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Database: PDB
Entry: 2A5F
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HEADER    PROTEIN TRANSPORT/TRANSFERASE           30-JUN-05   2A5F              
TITLE     CHOLERA TOXIN A1 SUBUNIT BOUND TO ITS SUBSTRATE, NAD+, AND ITS HUMAN  
TITLE    2 PROTEIN ACTIVATOR, ARF6                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADP-RIBOSYLATION FACTOR 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CHOLERA ENTEROTOXIN, A CHAIN;                              
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: CHOLERA TOXIN A1 SUBUNIT;                                  
COMPND   9 SYNONYM: NAD(+)--DIPHTHAMIDE ADP-RIBOSYLTRANSFERASE, CHOLERA         
COMPND  10 ENTEROTOXIN A SUBUNIT;                                               
COMPND  11 EC: 2.4.2.36;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ARF6;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE  11 ORGANISM_TAXID: 666;                                                 
SOURCE  12 GENE: CTXA, TOXA;                                                    
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    PROTEIN TRANSPORT/TRANSFERASE, PROTEIN TRANSPORT-TRANSFERASE COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.O'NEAL,M.G.JOBLING,R.K.HOLMES,W.G.J.HOL                           
REVDAT   4   30-NOV-16 2A5F    1       REMARK                                   
REVDAT   3   13-JUL-11 2A5F    1       VERSN                                    
REVDAT   2   24-FEB-09 2A5F    1       VERSN                                    
REVDAT   1   16-AUG-05 2A5F    0                                                
JRNL        AUTH   C.J.O'NEAL,M.G.JOBLING,R.K.HOLMES,W.G.HOL                    
JRNL        TITL   STRUCTURAL BASIS FOR THE ACTIVATION OF CHOLERA TOXIN BY      
JRNL        TITL 2 HUMAN ARF6-GTP.                                              
JRNL        REF    SCIENCE                       V. 309  1093 2005              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   16099990                                                     
JRNL        DOI    10.1126/SCIENCE.1113398                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24930                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1329                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.02                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1354                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2740                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 169                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.181         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.622         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2901 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2497 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3963 ; 1.561 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5774 ; 0.773 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   345 ; 6.546 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   140 ;38.041 ;23.214       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   427 ;14.168 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;18.162 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   416 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3231 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   609 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   575 ; 0.214 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2530 ; 0.206 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1404 ; 0.189 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1577 ; 0.090 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   269 ; 0.217 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.075 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.082 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.122 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    49 ; 0.297 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.241 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1718 ; 1.438 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   711 ; 0.285 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2760 ; 2.421 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1250 ; 1.399 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1203 ; 2.169 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2A5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033509.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97943                            
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25861                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT      
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: CTA1:ARF6-GTP                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000MME, CACODYLATE, PH 6.5, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.45250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.00050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.46250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.00050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.45250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.46250            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE HETERODIMER PRESENT IN THE    
REMARK 300 ASYMMETRIC UNIT.                                                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     SER B     0                                                      
REMARK 465     ASN B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     GLY B   188                                                      
REMARK 465     ASN B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     PRO B   191                                                      
REMARK 465     ARG B   192                                                      
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     LYS A  12    CG   CD   CE   NZ                                   
REMARK 470     GLN A  37    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     LYS A  58    CD   CE   NZ                                        
REMARK 470     LYS A  69    CD   CE   NZ                                        
REMARK 470     ARG A 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 128    CB   CG   OD1  OD2                                  
REMARK 470     GLN B  18    CD   OE1  NE2                                       
REMARK 470     GLN B  49    CG   CD   OE1  NE2                                  
REMARK 470     ILE B  76    CD1                                                 
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 143    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 148    CG   CD   NE   CZ   NH1  NH2                        
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   OD2  ASP A    97     NH1  ARG A   100              2.02            
REMARK 500   OE1  GLU A   134     O    HOH A  1543              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1552     O    HOH B  1625     3545     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  23        9.83     80.11                                   
REMARK 500    LYS A 123       36.52     71.97                                   
REMARK 500    ARG B  33       24.18   -149.96                                   
REMARK 500    GLN B 111       58.02     38.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1081        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 288        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B1604        DISTANCE =  5.65 ANGSTROMS                       
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 231  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GTP A 230   O2G                                                    
REMARK 620 2 GTP A 230   O2B  94.5                                              
REMARK 620 3 HOH A 274   O    87.0  85.6                                        
REMARK 620 4 THR A  27   OG1 171.9  90.9  99.5                                  
REMARK 620 5 HOH A 291   O    82.2  93.4 169.0  91.5                            
REMARK 620 6 THR A  44   OG1  85.4 179.8  94.3  89.2  86.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1326  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 150   O                                                      
REMARK 620 2 LEU B 153   O    88.2                                              
REMARK 620 3 HOH B1597   O    95.3 159.3                                        
REMARK 620 4 HOH B1641   O    95.7  78.1  81.3                                  
REMARK 620 5 THR B  90   OG1 176.0  94.8  82.9  87.6                            
REMARK 620 6 THR B  90   O    95.2  99.9 100.1 168.8  81.6                      
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 231                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1536                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1114                
DBREF  2A5F A    2   175  UNP    P62330   ARF6_HUMAN       1    174             
DBREF  2A5F B    1   192  UNP    P01555   CHTA_VIBCH      19    210             
SEQADV 2A5F MET A    1  UNP  P62330              INITIATING METHIONINE          
SEQADV 2A5F SER B    0  UNP  P01555              CLONING ARTIFACT               
SEQADV 2A5F ASP B  110  UNP  P01555    GLU   128 ENGINEERED                     
SEQADV 2A5F ASP B  112  UNP  P01555    GLU   130 ENGINEERED                     
SEQADV 2A5F SER B  187  UNP  P01555    CYS   205 ENGINEERED                     
SEQRES   1 A  175  MET GLY LYS VAL LEU SER LYS ILE PHE GLY ASN LYS GLU          
SEQRES   2 A  175  MET ARG ILE LEU MET LEU GLY LEU ASP ALA ALA GLY LYS          
SEQRES   3 A  175  THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLN SER VAL          
SEQRES   4 A  175  THR THR ILE PRO THR VAL GLY PHE ASN VAL GLU THR VAL          
SEQRES   5 A  175  THR TYR LYS ASN VAL LYS PHE ASN VAL TRP ASP VAL GLY          
SEQRES   6 A  175  GLY GLN ASP LYS ILE ARG PRO LEU TRP ARG HIS TYR TYR          
SEQRES   7 A  175  THR GLY THR GLN GLY LEU ILE PHE VAL VAL ASP CYS ALA          
SEQRES   8 A  175  ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN GLU LEU HIS          
SEQRES   9 A  175  ARG ILE ILE ASN ASP ARG GLU MET ARG ASP ALA ILE ILE          
SEQRES  10 A  175  LEU ILE PHE ALA ASN LYS GLN ASP LEU PRO ASP ALA MET          
SEQRES  11 A  175  LYS PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU THR ARG          
SEQRES  12 A  175  ILE ARG ASP ARG ASN TRP TYR VAL GLN PRO SER CYS ALA          
SEQRES  13 A  175  THR SER GLY ASP GLY LEU TYR GLU GLY LEU THR TRP LEU          
SEQRES  14 A  175  THR SER ASN TYR LYS SER                                      
SEQRES   1 B  193  SER ASN ASP ASP LYS LEU TYR ARG ALA ASP SER ARG PRO          
SEQRES   2 B  193  PRO ASP GLU ILE LYS GLN SER GLY GLY LEU MET PRO ARG          
SEQRES   3 B  193  GLY GLN SER GLU TYR PHE ASP ARG GLY THR GLN MET ASN          
SEQRES   4 B  193  ILE ASN LEU TYR ASP HIS ALA ARG GLY THR GLN THR GLY          
SEQRES   5 B  193  PHE VAL ARG HIS ASP ASP GLY TYR VAL SER THR SER ILE          
SEQRES   6 B  193  SER LEU ARG SER ALA HIS LEU VAL GLY GLN THR ILE LEU          
SEQRES   7 B  193  SER GLY HIS SER THR TYR TYR ILE TYR VAL ILE ALA THR          
SEQRES   8 B  193  ALA PRO ASN MET PHE ASN VAL ASN ASP VAL LEU GLY ALA          
SEQRES   9 B  193  TYR SER PRO HIS PRO ASP ASP GLN ASP VAL SER ALA LEU          
SEQRES  10 B  193  GLY GLY ILE PRO TYR SER GLN ILE TYR GLY TRP TYR ARG          
SEQRES  11 B  193  VAL HIS PHE GLY VAL LEU ASP GLU GLN LEU HIS ARG ASN          
SEQRES  12 B  193  ARG GLY TYR ARG ASP ARG TYR TYR SER ASN LEU ASP ILE          
SEQRES  13 B  193  ALA PRO ALA ALA ASP GLY TYR GLY LEU ALA GLY PHE PRO          
SEQRES  14 B  193  PRO GLU HIS ARG ALA TRP ARG GLU GLU PRO TRP ILE HIS          
SEQRES  15 B  193  HIS ALA PRO PRO GLY SER GLY ASN ALA PRO ARG                  
HET     MG  A 231       1                                                       
HET     NA  B1326       1                                                       
HET    GTP  A 230      32                                                       
HET    NAD  B1536      44                                                       
HET    GOL  B1114       6                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  GTP    C10 H16 N5 O14 P3                                            
FORMUL   6  NAD    C21 H27 N7 O14 P2                                            
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *169(H2 O)                                                    
HELIX    1   1 GLY A   25  GLY A   36  1                                  12    
HELIX    2   2 GLN A   67  TYR A   78  5                                  12    
HELIX    3   3 ASP A   92  ASP A   94  5                                   3    
HELIX    4   4 ARG A   95  ASN A  108  1                                  14    
HELIX    5   5 ASP A  109  ARG A  113  5                                   5    
HELIX    6   6 LYS A  131  LEU A  139  1                                   9    
HELIX    7   7 GLY A  140  ILE A  144  5                                   5    
HELIX    8   8 GLY A  161  ASN A  172  1                                  12    
HELIX    9   9 PRO B   12  SER B   19  1                                   8    
HELIX   10  10 PRO B   24  GLY B   34  1                                  11    
HELIX   11  11 ASN B   40  GLY B   47  1                                   8    
HELIX   12  12 SER B   65  GLN B   74  1                                  10    
HELIX   13  13 VAL B   97  GLY B  102  1                                   6    
HELIX   14  14 ALA B  103  SER B  105  5                                   3    
HELIX   15  15 HIS B  107  ASP B  110  5                                   4    
HELIX   16  16 ARG B  146  SER B  151  1                                   6    
HELIX   17  17 PRO B  157  TYR B  162  1                                   6    
HELIX   18  18 GLY B  163  ALA B  165  5                                   3    
HELIX   19  19 HIS B  171  GLU B  176  5                                   6    
HELIX   20  20 PRO B  178  ALA B  183  5                                   6    
SHEET    1   A 6 PHE A  47  TYR A  54  0                                        
SHEET    2   A 6 VAL A  57  VAL A  64 -1  O  PHE A  59   N  VAL A  52           
SHEET    3   A 6 GLU A  13  GLY A  20  1  N  MET A  18   O  TRP A  62           
SHEET    4   A 6 GLY A  83  ASP A  89  1  O  ILE A  85   N  LEU A  17           
SHEET    5   A 6 ILE A 116  ASN A 122  1  O  ILE A 116   N  LEU A  84           
SHEET    6   A 6 TRP A 149  SER A 154  1  O  GLN A 152   N  ILE A 119           
SHEET    1   B 4 LYS B   4  ASP B   9  0                                        
SHEET    2   B 4 THR B  82  ALA B  89 -1  O  TYR B  86   N  ARG B   7           
SHEET    3   B 4 ILE B 124  HIS B 131 -1  O  GLY B 126   N  VAL B  87           
SHEET    4   B 4 HIS B 140  ARG B 141 -1  O  HIS B 140   N  TRP B 127           
SHEET    1   C 2 GLY B  21  LEU B  22  0                                        
SHEET    2   C 2 ILE B 119  PRO B 120 -1  O  ILE B 119   N  LEU B  22           
SHEET    1   D 3 TYR B  59  SER B  63  0                                        
SHEET    2   D 3 ASP B 112  LEU B 116 -1  O  VAL B 113   N  THR B  62           
SHEET    3   D 3 MET B  94  ASN B  96 -1  N  PHE B  95   O  SER B 114           
LINK         O2G GTP A 230                MG    MG A 231     1555   1555  2.01  
LINK        MG    MG A 231                 O2B GTP A 230     1555   1555  2.19  
LINK        MG    MG A 231                 O   HOH A 274     1555   1555  2.14  
LINK        MG    MG A 231                 OG1 THR A  27     1555   1555  2.01  
LINK        MG    MG A 231                 O   HOH A 291     1555   1555  2.07  
LINK        MG    MG A 231                 OG1 THR A  44     1555   1555  2.14  
LINK        NA    NA B1326                 O   TYR B 150     1555   1555  2.49  
LINK        NA    NA B1326                 O   LEU B 153     1555   1555  2.30  
LINK        NA    NA B1326                 O   HOH B1597     1555   1555  2.59  
LINK        NA    NA B1326                 O   HOH B1641     1555   1555  2.56  
LINK        NA    NA B1326                 OG1 THR B  90     1555   1555  2.36  
LINK        NA    NA B1326                 O   THR B  90     1555   1555  2.51  
CISPEP   1 GLU B  177    PRO B  178          0        -6.84                     
SITE     1 AC1  5 THR A  27  THR A  44  GTP A 230  HOH A 274                    
SITE     2 AC1  5 HOH A 291                                                     
SITE     1 AC2  5 THR B  90  TYR B 150  LEU B 153  HOH B1597                    
SITE     2 AC2  5 HOH B1641                                                     
SITE     1 AC3 23 ASP A  22  ALA A  23  ALA A  24  GLY A  25                    
SITE     2 AC3 23 LYS A  26  THR A  27  THR A  28  THR A  41                    
SITE     3 AC3 23 THR A  44  GLY A  65  GLY A  66  ASN A 122                    
SITE     4 AC3 23 LYS A 123  ASP A 125  LEU A 126  CYS A 155                    
SITE     5 AC3 23 ALA A 156  THR A 157   MG A 231  HOH A 274                    
SITE     6 AC3 23 HOH A 276  HOH A 291  HOH A1108                               
SITE     1 AC4 19 ARG B   7  ALA B   8  ASP B   9  SER B  10                    
SITE     2 AC4 19 ARG B  11  MET B  23  PRO B  24  ARG B  25                    
SITE     3 AC4 19 SER B  61  THR B  62  SER B  63  VAL B  72                    
SITE     4 AC4 19 LEU B  77  ASP B 110  ASP B 112  HOH B 242                    
SITE     5 AC4 19 HOH B 293  HOH B 295  GOL B1114                               
SITE     1 AC5  8 ARG B   7  HIS B  44  VAL B  53  ASP B  57                    
SITE     2 AC5  8 TYR B  59  VAL B  60  SER B  61  NAD B1536                    
CRYST1   44.905   90.925   98.001  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022269  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010998  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010204        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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