V.  55  3452 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22376051                                                     
JRNL        DOI    10.1021/JM300126X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 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) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 16557                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 825                             
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) : 3.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1117                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4153                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.38000                                             
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 0.75000                                              
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): 0.409         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.307         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.690        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4328 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2937 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5855 ; 1.132 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7162 ; 0.783 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   516 ; 5.915 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;36.786 ;23.797       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   778 ;18.536 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;17.987 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   639 ; 0.175 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4714 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   846 ; 0.001 ; 0.020       
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):  2582 ; 0.233 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1052 ; 0.030 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4174 ; 0.454 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1746 ; 0.615 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1669 ; 1.097 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   447        A   532                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6400 -31.1396  13.8098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2400 T22:   0.2292                                     
REMARK   3      T33:   0.3003 T12:   0.0489                                     
REMARK   3      T13:  -0.0090 T23:   0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1466 L22:   4.3038                                     
REMARK   3      L33:   7.8830 L12:  -0.2405                                     
REMARK   3      L13:   0.5870 L23:   0.8040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:  -0.6054 S13:  -0.0451                       
REMARK   3      S21:   0.6409 S22:   0.0544 S23:  -0.8751                       
REMARK   3      S31:   0.3730 S32:   0.9198 S33:  -0.1017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   533        A   720                          
REMARK   3    RESIDUE RANGE :   A   901        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.5362 -43.6015  -9.0645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:   0.1855                                     
REMARK   3      T33:   0.1162 T12:  -0.0034                                     
REMARK   3      T13:   0.0590 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1130 L22:   5.4529                                     
REMARK   3      L33:   3.1062 L12:  -1.5605                                     
REMARK   3      L13:  -1.6198 L23:   1.5187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1515 S12:   0.1999 S13:   0.0106                       
REMARK   3      S21:  -0.3553 S22:  -0.0425 S23:  -0.0160                       
REMARK   3      S31:  -0.2285 S32:  -0.0700 S33:  -0.1090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   447        B   532                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1387 -12.8069  -2.5515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3038 T22:   0.1154                                     
REMARK   3      T33:   0.2615 T12:   0.0849                                     
REMARK   3      T13:   0.0612 T23:   0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8879 L22:   4.4742                                     
REMARK   3      L33:   8.6581 L12:   0.0101                                     
REMARK   3      L13:  -0.5599 L23:  -0.5108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0406 S12:   0.3361 S13:   0.5317                       
REMARK   3      S21:  -0.6904 S22:  -0.1072 S23:  -0.1516                       
REMARK   3      S31:  -0.6861 S32:  -0.1393 S33:   0.0666                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   533        B   719                          
REMARK   3    RESIDUE RANGE :   B   901        B   901                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7864 -15.6041  18.5082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0792 T22:   0.0694                                     
REMARK   3      T33:   0.0826 T12:  -0.0254                                     
REMARK   3      T13:   0.0309 T23:   0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3059 L22:   3.0649                                     
REMARK   3      L33:   2.5667 L12:  -2.1218                                     
REMARK   3      L13:  -2.1056 L23:   2.0615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:   0.1987 S13:  -0.1066                       
REMARK   3      S21:   0.0794 S22:  -0.0060 S23:   0.1859                       
REMARK   3      S31:  -0.0022 S32:  -0.1282 S33:  -0.0319                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES: WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4DBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070127.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 92                                 
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED SI      
REMARK 200                                   (111)                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16557                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9.6% PEG 8000, 0.8M LICL, 100 MM TRIS,   
REMARK 280  PH 8.3, VAPOR DIFFUSION, SITTING 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       73.42200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       55.52000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       55.52000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.71100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       55.52000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       55.52000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.13300            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       55.52000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.52000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.71100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       55.52000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.52000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      110.13300            
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       73.42200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3                                                       
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     GLY A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     ASP A   444                                                      
REMARK 465     SER A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     THR A   598                                                      
REMARK 465     VAL A   599                                                      
REMARK 465     LYS A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     ARG A   602                                                      
REMARK 465     TRP A   603                                                      
REMARK 465     SER A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     SER A   606                                                      
REMARK 465     HIS A   607                                                      
REMARK 465     GLN A   608                                                      
REMARK 465     PHE A   609                                                      
REMARK 465     GLU A   610                                                      
REMARK 465     GLN A   611                                                      
REMARK 465     LEU A   612                                                      
REMARK 465     SER A   613                                                      
REMARK 465     PRO A   721                                                      
REMARK 465     LYS A   722                                                      
REMARK 465     ILE A   723                                                      
REMARK 465     HIS A   724                                                      
REMARK 465     ARG A   725                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     ASP B   444                                                      
REMARK 465     SER B   445                                                      
REMARK 465     SER B   446                                                      
REMARK 465     SER B   604                                                      
REMARK 465     GLY B   605                                                      
REMARK 465     SER B   606                                                      
REMARK 465     HIS B   607                                                      
REMARK 465     GLN B   608                                                      
REMARK 465     PHE B   609                                                      
REMARK 465     GLU B   610                                                      
REMARK 465     GLN B   611                                                      
REMARK 465     LEU B   612                                                      
REMARK 465     SER B   613                                                      
REMARK 465     LEU B   720                                                      
REMARK 465     PRO B   721                                                      
REMARK 465     LYS B   722                                                      
REMARK 465     ILE B   723                                                      
REMARK 465     HIS B   724                                                      
REMARK 465     ARG B   725                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A 467    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 521    CG   CD   CE   NZ                                   
REMARK 470     LYS B 521    CG   CD   CE   NZ                                   
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    PRO A 452      156.18    -47.16                                   
REMARK 500    SER A 466      -30.65     80.57                                   
REMARK 500    PHE A 467       38.18    -89.46                                   
REMARK 500    PRO A 522      -70.20   -111.82                                   
REMARK 500    ILE A 542      -66.52    -98.12                                   
REMARK 500    ARG A 574       -4.01     78.16                                   
REMARK 500    ASP A 575       47.31   -163.13                                   
REMARK 500    ASP A 586       18.09     50.21                                   
REMARK 500    LEU A 587      -47.64   -134.34                                   
REMARK 500    MET A 626       67.15     29.46                                   
REMARK 500    GLN A 627      -77.11    -58.16                                   
REMARK 500    GLN B 460      174.18    -54.27                                   
REMARK 500    ILE B 542      -63.39   -107.32                                   
REMARK 500    LYS B 546       68.60   -119.74                                   
REMARK 500    ARG B 574      -15.10     81.42                                   
REMARK 500    ASP B 575       45.17   -144.93                                   
REMARK 500    LEU B 587       81.78   -156.86                                   
REMARK 500    THR B 588      104.81    155.76                                   
REMARK 500    ALA B 717       21.71    -67.48                                   
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 0JA A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0JA B 901                 
DBREF  4DBN A  444   725  UNP    P15056   BRAF_HUMAN     445    726             
DBREF  4DBN B  444   725  UNP    P15056   BRAF_HUMAN     445    726             
SEQADV 4DBN GLY A  442  UNP  P15056              EXPRESSION TAG                 
SEQADV 4DBN SER A  443  UNP  P15056              EXPRESSION TAG                 
SEQADV 4DBN GLY B  442  UNP  P15056              EXPRESSION TAG                 
SEQADV 4DBN SER B  443  UNP  P15056              EXPRESSION TAG                 
SEQRES   1 A  284  GLY SER ASP SER SER ASP ASP TRP GLU ILE PRO ASP GLY          
SEQRES   2 A  284  GLN ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE          
SEQRES   3 A  284  GLY THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA          
SEQRES   4 A  284  VAL LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN          
SEQRES   5 A  284  LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS          
SEQRES   6 A  284  THR ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER          
SEQRES   7 A  284  THR LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU          
SEQRES   8 A  284  GLY SER SER LEU TYR HIS HIS LEU HIS ILE ILE GLU THR          
SEQRES   9 A  284  LYS PHE GLU MET ILE LYS LEU ILE ASP ILE ALA ARG GLN          
SEQRES  10 A  284  THR ALA GLN GLY MET ASP TYR LEU HIS ALA LYS SER ILE          
SEQRES  11 A  284  ILE HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS          
SEQRES  12 A  284  GLU ASP LEU THR VAL LYS ILE GLY ASP PHE GLY LEU ALA          
SEQRES  13 A  284  THR VAL LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU          
SEQRES  14 A  284  GLN LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL          
SEQRES  15 A  284  ILE ARG MET GLN ASP LYS ASN PRO TYR SER PHE GLN SER          
SEQRES  16 A  284  ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET          
SEQRES  17 A  284  THR GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP          
SEQRES  18 A  284  GLN ILE ILE PHE MET VAL GLY ARG GLY TYR LEU SER PRO          
SEQRES  19 A  284  ASP LEU SER LYS VAL ARG SER ASN CYS PRO LYS ALA MET          
SEQRES  20 A  284  LYS ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP          
SEQRES  21 A  284  GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA SER ILE GLU          
SEQRES  22 A  284  LEU LEU ALA ARG SER LEU PRO LYS ILE HIS ARG                  
SEQRES   1 B  284  GLY SER ASP SER SER ASP ASP TRP GLU ILE PRO ASP GLY          
SEQRES   2 B  284  GLN ILE THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE          
SEQRES   3 B  284  GLY THR VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA          
SEQRES   4 B  284  VAL LYS MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN          
SEQRES   5 B  284  LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS          
SEQRES   6 B  284  THR ARG HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER          
SEQRES   7 B  284  THR LYS PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU          
SEQRES   8 B  284  GLY SER SER LEU TYR HIS HIS LEU HIS ILE ILE GLU THR          
SEQRES   9 B  284  LYS PHE GLU MET ILE LYS LEU ILE ASP ILE ALA ARG GLN          
SEQRES  10 B  284  THR ALA GLN GLY MET ASP TYR LEU HIS ALA LYS SER ILE          
SEQRES  11 B  284  ILE HIS ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS          
SEQRES  12 B  284  GLU ASP LEU THR VAL LYS ILE GLY ASP PHE GLY LEU ALA          
SEQRES  13 B  284  THR VAL LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU          
SEQRES  14 B  284  GLN LEU SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL          
SEQRES  15 B  284  ILE ARG MET GLN ASP LYS ASN PRO TYR SER PHE GLN SER          
SEQRES  16 B  284  ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET          
SEQRES  17 B  284  THR GLY GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP          
SEQRES  18 B  284  GLN ILE ILE PHE MET VAL GLY ARG GLY TYR LEU SER PRO          
SEQRES  19 B  284  ASP LEU SER LYS VAL ARG SER ASN CYS PRO LYS ALA MET          
SEQRES  20 B  284  LYS ARG LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP          
SEQRES  21 B  284  GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA SER ILE GLU          
SEQRES  22 B  284  LEU LEU ALA ARG SER LEU PRO LYS ILE HIS ARG                  
HET    0JA  A 901      38                                                       
HET    0JA  B 901      38                                                       
HETNAM     0JA 2-CHLORO-3-(1-CYANOCYCLOPROPYL)-N-[5-({2-                        
HETNAM   2 0JA  [(CYCLOPROPYLCARBONYL)AMINO][1,3]THIAZOLO[5,4-                  
HETNAM   3 0JA  B]PYRIDIN-5-YL}OXY)-2-FLUOROPHENYL]BENZAMIDE                    
FORMUL   3  0JA    2(C27 H19 CL F N5 O3 S)                                      
FORMUL   5  HOH   *41(H2 O)                                                     
HELIX    1   1 THR A  490  ARG A  505  1                                  16    
HELIX    2   2 LEU A  536  ILE A  542  1                                   7    
HELIX    3   3 GLU A  548  LYS A  569  1                                  22    
HELIX    4   4 SER A  615  MET A  619  5                                   5    
HELIX    5   5 ALA A  620  ARG A  625  1                                   6    
HELIX    6   6 SER A  633  GLY A  651  1                                  19    
HELIX    7   7 ASN A  660  GLY A  671  1                                  12    
HELIX    8   8 ASP A  676  VAL A  680  5                                   5    
HELIX    9   9 PRO A  685  LEU A  696  1                                  12    
HELIX   10  10 LYS A  699  ARG A  703  5                                   5    
HELIX   11  11 LEU A  705  SER A  719  1                                  15    
HELIX   12  12 THR B  490  ARG B  505  1                                  16    
HELIX   13  13 SER B  535  ILE B  542  1                                   8    
HELIX   14  14 GLU B  548  LYS B  569  1                                  22    
HELIX   15  15 LYS B  577  ASN B  579  5                                   3    
HELIX   16  16 GLU B  585  LEU B  587  5                                   3    
HELIX   17  17 SER B  615  MET B  619  5                                   5    
HELIX   18  18 ALA B  620  MET B  626  1                                   7    
HELIX   19  19 SER B  633  GLY B  651  1                                  19    
HELIX   20  20 ASN B  660  ARG B  670  1                                  11    
HELIX   21  21 ASP B  676  VAL B  680  5                                   5    
HELIX   22  22 PRO B  685  LEU B  696  1                                  12    
HELIX   23  23 LYS B  699  ARG B  703  5                                   5    
HELIX   24  24 LEU B  705  ALA B  717  1                                  13    
SHEET    1   A 5 THR A 457  SER A 464  0                                        
SHEET    2   A 5 THR A 469  LYS A 474 -1  O  LYS A 472   N  GLN A 460           
SHEET    3   A 5 ASP A 478  MET A 483 -1  O  MET A 483   N  THR A 469           
SHEET    4   A 5 ALA A 525  GLN A 529 -1  O  ILE A 526   N  LYS A 482           
SHEET    5   A 5 PHE A 515  SER A 519 -1  N  GLY A 517   O  VAL A 527           
SHEET    1   B 3 GLY A 533  SER A 535  0                                        
SHEET    2   B 3 ILE A 581  HIS A 584 -1  O  LEU A 583   N  SER A 534           
SHEET    3   B 3 THR A 588  ILE A 591 -1  O  LYS A 590   N  PHE A 582           
SHEET    1   C 5 THR B 457  ARG B 461  0                                        
SHEET    2   C 5 THR B 469  LYS B 474 -1  O  LYS B 474   N  THR B 457           
SHEET    3   C 5 ASP B 478  MET B 483 -1  O  VAL B 479   N  GLY B 473           
SHEET    4   C 5 ALA B 525  GLN B 529 -1  O  THR B 528   N  ALA B 480           
SHEET    5   C 5 PHE B 515  SER B 519 -1  N  GLY B 517   O  VAL B 527           
SHEET    1   D 2 ILE B 581  LEU B 583  0                                        
SHEET    2   D 2 VAL B 589  ILE B 591 -1  O  LYS B 590   N  PHE B 582           
SITE     1 AC1 17 ALA A 480  LYS A 482  GLU A 500  LEU A 504                    
SITE     2 AC1 17 THR A 507  LEU A 513  ILE A 526  THR A 528                    
SITE     3 AC1 17 GLN A 529  TRP A 530  CYS A 531  GLY A 533                    
SITE     4 AC1 17 PHE A 582  GLY A 592  ASP A 593  PHE A 594                    
SITE     5 AC1 17 HOH A1002                                                     
SITE     1 AC2 15 ALA B 480  LYS B 482  GLU B 500  VAL B 503                    
SITE     2 AC2 15 LEU B 504  ILE B 526  THR B 528  GLN B 529                    
SITE     3 AC2 15 TRP B 530  CYS B 531  PHE B 582  GLY B 592                    
SITE     4 AC2 15 ASP B 593  PHE B 594  ALA B 597                               
CRYST1  111.040  111.040  146.844  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      0.009006  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009006  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006810        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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