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Database: PDB
Entry: 1GZS
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HEADER    TOXIN/CELL CYCLE                        05-JUN-02   1GZS              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF            
TITLE    2 THE SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN CDC42                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOPE;                                                      
COMPND   3 CHAIN: B, D;                                                         
COMPND   4 FRAGMENT: GUANINE NUCTLEOTIDE EXCHANGE FACTOR                        
COMPND   5  (GEF-DOMAIN), RESIDUES 78-240;                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GTP-BINDING PROTEIN;                                       
COMPND   9 CHAIN: A, C;                                                         
COMPND  10 FRAGMENT: RESIDUES 1-178;                                            
COMPND  11 SYNONYM: PLACENTAL ISOFORM, CDC42 G25K;                              
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    TOXIN/CELL CYCLE, COMPLEX (TOXIN/CELL CYCLE PROTEIN), SOPE,           
KEYWDS   2 CDC42, SALMONELLA TYPHIMURIUM, GEF, TOXIN, GTP- BINDING,             
KEYWDS   3 LIPOPROTEIN, PRENYLATION                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BUCHWALD,A.FRIEBEL,J.E.GALAN,W.D.HARDT,A.WITTINGHOFER,              
AUTHOR   2 K.SCHEFFZEK                                                          
REVDAT   3   24-FEB-09 1GZS    1       VERSN                                    
REVDAT   2   16-JAN-03 1GZS    1       DBREF                                    
REVDAT   1   12-SEP-02 1GZS    0                                                
JRNL        AUTH   G.BUCHWALD,A.FRIEBEL,J.E.GALAN,W.D.HARDT,                    
JRNL        AUTH 2 A.WITTINGHOFER,K.SCHEFFZEK                                   
JRNL        TITL   STRUCTURAL BASIS FOR THE REVERSIBLE ACTIVATION OF            
JRNL        TITL 2 A RHO PROTEIN BY THE BACTERIAL TOXIN SOPE                    
JRNL        REF    EMBO J.                       V.  21  3286 2002              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12093730                                                     
JRNL        DOI    10.1093/EMBOJ/CDF329                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5242854.30                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 40297                          
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 SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4012                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.8                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5943                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.230                        
REMARK   3   BIN FREE R VALUE                    : 0.274                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.0                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 659                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5308                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.0                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.34                                                
REMARK   3    B22 (A**2) : -1.34                                                
REMARK   3    B33 (A**2) : 2.69                                                 
REMARK   3    B12 (A**2) : 2.10                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.2                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.3                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.89                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.381516                                             
REMARK   3   BSOL        : 37.1614                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-JUN-02.                 
REMARK 100 THE PDBE ID CODE IS EBI-9921.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40507                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 58                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M (NH4)2SO4, 0.1 M SODIUM CITRATE    
REMARK 280  PH 5.6, 2% PEG400, 0.05 M BETAINE                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       66.83633            
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      133.67267            
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      133.67267            
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       66.83633            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     GLY D    76                                                      
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 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    LYS A  27      140.14    179.28                                   
REMARK 500    PRO A  29       87.83    -69.02                                   
REMARK 500    GLU A  31      -45.51     71.42                                   
REMARK 500    LYS A  96      -62.74   -132.78                                   
REMARK 500    LYS A 153      168.31    178.21                                   
REMARK 500    SER B  77      -92.58    -66.57                                   
REMARK 500    LEU B  78       82.84     38.46                                   
REMARK 500    ASP B  95       73.73     39.22                                   
REMARK 500    PRO C  29       85.93    -59.04                                   
REMARK 500    SER C  30     -104.37    -30.30                                   
REMARK 500    TYR C  32      123.79   -170.95                                   
REMARK 500    SER C  86       88.30   -151.06                                   
REMARK 500    LYS C  96      -64.34   -121.48                                   
REMARK 500    LYS C 131        6.90    -65.40                                   
REMARK 500    THR D  79      -16.27     52.83                                   
REMARK 500    THR D 239       79.62   -159.17                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A4R   RELATED DB: PDB                                   
REMARK 900  G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE                         
REMARK 900   IN THE GDP FORM                                                    
REMARK 900 RELATED ID: 1AJE   RELATED DB: PDB                                   
REMARK 900  CDC42 FROM HUMAN, NMR, 20 STRUCTURES                                
REMARK 900 RELATED ID: 1AN0   RELATED DB: PDB                                   
REMARK 900  CDC42HS-GDP COMPLEX                                                 
REMARK 900 RELATED ID: 1CEE   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH                         
REMARK 900   THE GTPASE BINDING DOMAIN OF WASP                                  
REMARK 900 RELATED ID: 1CF4   RELATED DB: PDB                                   
REMARK 900  CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX                             
REMARK 900 RELATED ID: 1DOA   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RHO FAMILY GTP-BINDING                             
REMARK 900  PROTEIN CDC42 INCOMPLEX WITH THE                                    
REMARK 900  MULTIFUNCTIONAL REGULATOR RHOGDI                                    
REMARK 900 RELATED ID: 1E0A   RELATED DB: PDB                                   
REMARK 900  CDC42 COMPLEXED WITH THE GTPASE BINDING                             
REMARK 900  DOMAIN OF P21 ACTIVATED KINASE                                      
REMARK 900 RELATED ID: 1EES   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH                        
REMARK 900  A PEPTIDE DERIVED FROM P-21 ACTIVATED                               
REMARK 900  KINASE, NMR, 20 STRUCTURES                                          
REMARK 900 RELATED ID: 1GRN   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3                        
REMARK 900   COMPLEX.                                                           
REMARK 900 RELATED ID: 1KI1   RELATED DB: PDB                                   
REMARK 900  GUANINE NUCLEOTIDE EXCHANGE REGION OF                               
REMARK 900  INTERSECTIN INCOMPLEX WITH CDC42                                    
REMARK 900 RELATED ID: 1KZ7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF                          
REMARK 900   MURINE DBS INCOMPLEX WITH THE PLACENTAL                            
REMARK 900  ISOFORM OF HUMAN CDC42                                              
REMARK 900 RELATED ID: 1KZG   RELATED DB: PDB                                   
REMARK 900  DBSCDC42(Y889F)                                                     
REMARK 900 RELATED ID: 2NGR   RELATED DB: PDB                                   
REMARK 900  TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS                         
REMARK 900  BY CDC42: COMPARISONS OF THE HIGH RESOLUTION                        
REMARK 900   STRUCTURES FOR CDC42 BOUND TO THE ACTIVE                           
REMARK 900  AND CATALYTICALLY COMPROMISED FORMS OF THE                          
REMARK 900  CDC42-GAP.                                                          
DBREF  1GZS A   -2    -1  PDB    1GZS     1GZS            -2     -1             
DBREF  1GZS A    1   178  UNP    P25763   G25P_HUMAN       1    178             
DBREF  1GZS B   76    77  PDB    1GZS     1GZS            76     77             
DBREF  1GZS B   78   240  UNP    O52623   O52623          78    240             
DBREF  1GZS C   -2    -1  PDB    1GZS     1GZS            -2     -1             
DBREF  1GZS C    1   178  UNP    P25763   G25P_HUMAN       1    178             
DBREF  1GZS D   76    77  PDB    1GZS     1GZS            76     77             
DBREF  1GZS D   78   240  UNP    O52623   O52623          78    240             
SEQRES   1 A  180  GLY SER MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP          
SEQRES   2 A  180  GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR          
SEQRES   3 A  180  THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE          
SEQRES   4 A  180  ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO          
SEQRES   5 A  180  TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 A  180  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP          
SEQRES   7 A  180  VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER SER          
SEQRES   8 A  180  PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR          
SEQRES   9 A  180  HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR          
SEQRES  10 A  180  GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS          
SEQRES  11 A  180  LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR          
SEQRES  12 A  180  ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR          
SEQRES  13 A  180  VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN          
SEQRES  14 A  180  VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU                  
SEQRES   1 B  165  GLY SER LEU THR ASN LYS VAL VAL LYS ASP PHE MET LEU          
SEQRES   2 B  165  GLN THR LEU ASN ASP ILE ASP ILE ARG GLY SER ALA SER          
SEQRES   3 B  165  LYS ASP PRO ALA TYR ALA SER GLN THR ARG GLU ALA ILE          
SEQRES   4 B  165  LEU SER ALA VAL TYR SER LYS ASN LYS ASP GLN CYS CYS          
SEQRES   5 B  165  ASN LEU LEU ILE SER LYS GLY ILE ASN ILE ALA PRO PHE          
SEQRES   6 B  165  LEU GLN GLU ILE GLY GLU ALA ALA LYS ASN ALA GLY LEU          
SEQRES   7 B  165  PRO GLY THR THR LYS ASN ASP VAL PHE THR PRO SER GLY          
SEQRES   8 B  165  ALA GLY ALA ASN PRO PHE ILE THR PRO LEU ILE SER SER          
SEQRES   9 B  165  ALA ASN SER LYS TYR PRO ARG MET PHE ILE ASN GLN HIS          
SEQRES  10 B  165  GLN GLN ALA SER PHE LYS ILE TYR ALA GLU LYS ILE ILE          
SEQRES  11 B  165  MET THR GLU VAL ALA PRO LEU PHE ASN GLU CYS ALA MET          
SEQRES  12 B  165  PRO THR PRO GLN GLN PHE GLN LEU ILE LEU GLU ASN ILE          
SEQRES  13 B  165  ALA ASN LYS TYR ILE GLN ASN THR PRO                          
SEQRES   1 C  180  GLY SER MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP          
SEQRES   2 C  180  GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR          
SEQRES   3 C  180  THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE          
SEQRES   4 C  180  ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO          
SEQRES   5 C  180  TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 C  180  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP          
SEQRES   7 C  180  VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER SER          
SEQRES   8 C  180  PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR          
SEQRES   9 C  180  HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR          
SEQRES  10 C  180  GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS          
SEQRES  11 C  180  LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR          
SEQRES  12 C  180  ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR          
SEQRES  13 C  180  VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN          
SEQRES  14 C  180  VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU                  
SEQRES   1 D  165  GLY SER LEU THR ASN LYS VAL VAL LYS ASP PHE MET LEU          
SEQRES   2 D  165  GLN THR LEU ASN ASP ILE ASP ILE ARG GLY SER ALA SER          
SEQRES   3 D  165  LYS ASP PRO ALA TYR ALA SER GLN THR ARG GLU ALA ILE          
SEQRES   4 D  165  LEU SER ALA VAL TYR SER LYS ASN LYS ASP GLN CYS CYS          
SEQRES   5 D  165  ASN LEU LEU ILE SER LYS GLY ILE ASN ILE ALA PRO PHE          
SEQRES   6 D  165  LEU GLN GLU ILE GLY GLU ALA ALA LYS ASN ALA GLY LEU          
SEQRES   7 D  165  PRO GLY THR THR LYS ASN ASP VAL PHE THR PRO SER GLY          
SEQRES   8 D  165  ALA GLY ALA ASN PRO PHE ILE THR PRO LEU ILE SER SER          
SEQRES   9 D  165  ALA ASN SER LYS TYR PRO ARG MET PHE ILE ASN GLN HIS          
SEQRES  10 D  165  GLN GLN ALA SER PHE LYS ILE TYR ALA GLU LYS ILE ILE          
SEQRES  11 D  165  MET THR GLU VAL ALA PRO LEU PHE ASN GLU CYS ALA MET          
SEQRES  12 D  165  PRO THR PRO GLN GLN PHE GLN LEU ILE LEU GLU ASN ILE          
SEQRES  13 D  165  ALA ASN LYS TYR ILE GLN ASN THR PRO                          
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  C 404       5                                                       
HET    SO4  C 406       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    6(O4 S 2-)                                                   
FORMUL  11  HOH   *160(H2 O1)                                                   
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 LEU A   67  TYR A   72  5                                   6    
HELIX    3   3 SER A   86  LYS A   96  1                                  11    
HELIX    4   4 LYS A   96  CYS A  105  1                                  10    
HELIX    5   5 GLN A  116  ARG A  120  5                                   5    
HELIX    6   6 ASP A  122  LYS A  131  1                                  10    
HELIX    7   7 THR A  138  LEU A  149  1                                  12    
HELIX    8   8 GLY A  164  GLU A  178  1                                  15    
HELIX    9   9 THR B   79  ASP B   95  1                                  17    
HELIX   10  10 ASP B   95  ASP B  103  1                                   9    
HELIX   11  11 ASP B  103  LYS B  133  1                                  31    
HELIX   12  12 ILE B  137  ALA B  151  1                                  15    
HELIX   13  13 PHE B  172  TYR B  184  1                                  13    
HELIX   14  14 PRO B  185  ILE B  189  5                                   5    
HELIX   15  15 ASN B  190  ALA B  210  1                                  21    
HELIX   16  16 PRO B  211  ASN B  214  5                                   4    
HELIX   17  17 THR B  220  GLN B  237  1                                  18    
HELIX   18  18 GLY C   15  ASN C   26  1                                  12    
HELIX   19  19 LEU C   67  TYR C   72  5                                   6    
HELIX   20  20 SER C   86  LYS C   96  1                                  11    
HELIX   21  21 LYS C   96  CYS C  105  1                                  10    
HELIX   22  22 GLN C  116  ARG C  120  5                                   5    
HELIX   23  23 ASP C  122  LYS C  131  1                                  10    
HELIX   24  24 THR C  138  LEU C  149  1                                  12    
HELIX   25  25 GLY C  164  LEU C  177  1                                  14    
HELIX   26  26 THR D   79  ASP D   95  1                                  17    
HELIX   27  27 ASP D   95  ASP D  103  1                                   9    
HELIX   28  28 ASP D  103  GLY D  134  1                                  32    
HELIX   29  29 ILE D  137  ALA D  151  1                                  15    
HELIX   30  30 PHE D  172  TYR D  184  1                                  13    
HELIX   31  31 PRO D  185  ILE D  189  5                                   5    
HELIX   32  32 ASN D  190  ALA D  210  1                                  21    
HELIX   33  33 PRO D  211  ASN D  214  5                                   4    
HELIX   34  34 THR D  220  GLN D  237  1                                  18    
SHEET    1  AA 6 ALA A  41  ILE A  46  0                                        
SHEET    2  AA 6 GLU A  49  PHE A  56 -1  O  GLU A  49   N  ILE A  46           
SHEET    3  AA 6 GLN A   2  GLY A  10  1  O  GLN A   2   N  THR A  52           
SHEET    4  AA 6 VAL A  77  SER A  83  1  O  VAL A  77   N  VAL A   7           
SHEET    5  AA 6 PHE A 110  THR A 115  1  O  LEU A 111   N  VAL A  80           
SHEET    6  AA 6 TYR A 154  GLU A 156  1  O  VAL A 155   N  GLY A 114           
SHEET    1  BA 2 GLY B 155  LYS B 158  0                                        
SHEET    2  BA 2 VAL B 161  PRO B 164 -1  O  VAL B 161   N  LYS B 158           
SHEET    1  CA 6 ALA C  41  ILE C  46  0                                        
SHEET    2  CA 6 GLU C  49  PHE C  56 -1  O  GLU C  49   N  ILE C  46           
SHEET    3  CA 6 GLN C   2  VAL C   9  1  O  GLN C   2   N  THR C  52           
SHEET    4  CA 6 VAL C  77  SER C  83  1  O  VAL C  77   N  VAL C   7           
SHEET    5  CA 6 PHE C 110  THR C 115  1  O  LEU C 111   N  VAL C  80           
SHEET    6  CA 6 TYR C 154  GLU C 156  1  O  VAL C 155   N  GLY C 114           
SHEET    1  DA 2 GLY D 155  LYS D 158  0                                        
SHEET    2  DA 2 VAL D 161  PRO D 164 -1  O  VAL D 161   N  LYS D 158           
SITE     1 AC1  5 GLU A  62  ASP A  63  ARG A  68  LYS A  96                    
SITE     2 AC1  5 ARG D 186                                                     
SITE     1 AC2  4 HIS A 104  CYS A 105  LYS A 107  THR A 108                    
SITE     1 AC3  9 ASP A  11  GLY A  12  ALA A  13  VAL A  14                    
SITE     2 AC3  9 GLY A  15  LYS A  16  THR A  17  ALA A  59                    
SITE     3 AC3  9 HOH A2038                                                     
SITE     1 AC4  3 SER A  86  PRO A  87  SER A  88                               
SITE     1 AC5  8 ASP C  11  GLY C  12  ALA C  13  VAL C  14                    
SITE     2 AC5  8 GLY C  15  LYS C  16  THR C  17  ALA C  59                    
SITE     1 AC6  5 HIS C 104  CYS C 105  PRO C 106  LYS C 107                    
SITE     2 AC6  5 THR C 108                                                     
CRYST1   87.545   87.545  200.509  90.00  90.00 120.00 P 31 2 1     12          
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      0.011423  0.006595  0.000000        0.00000                         
SCALE2      0.000000  0.013190  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004987        0.00000                         
MTRIX1   1  0.367580 -0.263080  0.892000      -96.45638    1                    
MTRIX2   1  0.168370 -0.924480 -0.342040      136.63788    1                    
MTRIX3   1  0.914620  0.275910 -0.295520       56.71050    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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