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Database: PDB
Entry: 3GCG
LinkDB: 3GCG
Original site: 3GCG 
HEADER    SIGNALING PROTEIN/TRANSCRIPTION         22-FEB-09   3GCG              
TITLE     CRYSTAL STRUCTURE OF MAP AND CDC42 COMPLEX                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2-178;                                        
COMPND   5 SYNONYM: CDC42, G25K GTP-BINDING PROTEIN;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: L0028 (MITOCHONDRIA ASSOCIATED PROTEIN);                   
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 37-203;                                       
COMPND  11 SYNONYM: MAP;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PGEX6P-1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: PGEX6P-1                                   
KEYWDS    MAP, CDC42, COMPLEX, ALTERNATIVE SPLICING, CELL MEMBRANE,             
KEYWDS   2 GTP-BINDING, LIPOPROTEIN, MEMBRANE, METHYLATION,                     
KEYWDS   3 NUCLEOTIDE-BINDING, PRENYLATION CDC42, SIGNALING                     
KEYWDS   4 PROTEIN/TRANSCRIPTION COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.CHAI,Z.HUANG,Y.FENG,X.WU                                            
REVDAT   2   27-OCT-09 3GCG    1       JRNL                                     
REVDAT   1   21-JUL-09 3GCG    0                                                
JRNL        AUTH   Z.HUANG,S.E.SUTTON,A.J.WALLENFANG,R.C.ORCHARD,X.WU,          
JRNL        AUTH 2 Y.FENG,J.CHAI,N.M.ALTO                                       
JRNL        TITL   STRUCTURAL INSIGHTS INTO HOST GTPASE ISOFORM                 
JRNL        TITL 2 SELECTION BY A FAMILY OF BACTERIAL GEF MIMICS                
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   853 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19620963                                                     
JRNL        DOI    10.1038/NSMB.1647                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 388.000                        
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 15451                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 755                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2581                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.83500                                             
REMARK   3    B22 (A**2) : 4.58100                                              
REMARK   3    B33 (A**2) : 3.25400                                              
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 47.24                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GCG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051689.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15835                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SIR                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 10% PEG 6000, 5%      
REMARK 280  MPD, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.81500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.76000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.51500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.76000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.81500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.51500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     MET B    38                                                      
REMARK 465     ARG B    39                                                      
REMARK 465     PHE B    40                                                      
REMARK 465     MET B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     VAL B    43                                                      
REMARK 465     GLN B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     GLN B   199                                                      
REMARK 465     ASP B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     ARG B   202                                                      
REMARK 465     LEU B   203                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   146     NH1  ARG B   158              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 154   N   -  CA  -  C   ANGL. DEV. = -18.2 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       14.11     56.27                                   
REMARK 500    THR A  25       39.79    -85.16                                   
REMARK 500    VAL A  85       34.17    -99.08                                   
REMARK 500    SER A  86       84.73   -150.54                                   
REMARK 500    LYS A  96      -50.39   -125.23                                   
REMARK 500    ASP A 121       42.19    -99.90                                   
REMARK 500    LYS A 128       38.13    -80.43                                   
REMARK 500    LEU A 129      -34.02   -139.18                                   
REMARK 500    LYS A 131      -72.38    -74.07                                   
REMARK 500    ASN A 132       33.68    -69.20                                   
REMARK 500    THR B  66     -129.23   -103.48                                   
REMARK 500    ARG B  67      -34.00   -149.04                                   
REMARK 500    ALA B 127      -11.96   -161.31                                   
REMARK 500    VAL B 153       64.60   -154.33                                   
REMARK 500    PHE B 181      145.92    176.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 246        DISTANCE =  5.18 ANGSTROMS                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF ENTITY 1 BASED ON ISOFORM 2 OF UNIPROTKB/SWISS-      
REMARK 999 PROT P60953 (CDC42_HUMAN). R163K IS ALTERNATIVE SEQUENCE OF          
REMARK 999 CDC42_HUMAN.                                                         
DBREF  3GCG A    2   178  UNP    P60953   CDC42_HUMAN      2    178             
DBREF  3GCG B   37   203  UNP    Q9R8E4   Q9R8E4_ECOLX    37    203             
SEQADV 3GCG GLY A   -3  UNP  P60953              EXPRESSION TAG                 
SEQADV 3GCG PRO A   -2  UNP  P60953              EXPRESSION TAG                 
SEQADV 3GCG LEU A   -1  UNP  P60953              EXPRESSION TAG                 
SEQADV 3GCG GLY A    0  UNP  P60953              EXPRESSION TAG                 
SEQADV 3GCG SER A    1  UNP  P60953              EXPRESSION TAG                 
SEQADV 3GCG LYS A  163  UNP  P60953    ARG   163 SEE REMARK 999                 
SEQADV 3GCG GLY B   32  UNP  Q9R8E4              EXPRESSION TAG                 
SEQADV 3GCG PRO B   33  UNP  Q9R8E4              EXPRESSION TAG                 
SEQADV 3GCG LEU B   34  UNP  Q9R8E4              EXPRESSION TAG                 
SEQADV 3GCG GLY B   35  UNP  Q9R8E4              EXPRESSION TAG                 
SEQADV 3GCG SER B   36  UNP  Q9R8E4              EXPRESSION TAG                 
SEQRES   1 A  182  GLY PRO LEU GLY SER GLN THR ILE LYS CYS VAL VAL VAL          
SEQRES   2 A  182  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 A  182  TYR THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR          
SEQRES   4 A  182  VAL PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY          
SEQRES   5 A  182  GLU PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN          
SEQRES   6 A  182  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 A  182  THR ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO          
SEQRES   8 A  182  SER SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU          
SEQRES   9 A  182  ILE THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL          
SEQRES  10 A  182  GLY THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE          
SEQRES  11 A  182  GLU LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO          
SEQRES  12 A  182  GLU THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL          
SEQRES  13 A  182  LYS TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU          
SEQRES  14 A  182  LYS ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU          
SEQRES   1 B  172  GLY PRO LEU GLY SER GLY MET ARG PHE MET PRO VAL GLN          
SEQRES   2 B  172  SER ASN PHE VAL ILE ASN HIS GLY LYS LEU THR ASN GLN          
SEQRES   3 B  172  LEU LEU GLN ALA VAL ALA LYS GLN THR ARG ASN GLY ASP          
SEQRES   4 B  172  THR GLN GLN TRP PHE GLN GLN GLU GLN THR THR TYR ILE          
SEQRES   5 B  172  SER ARG THR VAL ASN ARG THR LEU ASP ASP TYR CYS ARG          
SEQRES   6 B  172  SER ASN ASN SER VAL ILE SER LYS GLU THR LYS GLY HIS          
SEQRES   7 B  172  ILE PHE ARG ALA VAL GLU ASN ALA LEU GLN GLN PRO LEU          
SEQRES   8 B  172  ASP MET ASN GLY ALA GLN SER SER ILE GLY HIS PHE LEU          
SEQRES   9 B  172  GLN SER ASN LYS TYR PHE ASN GLN LYS VAL ASP GLU GLN          
SEQRES  10 B  172  CYS GLY LYS ARG VAL ASP PRO ILE THR ARG PHE ASN THR          
SEQRES  11 B  172  GLN THR LYS MET ILE GLU GLN VAL SER GLN GLU ILE PHE          
SEQRES  12 B  172  GLU ARG ASN PHE SER GLY PHE LYS VAL SER GLU ILE LYS          
SEQRES  13 B  172  ALA ILE THR GLN ASN ALA ILE LEU GLU HIS VAL GLN ASP          
SEQRES  14 B  172  THR ARG LEU                                                  
FORMUL   3  HOH   *186(H2 O)                                                    
HELIX    1   1 GLY A   15  THR A   25  1                                  11    
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 ASP A  122  LYS A  128  1                                   7    
HELIX    6   6 THR A  138  LEU A  149  1                                  12    
HELIX    7   7 GLY A  164  LEU A  177  1                                  14    
HELIX    8   8 ASN B   50  LYS B   64  1                                  15    
HELIX    9   9 THR B   71  ASN B   99  1                                  29    
HELIX   10  10 SER B  103  GLN B  119  1                                  17    
HELIX   11  11 SER B  129  SER B  137  1                                   9    
HELIX   12  12 ASN B  138  GLY B  150  1                                  13    
HELIX   13  13 ASP B  154  PHE B  178  1                                  25    
HELIX   14  14 LYS B  182  VAL B  198  1                                  17    
SHEET    1   A 6 TYR A  40  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  ASP A  57 -1  O  TYR A  51   N  VAL A  44           
SHEET    3   A 6 THR A   3  GLY A  10  1  N  ILE A   4   O  GLY A  54           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  CYS A  81   N  VAL A   9           
SHEET    5   A 6 PHE A 110  THR A 115  1  O  VAL A 113   N  VAL A  80           
SHEET    6   A 6 TYR A 154  GLU A 156  1  O  VAL A 155   N  LEU A 112           
CRYST1   41.630   83.030   99.520  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024021  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012044  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010048        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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