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Database: PDB
Entry: 1AM4
LinkDB: 1AM4
Original site: 1AM4 
HEADER    COMPLEX (GTPASE-ACTIVATING/GTP-BINDING) 22-JUN-97   1AM4              
TITLE     COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P50-RHOGAP;                                                
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CDC42HS;                                                   
COMPND   7 CHAIN: D, E, F;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: HETERODIMER                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COMPLEX (GTPASE-ACTIVATING/GTP-BINDING), GTPASE ACTIVATION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.RITTINGER,P.WALKER,S.J.GAMBLIN,S.J.SMERDON                          
REVDAT   2   24-FEB-09 1AM4    1       VERSN                                    
REVDAT   1   15-JUL-98 1AM4    0                                                
JRNL        AUTH   K.RITTINGER,P.A.WALKER,J.F.ECCLESTON,K.NURMAHOMED,           
JRNL        AUTH 2 D.OWEN,E.LAUE,S.J.GAMBLIN,S.J.SMERDON                        
JRNL        TITL   CRYSTAL STRUCTURE OF A SMALL G PROTEIN IN COMPLEX            
JRNL        TITL 2 WITH THE GTPASE-ACTIVATING PROTEIN RHOGAP.                   
JRNL        REF    NATURE                        V. 388   693 1997              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9262406                                                      
JRNL        DOI    10.1038/41805                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CCP4                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8907                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 297                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.00                          
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 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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.014 ; 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 1AM4 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        : MAR-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
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   : 49357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
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 ENTRIES 1RGP, 1MH1                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.9                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 17200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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     PRO D   529                                                      
REMARK 465     SER D   530                                                      
REMARK 465     GLU D   531                                                      
REMARK 465     PRO E   529                                                      
REMARK 465     SER E   530                                                      
REMARK 465     GLU E   531                                                      
REMARK 465     PRO F   529                                                      
REMARK 465     SER F   530                                                      
REMARK 465     GLU F   531                                                      
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     ASP A 107    CG   OD1  OD2                                       
REMARK 470     ASP A 109    CG   OD1  OD2                                       
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 133    CG   CD1  CD2                                       
REMARK 470     THR A 134    OG1  CG2                                            
REMARK 470     THR D 503    OG1  CG2                                            
REMARK 470     VAL D 542    CG1  CG2                                            
REMARK 470     THR D 543    OG1  CG2                                            
REMARK 470     ILE D 546    CG1  CG2  CD1                                       
REMARK 470     GLU D 549    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 627    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 628    CG   CD   CE   NZ                                   
REMARK 470     ASP B 107    CG   OD1  OD2                                       
REMARK 470     ASP B 109    CG   OD1  OD2                                       
REMARK 470     GLU B 113    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 133    CG   CD1  CD2                                       
REMARK 470     THR B 134    OG1  CG2                                            
REMARK 470     THR E 503    OG1  CG2                                            
REMARK 470     VAL E 542    CG1  CG2                                            
REMARK 470     THR E 543    OG1  CG2                                            
REMARK 470     ILE E 546    CG1  CG2  CD1                                       
REMARK 470     GLU E 549    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 627    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 628    CG   CD   CE   NZ                                   
REMARK 470     ASP C 107    CG   OD1  OD2                                       
REMARK 470     ASP C 109    CG   OD1  OD2                                       
REMARK 470     GLU C 113    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 133    CG   CD1  CD2                                       
REMARK 470     THR C 134    OG1  CG2                                            
REMARK 470     THR F 503    OG1  CG2                                            
REMARK 470     VAL F 542    CG1  CG2                                            
REMARK 470     THR F 543    OG1  CG2                                            
REMARK 470     ILE F 546    CG1  CG2  CD1                                       
REMARK 470     GLU F 549    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 627    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 628    CG   CD   CE   NZ                                   
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   O3G  GNP D   678     O    HOH D     1              2.08            
REMARK 500   O3G  GNP F   678     O    HOH F     3              2.10            
REMARK 500   NZ   LYS F   596     O    HOH F   279              2.14            
REMARK 500   O    ILE B   147     NH1  ARG B   152              2.18            
REMARK 500   O    ILE A   147     NH1  ARG A   152              2.18            
REMARK 500   O    ILE C   147     NH1  ARG C   152              2.19            
REMARK 500   O    ASP E   622     OG1  THR E   625              2.19            
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    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU A  49   O   -  C   -  N   ANGL. DEV. =  10.4 DEGREES          
REMARK 500    GLU A  54   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    GLU A  60   CA  -  CB  -  CG  ANGL. DEV. =  19.1 DEGREES          
REMARK 500    ILE A  64   CB  -  CG1 -  CD1 ANGL. DEV. =  21.9 DEGREES          
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    GLU A  68   CA  -  C   -  O   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    GLU A  81   CA  -  CB  -  CG  ANGL. DEV. =  20.3 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    GLN A  91   CB  -  CG  -  CD  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    VAL A 106   CA  -  CB  -  CG2 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ASP A 107   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP A 109   CB  -  CA  -  C   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    TYR A 138   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TYR A 138   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 148   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    GLU A 149   CG  -  CD  -  OE2 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    GLU A 166   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLU A 166   C   -  N   -  CA  ANGL. DEV. =  20.9 DEGREES          
REMARK 500    TYR A 168   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 172   CD  -  NE  -  CZ  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG A 172   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    LEU A 195   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU A 203   CA  -  CB  -  CG  ANGL. DEV. =  23.2 DEGREES          
REMARK 500    ASP A 208   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    THR D 517   CA  -  CB  -  OG1 ANGL. DEV. = -14.1 DEGREES          
REMARK 500    CYS D 518   CB  -  CA  -  C   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    LEU D 519   CA  -  CB  -  CG  ANGL. DEV. =  26.2 DEGREES          
REMARK 500    TYR D 532   CA  -  CB  -  CG  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    TYR D 532   CB  -  CG  -  CD2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    TYR D 532   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    THR D 535   CA  -  CB  -  OG1 ANGL. DEV. = -21.0 DEGREES          
REMARK 500    THR D 535   CA  -  CB  -  CG2 ANGL. DEV. =  13.7 DEGREES          
REMARK 500    VAL D 536   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    VAL D 536   CA  -  CB  -  CG1 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    PHE D 537   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASP D 557   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP D 557   CB  -  CG  -  OD2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    GLU D 562   CG  -  CD  -  OE1 ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ASP D 563   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    SER D 571   C   -  N   -  CA  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    TYR D 572   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU D 579   CA  -  CB  -  CG  ANGL. DEV. =  22.6 DEGREES          
REMARK 500    GLU D 595   CG  -  CD  -  OE1 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    TRP D 597   CA  -  CB  -  CG  ANGL. DEV. = -12.2 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     188 ANGLE DEVIATIONS.                             
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    ARG A  37       62.00   -160.41                                   
REMARK 500    PRO A  39      105.19    -48.55                                   
REMARK 500    LEU A  40     -174.61    -70.00                                   
REMARK 500    GLN A  43      150.04    -49.84                                   
REMARK 500    GLN A  44      -52.49   -127.72                                   
REMARK 500    ALA A  75      -76.75    -52.03                                   
REMARK 500    PHE A  84       -1.83     51.37                                   
REMARK 500    PHE A 108       27.17    -74.87                                   
REMARK 500    GLU A 113      -13.46   -149.69                                   
REMARK 500    LEU A 114      -80.96     75.27                                   
REMARK 500    HIS A 115       32.46    -87.85                                   
REMARK 500    PRO A 129      -65.88    -25.70                                   
REMARK 500    THR A 134      146.78     84.16                                   
REMARK 500    LEU A 145       33.49    -86.72                                   
REMARK 500    ASP A 148      153.14    -43.53                                   
REMARK 500    PRO A 164      169.27    -49.26                                   
REMARK 500    GLN A 187      -80.23    -91.22                                   
REMARK 500    LYS A 189      -15.26     87.08                                   
REMARK 500    ASP A 208     -116.05     49.80                                   
REMARK 500    ALA A 209     -169.27    -56.84                                   
REMARK 500    ALA A 210      -43.40    104.32                                   
REMARK 500    ILE A 211      -86.73     -7.69                                   
REMARK 500    THR A 212     -155.71     45.38                                   
REMARK 500    ILE A 216     -145.84    100.05                                   
REMARK 500    ASN A 217      -61.93     31.51                                   
REMARK 500    HIS A 229       67.07   -112.92                                   
REMARK 500    GLN D 502      123.44    -16.05                                   
REMARK 500    ALA D 513       78.46     62.94                                   
REMARK 500    VAL D 533       69.44    166.10                                   
REMARK 500    VAL D 536      -96.06   -103.54                                   
REMARK 500    PHE D 537       94.34   -167.80                                   
REMARK 500    ILE D 546       73.40   -158.57                                   
REMARK 500    PRO D 573      132.68    -38.21                                   
REMARK 500    VAL D 577      122.94    167.72                                   
REMARK 500    VAL D 584      -38.62    -39.19                                   
REMARK 500    GLU D 595       57.77    -93.91                                   
REMARK 500    LYS D 596      -68.59    165.14                                   
REMARK 500    HIS D 604      -64.24   -105.75                                   
REMARK 500    LYS D 607        7.24     97.73                                   
REMARK 500    PRO D 609      130.91    -26.68                                   
REMARK 500    LEU D 619       14.47    -68.26                                   
REMARK 500    PRO D 623      -70.10    -22.14                                   
REMARK 500    LYS D 628        2.77    -64.94                                   
REMARK 500    LYS D 633       -4.17    108.79                                   
REMARK 500    PRO D 639        4.85    -60.44                                   
REMARK 500    ALA D 646      -77.31    -46.24                                   
REMARK 500    LYS D 650       18.79     82.94                                   
REMARK 500    ARG B  37       61.86   -160.37                                   
REMARK 500    PRO B  39      105.91    -47.33                                   
REMARK 500    GLN B  43      151.07    -48.64                                   
REMARK 500    GLN B  44      -53.60   -129.89                                   
REMARK 500    ALA B  75      -77.68    -52.48                                   
REMARK 500    PHE B  84       -2.70     51.29                                   
REMARK 500    PHE B 108       27.16    -74.73                                   
REMARK 500    GLU B 113      -13.48   -150.30                                   
REMARK 500    LEU B 114      -80.63     76.16                                   
REMARK 500    HIS B 115       33.72    -88.27                                   
REMARK 500    PRO B 129      -66.70    -25.44                                   
REMARK 500    THR B 134      145.93     84.86                                   
REMARK 500    LEU B 145       33.77    -85.69                                   
REMARK 500    ASP B 148      154.01    -44.84                                   
REMARK 500    PRO B 164      168.69    -48.95                                   
REMARK 500    GLN B 187      -79.89    -90.19                                   
REMARK 500    LYS B 189      -15.50     86.74                                   
REMARK 500    MET B 190       82.81    -69.65                                   
REMARK 500    ASP B 208     -115.87     48.80                                   
REMARK 500    ALA B 209     -168.85    -56.97                                   
REMARK 500    ALA B 210      -43.60    104.93                                   
REMARK 500    ILE B 211      -88.45     -6.89                                   
REMARK 500    THR B 212     -157.75     47.47                                   
REMARK 500    ILE B 216     -144.74     99.56                                   
REMARK 500    ASN B 217      -62.45     31.59                                   
REMARK 500    HIS B 229       68.08   -114.63                                   
REMARK 500    GLN E 502      125.56    -15.86                                   
REMARK 500    ALA E 513       78.75     63.18                                   
REMARK 500    VAL E 533       60.75    154.28                                   
REMARK 500    VAL E 536      -97.35   -102.89                                   
REMARK 500    PHE E 537       93.94   -166.07                                   
REMARK 500    ILE E 546       72.55   -157.71                                   
REMARK 500    PRO E 573      133.65    -38.49                                   
REMARK 500    VAL E 577      121.38    166.40                                   
REMARK 500    GLU E 595       56.80    -95.19                                   
REMARK 500    LYS E 596      -68.91    166.42                                   
REMARK 500    HIS E 604      -64.95   -106.24                                   
REMARK 500    LYS E 607        6.76     97.30                                   
REMARK 500    PRO E 609      130.05    -24.45                                   
REMARK 500    LEU E 619       14.37    -67.78                                   
REMARK 500    PRO E 623      -72.16    -22.35                                   
REMARK 500    LYS E 628        3.06    -65.30                                   
REMARK 500    LYS E 633       -3.56    109.28                                   
REMARK 500    PRO E 639        4.69    -59.05                                   
REMARK 500    LYS E 644      -68.60    -28.70                                   
REMARK 500    ALA E 646      -77.17    -45.58                                   
REMARK 500    LYS E 650       19.77     83.04                                   
REMARK 500    ARG C  37       63.33   -159.93                                   
REMARK 500    PRO C  39      106.17    -46.10                                   
REMARK 500    GLN C  43      150.71    -49.80                                   
REMARK 500    GLN C  44      -53.37   -128.81                                   
REMARK 500    TYR C  72      -71.03    -66.16                                   
REMARK 500    ALA C  75      -78.23    -50.16                                   
REMARK 500    PHE C  84       -3.16     51.50                                   
REMARK 500    PHE C 108       27.00    -74.84                                   
REMARK 500    ASN C 112       59.98    -94.79                                   
REMARK 500    GLU C 113      -13.99   -149.56                                   
REMARK 500    LEU C 114      -81.31     75.80                                   
REMARK 500    HIS C 115       31.51    -87.38                                   
REMARK 500    PRO C 129      -67.46    -25.13                                   
REMARK 500    THR C 134      146.32     83.53                                   
REMARK 500    LEU C 145       33.45    -86.25                                   
REMARK 500    ASP C 148      154.06    -44.02                                   
REMARK 500    PRO C 164      169.33    -48.87                                   
REMARK 500    GLN C 187      -78.80    -91.25                                   
REMARK 500    LYS C 189      -15.16     86.47                                   
REMARK 500    ASP C 208     -115.70     49.40                                   
REMARK 500    ALA C 209     -168.80    -56.75                                   
REMARK 500    ALA C 210      -43.85    103.84                                   
REMARK 500    ILE C 211      -86.71     -8.36                                   
REMARK 500    THR C 212     -157.47     46.73                                   
REMARK 500    ILE C 216     -145.85    100.95                                   
REMARK 500    ASN C 217      -62.59     33.27                                   
REMARK 500    HIS C 229       69.06   -112.98                                   
REMARK 500    GLN F 502      126.15    -16.25                                   
REMARK 500    ALA F 513       78.39     61.73                                   
REMARK 500    VAL F 533       57.89    159.96                                   
REMARK 500    VAL F 536      -96.39   -102.73                                   
REMARK 500    PHE F 537       93.66   -167.48                                   
REMARK 500    ILE F 546       72.74   -160.11                                   
REMARK 500    PRO F 573      133.09    -38.14                                   
REMARK 500    VAL F 577      122.01    167.00                                   
REMARK 500    VAL F 584      -39.17    -39.88                                   
REMARK 500    GLU F 595       57.19    -95.59                                   
REMARK 500    LYS F 596      -67.88    166.10                                   
REMARK 500    HIS F 604      -65.51   -105.26                                   
REMARK 500    LYS F 607        6.23     97.75                                   
REMARK 500    PRO F 609      131.33    -26.63                                   
REMARK 500    LEU F 619       13.47    -67.01                                   
REMARK 500    PRO F 623      -70.42    -22.34                                   
REMARK 500    LYS F 628        2.09    -64.25                                   
REMARK 500    LYS F 633       -3.78    107.25                                   
REMARK 500    PRO F 639        4.91    -59.42                                   
REMARK 500    ALA F 646      -76.77    -45.62                                   
REMARK 500    LYS F 650       18.88     82.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A 118        -13.55                                           
REMARK 500    THR A 156        -10.45                                           
REMARK 500    THR A 193        -10.41                                           
REMARK 500    ILE A 216         12.94                                           
REMARK 500    TYR D 532         10.74                                           
REMARK 500    VAL D 533        -15.52                                           
REMARK 500    MET D 545         10.72                                           
REMARK 500    VAL D 593         10.24                                           
REMARK 500    LYS D 666        -12.48                                           
REMARK 500    ALA B 118        -13.41                                           
REMARK 500    THR B 156        -10.82                                           
REMARK 500    THR B 193        -10.87                                           
REMARK 500    ILE B 216         13.22                                           
REMARK 500    MET E 545         10.48                                           
REMARK 500    LYS E 666        -12.84                                           
REMARK 500    ALA C 118        -13.04                                           
REMARK 500    THR C 156        -11.35                                           
REMARK 500    THR C 193        -10.01                                           
REMARK 500    ILE C 216         12.78                                           
REMARK 500    VAL F 593         10.22                                           
REMARK 500    LYS F 666        -12.64                                           
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 D 679  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP D 678   O2G                                                    
REMARK 620 2 GNP D 678   O2B  89.1                                              
REMARK 620 3 THR D 517   OG1 172.1  86.2                                        
REMARK 620 4 THR D 535   OG1  93.6 172.2  91.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 679  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP E 678   O2G                                                    
REMARK 620 2 GNP E 678   O2B  90.0                                              
REMARK 620 3 THR E 517   OG1 173.2  86.4                                        
REMARK 620 4 THR E 535   OG1  93.7 172.7  90.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 679  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP F 678   O2G                                                    
REMARK 620 2 GNP F 678   O2B  90.2                                              
REMARK 620 3 THR F 517   OG1 173.0  85.2                                        
REMARK 620 4 THR F 535   OG1  93.4 172.2  91.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 679                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 679                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 679                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP D 678                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP E 678                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP F 678                 
DBREF  1AM4 A   36   234  UNP    Q07960   RHG01_HUMAN    233    431             
DBREF  1AM4 D  502   677  UNP    P60953   CDC42_HUMAN      2    177             
DBREF  1AM4 B   36   234  UNP    Q07960   RHG01_HUMAN    233    431             
DBREF  1AM4 E  502   677  UNP    P60953   CDC42_HUMAN      2    177             
DBREF  1AM4 C   36   234  UNP    Q07960   RHG01_HUMAN    233    431             
DBREF  1AM4 F  502   677  UNP    P60953   CDC42_HUMAN      2    177             
SEQRES   1 A  199  PRO ARG PRO PRO LEU PRO ASN GLN GLN PHE GLY VAL SER          
SEQRES   2 A  199  LEU GLN HIS LEU GLN GLU LYS ASN PRO GLU GLN GLU PRO          
SEQRES   3 A  199  ILE PRO ILE VAL LEU ARG GLU THR VAL ALA TYR LEU GLN          
SEQRES   4 A  199  ALA HIS ALA LEU THR THR GLU GLY ILE PHE ARG ARG SER          
SEQRES   5 A  199  ALA ASN THR GLN VAL VAL ARG GLU VAL GLN GLN LYS TYR          
SEQRES   6 A  199  ASN MET GLY LEU PRO VAL ASP PHE ASP GLN TYR ASN GLU          
SEQRES   7 A  199  LEU HIS LEU PRO ALA VAL ILE LEU LYS THR PHE LEU ARG          
SEQRES   8 A  199  GLU LEU PRO GLU PRO LEU LEU THR PHE ASP LEU TYR PRO          
SEQRES   9 A  199  HIS VAL VAL GLY PHE LEU ASN ILE ASP GLU SER GLN ARG          
SEQRES  10 A  199  VAL PRO ALA THR LEU GLN VAL LEU GLN THR LEU PRO GLU          
SEQRES  11 A  199  GLU ASN TYR GLN VAL LEU ARG PHE LEU THR ALA PHE LEU          
SEQRES  12 A  199  VAL GLN ILE SER ALA HIS SER ASP GLN ASN LYS MET THR          
SEQRES  13 A  199  ASN THR ASN LEU ALA VAL VAL PHE GLY PRO ASN LEU LEU          
SEQRES  14 A  199  TRP ALA LYS ASP ALA ALA ILE THR LEU LYS ALA ILE ASN          
SEQRES  15 A  199  PRO ILE ASN THR PHE THR LYS PHE LEU LEU ASP HIS GLN          
SEQRES  16 A  199  GLY GLU LEU PHE                                              
SEQRES   1 D  177  PRO GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 D  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 D  177  LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN          
SEQRES   4 D  177  TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR          
SEQRES   5 D  177  LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 D  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 D  177  LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU          
SEQRES   8 D  177  ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS          
SEQRES   9 D  177  CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE          
SEQRES  10 D  177  ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA          
SEQRES  11 D  177  LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU          
SEQRES  12 D  177  LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU          
SEQRES  13 D  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS ASN VAL PHE          
SEQRES  14 D  177  ASP GLU ALA ILE LEU ALA ALA LEU                              
SEQRES   1 B  199  PRO ARG PRO PRO LEU PRO ASN GLN GLN PHE GLY VAL SER          
SEQRES   2 B  199  LEU GLN HIS LEU GLN GLU LYS ASN PRO GLU GLN GLU PRO          
SEQRES   3 B  199  ILE PRO ILE VAL LEU ARG GLU THR VAL ALA TYR LEU GLN          
SEQRES   4 B  199  ALA HIS ALA LEU THR THR GLU GLY ILE PHE ARG ARG SER          
SEQRES   5 B  199  ALA ASN THR GLN VAL VAL ARG GLU VAL GLN GLN LYS TYR          
SEQRES   6 B  199  ASN MET GLY LEU PRO VAL ASP PHE ASP GLN TYR ASN GLU          
SEQRES   7 B  199  LEU HIS LEU PRO ALA VAL ILE LEU LYS THR PHE LEU ARG          
SEQRES   8 B  199  GLU LEU PRO GLU PRO LEU LEU THR PHE ASP LEU TYR PRO          
SEQRES   9 B  199  HIS VAL VAL GLY PHE LEU ASN ILE ASP GLU SER GLN ARG          
SEQRES  10 B  199  VAL PRO ALA THR LEU GLN VAL LEU GLN THR LEU PRO GLU          
SEQRES  11 B  199  GLU ASN TYR GLN VAL LEU ARG PHE LEU THR ALA PHE LEU          
SEQRES  12 B  199  VAL GLN ILE SER ALA HIS SER ASP GLN ASN LYS MET THR          
SEQRES  13 B  199  ASN THR ASN LEU ALA VAL VAL PHE GLY PRO ASN LEU LEU          
SEQRES  14 B  199  TRP ALA LYS ASP ALA ALA ILE THR LEU LYS ALA ILE ASN          
SEQRES  15 B  199  PRO ILE ASN THR PHE THR LYS PHE LEU LEU ASP HIS GLN          
SEQRES  16 B  199  GLY GLU LEU PHE                                              
SEQRES   1 E  177  PRO GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 E  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 E  177  LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN          
SEQRES   4 E  177  TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR          
SEQRES   5 E  177  LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 E  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 E  177  LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU          
SEQRES   8 E  177  ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS          
SEQRES   9 E  177  CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE          
SEQRES  10 E  177  ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA          
SEQRES  11 E  177  LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU          
SEQRES  12 E  177  LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU          
SEQRES  13 E  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS ASN VAL PHE          
SEQRES  14 E  177  ASP GLU ALA ILE LEU ALA ALA LEU                              
SEQRES   1 C  199  PRO ARG PRO PRO LEU PRO ASN GLN GLN PHE GLY VAL SER          
SEQRES   2 C  199  LEU GLN HIS LEU GLN GLU LYS ASN PRO GLU GLN GLU PRO          
SEQRES   3 C  199  ILE PRO ILE VAL LEU ARG GLU THR VAL ALA TYR LEU GLN          
SEQRES   4 C  199  ALA HIS ALA LEU THR THR GLU GLY ILE PHE ARG ARG SER          
SEQRES   5 C  199  ALA ASN THR GLN VAL VAL ARG GLU VAL GLN GLN LYS TYR          
SEQRES   6 C  199  ASN MET GLY LEU PRO VAL ASP PHE ASP GLN TYR ASN GLU          
SEQRES   7 C  199  LEU HIS LEU PRO ALA VAL ILE LEU LYS THR PHE LEU ARG          
SEQRES   8 C  199  GLU LEU PRO GLU PRO LEU LEU THR PHE ASP LEU TYR PRO          
SEQRES   9 C  199  HIS VAL VAL GLY PHE LEU ASN ILE ASP GLU SER GLN ARG          
SEQRES  10 C  199  VAL PRO ALA THR LEU GLN VAL LEU GLN THR LEU PRO GLU          
SEQRES  11 C  199  GLU ASN TYR GLN VAL LEU ARG PHE LEU THR ALA PHE LEU          
SEQRES  12 C  199  VAL GLN ILE SER ALA HIS SER ASP GLN ASN LYS MET THR          
SEQRES  13 C  199  ASN THR ASN LEU ALA VAL VAL PHE GLY PRO ASN LEU LEU          
SEQRES  14 C  199  TRP ALA LYS ASP ALA ALA ILE THR LEU LYS ALA ILE ASN          
SEQRES  15 C  199  PRO ILE ASN THR PHE THR LYS PHE LEU LEU ASP HIS GLN          
SEQRES  16 C  199  GLY GLU LEU PHE                                              
SEQRES   1 F  177  PRO GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 F  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 F  177  LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN          
SEQRES   4 F  177  TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR          
SEQRES   5 F  177  LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 F  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 F  177  LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU          
SEQRES   8 F  177  ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS          
SEQRES   9 F  177  CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE          
SEQRES  10 F  177  ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA          
SEQRES  11 F  177  LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU          
SEQRES  12 F  177  LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU          
SEQRES  13 F  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS ASN VAL PHE          
SEQRES  14 F  177  ASP GLU ALA ILE LEU ALA ALA LEU                              
HET     MG  D 679       1                                                       
HET     MG  E 679       1                                                       
HET     MG  F 679       1                                                       
HET    GNP  D 678      32                                                       
HET    GNP  E 678      32                                                       
HET    GNP  F 678      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   7   MG    3(MG 2+)                                                     
FORMUL  10  GNP    3(C10 H17 N6 O13 P3)                                         
FORMUL  13  HOH   *302(H2 O)                                                    
HELIX    1   1 LEU A   49  LEU A   52  1                                   4    
HELIX    2   2 ILE A   64  ALA A   75  1                                  12    
HELIX    3   3 THR A   90  LYS A   99  1                                  10    
HELIX    4   4 LEU A  116  GLU A  127  1                                  12    
HELIX    5   5 PHE A  135  VAL A  142  5                                   8    
HELIX    6   6 PHE A  144  ASN A  146  5                                   3    
HELIX    7   7 ARG A  152  GLN A  161  1                                  10    
HELIX    8   8 GLU A  165  ASN A  188  1                                  24    
HELIX    9   9 ASN A  192  LEU A  203  1                                  12    
HELIX   10  10 PRO A  218  ASP A  228  1                                  11    
HELIX   11  11 LYS D  516  THR D  525  1                                  10    
HELIX   12  12 ASP D  563  ASP D  565  5                                   3    
HELIX   13  13 PRO D  569  SER D  571  5                                   3    
HELIX   14  14 SER D  588  GLU D  591  1                                   4    
HELIX   15  15 TRP D  597  THR D  602  1                                   6    
HELIX   16  16 ASP D  618  ARG D  620  5                                   3    
HELIX   17  17 PRO D  623  LEU D  629  1                                   7    
HELIX   18  18 GLU D  643  LEU D  649  1                                   7    
HELIX   19  19 LEU D  665  ILE D  673  1                                   9    
HELIX   20  20 LEU B   49  GLU B   54  1                                   6    
HELIX   21  21 ILE B   64  ALA B   75  1                                  12    
HELIX   22  22 THR B   90  LYS B   99  1                                  10    
HELIX   23  23 LEU B  116  GLU B  127  1                                  12    
HELIX   24  24 PHE B  135  VAL B  142  5                                   8    
HELIX   25  25 ARG B  152  GLN B  161  1                                  10    
HELIX   26  26 GLU B  165  ASN B  188  1                                  24    
HELIX   27  27 ASN B  192  LEU B  203  1                                  12    
HELIX   28  28 PRO B  218  ASP B  228  1                                  11    
HELIX   29  29 LYS E  516  THR E  525  1                                  10    
HELIX   30  30 ASP E  563  ASP E  565  5                                   3    
HELIX   31  31 PRO E  569  SER E  571  5                                   3    
HELIX   32  32 SER E  588  GLU E  591  1                                   4    
HELIX   33  33 TRP E  597  THR E  602  1                                   6    
HELIX   34  34 ASP E  618  ARG E  620  5                                   3    
HELIX   35  35 PRO E  623  LEU E  629  1                                   7    
HELIX   36  36 GLU E  643  LEU E  649  1                                   7    
HELIX   37  37 LEU E  665  ILE E  673  1                                   9    
HELIX   38  38 LEU C   49  GLU C   54  1                                   6    
HELIX   39  39 ILE C   64  ALA C   75  1                                  12    
HELIX   40  40 THR C   90  LYS C   99  1                                  10    
HELIX   41  41 LEU C  116  GLU C  127  1                                  12    
HELIX   42  42 PHE C  135  VAL C  142  5                                   8    
HELIX   43  43 PHE C  144  ASN C  146  5                                   3    
HELIX   44  44 ARG C  152  GLN C  161  1                                  10    
HELIX   45  45 GLU C  165  ASN C  188  1                                  24    
HELIX   46  46 ASN C  192  LEU C  203  1                                  12    
HELIX   47  47 PRO C  218  ASP C  228  1                                  11    
HELIX   48  48 LYS F  516  THR F  525  1                                  10    
HELIX   49  49 ASP F  563  ASP F  565  5                                   3    
HELIX   50  50 ARG F  568  SER F  571  5                                   4    
HELIX   51  51 SER F  588  GLU F  591  1                                   4    
HELIX   52  52 TRP F  597  THR F  602  1                                   6    
HELIX   53  53 ASP F  618  ARG F  620  5                                   3    
HELIX   54  54 PRO F  623  GLU F  627  1                                   5    
HELIX   55  55 GLU F  643  LEU F  649  1                                   7    
HELIX   56  56 LEU F  665  ILE F  673  1                                   9    
SHEET    1   A 6 ALA D 651  GLU D 656  0                                        
SHEET    2   A 6 PHE D 610  THR D 615  1  N  PHE D 610   O  VAL D 652           
SHEET    3   A 6 PHE D 578  SER D 583  1  N  VAL D 580   O  VAL D 613           
SHEET    4   A 6 THR D 503  GLY D 510  1  N  VAL D 507   O  LEU D 579           
SHEET    5   A 6 PRO D 550  ASP D 557  1  N  THR D 552   O  ILE D 504           
SHEET    6   A 6 ALA D 541  MET D 545 -1  N  VAL D 544   O  TYR D 551           
SHEET    1   B 6 ALA E 651  GLU E 656  0                                        
SHEET    2   B 6 PHE E 610  THR E 615  1  N  PHE E 610   O  VAL E 652           
SHEET    3   B 6 PHE E 578  SER E 583  1  N  VAL E 580   O  VAL E 613           
SHEET    4   B 6 THR E 503  GLY E 510  1  N  VAL E 507   O  LEU E 579           
SHEET    5   B 6 GLU E 549  ASP E 557  1  N  THR E 552   O  ILE E 504           
SHEET    6   B 6 ALA E 541  ILE E 546 -1  N  ILE E 546   O  GLU E 549           
SHEET    1   C 6 ALA F 651  GLU F 656  0                                        
SHEET    2   C 6 PHE F 610  THR F 615  1  N  PHE F 610   O  VAL F 652           
SHEET    3   C 6 PHE F 578  SER F 583  1  N  VAL F 580   O  VAL F 613           
SHEET    4   C 6 THR F 503  GLY F 510  1  N  VAL F 507   O  LEU F 579           
SHEET    5   C 6 PRO F 550  ASP F 557  1  N  THR F 552   O  ILE F 504           
SHEET    6   C 6 ALA F 541  MET F 545 -1  N  VAL F 544   O  TYR F 551           
LINK         O2G GNP D 678                MG    MG D 679     1555   1555  2.20  
LINK         O2B GNP D 678                MG    MG D 679     1555   1555  2.20  
LINK        MG    MG D 679                 OG1 THR D 517     1555   1555  2.20  
LINK        MG    MG D 679                 OG1 THR D 535     1555   1555  2.20  
LINK         O2G GNP E 678                MG    MG E 679     1555   1555  2.20  
LINK         O2B GNP E 678                MG    MG E 679     1555   1555  2.20  
LINK        MG    MG E 679                 OG1 THR E 517     1555   1555  2.20  
LINK        MG    MG E 679                 OG1 THR E 535     1555   1555  2.20  
LINK         O2G GNP F 678                MG    MG F 679     1555   1555  2.20  
LINK         O2B GNP F 678                MG    MG F 679     1555   1555  2.20  
LINK        MG    MG F 679                 OG1 THR F 517     1555   1555  2.20  
LINK        MG    MG F 679                 OG1 THR F 535     1555   1555  2.20  
SITE     1 AC1  3 THR D 517  THR D 535  GNP D 678                               
SITE     1 AC2  3 THR E 517  THR E 535  GNP E 678                               
SITE     1 AC3  3 THR F 517  THR F 535  GNP F 678                               
SITE     1 AC4 22 HOH D   1  HOH D  66  HOH D 227  HOH D 274                    
SITE     2 AC4 22 GLY D 512  ALA D 513  VAL D 514  GLY D 515                    
SITE     3 AC4 22 LYS D 516  THR D 517  CYS D 518  TYR D 532                    
SITE     4 AC4 22 PRO D 534  THR D 535  GLY D 560  GLN D 561                    
SITE     5 AC4 22 GLN D 616  ASP D 618  LEU D 619  ALA D 659                    
SITE     6 AC4 22 LEU D 660   MG D 679                                          
SITE     1 AC5 20 HOH E   2  HOH E  71  GLY E 512  ALA E 513                    
SITE     2 AC5 20 VAL E 514  GLY E 515  LYS E 516  THR E 517                    
SITE     3 AC5 20 CYS E 518  TYR E 532  PRO E 534  THR E 535                    
SITE     4 AC5 20 GLY E 560  GLN E 561  GLN E 616  ASP E 618                    
SITE     5 AC5 20 LEU E 619  ALA E 659  LEU E 660   MG E 679                    
SITE     1 AC6 20 HOH F   3  HOH F  96  GLY F 512  ALA F 513                    
SITE     2 AC6 20 VAL F 514  GLY F 515  LYS F 516  THR F 517                    
SITE     3 AC6 20 CYS F 518  TYR F 532  PRO F 534  THR F 535                    
SITE     4 AC6 20 GLY F 560  GLN F 561  GLN F 616  ASP F 618                    
SITE     5 AC6 20 LEU F 619  ALA F 659  LEU F 660   MG F 679                    
CRYST1   78.110   78.120   78.100  90.01  90.00  90.05 P 1           3          
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      0.012802  0.000011  0.000000        0.00000                         
SCALE2      0.000000  0.012801  0.000002        0.00000                         
SCALE3      0.000000  0.000000  0.012804        0.00000                         
MTRIX1   1 -0.000097  1.000000  0.000273       32.64486    1                    
MTRIX2   1 -0.000024  0.000273 -1.000000        6.77250    1                    
MTRIX3   1 -1.000000 -0.000097  0.000024       39.41171    1                    
MTRIX1   2 -0.000550  0.000021 -1.000000       39.37717    1                    
MTRIX2   2  1.000000 -0.000061 -0.000550       45.48096    1                    
MTRIX3   2 -0.000061 -1.000000 -0.000021        6.77439    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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