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Database: PDB
Entry: 3KUC
LinkDB: 3KUC
Original site: 3KUC 
HEADER    GTP BINDING PROTEIN/TRANSFERASE         27-NOV-09   3KUC              
TITLE     COMPLEX OF RAP1A(E30D/K31E)GDP WITH RAFRBD(A85K/N71R)                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED PROTEIN RAP-1A;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-167;                                        
COMPND   5 SYNONYM: GTP-BINDING PROTEIN SMG-P21A, RAS-RELATED PROTEIN KREV-1,   
COMPND   6 C21KG, G-22K;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE;        
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 51-131;                                       
COMPND  13 SYNONYM: C-RAF, CRAF, RAF-1;                                         
COMPND  14 EC: 2.7.11.1;                                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 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: RAP1A, KREV1;                                                  
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 3KUC    1       REMARK                                   
REVDAT   3   13-JUL-11 3KUC    1       VERSN                                    
REVDAT   2   01-SEP-10 3KUC    1       JRNL                                     
REVDAT   1   23-MAR-10 3KUC    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.    1.92 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) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22491                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1184                            
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) : 1.92                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1654                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1946                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : 1.20000                                              
REMARK   3    B33 (A**2) : -1.08000                                             
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): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.148         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2051 ; 0.027 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2779 ; 2.171 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 6.664 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;37.882 ;24.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   391 ;15.950 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;16.565 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   312 ; 0.172 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1541 ; 0.011 ; 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):  1228 ; 1.407 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1990 ; 2.345 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   823 ; 3.672 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   781 ; 5.585 ; 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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8037 -14.7357  26.0052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0864 T22:   0.0680                                     
REMARK   3      T33:   0.0813 T12:  -0.0418                                     
REMARK   3      T13:   0.0453 T23:  -0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9225 L22:   2.1707                                     
REMARK   3      L33:   5.6321 L12:   0.1971                                     
REMARK   3      L13:   0.3314 L23:   2.7931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0684 S12:  -0.0408 S13:   0.0438                       
REMARK   3      S21:   0.3817 S22:  -0.3020 S23:   0.2512                       
REMARK   3      S31:   0.4332 S32:  -0.4007 S33:   0.3703                       
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):   3.7496 -22.5269   3.3028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0103 T22:   0.0636                                     
REMARK   3      T33:   0.0692 T12:   0.0171                                     
REMARK   3      T13:   0.0063 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9488 L22:   2.0047                                     
REMARK   3      L33:   3.2962 L12:   0.3503                                     
REMARK   3      L13:  -1.4799 L23:  -0.5534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0080 S12:   0.0833 S13:  -0.0423                       
REMARK   3      S21:  -0.0656 S22:  -0.0623 S23:  -0.0327                       
REMARK   3      S31:   0.1141 S32:   0.0080 S33:   0.0543                       
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 3KUC 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_1000056457.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : 1.00472                            
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   : 23432                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 7.710                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.2700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.66                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.520                              
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   (%): 53.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 8000, 100 MM TRIS OR HEPES    
REMARK 280  PH 7.2-7.6, 10-200 MM CA ACETATE OR 100 MM AMMONIUM SULFATE,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 7.5             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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       21.56000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.81500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.27000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.81500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.56000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.27000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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     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   268     O    HOH A   288              1.92            
REMARK 500   O    HOH A   300     O    HOH A   303              1.95            
REMARK 500   N    ASN B    56     O    HOH B   255              1.96            
REMARK 500   NH1  ARG B    71     O    HOH B   273              2.14            
REMARK 500   O    HOH A   300     O    HOH A   302              2.15            
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    VAL A 126   CB    VAL A 126   CG2     0.128                       
REMARK 500    SER A 146   CB    SER A 146   OG      0.102                       
REMARK 500    CYS B  81   CB    CYS B  81   SG     -0.106                       
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    LEU A  56   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B  59   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B  71   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    MET B  76   CG  -  SD  -  CE  ANGL. DEV. = -28.4 DEGREES          
REMARK 500    ARG B  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 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    ILE A  36      -62.20   -100.17                                   
REMARK 500    ASP A  47      -98.96     52.96                                   
REMARK 500    LYS A 117       30.65     76.64                                   
REMARK 500    LEU A 120       51.79    -92.14                                   
REMARK 500    HIS B 105       51.46   -101.14                                   
REMARK 500    LYS B 106       28.09     49.27                                   
REMARK 500    LYS B 108      138.38    -36.05                                   
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 172                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KUD   RELATED DB: PDB                                   
DBREF  3KUC A    1   167  UNP    P62834   RAP1A_HUMAN      1    167             
DBREF  3KUC B   51   131  UNP    P04049   RAF1_HUMAN      51    131             
SEQADV 3KUC ASP A   30  UNP  P62834    GLU    30 ENGINEERED                     
SEQADV 3KUC GLU A   31  UNP  P62834    LYS    31 ENGINEERED                     
SEQADV 3KUC ARG B   71  UNP  P04049    ASN    71 ENGINEERED                     
SEQADV 3KUC LYS B   85  UNP  P04049    ALA    85 ENGINEERED                     
SEQRES   1 A  167  MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY          
SEQRES   2 A  167  VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY          
SEQRES   3 A  167  ILE PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  167  TYR ARG LYS GLN VAL GLU VAL ASP CYS GLN GLN CYS MET          
SEQRES   5 A  167  LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR          
SEQRES   6 A  167  ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE          
SEQRES   7 A  167  ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN          
SEQRES   8 A  167  ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS          
SEQRES   9 A  167  ASP THR GLU ASP VAL PRO MET ILE LEU VAL GLY ASN LYS          
SEQRES  10 A  167  CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN          
SEQRES  11 A  167  GLY GLN ASN LEU ALA ARG GLN TRP CYS ASN CYS ALA PHE          
SEQRES  12 A  167  LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU          
SEQRES  13 A  167  ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG                  
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 ARG 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                                                       
HET     CA  B 172       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *181(H2 O)                                                    
HELIX    1   1 GLY A   15  GLY A   26  1                                  12    
HELIX    2   2 THR A   61  GLY A   75  1                                  15    
HELIX    3   3 ALA A   86  ASP A   92  1                                   7    
HELIX    4   4 ASP A   92  ASP A  105  1                                  14    
HELIX    5   5 LEU A  120  ARG A  124  5                                   5    
HELIX    6   6 GLY A  127  TRP A  138  1                                  12    
HELIX    7   7 ASN A  153  ARG A  167  1                                  15    
HELIX    8   8 SER B   77  VAL B   88  1                                  12    
HELIX    9   9 GLN B   92  GLU B   94  5                                   3    
HELIX   10  10 HIS B  103  LYS B  106  5                                   4    
HELIX   11  11 ALA B  118  ILE B  122  5                                   5    
SHEET    1   A11 ALA A 142  GLU A 145  0                                        
SHEET    2   A11 MET A 111  ASN A 116  1  N  LEU A 113   O  LEU A 144           
SHEET    3   A11 GLY A  77  SER A  83  1  N  LEU A  80   O  ILE A 112           
SHEET    4   A11 ARG A   2  LEU A   9  1  N  LEU A   9   O  ALA A  79           
SHEET    5   A11 GLN A  49  ASP A  57  1  O  GLU A  54   N  LEU A   6           
SHEET    6   A11 GLU A  37  VAL A  46 -1  N  LYS A  42   O  LEU A  53           
SHEET    7   A11 GLN B  66  ARG B  71 -1  O  ARG B  67   N  SER A  39           
SHEET    8   A11 THR B  57  LEU B  62 -1  N  VAL B  60   O  THR B  68           
SHEET    9   A11 GLU B 125  PHE B 130  1  O  VAL B 128   N  PHE B  61           
SHEET   10   A11 CYS B  96  LEU B 101 -1  N  ALA B  97   O  ASP B 129           
SHEET   11   A11 LYS B 109  LEU B 112 -1  O  LEU B 112   N  VAL B  98           
SITE     1 AC1 24 GLY A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC1 24 SER A  17  ALA A  18  PHE A  28  VAL A  29                    
SITE     3 AC1 24 ASP A  30  TYR A  32  ASN A 116  LYS A 117                    
SITE     4 AC1 24 ASP A 119  LEU A 120  SER A 147  ALA A 148                    
SITE     5 AC1 24 LYS A 149   MG A 171  HOH A 202  HOH A 204                    
SITE     6 AC1 24 HOH A 206  HOH A 227  HOH A 231  HOH A 237                    
SITE     1 AC2  6 SER A  17  THR A  35  GDP A 170  HOH A 202                    
SITE     2 AC2  6 HOH A 204  HOH A 231                                          
SITE     1 AC3  6 ASP B  80  GLY B 123  GLU B 125  HOH B 238                    
SITE     2 AC3  6 HOH B 242  HOH B 249                                          
CRYST1   43.120   68.540  101.630  90.00  90.00  90.00 P 21 21 21    4          
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      0.023191  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014590  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009840        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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