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Database: PDB
Entry: 3KUD
LinkDB: 3KUD
Original site: 3KUD 
HEADER    GTP BINDING PROTEIN/TRANSFERASE         27-NOV-09   3KUD              
TITLE     COMPLEX OF RAS-GDP WITH RAFRBD(A85K)                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-166;                                        
COMPND   5 SYNONYM: TRANSFORMING PROTEIN P21, P21RAS, H-RAS-1, C-H-RAS, HA-RAS, 
COMPND   6 GTPASE HRAS, N-TERMINALLY PROCESSED;                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE;        
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 51-131;                                       
COMPND  12 SYNONYM: C-RAF, CRAF, RAF-1;                                         
COMPND  13 EC: 2.7.11.1;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HRAS, HRAS1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: RAF1, RAF;                                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RAS-EFFECTOR COMPLEX, GTP-BINDING, NUCLEOTIDE-BINDING, PROTO-         
KEYWDS   2 ONCOGENE, TRANSFERASE, GTP BINDING PROTEIN-TRANSFERASE COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.FILCHTINSKI,O.SHARABI,A.RUEPPEL,I.R.VETTER,C.HERRMANN,J.M.SHIFMAN   
REVDAT   4   01-NOV-17 3KUD    1       REMARK                                   
REVDAT   3   13-JUL-11 3KUD    1       VERSN                                    
REVDAT   2   01-SEP-10 3KUD    1       JRNL                                     
REVDAT   1   23-MAR-10 3KUD    0                                                
JRNL        AUTH   D.FILCHTINSKI,O.SHARABI,A.RUPPEL,I.R.VETTER,C.HERRMANN,      
JRNL        AUTH 2 J.M.SHIFMAN                                                  
JRNL        TITL   WHAT MAKES RAS AN EFFICIENT MOLECULAR SWITCH: A              
JRNL        TITL 2 COMPUTATIONAL, BIOPHYSICAL, AND STRUCTURAL STUDY OF RAS-GDP  
JRNL        TITL 3 INTERACTIONS WITH MUTANTS OF RAF.                            
JRNL        REF    J.MOL.BIOL.                   V. 399   422 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20361980                                                     
JRNL        DOI    10.1016/J.JMB.2010.03.046                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 23353                          
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) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1230                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1687                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.3980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1924                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 39                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 54.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.06000                                              
REMARK   3    B22 (A**2) : 2.06000                                              
REMARK   3    B33 (A**2) : -3.10000                                             
REMARK   3    B12 (A**2) : 1.03000                                              
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): 0.187         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.141         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.576        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1996 ; 0.028 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2699 ; 2.571 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   243 ; 9.471 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;39.365 ;24.040       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   368 ;23.407 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.343 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   304 ; 0.218 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1490 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1200 ; 1.302 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1940 ; 2.207 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   796 ; 3.302 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   757 ; 4.941 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   165                          
REMARK   3    RESIDUE RANGE :   A   170        A   171                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9119 -17.1967 -33.7723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1562 T22:   0.3187                                     
REMARK   3      T33:   0.0989 T12:  -0.0950                                     
REMARK   3      T13:  -0.0522 T23:  -0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5210 L22:   3.2543                                     
REMARK   3      L33:   2.7257 L12:   3.6079                                     
REMARK   3      L13:  -2.1541 L23:  -1.2339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5110 S12:  -1.3656 S13:  -0.0042                       
REMARK   3      S21:   0.4972 S22:  -0.5339 S23:   0.0281                       
REMARK   3      S31:  -0.3906 S32:   0.5373 S33:   0.0229                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    56        B   131                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8348 -21.7460 -10.5786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6926 T22:   0.4169                                     
REMARK   3      T33:   0.1256 T12:  -0.2755                                     
REMARK   3      T13:  -0.2147 T23:   0.1819                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.9261 L22:   4.4922                                     
REMARK   3      L33:  13.3426 L12:   0.2572                                     
REMARK   3      L13:   4.9273 L23:   1.9644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4179 S12:   0.3755 S13:  -0.2566                       
REMARK   3      S21:   0.5229 S22:  -0.4745 S23:  -0.0628                       
REMARK   3      S31:   0.8494 S32:  -0.1352 S33:   0.0565                       
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                                                           
REMARK   4                                                                      
REMARK   4 3KUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056458.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97935                            
REMARK 200  MONOCHROMATOR                  : FOCUSED SI(111) MONOCHROMATOR      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24583                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 3.830                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.83                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.37900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.830                              
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 1GUA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M NA-MALONAT PH 6.0, 100 MM MES PH    
REMARK 280  6.1, 4% BETAINE, 2% SARCOSINE, 2% N,N-DIMETHYLGLYCINE, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       45.56500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       26.30697            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       92.66000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       45.56500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       26.30697            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       92.66000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       45.56500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       26.30697            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       92.66000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       45.56500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       26.30697            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       92.66000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       45.56500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       26.30697            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       92.66000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       45.56500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       26.30697            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       92.66000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       52.61393            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      185.32000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       52.61393            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      185.32000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       52.61393            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      185.32000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       52.61393            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      185.32000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       52.61393            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      185.32000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       52.61393            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      185.32000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     HIS A   166                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     SER B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     THR B    54                                                      
REMARK 465     SER B    55                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   500     O    HOH A   501              1.48            
REMARK 500   O3B  GDP A   170     O    HOH A   501              1.86            
REMARK 500   O    LEU B    62     O    HOH B   505              2.06            
REMARK 500   O    GLN A    61     CA   GLU A    63              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   539     O    HOH A   541    18444     1.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A  25   CG    GLN A  25   CD      0.236                       
REMARK 500    HIS A  27   CE1   HIS A  27   NE2    -0.070                       
REMARK 500    GLU A 126   CB    GLU A 126   CG      0.119                       
REMARK 500    GLU A 143   CB    GLU A 143   CG      0.116                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  64   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A 154   CB  -  CG  -  OD1 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP A 154   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    LEU B  82   CA  -  CB  -  CG  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    LEU B 131   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  11      160.20    -44.14                                   
REMARK 500    ILE A  36      -65.14    -98.78                                   
REMARK 500    GLU A  62       91.08    -67.05                                   
REMARK 500    ALA A  66       41.14    -52.42                                   
REMARK 500    MET A  67      -58.11   -137.09                                   
REMARK 500    ASP A  69       12.68   -141.46                                   
REMARK 500    GLN A  70      -20.72   -163.28                                   
REMARK 500    MET A  72      -44.13    168.74                                   
REMARK 500    LYS A 104     -148.50   -105.06                                   
REMARK 500    ASP A 105       13.49   -142.83                                   
REMARK 500    LYS A 117       31.64     73.05                                   
REMARK 500    ARG A 149       -0.08     75.74                                   
REMARK 500    THR B  57     -169.23   -123.63                                   
REMARK 500    ASN B  64       -5.78     92.76                                   
REMARK 500    LYS B  65       41.22    107.28                                   
REMARK 500    ARG B  73     -146.02    -92.88                                   
REMARK 500    SER B  77     -163.52    -75.12                                   
REMARK 500    ARG B  89       29.72    -74.04                                   
REMARK 500    HIS B 103       44.07    -95.66                                   
REMARK 500    GLU B 104       64.48   -110.64                                   
REMARK 500    HIS B 105       -6.70    145.11                                   
REMARK 500    LYS B 106       75.86     71.41                                   
REMARK 500    ASP B 117      154.91    -41.82                                   
REMARK 500    SER B 120       18.87    -56.77                                   
REMARK 500    ILE B 122       29.35    -39.29                                   
REMARK 500    GLU B 124     -156.40   -120.72                                   
REMARK 500    PHE B 130      125.45    -31.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A   61     GLU A   62                  141.86                    
REMARK 500 GLU A   62     GLU A   63                  -38.75                    
REMARK 500 GLU A   63     TYR A   64                  -44.85                    
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 GDP A 170                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 171                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KUC   RELATED DB: PDB                                   
DBREF  3KUD A    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  3KUD B   51   131  UNP    P04049   RAF1_HUMAN      51    131             
SEQADV 3KUD LYS B   85  UNP  P04049    ALA    85 ENGINEERED                     
SEQRES   1 A  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 A  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 A  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 A  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 A  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 A  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 A  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 A  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 A  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 A  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 A  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 A  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
SEQRES   1 B   81  PRO SER LYS THR SER ASN THR ILE ARG VAL PHE LEU PRO          
SEQRES   2 B   81  ASN LYS GLN ARG THR VAL VAL ASN VAL ARG ASN GLY MET          
SEQRES   3 B   81  SER LEU HIS ASP CYS LEU MET LYS LYS LEU LYS VAL ARG          
SEQRES   4 B   81  GLY LEU GLN PRO GLU CYS CYS ALA VAL PHE ARG LEU LEU          
SEQRES   5 B   81  HIS GLU HIS LYS GLY LYS LYS ALA ARG LEU ASP TRP ASN          
SEQRES   6 B   81  THR ASP ALA ALA SER LEU ILE GLY GLU GLU LEU GLN VAL          
SEQRES   7 B   81  ASP PHE LEU                                                  
HET    GDP  A 170      28                                                       
HET     MG  A 171       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  HOH   *39(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 ASN A   86  LYS A  104  1                                  19    
HELIX    3   3 GLU A  126  GLY A  138  1                                  13    
HELIX    4   4 GLY A  151  GLN A  165  1                                  15    
HELIX    5   5 SER B   77  ARG B   89  1                                  13    
HELIX    6   6 GLN B   92  GLU B   94  5                                   3    
HELIX    7   7 ALA B  118  ILE B  122  5                                   5    
SHEET    1   A 6 GLU A  37  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  THR A  58 -1  O  LEU A  53   N  LYS A  42           
SHEET    3   A 6 GLU A   3  VAL A   9  1  N  TYR A   4   O  LEU A  52           
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  LEU A  79   N  VAL A   7           
SHEET    5   A 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6   A 6 TYR A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
SHEET    1   B 5 ARG B  67  VAL B  69  0                                        
SHEET    2   B 5 ARG B  59  PHE B  61 -1  N  VAL B  60   O  THR B  68           
SHEET    3   B 5 GLU B 125  PHE B 130  1  O  LEU B 126   N  PHE B  61           
SHEET    4   B 5 CYS B  96  LEU B 102 -1  N  ALA B  97   O  ASP B 129           
SHEET    5   B 5 LYS B 108  ARG B 111 -1  O  ALA B 110   N  ARG B 100           
SITE     1 AC1 23 GLY A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC1 23 SER A  17  ALA A  18  PHE A  28  VAL A  29                    
SITE     3 AC1 23 ASP A  30  GLU A  31  TYR A  32  ASN A 116                    
SITE     4 AC1 23 LYS A 117  ASP A 119  LEU A 120  SER A 145                    
SITE     5 AC1 23 ALA A 146  LYS A 147   MG A 171  HOH A 500                    
SITE     6 AC1 23 HOH A 501  HOH A 503  HOH A 548                               
SITE     1 AC2  6 SER A  17  THR A  35  GDP A 170  HOH A 501                    
SITE     2 AC2  6 HOH A 503  HOH A 548                                          
CRYST1   91.130   91.130  277.980  90.00  90.00 120.00 H 3 2        18          
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      0.010973  0.006335  0.000000        0.00000                         
SCALE2      0.000000  0.012671  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003597        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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