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Database: PDB
Entry: 1DOA
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Original site: 1DOA 
HEADER    CELL CYCLE                              20-DEC-99   1DOA              
TITLE     STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH 
TITLE    2 THE MULTIFUNCTIONAL REGULATOR RHOGDI                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GTP-BINDING PROTEIN);                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CDC42;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN (GDP-DISSOCIATION INHIBITOR 1);                    
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: RHO GDI 1;                                                  
COMPND  10 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: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL: SF9 CELLS;                                   
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: CATTLE;                                             
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PGEX-KG                                   
KEYWDS    GTP-BINDING PROTEIN, CDC42, RHOGDI, CELL CYCLE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.R.HOFFMAN,N.NASSAR,R.C.CERIONE                                      
REVDAT   4   31-AUG-11 1DOA    1       HETATM VERSN                             
REVDAT   3   24-FEB-09 1DOA    1       VERSN                                    
REVDAT   2   01-APR-03 1DOA    1       JRNL                                     
REVDAT   1   09-FEB-00 1DOA    0                                                
JRNL        AUTH   G.R.HOFFMAN,N.NASSAR,R.A.CERIONE                             
JRNL        TITL   STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN     
JRNL        TITL 2 COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI.           
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 100   345 2000              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10676816                                                     
JRNL        DOI    10.1016/S0092-8674(00)80670-4                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1370695.270                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15437                          
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) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.320                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1563                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2344                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4570                       
REMARK   3   BIN FREE R VALUE                    : 0.4610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 241                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3101                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 50                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.52                            
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) : 0.58                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.66                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.28                            
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        : 0.20                                                 
REMARK   3   BSOL        : 20.02                                                
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.PARAM                                  
REMARK   3  PARAMETER FILE  2  : GDP_UPPSALA.PAR                                
REMARK   3  PARAMETER FILE  3  : CARB.PAR                                       
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : GDP_UPPSALA.TOP                                
REMARK   3  TOPOLOGY FILE  3   : CARB.TOP                                       
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DOA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010246.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 56.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000,   100 MM GLUTAMIC ACID,    
REMARK 280  25 MM MGSO4, 50 MM TRIS, 2 MM NAN3, 2 MM LDAO , PH 7.4, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 18K, TEMPERATURE 291K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.97000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.23139            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.72000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       41.97000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       24.23139            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       63.72000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       41.97000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       24.23139            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.72000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.46278            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      127.44000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       48.46278            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      127.44000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       48.46278            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      127.44000            
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 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: 5010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20880 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000      125.91000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -72.69417            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      125.91000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       72.69417            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 200  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     PRO B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     ILE B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     ILE B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B   5    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
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    PRO A 180   C   -  N   -  CA  ANGL. DEV. =   9.4 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    ALA A  13        5.56     58.18                                   
REMARK 500    ASN A  26      -16.04     79.42                                   
REMARK 500    SER A  30      -70.51    -68.31                                   
REMARK 500    GLU A  31      -78.37    -81.88                                   
REMARK 500    VAL A  85       30.75    -88.57                                   
REMARK 500    SER A  86       88.35   -154.29                                   
REMARK 500    LYS A  96      -64.07    -92.67                                   
REMARK 500    PRO A 106      -73.67    -44.76                                   
REMARK 500    GLN A 116       73.09     60.44                                   
REMARK 500    PRO A 123      -84.42    -48.76                                   
REMARK 500    LEU A 129      -75.26    -74.75                                   
REMARK 500    ASN A 132       33.84    -83.73                                   
REMARK 500    LYS A 150       35.50     70.55                                   
REMARK 500    LYS A 153     -177.95   -171.75                                   
REMARK 500    GLN A 162       22.37     47.07                                   
REMARK 500    GLU A 181       90.48     76.58                                   
REMARK 500    PRO A 182      -76.22    -34.63                                   
REMARK 500    LYS A 184       56.82   -108.94                                   
REMARK 500    ALA B   8     -138.44   -124.06                                   
REMARK 500    ALA B  15       40.17    -67.73                                   
REMARK 500    ALA B  16       36.98    -87.58                                   
REMARK 500    GLU B  17      -81.10   -145.26                                   
REMARK 500    ASN B  18     -135.19     34.03                                   
REMARK 500    GLU B  20       -7.59    179.43                                   
REMARK 500    HIS B  23       74.58     -0.53                                   
REMARK 500    LYS B  28      103.06    100.23                                   
REMARK 500    ASP B  42       62.09   -151.95                                   
REMARK 500    VAL B  59     -168.36     55.10                                   
REMARK 500    ALA B  60       86.07     72.08                                   
REMARK 500    SER B  62     -133.39    -88.55                                   
REMARK 500    PRO B  65      -82.27    -63.97                                   
REMARK 500    LEU B  90       36.72    -70.82                                   
REMARK 500    LYS B  99       26.94   -150.61                                   
REMARK 500    ASN B 119      -62.49   -106.58                                   
REMARK 500    ARG B 120      -60.99   -104.06                                   
REMARK 500    GLU B 121     -163.37   -104.59                                   
REMARK 500    LEU B 170      -90.64   -123.73                                   
REMARK 500    THR B 182     -157.84   -117.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 154         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TRP A  97        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A 200  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   0   ND1                                                    
REMARK 620 2 HOH A 709   O    87.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 199  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  17   OG1                                                    
REMARK 620 2 THR A  35   O    84.4                                              
REMARK 620 3 HOH A 749   O    71.6  66.7                                        
REMARK 620 4 GDP A 198   O2B  74.0 125.2  58.8                                  
REMARK 620 5 HOH A 701   O   136.8  73.2  65.8  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 199                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 198                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GER A 952                 
DBREF  1DOA A    1   188  UNP    P60953   CDC42_HUMAN      1    188             
DBREF  1DOA B    1   204  UNP    P19803   GDIR_BOVIN       1    204             
SEQADV 1DOA GLY A   -2  UNP  P60953              SEE REMARK 999                 
SEQADV 1DOA SER A   -1  UNP  P60953              SEE REMARK 999                 
SEQADV 1DOA HIS A    0  UNP  P60953              SEE REMARK 999                 
SEQADV 1DOA CMT A  188  UNP  P60953    CYS   188 MODIFIED RESIDUE               
SEQADV 1DOA GLY B  -14  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA SER B  -13  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA PRO B  -12  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B  -11  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA ILE B  -10  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA SER B   -9  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -8  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -7  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -6  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -5  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -4  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA ILE B   -3  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA LEU B   -2  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA GLY B   -1  UNP  P19803              SEE REMARK 999                 
SEQADV 1DOA LEU B    0  UNP  P19803              SEE REMARK 999                 
SEQRES   1 A  191  GLY SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 A  191  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 A  191  THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL          
SEQRES   4 A  191  PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU          
SEQRES   5 A  191  PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU          
SEQRES   6 A  191  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 A  191  ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER          
SEQRES   8 A  191  SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE          
SEQRES   9 A  191  THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY          
SEQRES  10 A  191  THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU          
SEQRES  11 A  191  LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU          
SEQRES  12 A  191  THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS          
SEQRES  13 A  191  TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS          
SEQRES  14 A  191  ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO          
SEQRES  15 A  191  PRO GLU PRO LYS LYS SER ARG ARG CMT                          
SEQRES   1 B  219  GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU          
SEQRES   2 B  219  GLY LEU MET ALA GLU GLN GLU PRO THR ALA GLU GLN LEU          
SEQRES   3 B  219  ALA GLN ILE ALA ALA GLU ASN GLU GLU ASP GLU HIS SER          
SEQRES   4 B  219  VAL ASN TYR LYS PRO PRO ALA GLN LYS SER ILE GLN GLU          
SEQRES   5 B  219  ILE GLN GLU LEU ASP LYS ASP ASP GLU SER LEU ARG LYS          
SEQRES   6 B  219  TYR LYS GLU ALA LEU LEU GLY ARG VAL ALA VAL SER ALA          
SEQRES   7 B  219  ASP PRO ASN VAL PRO ASN VAL VAL VAL THR ARG LEU THR          
SEQRES   8 B  219  LEU VAL CYS SER THR ALA PRO GLY PRO LEU GLU LEU ASP          
SEQRES   9 B  219  LEU THR GLY ASP LEU GLU SER PHE LYS LYS GLN SER PHE          
SEQRES  10 B  219  VAL LEU LYS GLU GLY VAL GLU TYR ARG ILE LYS ILE SER          
SEQRES  11 B  219  PHE ARG VAL ASN ARG GLU ILE VAL SER GLY MET LYS TYR          
SEQRES  12 B  219  ILE GLN HIS THR TYR ARG LYS GLY VAL LYS ILE ASP LYS          
SEQRES  13 B  219  THR ASP TYR MET VAL GLY SER TYR GLY PRO ARG ALA GLU          
SEQRES  14 B  219  GLU TYR GLU PHE LEU THR PRO MET GLU GLU ALA PRO LYS          
SEQRES  15 B  219  GLY MET LEU ALA ARG GLY SER TYR ASN ILE LYS SER ARG          
SEQRES  16 B  219  PHE THR ASP ASP ASP ARG THR ASP HIS LEU SER TRP GLU          
SEQRES  17 B  219  TRP ASN LEU THR ILE LYS LYS GLU TRP LYS ASP                  
MODRES 1DOA CMT A  188  CYS  O-METHYLCYSTEINE                                   
HET    CMT  A 188       8                                                       
HET     MG  A 199       1                                                       
HET     MG  A 200       1                                                       
HET    GDP  A 198      28                                                       
HET    GER  A 952      20                                                       
HETNAM     CMT O-METHYLCYSTEINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     GER GERAN-8-YL GERAN                                                 
FORMUL   1  CMT    C4 H9 N O2 S                                                 
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  GER    C20 H34                                                      
FORMUL   7  HOH   *50(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 ILE A  117  ASP A  121  5                                   5    
HELIX    7   7 ASP A  122  ALA A  130  1                                   9    
HELIX    8   8 THR A  138  LYS A  150  1                                  13    
HELIX    9   9 GLY A  164  GLU A  178  1                                  15    
HELIX   10  10 SER B   34  LEU B   41  1                                   8    
HELIX   11  11 ASP B   45  GLY B   57  1                                  13    
HELIX   12  12 LEU B   94  GLN B  100  5                                   7    
SHEET    1   A 6 TYR A  40  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  PHE A  56 -1  N  GLU A  49   O  ILE A  46           
SHEET    3   A 6 GLN A   2  VAL A   9  1  O  GLN A   2   N  THR A  52           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  VAL A  77   N  VAL A   7           
SHEET    5   A 6 PHE A 110  THR A 115  1  O  LEU A 111   N  VAL A  80           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LYS A 153   N  LEU A 112           
SHEET    1   B 4 GLU B  87  ASP B  89  0                                        
SHEET    2   B 4 ARG B  74  VAL B  78 -1  N  LEU B  75   O  LEU B  88           
SHEET    3   B 4 GLU B 109  PHE B 116 -1  O  ARG B 111   N  VAL B  78           
SHEET    4   B 4 TYR B 156  LEU B 159 -1  N  TYR B 156   O  PHE B 116           
SHEET    1   C 4 GLU B  87  ASP B  89  0                                        
SHEET    2   C 4 ARG B  74  VAL B  78 -1  N  LEU B  75   O  LEU B  88           
SHEET    3   C 4 GLU B 109  PHE B 116 -1  O  ARG B 111   N  VAL B  78           
SHEET    4   C 4 GLU B 163  GLU B 164 -1  O  GLU B 163   N  TYR B 110           
SHEET    1   D 5 PHE B 102  LYS B 105  0                                        
SHEET    2   D 5 LEU B 190  LYS B 199  1  O  ASN B 195   N  PHE B 102           
SHEET    3   D 5 SER B 174  THR B 182 -1  N  TYR B 175   O  LEU B 196           
SHEET    4   D 5 VAL B 123  ARG B 134 -1  N  LYS B 127   O  THR B 182           
SHEET    5   D 5 VAL B 137  TYR B 149 -1  O  VAL B 137   N  ARG B 134           
LINK         SG  CMT A 188                 C1  GER A 952     1555   1555  1.82  
LINK         C   ARG A 187                 N   CMT A 188     1555   1555  1.33  
LINK         ND1 HIS A   0                MG    MG A 200     1555   1555  1.81  
LINK         OG1 THR A  17                MG    MG A 199     1555   1555  2.13  
LINK         O   THR A  35                MG    MG A 199     1555   1555  2.29  
LINK        MG    MG A 199                 O   HOH A 749     1555   1555  2.06  
LINK        MG    MG A 199                 O2B GDP A 198     1555   1555  2.60  
LINK        MG    MG A 199                 O   HOH A 701     1555   1555  2.89  
LINK        MG    MG A 200                 O   HOH A 709     1555   1555  2.90  
SITE     1 AC1  6 THR A  17  THR A  35  ASP A  57  GDP A 198                    
SITE     2 AC1  6 HOH A 701  HOH A 749                                          
SITE     1 AC2  2 HIS A   0  HOH A 709                                          
SITE     1 AC3 17 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC3 17 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC3 17 VAL A  33  GLN A 116  ASP A 118  SER A 158                    
SITE     4 AC3 17 ALA A 159  LEU A 160   MG A 199  HOH A 701                    
SITE     5 AC3 17 HOH A 749                                                     
SITE     1 AC4 11 ARG A 186  CMT A 188  ILE B  14  LEU B  75                    
SITE     2 AC4 11 TYR B 110  GLN B 130  THR B 132  ASP B 140                    
SITE     3 AC4 11 ALA B 171  TRP B 194  LEU B 196                               
CRYST1   83.940   83.940  191.160  90.00  90.00 120.00 H 3           9          
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      0.011913  0.006878  0.000000        0.00000                         
SCALE2      0.000000  0.013756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005231        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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