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Database: PDB
Entry: 4H58
LinkDB: 4H58
Original site: 4H58 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-SEP-12   4H58              
TITLE     BRAF IN COMPLEX WITH COMPOUND 3                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN (UNP RESIDUES 448-722);              
COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL       
COMPND   6 ONCOGENE HOMOLOG B1;                                                 
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROTEIN KINASE, STRUCTURE BASED DRUG DISCOVERY, TRANSFERASE-          
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.VASBINDER,B.AQUILA,M.AUGUSTIN,T.CHUENG,D.COOK,L.DREW,B.FAUBER,      
AUTHOR   2 S.GLOSSOP,R.GODIN,M.GRONDINE,E.HENNESSY,J.JOHANNES,S.LEE,P.LYNE,     
AUTHOR   3 M.MOERTL,C.OMER,S.PALAKURTHI,T.PONTZ,J.READ,L.SHA,M.SHEN,            
AUTHOR   4 S.STEINBACHER,H.WANG,A.WU,M.YE,B.BAGAL                               
REVDAT   3   15-NOV-17 4H58    1       REMARK                                   
REVDAT   2   27-MAR-13 4H58    1       JRNL                                     
REVDAT   1   27-FEB-13 4H58    0                                                
JRNL        AUTH   M.M.VASBINDER,B.AQUILA,M.AUGUSTIN,H.CHEN,T.CHEUNG,D.COOK,    
JRNL        AUTH 2 L.DREW,B.P.FAUBER,S.GLOSSOP,M.GRONDINE,E.HENNESSY,           
JRNL        AUTH 3 J.JOHANNES,S.LEE,P.LYNE,M.MORTL,C.OMER,S.PALAKURTHI,T.PONTZ, 
JRNL        AUTH 4 J.READ,L.SHA,M.SHEN,S.STEINBACHER,H.WANG,A.WU,M.YE           
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF A NOVEL SERIES OF POTENT       
JRNL        TITL 2 MUTANT B-RAF(V600E) SELECTIVE KINASE INHIBITORS.             
JRNL        REF    J.MED.CHEM.                   V.  56  1996 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23398453                                                     
JRNL        DOI    10.1021/JM301658D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 26825                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1412                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1816                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 96                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6367                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.52000                                             
REMARK   3    B22 (A**2) : -1.52000                                             
REMARK   3    B33 (A**2) : 3.04000                                              
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): 1.983         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.422         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.310         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.585        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.870                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6639 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6124 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8965 ; 1.266 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14264 ; 0.789 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   795 ; 7.012 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   286 ;37.695 ;23.811       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1199 ;18.487 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;17.688 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   980 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7210 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1336 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1593 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6485 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3253 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3724 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   158 ; 0.144 ; 0.200       
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):    21 ; 0.218 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    98 ; 0.205 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.102 ; 0.200       
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):  5188 ; 1.160 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1623 ; 0.101 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6430 ; 1.326 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3196 ; 1.297 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2535 ; 2.016 ; 6.000       
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   : 1.20                                          
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                                                           
REMARK   4                                                                      
REMARK   4 4H58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075034.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.14000                            
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) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79500                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1UWH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SALT, PH 6.5, VAPOR DIFFUSION, SITTING   
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-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      102.37000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000      102.37000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.47500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       38.23750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      102.37000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      114.71250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      114.71250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.37000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.23750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000      102.37000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       76.47500            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000      102.37000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       76.47500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000      102.37000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      114.71250            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       38.23750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      102.37000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       38.23750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      114.71250            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      102.37000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000      102.37000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       76.47500            
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: MONOMERIC                         
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 801  LIES ON A SPECIAL POSITION.                          
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     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     VAL B   599                                                      
REMARK 465     LYS B   600                                                      
REMARK 465     SER B   601                                                      
REMARK 465     ARG B   602                                                      
REMARK 465     TRP B   603                                                      
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     ASP C   447                                                      
REMARK 465     ASP C   628                                                      
REMARK 465     LYS C   629                                                      
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      152.47    -44.18                                   
REMARK 500    ILE A 462      -43.23   -140.25                                   
REMARK 500    SER A 466      -55.50    -26.08                                   
REMARK 500    TRP A 475      103.05   -174.13                                   
REMARK 500    PRO A 491       -3.27    -45.69                                   
REMARK 500    GLU A 532       98.53    -63.48                                   
REMARK 500    SER A 534     -174.68     73.88                                   
REMARK 500    THR A 545      113.30    -37.72                                   
REMARK 500    LYS A 569        3.42    -68.52                                   
REMARK 500    ASP A 575       45.83   -157.81                                   
REMARK 500    LYS A 577      147.80    170.91                                   
REMARK 500    ASP A 586        7.35     46.37                                   
REMARK 500    ASP A 593      108.26    -39.31                                   
REMARK 500    ALA A 597      149.90    166.09                                   
REMARK 500    ARG A 625      -73.36    -71.44                                   
REMARK 500    MET A 626       79.39     95.28                                   
REMARK 500    ASP A 628      -24.82    153.05                                   
REMARK 500    ASN A 630       37.09   -148.13                                   
REMARK 500    SER A 719       43.50    -93.47                                   
REMARK 500    SER B 466      -95.17     13.81                                   
REMARK 500    PHE B 467       55.28   -116.11                                   
REMARK 500    ALA B 488      128.05    -34.18                                   
REMARK 500    ARG B 505        4.97    -68.04                                   
REMARK 500    HIS B 509      143.20   -171.78                                   
REMARK 500    LEU B 524       81.85     56.46                                   
REMARK 500    ILE B 542      -83.33    -94.29                                   
REMARK 500    MET B 549      -45.96    -26.03                                   
REMARK 500    ARG B 574      -17.44     87.58                                   
REMARK 500    ASP B 575       48.88   -148.86                                   
REMARK 500    LEU B 583       78.89   -110.26                                   
REMARK 500    LEU B 583       78.89   -105.76                                   
REMARK 500    LEU B 587      -60.01   -143.98                                   
REMARK 500    MET B 626       91.08     72.73                                   
REMARK 500    ASP B 628     -133.59   -161.92                                   
REMARK 500    LEU B 677        7.91    -69.17                                   
REMARK 500    PRO C 452      172.52    -55.77                                   
REMARK 500    ASN C 485       70.55   -100.31                                   
REMARK 500    THR C 487      -63.59    -91.28                                   
REMARK 500    ALA C 496       35.88    -80.02                                   
REMARK 500    PHE C 497      -62.13   -142.38                                   
REMARK 500    LYS C 498      -13.34    -49.24                                   
REMARK 500    GLU C 544       17.23     53.09                                   
REMARK 500    ASP C 575       34.46   -166.02                                   
REMARK 500    LEU C 587      -53.55   -145.92                                   
REMARK 500    SER C 604     -164.23    -79.70                                   
REMARK 500    HIS C 607       59.14   -111.29                                   
REMARK 500    GLN C 608      -36.33    -39.54                                   
REMARK 500    GLN C 611      -87.75    -74.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A  626     GLN A  627                  145.53                    
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 10Z A 801                 
DBREF  4H58 A  447   721  UNP    P15056   BRAF_HUMAN     448    722             
DBREF  4H58 B  447   721  UNP    P15056   BRAF_HUMAN     448    722             
DBREF  4H58 C  447   721  UNP    P15056   BRAF_HUMAN     448    722             
SEQRES   1 A  275  ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR VAL GLY          
SEQRES   2 A  275  GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL TYR LYS          
SEQRES   3 A  275  GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET LEU ASN          
SEQRES   4 A  275  VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA PHE LYS          
SEQRES   5 A  275  ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS VAL ASN          
SEQRES   6 A  275  ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO GLN LEU          
SEQRES   7 A  275  ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER LEU TYR          
SEQRES   8 A  275  HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU MET ILE          
SEQRES   9 A  275  LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN GLY MET          
SEQRES  10 A  275  ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG ASP LEU          
SEQRES  11 A  275  LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU THR VAL          
SEQRES  12 A  275  LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS SER ARG          
SEQRES  13 A  275  TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER GLY SER          
SEQRES  14 A  275  ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET GLN ASP          
SEQRES  15 A  275  LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR ALA PHE          
SEQRES  16 A  275  GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN LEU PRO          
SEQRES  17 A  275  TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE PHE MET          
SEQRES  18 A  275  VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER LYS VAL          
SEQRES  19 A  275  ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU MET ALA          
SEQRES  20 A  275  GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO LEU PHE          
SEQRES  21 A  275  PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA ARG SER          
SEQRES  22 A  275  LEU PRO                                                      
SEQRES   1 B  275  ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR VAL GLY          
SEQRES   2 B  275  GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL TYR LYS          
SEQRES   3 B  275  GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET LEU ASN          
SEQRES   4 B  275  VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA PHE LYS          
SEQRES   5 B  275  ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS VAL ASN          
SEQRES   6 B  275  ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO GLN LEU          
SEQRES   7 B  275  ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER LEU TYR          
SEQRES   8 B  275  HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU MET ILE          
SEQRES   9 B  275  LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN GLY MET          
SEQRES  10 B  275  ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG ASP LEU          
SEQRES  11 B  275  LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU THR VAL          
SEQRES  12 B  275  LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS SER ARG          
SEQRES  13 B  275  TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER GLY SER          
SEQRES  14 B  275  ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET GLN ASP          
SEQRES  15 B  275  LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR ALA PHE          
SEQRES  16 B  275  GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN LEU PRO          
SEQRES  17 B  275  TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE PHE MET          
SEQRES  18 B  275  VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER LYS VAL          
SEQRES  19 B  275  ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU MET ALA          
SEQRES  20 B  275  GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO LEU PHE          
SEQRES  21 B  275  PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA ARG SER          
SEQRES  22 B  275  LEU PRO                                                      
SEQRES   1 C  275  ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR VAL GLY          
SEQRES   2 C  275  GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL TYR LYS          
SEQRES   3 C  275  GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET LEU ASN          
SEQRES   4 C  275  VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA PHE LYS          
SEQRES   5 C  275  ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS VAL ASN          
SEQRES   6 C  275  ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO GLN LEU          
SEQRES   7 C  275  ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER LEU TYR          
SEQRES   8 C  275  HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU MET ILE          
SEQRES   9 C  275  LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN GLY MET          
SEQRES  10 C  275  ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG ASP LEU          
SEQRES  11 C  275  LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU THR VAL          
SEQRES  12 C  275  LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS SER ARG          
SEQRES  13 C  275  TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER GLY SER          
SEQRES  14 C  275  ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET GLN ASP          
SEQRES  15 C  275  LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR ALA PHE          
SEQRES  16 C  275  GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN LEU PRO          
SEQRES  17 C  275  TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE PHE MET          
SEQRES  18 C  275  VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER LYS VAL          
SEQRES  19 C  275  ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU MET ALA          
SEQRES  20 C  275  GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO LEU PHE          
SEQRES  21 C  275  PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA ARG SER          
SEQRES  22 C  275  LEU PRO                                                      
HET    10Z  A 801      29                                                       
HET     CL  C 801       1                                                       
HETNAM     10Z N-(4-{[(2-METHOXYETHYL)AMINO]METHYL}PHENYL)-6-(PYRIDIN-          
HETNAM   2 10Z  4-YL)QUINAZOLIN-2-AMINE                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4  10Z    C23 H23 N5 O                                                 
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *15(H2 O)                                                     
HELIX    1   1 GLN A  492  ARG A  505  1                                  14    
HELIX    2   2 SER A  535  ILE A  542  1                                   8    
HELIX    3   3 GLU A  548  LYS A  569  1                                  22    
HELIX    4   4 LYS A  577  ASN A  579  5                                   3    
HELIX    5   5 GLU A  585  LEU A  587  5                                   3    
HELIX    6   6 ALA A  620  MET A  626  1                                   7    
HELIX    7   7 SER A  633  GLY A  651  1                                  19    
HELIX    8   8 ASN A  660  GLY A  671  1                                  12    
HELIX    9   9 ASP A  676  VAL A  680  5                                   5    
HELIX   10  10 PRO A  685  LYS A  697  1                                  13    
HELIX   11  11 LYS A  699  ARG A  703  5                                   5    
HELIX   12  12 LEU A  705  SER A  719  1                                  15    
HELIX   13  13 THR B  490  ARG B  505  1                                  16    
HELIX   14  14 SER B  535  ILE B  542  1                                   8    
HELIX   15  15 GLU B  548  LYS B  569  1                                  22    
HELIX   16  16 LYS B  577  ASN B  579  5                                   3    
HELIX   17  17 GLU B  585  LEU B  587  5                                   3    
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 PRO B  685  LEU B  696  1                                  12    
HELIX   22  22 LYS B  699  ARG B  703  5                                   5    
HELIX   23  23 LEU B  705  SER B  719  1                                  15    
HELIX   24  24 THR C  490  ARG C  505  1                                  16    
HELIX   25  25 LEU C  536  ILE C  542  1                                   7    
HELIX   26  26 GLU C  548  LYS C  569  1                                  22    
HELIX   27  27 PHE C  594  THR C  598  5                                   5    
HELIX   28  28 ALA C  620  ARG C  625  1                                   6    
HELIX   29  29 SER C  633  GLY C  651  1                                  19    
HELIX   30  30 ASN C  660  GLY C  671  1                                  12    
HELIX   31  31 ASP C  676  VAL C  680  5                                   5    
HELIX   32  32 PRO C  685  LEU C  696  1                                  12    
HELIX   33  33 LYS C  699  ARG C  703  5                                   5    
HELIX   34  34 LEU C  705  ARG C  718  1                                  14    
SHEET    1   A 5 THR A 457  GLY A 463  0                                        
SHEET    2   A 5 THR A 469  LYS A 474 -1  O  LYS A 472   N  GLY A 459           
SHEET    3   A 5 ASP A 478  LEU A 484 -1  O  MET A 483   N  THR A 469           
SHEET    4   A 5 LEU A 524  GLN A 529 -1  O  ILE A 526   N  LYS A 482           
SHEET    5   A 5 PHE A 515  SER A 519 -1  N  MET A 516   O  VAL A 527           
SHEET    1   B 2 ILE A 571  ILE A 572  0                                        
SHEET    2   B 2 THR A 598  VAL A 599 -1  O  THR A 598   N  ILE A 572           
SHEET    1   C 2 ILE A 581  HIS A 584  0                                        
SHEET    2   C 2 THR A 588  ILE A 591 -1  O  THR A 588   N  HIS A 584           
SHEET    1   D 5 ARG B 461  GLY B 465  0                                        
SHEET    2   D 5 GLY B 468  LYS B 474 -1  O  VAL B 470   N  GLY B 463           
SHEET    3   D 5 ASP B 478  MET B 483 -1  O  MET B 483   N  THR B 469           
SHEET    4   D 5 ALA B 525  GLN B 529 -1  O  ILE B 526   N  LYS B 482           
SHEET    5   D 5 PHE B 515  SER B 519 -1  N  GLY B 517   O  VAL B 527           
SHEET    1   E 2 ILE B 581  HIS B 584  0                                        
SHEET    2   E 2 THR B 588  ILE B 591 -1  O  LYS B 590   N  PHE B 582           
SHEET    1   F 5 THR C 457  GLY C 463  0                                        
SHEET    2   F 5 THR C 469  LYS C 474 -1  O  LYS C 472   N  GLN C 460           
SHEET    3   F 5 ASP C 478  MET C 483 -1  O  MET C 483   N  THR C 469           
SHEET    4   F 5 ALA C 525  GLN C 529 -1  O  ILE C 526   N  LYS C 482           
SHEET    5   F 5 PHE C 515  SER C 519 -1  N  GLY C 517   O  VAL C 527           
SHEET    1   G 3 GLY C 533  SER C 535  0                                        
SHEET    2   G 3 ILE C 581  HIS C 584 -1  O  LEU C 583   N  SER C 534           
SHEET    3   G 3 THR C 588  ILE C 591 -1  O  LYS C 590   N  PHE C 582           
CISPEP   1 LYS A  521    PRO A  522          0        -9.00                     
CISPEP   2 LYS B  521    PRO B  522          0         1.88                     
CISPEP   3 LYS C  521    PRO C  522          0       -11.87                     
SITE     1 AC1  7 VAL A 470  LEU A 513  THR A 528  TRP A 530                    
SITE     2 AC1  7 CYS A 531  HIS A 538  PHE A 582                               
CRYST1  204.740  204.740  152.950  90.00  90.00  90.00 I 41 2 2     48          
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      0.004884  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006538        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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