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Database: PDB
Entry: 1E96
LinkDB: 1E96
Original site: 1E96 
HEADER    SIGNALING PROTEIN                       10-OCT-00   1E96              
TITLE     STRUCTURE OF THE RAC/P67PHOX COMPLEX                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RAC1;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 2 (NCF-2) TPR DOMAIN,            
COMPND   9  RESIDUES 1-203;                                                     
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: YES;                                                       
COMPND  12 SYNONYM: P67PHOX;                                                    
COMPND  13 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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX-4T                                   
KEYWDS    SIGNALING PROTEIN, SIGNALLING COMPLEX, GTPASE, NADPH                  
KEYWDS   2 OXIDASE, PROTEIN-PROTEIN COMPLEX, TPR MOTIF                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.LAPOUGE,S.J.M.SMITH,P.A.WALKER,S.J.GAMBLIN,S.J.SMERDON,             
AUTHOR   2 K.RITTINGER                                                          
REVDAT   2   24-FEB-09 1E96    1       VERSN                                    
REVDAT   1   17-NOV-00 1E96    0                                                
JRNL        AUTH   K.LAPOUGE,S.J.M.SMTIH,P.A.WALKER,S.J.GAMBLIN,                
JRNL        AUTH 2 S.J.SMERDON,K.RITTINGER                                      
JRNL        TITL   STRUCTURE OF THE TPR DOMAIN OF P67PHOX IN COMPLEX            
JRNL        TITL 2 WITH RAC.GTP                                                 
JRNL        REF    MOL.CELL                      V.   6   899 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11090627                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.4  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18798                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2889                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 77                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64                                                 
REMARK   3    B22 (A**2) : 0.64                                                 
REMARK   3    B33 (A**2) : -0.96                                                
REMARK   3    B12 (A**2) : 0.32                                                 
REMARK   3    B13 (A**2) : 00                                                   
REMARK   3    B23 (A**2) : 00                                                   
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.411         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.288         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.01  ; 0.022               
REMARK   3    ANGLE DISTANCE                  (A) : 1.39  ; 1.98                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.736 ; 1.5                  
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.406 ; 2                    
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.923 ; 3                    
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.269 ; 4.5                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E96 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5419.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 10.50                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX7.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 123873                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1MH1, 1A17                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 54.6                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CAPS PH 10.5,                      
REMARK 280  0.2 M LI ACETATE, 0.8 M NAH2PO4, 1.2 M K2HPO4                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-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       92.35333            
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       46.17667            
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       46.17667            
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       92.35333            
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 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CHAIN A ENGINEERED MUTATION MET1PRO, GLN61LEU                       
REMARK 400  RAC1 ARE GTP-BINDING PROTEINS ASSOCIATED WITH PLASMA MEMBRANE       
REMARK 400  WHICH COULD REGULATE SECRETORY PROCESSES.                           
REMARK 400  THE NCF2 IS INVOLVED IN  ACTIVATION OF THE LATENT NADPH OXIDASE     
REMARK 400  IN ASSOCIATION WITH NCF1, AND A MEMBRANE BOUND CYTOCHROME B558      
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     VAL A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     ARG A   185                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     ARG A   187                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     CYS A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   187                                                      
REMARK 465     ARG B   188                                                      
REMARK 465     GLN B   189                                                      
REMARK 465     VAL B   190                                                      
REMARK 465     ALA B   191                                                      
REMARK 465     GLN B   192                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     ALA B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     LYS B   196                                                      
REMARK 465     ASP B   197                                                      
REMARK 465     TYR B   198                                                      
REMARK 465     LEU B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ALA B   202                                                      
REMARK 465     THR B   203                                                      
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     SER B   2    OG                                                  
REMARK 470     ASN B 186    O    CG   OD1  ND2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS A   178  -  O    HOH A  2042              2.04            
REMARK 500   OE1  GLU B    85  -  OH   TYR B    87              1.99            
REMARK 500   O    GLY B   103  -  O    HOH B  2017              2.15            
REMARK 500   O    GLU B   164  -  O    HOH B  2032              1.71            
REMARK 500   O    HOH B  2001  -  O    HOH B  2004              1.75            
REMARK 500   O    HOH B  2007  -  O    HOH B  2019              1.90            
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 A  38   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A  47   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 118   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B  21   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B  34   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 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 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    ASN A  26       -6.65     73.11                                   
REMARK 500    LYS A  96      -57.13   -130.30                                   
REMARK 500    ASN A 107      -39.84     81.29                                   
REMARK 500    GLU B 135       -1.89     74.56                                   
REMARK 500    LYS B 158        1.04    -63.21                                   
REMARK 500    PRO B 185      -67.36    -26.21                                   
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 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    TYR A  72        25.0      L          L   OUTSIDE RANGE           
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 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 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  17   OG1                                                    
REMARK 620 2 THR A  35   OG1  96.0                                              
REMARK 620 3 GTP A 200   O3G 162.6  76.2                                        
REMARK 620 4 GTP A 200   O2B  92.5 170.5  94.5                                  
REMARK 620 5 HOH A2008   O    89.9  91.1  74.9  84.6                            
REMARK 620 6 HOH A2009   O    92.8  79.3 100.8 104.6 170.3                      
REMARK 620 N                    1     2     3     4     5                       
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 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MH1   RELATED DB: PDB                                   
REMARK 900  SMALL G-PROTEIN                                                     
REMARK 900 RELATED ID: 1A17   RELATED DB: PDB                                   
REMARK 900  TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5                  
DBREF  1E96 A    1   192  UNP    P15154   RAC1_HUMAN       1    192             
DBREF  1E96 B    1   203  UNP    P19878   NCF2_HUMAN       1    203             
SEQADV 1E96 PRO A    1  UNP  P15154    MET     1 CLONING ARTEFACT               
SEQADV 1E96 LEU A   61  UNP  P15154    GLN    61 ENGINEERED                     
SEQRES   1 A  192  PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  192  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  192  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  192  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  192  LEU GLY LEU TRP ASP THR ALA GLY LEU GLU ASP TYR ASP          
SEQRES   6 A  192  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 A  192  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  192  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  192  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  192  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  192  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  192  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  192  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  192  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 A  192  LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU                      
SEQRES   1 B  203  MET SER LEU VAL GLU ALA ILE SER LEU TRP ASN GLU GLY          
SEQRES   2 B  203  VAL LEU ALA ALA ASP LYS LYS ASP TRP LYS GLY ALA LEU          
SEQRES   3 B  203  ASP ALA PHE SER ALA VAL GLN ASP PRO HIS SER ARG ILE          
SEQRES   4 B  203  CYS PHE ASN ILE GLY CYS MET TYR THR ILE LEU LYS ASN          
SEQRES   5 B  203  MET THR GLU ALA GLU LYS ALA PHE THR ARG SER ILE ASN          
SEQRES   6 B  203  ARG ASP LYS HIS LEU ALA VAL ALA TYR PHE GLN ARG GLY          
SEQRES   7 B  203  MET LEU TYR TYR GLN THR GLU LYS TYR ASP LEU ALA ILE          
SEQRES   8 B  203  LYS ASP LEU LYS GLU ALA LEU ILE GLN LEU ARG GLY ASN          
SEQRES   9 B  203  GLN LEU ILE ASP TYR LYS ILE LEU GLY LEU GLN PHE LYS          
SEQRES  10 B  203  LEU PHE ALA CYS GLU VAL LEU TYR ASN ILE ALA PHE MET          
SEQRES  11 B  203  TYR ALA LYS LYS GLU GLU TRP LYS LYS ALA GLU GLU GLN          
SEQRES  12 B  203  LEU ALA LEU ALA THR SER MET LYS SER GLU PRO ARG HIS          
SEQRES  13 B  203  SER LYS ILE ASP LYS ALA MET GLU CYS VAL TRP LYS GLN          
SEQRES  14 B  203  LYS LEU TYR GLU PRO VAL VAL ILE PRO VAL GLY LYS LEU          
SEQRES  15 B  203  PHE ARG PRO ASN GLU ARG GLN VAL ALA GLN LEU ALA LYS          
SEQRES  16 B  203  LYS ASP TYR LEU GLY LYS ALA THR                              
HET     MG  A 201       1                                                       
HET    GTP  A 200      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GTP    C10 H16 N5 O14 P3                                            
FORMUL   5  HOH   *77(H2 O1)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 LEU 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 LYS A  116  ASP A  121  5                                   6    
HELIX    7   7 ASP A  122  LYS A  132  1                                  11    
HELIX    8   8 THR A  138  ILE A  149  1                                  12    
HELIX    9   9 GLY A  164  CYS A  178  1                                  15    
HELIX   10  10 SER B    2  LYS B   19  1                                  18    
HELIX   11  11 ASP B   21  ALA B   31  1                                  11    
HELIX   12  12 HIS B   36  LEU B   50  1                                  15    
HELIX   13  13 ASN B   52  ASP B   67  1                                  16    
HELIX   14  14 LEU B   70  THR B   84  1                                  15    
HELIX   15  15 LYS B   86  GLN B  100  1                                  15    
HELIX   16  16 LYS B  110  GLY B  113  5                                   4    
HELIX   17  17 ALA B  120  LYS B  134  1                                  15    
HELIX   18  18 GLU B  136  MET B  150  1                                  15    
HELIX   19  19 GLU B  153  HIS B  156  5                                   4    
HELIX   20  20 SER B  157  TRP B  167  1                                  11    
SHEET    1   A 6 LYS A 153  GLU A 156  0                                        
SHEET    2   A 6 PRO A 109  THR A 115  1  N  LEU A 112   O  LYS A 153           
SHEET    3   A 6 VAL A  77  SER A  83  1  N  PHE A  78   O  PRO A 109           
SHEET    4   A 6 GLN A   2  GLY A  10  1  N  VAL A   7   O  VAL A  77           
SHEET    5   A 6 LYS A  49  THR A  58  1  N  ASN A  52   O  GLN A   2           
SHEET    6   A 6 PHE A  37  VAL A  46 -1  N  VAL A  46   O  LYS A  49           
SHEET    1   B 2 LEU B 106  ASP B 108  0                                        
SHEET    2   B 2 LYS B 117  PHE B 119 -1  N  LEU B 118   O  ILE B 107           
LINK        MG    MG A 201                 OG1 THR A  17     1555   1555  2.18  
LINK        MG    MG A 201                 OG1 THR A  35     1555   1555  2.16  
LINK        MG    MG A 201                 O3G GTP A 200     1555   1555  2.16  
LINK        MG    MG A 201                 O2B GTP A 200     1555   1555  2.16  
LINK        MG    MG A 201                 O   HOH A2008     1555   1555  2.29  
LINK        MG    MG A 201                 O   HOH A2009     1555   1555  2.19  
SITE     1 AC1  6 THR A  17  THR A  35  ASP A  57  GTP A 200                    
SITE     2 AC1  6 HOH A2008  HOH A2009                                          
SITE     1 AC2 25 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 25 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC2 25 PRO A  29  GLY A  30  TYR A  32  PRO A  34                    
SITE     4 AC2 25 THR A  35  GLY A  60  LYS A 116  ASP A 118                    
SITE     5 AC2 25 LEU A 119  SER A 158  ALA A 159  LEU A 160                    
SITE     6 AC2 25  MG A 201  HOH A2003  HOH A2008  HOH A2043                    
SITE     7 AC2 25 HOH A2045                                                     
CRYST1   83.220   83.220  138.530  90.00  90.00 120.00 P 32 2 1      6          
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      0.012016  0.006938  0.000000        0.00000                         
SCALE2      0.000000  0.013875  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007219        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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