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Database: PDB
Entry: 2A5D
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HEADER    PROTEIN TRANSPORT/TRANSFERASE           30-JUN-05   2A5D              
TITLE     STRUCTURAL BASIS FOR THE ACTIVATION OF CHOLERA TOXIN BY HUMAN ARF6-GTP
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: 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   3   13-JUL-11 2A5D    1       VERSN                                    
REVDAT   2   24-FEB-09 2A5D    1       VERSN                                    
REVDAT   1   16-AUG-05 2A5D    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.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34206                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1798                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1422                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2762                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 291                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : -0.25000                                             
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): 0.118         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.246         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2884 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2507 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3927 ; 2.025 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5800 ; 0.869 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   348 ; 6.128 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   143 ;35.837 ;23.217       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   439 ;13.128 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;18.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3244 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   616 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   600 ; 0.235 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2638 ; 0.219 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1425 ; 0.190 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1562 ; 0.101 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   407 ; 0.231 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.165 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.090 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    15 ; 0.161 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.357 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.236 ; 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):  1731 ; 1.578 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   718 ; 0.449 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2777 ; 2.495 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1215 ; 1.870 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1150 ; 2.708 ; 3.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    20        A   174                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8800  33.5170  29.2760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3478 T22:  -0.2342                                     
REMARK   3      T33:  -0.0983 T12:   0.0183                                     
REMARK   3      T13:  -0.0367 T23:   0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3466 L22:   3.5006                                     
REMARK   3      L33:   2.0554 L12:   1.1026                                     
REMARK   3      L13:   0.4458 L23:   1.7825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:  -0.0522 S13:  -0.1404                       
REMARK   3      S21:   0.1953 S22:   0.0969 S23:  -0.1461                       
REMARK   3      S31:   0.3900 S32:   0.0602 S33:  -0.1484                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B   180                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4280  54.9110  44.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4274 T22:  -0.1555                                     
REMARK   3      T33:  -0.0539 T12:   0.0161                                     
REMARK   3      T13:  -0.0021 T23:  -0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5215 L22:   1.0143                                     
REMARK   3      L33:   0.7304 L12:   0.5422                                     
REMARK   3      L13:   1.1274 L23:   0.5584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1245 S12:  -0.1701 S13:  -0.1771                       
REMARK   3      S21:   0.0907 S22:   0.0192 S23:  -0.2166                       
REMARK   3      S31:   0.0411 S32:   0.0085 S33:  -0.1438                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2A5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033508.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-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               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0781                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36064                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 93.3                               
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.7                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1. MOUSE ARF1 (1O3Y)  2. CTA1 (1S5E)                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
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       22.45750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.27350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.72300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.27350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.45750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.72300            
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: 3310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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     SER A   175                                                      
REMARK 465     SER B     0                                                      
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     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     ASN A  56    CB   CG   OD1                                       
REMARK 470     LYS A  58    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     LYS A 174    CB   CG   CD   CE   NZ                              
REMARK 470     ASP B  14    CG   OD1  OD2                                       
REMARK 470     ARG B  25    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B  49    CB   CG   CD   OE1  NE2                             
REMARK 470     THR B  50    OG1  CG2                                            
REMARK 470     ARG B  67    NE   CZ   NH1  NH2                                  
REMARK 470     ASP B 136    CG   OD1  OD2                                       
REMARK 470     ARG B 143    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   O    HOH B   196     O    HOH B  1444              1.76            
REMARK 500   NE2  GLN B    74     O    HOH B   283              1.95            
REMARK 500   CD   GLN B    74     O    HOH B   283              1.99            
REMARK 500   O1   GOL B  1496     O    HOH B  1393              2.03            
REMARK 500   OE1  GLN B    74     O    HOH B   283              2.04            
REMARK 500   O    HOH A  1325     O    HOH A  1375              2.11            
REMARK 500   NH2  ARG B    11     O    HOH B  1251              2.14            
REMARK 500   O    HOH B   272     O    HOH B  1295              2.17            
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   NE2  GLN B    74     O    PRO B   106     4566     2.03            
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 B 172   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    LYS A 123       40.23     70.05                                   
REMARK 500    PRO A 127      -72.41    -42.27                                   
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 A1231  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GTP A1230   O2G                                                    
REMARK 620 2 GTP A1230   O2B  93.0                                              
REMARK 620 3 HOH A1233   O    89.8  91.1                                        
REMARK 620 4 THR A  44   OG1  84.7 177.7  89.0                                  
REMARK 620 5 THR A  27   OG1 175.5  91.5  89.5  90.7                            
REMARK 620 6 HOH A1232   O    90.5  91.7 177.1  88.2  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 326  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 270   O                                                      
REMARK 620 2 ASN B   1   O    72.2                                              
REMARK 620 3 LEU B 153   O   151.7  79.9                                        
REMARK 620 4 TYR B 150   O    98.0  88.5  85.3                                  
REMARK 620 5 THR B  90   OG1  83.7  88.9  91.6 176.3                            
REMARK 620 6 THR B  90   O   105.4 171.0 101.5 100.4  82.2                      
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 NA B 326                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1231                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1496                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2A5F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A5G   RELATED DB: PDB                                   
DBREF  2A5D A    2   175  UNP    P62330   ARF6_HUMAN       1    174             
DBREF  2A5D B    1   192  UNP    P01555   CHTA_VIBCH      19    210             
SEQADV 2A5D MET A    1  UNP  P62330              INITIATING METHIONINE          
SEQADV 2A5D SER B    0  UNP  P01555              CLONING ARTIFACT               
SEQADV 2A5D ASP B  110  UNP  P01555    GLU   128 ENGINEERED                     
SEQADV 2A5D ASP B  112  UNP  P01555    GLU   130 ENGINEERED                     
SEQADV 2A5D 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     NA  B 326       1                                                       
HET     MG  A1231       1                                                       
HET    GTP  A1230      32                                                       
HET    GOL  B1496       6                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   NA    NA 1+                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GTP    C10 H16 N5 O14 P3                                            
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *291(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  TYR A  173  1                                  13    
HELIX    9   9 PRO B   12  GLY B   20  1                                   9    
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  LEU B   77  1                                  13    
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  ASP A  63   N  ASN A  48           
SHEET    3   A 6 GLU A  13  LEU A  19  1  N  MET A  18   O  TRP A  62           
SHEET    4   A 6 GLY A  83  ASP A  89  1  O  VAL A  87   N  LEU A  19           
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  PRO A 153  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  ILE B  88   N  LEU B   5           
SHEET    3   B 4 ILE B 124  HIS B 131 -1  O  VAL B 130   N  TYR B  83           
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  ALA B 115   N  VAL B  60           
SHEET    3   D 3 MET B  94  ASN B  96 -1  N  PHE B  95   O  SER B 114           
LINK         O2G GTP A1230                MG    MG A1231     1555   1555  2.05  
LINK         O2B GTP A1230                MG    MG A1231     1555   1555  2.03  
LINK        MG    MG A1231                 O   HOH A1233     1555   1555  1.98  
LINK        MG    MG A1231                 OG1 THR A  44     1555   1555  2.07  
LINK        MG    MG A1231                 OG1 THR A  27     1555   1555  2.01  
LINK        MG    MG A1231                 O   HOH A1232     1555   1555  2.07  
LINK        NA    NA B 326                 O   HOH B 270     1555   1555  2.53  
LINK        NA    NA B 326                 O   ASN B   1     1555   1555  2.43  
LINK        NA    NA B 326                 O   LEU B 153     1555   1555  2.43  
LINK        NA    NA B 326                 O   TYR B 150     1555   1555  2.51  
LINK        NA    NA B 326                 OG1 THR B  90     1555   1555  2.28  
LINK        NA    NA B 326                 O   THR B  90     1555   1555  2.46  
CISPEP   1 GLU B  177    PRO B  178          0        -2.31                     
SITE     1 AC1  5 ASN B   1  THR B  90  TYR B 150  LEU B 153                    
SITE     2 AC1  5 HOH B 270                                                     
SITE     1 AC2  5 THR A  27  THR A  44  GTP A1230  HOH A1232                    
SITE     2 AC2  5 HOH A1233                                                     
SITE     1 AC3 28 ASP A  22  ALA A  23  ALA A  24  GLY A  25                    
SITE     2 AC3 28 LYS A  26  THR A  27  THR A  28  THR A  41                    
SITE     3 AC3 28 THR A  44  GLY A  65  GLY A  66  ASN A 122                    
SITE     4 AC3 28 LYS A 123  ASP A 125  LEU A 126  CYS A 155                    
SITE     5 AC3 28 ALA A 156  THR A 157  HOH A 200  HOH A 238                    
SITE     6 AC3 28 HOH A 281   MG A1231  HOH A1232  HOH A1233                    
SITE     7 AC3 28 HOH A1268  HOH A1322  HOH A1342  HOH A1345                    
SITE     1 AC4 10 LYS A  69  PRO A  72  ALA B 159  ASP B 160                    
SITE     2 AC4 10 TYR B 162  GLY B 163  HIS B 182  HOH B1308                    
SITE     3 AC4 10 HOH B1313  HOH B1393                                          
CRYST1   44.915   91.446   98.547  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      0.022264  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010935  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010147        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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