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Database: PDB
Entry: 1MH1
LinkDB: 1MH1
Original site: 1MH1 
HEADER    GTP-BINDING                             21-JAN-97   1MH1              
TITLE     SMALL G-PROTEIN                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAC1;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1 - 184;                                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: COMPLEXED WITH GUANOSINE-5'-(BETA,GAMMA-              
COMPND   8 IMIDO) TRIPHOSPHATE (GPPNP)                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RHO;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_GENE: RHO                                          
KEYWDS    GTP-BINDING, GTPASE, SMALL G-PROTEIN, RHO FAMILY, RAS SUPER           
KEYWDS   2 FAMILY                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HIRSHBERG,R.W.STOCKLEY,G.DODSON,M.R.WEBB                            
REVDAT   2   24-FEB-09 1MH1    1       VERSN                                    
REVDAT   1   21-JAN-98 1MH1    0                                                
JRNL        AUTH   M.HIRSHBERG,R.W.STOCKLEY,G.DODSON,M.R.WEBB                   
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN RAC1, A MEMBER OF             
JRNL        TITL 2 THE RHO-FAMILY COMPLEXED WITH A GTP ANALOGUE.                
JRNL        REF    NAT.STRUCT.BIOL.              V.   4   147 1997              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9033596                                                      
JRNL        DOI    10.1038/NSB0297-147                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1395                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 256                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MH1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 101                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42134                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 821P                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       23.22000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.22000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.52500            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     VAL A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
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     TYR A  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A  33    CG1  CG2  CD1                                       
REMARK 470     VAL A  36    CG1  CG2                                            
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 128    CG   CD   CE   NZ                                   
REMARK 470     LYS A 130    CE   NZ                                             
REMARK 470     GLU A 131    CD   OE1  OE2                                       
REMARK 470     LYS A 132    CD   CE   NZ                                        
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A  28   CG    PHE A  28   CD2     1.039                       
REMARK 500    PHE A  28   CG    PHE A  28   CD1     1.046                       
REMARK 500    PHE A  28   CE1   PHE A  28   CZ      1.054                       
REMARK 500    PHE A  28   CZ    PHE A  28   CE2     1.054                       
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    PHE A  28   CB  -  CG  -  CD2 ANGL. DEV. =  28.6 DEGREES          
REMARK 500    PHE A  28   CD1 -  CG  -  CD2 ANGL. DEV. = -58.3 DEGREES          
REMARK 500    PHE A  28   CB  -  CG  -  CD1 ANGL. DEV. =  29.8 DEGREES          
REMARK 500    PHE A  28   CG  -  CD1 -  CE1 ANGL. DEV. = -90.7 DEGREES          
REMARK 500    PHE A  28   CG  -  CD2 -  CE2 ANGL. DEV. = -90.9 DEGREES          
REMARK 500    PHE A  28   CD1 -  CE1 -  CZ  ANGL. DEV. = -90.1 DEGREES          
REMARK 500    PHE A  28   CE1 -  CZ  -  CE2 ANGL. DEV. = -60.0 DEGREES          
REMARK 500    PHE A  28   CZ  -  CE2 -  CD2 ANGL. DEV. = -90.1 DEGREES          
REMARK 500    TYR A  40   CB  -  CG  -  CD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TYR A  40   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A  94   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    TYR A 139   CB  -  CG  -  CD2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    TYR A 139   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 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    TYR A  32      148.99     -7.32                                   
REMARK 500    ILE A  33      116.38    172.02                                   
REMARK 500    PHE A  37       81.85     74.78                                   
REMARK 500    LYS A  96      -58.93   -129.40                                   
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 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP A 200   O2G                                                    
REMARK 620 2 GNP A 200   O2B  93.6                                              
REMARK 620 3 THR A  17   OG1 173.5  88.8                                        
REMARK 620 4 THR A  35   OG1 102.9 163.3  75.0                                  
REMARK 620 5 HOH A 534   O    90.7  89.8  83.3  92.1                            
REMARK 620 6 HOH A 535   O    96.1  89.1  89.9  87.1 173.1                      
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 200                 
DBREF  1MH1 A    2   184  UNP    P63000   RAC1_HUMAN       2    184             
SEQADV 1MH1 SER A   78  UNP  P63000    PHE    78 ENGINEERED                     
SEQRES   1 A  186  GLY SER PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP          
SEQRES   2 A  186  GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR          
SEQRES   3 A  186  THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE          
SEQRES   4 A  186  ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO          
SEQRES   5 A  186  VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 A  186  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP          
SEQRES   7 A  186  VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER          
SEQRES   8 A  186  PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG          
SEQRES   9 A  186  HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR          
SEQRES  10 A  186  LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS          
SEQRES  11 A  186  LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN          
SEQRES  12 A  186  GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR          
SEQRES  13 A  186  LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR          
SEQRES  14 A  186  VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO          
SEQRES  15 A  186  PRO VAL LYS LYS                                              
HET     MG  A 201       1                                                       
HET    GNP  A 200      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GNP    C10 H17 N6 O13 P3                                            
FORMUL   4  HOH   *256(H2 O)                                                    
HELIX    1   1 LYS A   16  THR A   25  1                                  10    
HELIX    2   2 GLU A   62  SER A   71  5                                  10    
HELIX    3   3 PRO A   87  ALA A   95  1                                   9    
HELIX    4   4 TRP A   97  HIS A  104  1                                   8    
HELIX    5   5 LEU A  117  ARG A  120  1                                   4    
HELIX    6   6 LYS A  123  LYS A  130  1                                   8    
HELIX    7   7 TYR A  139  GLU A  148  1                                  10    
HELIX    8   8 LEU A  165  VAL A  176  1                                  12    
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  SER 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  ASP A  57  1  N  ASN A  52   O  GLN A   2           
SHEET    6   A 6 ASN A  39  VAL A  46 -1  N  VAL A  46   O  LYS A  49           
LINK         O2G GNP A 200                MG    MG A 201     1555   1555  2.08  
LINK         O2B GNP A 200                MG    MG A 201     1555   1555  2.13  
LINK        MG    MG A 201                 OG1 THR A  17     1555   1555  2.08  
LINK        MG    MG A 201                 OG1 THR A  35     1555   1555  2.13  
LINK        MG    MG A 201                 O   HOH A 534     1555   1555  2.08  
LINK        MG    MG A 201                 O   HOH A 535     1555   1555  2.11  
SITE     1 AC1  5 THR A  17  THR A  35  GNP A 200  HOH A 534                    
SITE     2 AC1  5 HOH A 535                                                     
SITE     1 AC2 29 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 29 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC2 29 GLU A  31  TYR A  32  PRO A  34  THR A  35                    
SITE     4 AC2 29 GLY A  60  LYS A 116  ASP A 118  LEU A 119                    
SITE     5 AC2 29 SER A 158  ALA A 159  LEU A 160   MG A 201                    
SITE     6 AC2 29 HOH A 470  HOH A 472  HOH A 495  HOH A 534                    
SITE     7 AC2 29 HOH A 535  HOH A 536  HOH A 537  HOH A 549                    
SITE     8 AC2 29 HOH A 555                                                     
CRYST1   46.440  103.050   43.673  90.00  90.00  90.00 P 21 21 2     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      0.021533  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009704  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022897        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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