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Database: PDB
Entry: 1TX4
LinkDB: 1TX4
Original site: 1TX4 
HEADER    COMPLEX(GTPASE ACTIVATN/PROTO-ONCOGENE) 29-JUL-97   1TX4              
TITLE     RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P50-RHOGAP;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GTPASE-ACTIVATING PROTEIN RHOGAP;                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;                            
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;                            
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    COMPLEX (GTPASE ACTIVATION/PROTO-ONCOGENE), GTPASE,                   
KEYWDS   2 TRANSITION STATE, GAP, COMPLEX(GTPASE ACTIVATN/PROTO-                
KEYWDS   3 ONCOGENE) COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.RITTINGER,P.A.WALKER,S.J.SMERDON,S.J.GAMBLIN                        
REVDAT   2   24-FEB-09 1TX4    1       VERSN                                    
REVDAT   1   16-SEP-98 1TX4    0                                                
JRNL        AUTH   K.RITTINGER,P.A.WALKER,J.F.ECCLESTON,S.J.SMERDON,            
JRNL        AUTH 2 S.J.GAMBLIN                                                  
JRNL        TITL   STRUCTURE AT 1.65 A OF RHOA AND ITS                          
JRNL        TITL 2 GTPASE-ACTIVATING PROTEIN IN COMPLEX WITH A                  
JRNL        TITL 3 TRANSITION-STATE ANALOGUE.                                   
JRNL        REF    NATURE                        V. 389   758 1997              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9338791                                                      
JRNL        DOI    10.1038/39651                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 37875                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2991                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 497                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TX4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLAGE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 6.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.5                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1AM4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 18%        
REMARK 280  PEG 2000 MME 100MM MES PH6.0 10MM MGCL2, 3MM DTT, 3MM NAN3,         
REMARK 280  114MM AMMONIUM SULFATE 400UM PROTEIN COMPLEX WITH 1MM ALCL3         
REMARK 280  AND 10MM NAF.                                                       
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       33.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.65000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.65000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.00000            
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 TOTAL BURIED SURFACE AREA: 3480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
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     ARG A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     VAL B    33                                                      
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 B   703     O    HOH B   822              2.06            
REMARK 500   O    HOH A   249     O    HOH A   265              2.17            
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   319     O    HOH B   725     2555     2.17            
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    LYS B   6   C     LYS B   7   N       0.188                       
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    GLN A  50   CB  -  CG  -  CD  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    THR A  79   N   -  CA  -  CB  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    THR A  79   OG1 -  CB  -  CG2 ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ARG A  94   CD  -  NE  -  CZ  ANGL. DEV. =  17.6 DEGREES          
REMARK 500    ARG A  94   NE  -  CZ  -  NH1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A  94   NE  -  CZ  -  NH2 ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ARG A 126   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 126   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    GLU A 130   OE1 -  CD  -  OE2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PHE A 144   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    TYR A 168   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 208   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    PHE A 234   CA  -  C   -  O   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    VAL B   9   CA  -  CB  -  CG1 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ASP B  49   CB  -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ASP B  65   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B  67   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B  67   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP B  90   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG B 122   CD  -  NE  -  CZ  ANGL. DEV. =  44.6 DEGREES          
REMARK 500    GLU B 137   CA  -  CB  -  CG  ANGL. DEV. =  14.4 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    PHE A  84      -10.50     80.65                                   
REMARK 500    THR A 134      153.79     78.94                                   
REMARK 500    VAL B  38      -90.40    -93.99                                   
REMARK 500    ASP B  49     -107.44     61.19                                   
REMARK 500    LYS B  98      -64.10   -131.22                                   
REMARK 500    LYS B 164       -5.18     82.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 878        DISTANCE =  5.33 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 681  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B 680   O2B                                                    
REMARK 620 2 THR B  19   OG1  93.4                                              
REMARK 620 3 THR B  37   OG1 173.5  83.3                                        
REMARK 620 4 ALF B 682   F2   98.8 167.1  84.1                                  
REMARK 620 5 HOH B 683   O    88.4  90.5  86.0  85.8                            
REMARK 620 6 HOH B 685   O    95.4  90.4  90.2  92.5 176.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF B 682  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B 680   O3B                                                    
REMARK 620 2 HOH B 684   O   173.0                                              
REMARK 620 3  MG B 681  MG    72.6 104.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: TS                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: TRANSITION STATE ANALOG GDP.ALF4.                  
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 681                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF B 682                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 680                 
DBREF  1TX4 A   37   234  UNP    Q07960   RHG01_HUMAN    234    431             
DBREF  1TX4 B    3   179  UNP    P61586   RHOA_HUMAN       3    179             
SEQADV 1TX4 ALA A  113  UNP  Q07960    GLU   310 CONFLICT                       
SEQADV 1TX4 ASN B   25  UNP  P61586    PHE    25 SUBSTITUTION                   
SEQRES   1 A  198  ARG PRO PRO LEU PRO ASN GLN GLN PHE GLY VAL SER LEU          
SEQRES   2 A  198  GLN HIS LEU GLN GLU LYS ASN PRO GLU GLN GLU PRO ILE          
SEQRES   3 A  198  PRO ILE VAL LEU ARG GLU THR VAL ALA TYR LEU GLN ALA          
SEQRES   4 A  198  HIS ALA LEU THR THR GLU GLY ILE PHE ARG ARG SER ALA          
SEQRES   5 A  198  ASN THR GLN VAL VAL ARG GLU VAL GLN GLN LYS TYR ASN          
SEQRES   6 A  198  MET GLY LEU PRO VAL ASP PHE ASP GLN TYR ASN ALA LEU          
SEQRES   7 A  198  HIS LEU PRO ALA VAL ILE LEU LYS THR PHE LEU ARG GLU          
SEQRES   8 A  198  LEU PRO GLU PRO LEU LEU THR PHE ASP LEU TYR PRO HIS          
SEQRES   9 A  198  VAL VAL GLY PHE LEU ASN ILE ASP GLU SER GLN ARG VAL          
SEQRES  10 A  198  PRO ALA THR LEU GLN VAL LEU GLN THR LEU PRO GLU GLU          
SEQRES  11 A  198  ASN TYR GLN VAL LEU ARG PHE LEU THR ALA PHE LEU VAL          
SEQRES  12 A  198  GLN ILE SER ALA HIS SER ASP GLN ASN LYS MET THR ASN          
SEQRES  13 A  198  THR ASN LEU ALA VAL VAL PHE GLY PRO ASN LEU LEU TRP          
SEQRES  14 A  198  ALA LYS ASP ALA ALA ILE THR LEU LYS ALA ILE ASN PRO          
SEQRES  15 A  198  ILE ASN THR PHE THR LYS PHE LEU LEU ASP HIS GLN GLY          
SEQRES  16 A  198  GLU LEU PHE                                                  
SEQRES   1 B  177  ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP GLY ALA          
SEQRES   2 B  177  CYS GLY LYS THR CYS LEU LEU ILE VAL ASN SER LYS ASP          
SEQRES   3 B  177  GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE GLU ASN          
SEQRES   4 B  177  TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN VAL GLU          
SEQRES   5 B  177  LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 B  177  ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP VAL ILE          
SEQRES   7 B  177  LEU MET CYS PHE SER ILE ASP SER PRO ASP SER LEU GLU          
SEQRES   8 B  177  ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS HIS PHE          
SEQRES   9 B  177  CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN LYS LYS          
SEQRES  10 B  177  ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU LEU ALA          
SEQRES  11 B  177  LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU GLY ARG          
SEQRES  12 B  177  ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR MET GLU          
SEQRES  13 B  177  CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU VAL PHE          
SEQRES  14 B  177  GLU MET ALA THR ARG ALA ALA LEU                              
HET     MG  B 681       1                                                       
HET    ALF  B 682       5                                                       
HET    GDP  B 680      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  ALF    AL F4 1-                                                     
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  HOH   *497(H2 O)                                                    
HELIX    1   1 LEU A   49  LYS A   55  1                                   7    
HELIX    2   2 ILE A   64  HIS A   76  1                                  13    
HELIX    3   3 THR A   90  ASN A  101  1                                  12    
HELIX    4   4 PHE A  108  GLN A  110  5                                   3    
HELIX    5   5 HIS A  115  GLU A  127  1                                  13    
HELIX    6   6 PHE A  135  VAL A  142  5                                   8    
HELIX    7   7 PHE A  144  ASN A  146  5                                   3    
HELIX    8   8 GLU A  149  THR A  162  5                                  14    
HELIX    9   9 GLU A  165  ASN A  188  1                                  24    
HELIX   10  10 ASN A  192  LEU A  203  1                                  12    
HELIX   11  11 ALA A  209  LYS A  214  1                                   6    
HELIX   12  12 ILE A  216  ASP A  228  1                                  13    
HELIX   13  13 LYS B   18  LYS B   27  1                                  10    
HELIX   14  14 GLU B   64  SER B   73  5                                  10    
HELIX   15  15 PRO B   89  GLU B   97  1                                   9    
HELIX   16  16 TRP B   99  PHE B  106  1                                   8    
HELIX   17  17 LYS B  119  LEU B  121  5                                   3    
HELIX   18  18 GLU B  125  MET B  134  1                                  10    
HELIX   19  19 PRO B  141  ILE B  151  1                                  11    
HELIX   20  20 VAL B  167  ALA B  177  1                                  11    
SHEET    1   A 6 GLY B 155  GLU B 158  0                                        
SHEET    2   A 6 PRO B 111  ASN B 117  1  N  LEU B 114   O  GLY B 155           
SHEET    3   A 6 VAL B  79  SER B  85  1  N  ILE B  80   O  PRO B 111           
SHEET    4   A 6 ILE B   4  GLY B  12  1  N  VAL B   9   O  VAL B  79           
SHEET    5   A 6 LYS B  51  THR B  60  1  N  GLU B  54   O  ILE B   4           
SHEET    6   A 6 PHE B  39  VAL B  48 -1  N  VAL B  48   O  LYS B  51           
LINK         O2B GDP B 680                MG    MG B 681     1555   1555  2.20  
LINK         O3B GDP B 680                AL   ALF B 682     1555   1555  1.92  
LINK        MG    MG B 681                 OG1 THR B  19     1555   1555  2.27  
LINK        MG    MG B 681                 OG1 THR B  37     1555   1555  2.32  
LINK        MG    MG B 681                 F2  ALF B 682     1555   1555  2.30  
LINK        MG    MG B 681                 O   HOH B 683     1555   1555  2.10  
LINK        MG    MG B 681                 O   HOH B 685     1555   1555  2.13  
LINK        AL   ALF B 682                 O   HOH B 684     1555   1555  1.87  
LINK        AL   ALF B 682                MG    MG B 681     1555   1555  3.53  
SITE     1  TS  1 GDP B 680                                                     
SITE     1 AC1  6 THR B  19  THR B  37  GDP B 680  ALF B 682                    
SITE     2 AC1  6 HOH B 683  HOH B 685                                          
SITE     1 AC2 15 ARG A  85  GLY B  14  ALA B  15  LYS B  18                    
SITE     2 AC2 15 PRO B  36  THR B  37  THR B  60  ALA B  61                    
SITE     3 AC2 15 GLY B  62  GLN B  63  GDP B 680   MG B 681                    
SITE     4 AC2 15 HOH B 683  HOH B 684  HOH B 685                               
SITE     1 AC3 27 ARG A  85  ALA B  15  CYS B  16  GLY B  17                    
SITE     2 AC3 27 LYS B  18  THR B  19  CYS B  20  PHE B  30                    
SITE     3 AC3 27 TYR B  34  LYS B 118  ASP B 120  LEU B 121                    
SITE     4 AC3 27 SER B 160  ALA B 161  LYS B 162   MG B 681                    
SITE     5 AC3 27 ALF B 682  HOH B 683  HOH B 689  HOH B 714                    
SITE     6 AC3 27 HOH B 718  HOH B 740  HOH B 747  HOH B 764                    
SITE     7 AC3 27 HOH B 777  HOH B 788  HOH B 806                               
CRYST1   66.500   72.000   91.300  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      0.015038  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013889  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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