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Database: PDB
Entry: 4FMB
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Original site: 4FMB 
HEADER    PROTEIN BINDING                         16-JUN-12   4FMB              
TITLE     VIRA-RAB1 COMPLEX STRUCTURE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE PROTEASE-LIKE VIRA;                               
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 SYNONYM: EFFECTOR PROTEIN VIRA;                                      
COMPND   5 EC: 3.4.22.-;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RAS-RELATED PROTEIN RAB-1A;                                
COMPND   9 CHAIN: B, D, F;                                                      
COMPND  10 SYNONYM: YPT1-RELATED PROTEIN;                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;                              
SOURCE   3 ORGANISM_TAXID: 623;                                                 
SOURCE   4 STRAIN: 301;                                                         
SOURCE   5 GENE: CP0181, PWR501_0191, VIRA;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RAB1, RAB1A;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALPHA-BETA FOLD, RAB1-GAP COMPLEX, RAB1, PROTEIN BINDING              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.SHAO,Y.ZHU                                                          
REVDAT   2   03-OCT-12 4FMB    1       JRNL                                     
REVDAT   1   05-SEP-12 4FMB    0                                                
JRNL        AUTH   N.DONG,Y.ZHU,Q.LU,L.HU,Y.ZHENG,F.SHAO                        
JRNL        TITL   STRUCTURALLY DISTINCT BACTERIAL TBC-LIKE GAPS LINK ARF       
JRNL        TITL 2 GTPASE TO RAB1 INACTIVATION TO COUNTERACT HOST DEFENSES.     
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 150  1029 2012              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   22939626                                                     
JRNL        DOI    10.1016/J.CELL.2012.06.050                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37746                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1886                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2594                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4134                       
REMARK   3   BIN FREE R VALUE                    : 0.3884                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 142                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12327                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 105.24                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -16.36800                                            
REMARK   3    B22 (A**2) : 24.74700                                             
REMARK   3    B33 (A**2) : -8.37900                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 32.26300                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.603 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.284 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.426 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.825 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 55.06                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:CARBOHYDRATE.PARAM                  
REMARK   3  PARAMETER FILE  6  : GDP.PAR                                        
REMARK   3  PARAMETER FILE  7  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073077.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40511                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M AMMONIUM SULFATE AND 0.1 M TRIS-   
REMARK 280  HCL (PH 7.6), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       93.05900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.65550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.05900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       63.65550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 4340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 38290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 126990 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -246.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     ASN A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     THR A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     ILE A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ALA A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     ASN C   330                                                      
REMARK 465     ASP C   331                                                      
REMARK 465     THR C   332                                                      
REMARK 465     ALA C   333                                                      
REMARK 465     ILE C   334                                                      
REMARK 465     SER C   335                                                      
REMARK 465     ALA C   336                                                      
REMARK 465     SER C   337                                                      
REMARK 465     GLY C   338                                                      
REMARK 465     GLY C   339                                                      
REMARK 465     LYS E   329                                                      
REMARK 465     ASN E   330                                                      
REMARK 465     ASP E   331                                                      
REMARK 465     THR E   332                                                      
REMARK 465     ALA E   333                                                      
REMARK 465     ILE E   334                                                      
REMARK 465     SER E   335                                                      
REMARK 465     ALA E   336                                                      
REMARK 465     SER E   337                                                      
REMARK 465     GLY E   338                                                      
REMARK 465     GLY E   339                                                      
REMARK 465     PRO F     6                                                      
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     VAL A 400    CG1  CG2                                            
REMARK 470     VAL C 400    CG1  CG2                                            
REMARK 470     VAL E 400    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 312   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG B  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG B  82   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG C 312   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG C 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG D  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG D  82   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 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    SER A  70      155.22    -44.98                                   
REMARK 500    PRO A 126       64.56    -68.23                                   
REMARK 500    LYS A 133      139.95   -177.07                                   
REMARK 500    VAL A 141      140.17   -173.17                                   
REMARK 500    PHE A 145       40.92   -106.28                                   
REMARK 500    ASP A 170       33.81    -91.43                                   
REMARK 500    ALA A 192       36.16    -92.15                                   
REMARK 500    MET A 233      174.88    -55.24                                   
REMARK 500    PHE A 254       52.30   -103.62                                   
REMARK 500    ALA A 277      -16.69    -47.41                                   
REMARK 500    MET A 308       77.64   -160.38                                   
REMARK 500    LEU A 349       67.66   -114.89                                   
REMARK 500    PRO A 375       83.66    -68.52                                   
REMARK 500    PRO A 398     -165.12    -72.79                                   
REMARK 500    ILE B  41     -168.00    -75.58                                   
REMARK 500    TYR B 112      -47.95   -137.23                                   
REMARK 500    VAL B 133       -2.52   -143.13                                   
REMARK 500    ASN B 160       18.89     55.70                                   
REMARK 500    ARG B 175      -70.85   -129.77                                   
REMARK 500    SER C  70      155.37    -44.42                                   
REMARK 500    ASP C 105      -33.03   -130.13                                   
REMARK 500    PRO C 126       64.46    -69.50                                   
REMARK 500    LYS C 133      141.51   -177.02                                   
REMARK 500    VAL C 141      141.18   -173.77                                   
REMARK 500    PHE C 145       40.14   -104.65                                   
REMARK 500    ASP C 170       32.78    -91.16                                   
REMARK 500    ALA C 192       36.93    -91.16                                   
REMARK 500    MET C 233      175.51    -56.06                                   
REMARK 500    CYS C 253      -79.17    -57.52                                   
REMARK 500    PHE C 254       51.39    -90.34                                   
REMARK 500    ALA C 277      -17.02    -48.10                                   
REMARK 500    MET C 308       76.26   -159.79                                   
REMARK 500    LEU C 349       68.61   -115.22                                   
REMARK 500    PRO C 375       84.26    -68.98                                   
REMARK 500    ILE C 384       65.88   -119.81                                   
REMARK 500    PRO C 398     -164.58    -72.56                                   
REMARK 500    ILE D  41     -168.41    -78.47                                   
REMARK 500    TYR D 112      -48.38   -137.66                                   
REMARK 500    VAL D 133       -2.26   -142.37                                   
REMARK 500    GLU D 141      -70.46    -64.85                                   
REMARK 500    ASN D 160       19.06     54.83                                   
REMARK 500    ARG D 175      -70.33   -130.22                                   
REMARK 500    SER E  70      155.30    -44.21                                   
REMARK 500    ASP E 105      -32.65   -130.02                                   
REMARK 500    PRO E 126       63.77    -68.15                                   
REMARK 500    LYS E 133      142.81   -175.48                                   
REMARK 500    VAL E 141      140.96   -173.43                                   
REMARK 500    PHE E 145       40.89   -104.48                                   
REMARK 500    ASP E 170       33.96    -91.54                                   
REMARK 500    PHE E 179       19.43     52.92                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 RAMACHANDRAN OUTLIERS.                        
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 B 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 303   O                                                      
REMARK 620 2 HOH B 302   O   178.6                                              
REMARK 620 3 SER B  25   OG   90.9  87.7                                        
REMARK 620 4 GDP B 202   O3B  92.4  87.8  84.8                                  
REMARK 620 5 THR B  43   OG1  92.6  87.3  99.2 173.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 302   O                                                      
REMARK 620 2 HOH D 301   O   176.0                                              
REMARK 620 3 SER D  25   OG   89.7  94.3                                        
REMARK 620 4 THR D  43   OG1  91.1  88.2  98.3                                  
REMARK 620 5 GDP D 202   O3B  90.0  90.8  79.5 177.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F 302   O                                                      
REMARK 620 2 HOH F 301   O   179.6                                              
REMARK 620 3 SER F  25   OG   89.7  90.2                                        
REMARK 620 4 THR F  43   OG1  87.1  92.4  98.5                                  
REMARK 620 5 GDP F 202   O3B  97.2  83.2  82.9 175.4                            
REMARK 620 6 GDP F 202   O1B  75.2 105.2 127.8 129.3  51.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 B 201  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B 202   O1B                                                    
REMARK 620 2 AF3 B 201   F1   89.3                                              
REMARK 620 3 AF3 B 201   F2   90.2 116.9                                        
REMARK 620 4 AF3 B 201   F3   93.4 119.9 123.2                                  
REMARK 620 5 HOH B 301   O   173.5  92.3  94.7  80.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 F 201  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP F 202   O1B                                                    
REMARK 620 2 AF3 F 201   F1   94.7                                              
REMARK 620 3 AF3 F 201   F2   90.3 118.6                                        
REMARK 620 4 AF3 F 201   F3   86.3 122.5 118.9                                  
REMARK 620 5 HOH E 501   O   173.7  88.5  93.0  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 D 201  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP D 202   O1B                                                    
REMARK 620 2 AF3 D 201   F1   96.2                                              
REMARK 620 3 AF3 D 201   F2   87.2 114.3                                        
REMARK 620 4 AF3 D 201   F3   92.9 126.0 119.3                                  
REMARK 620 5 HOH C 501   O   173.2  90.3  92.3  81.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 203                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FMA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FMC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FMD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FME   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES WERE CONFIRMED BY GENE SEQUENCING                           
DBREF  4FMB A   45   400  UNP    Q7BU69   VIRA_SHIFL      45    400             
DBREF  4FMB B    6   176  UNP    P62820   RAB1A_HUMAN      6    176             
DBREF  4FMB C   45   400  UNP    Q7BU69   VIRA_SHIFL      45    400             
DBREF  4FMB D    6   176  UNP    P62820   RAB1A_HUMAN      6    176             
DBREF  4FMB E   45   400  UNP    Q7BU69   VIRA_SHIFL      45    400             
DBREF  4FMB F    6   176  UNP    P62820   RAB1A_HUMAN      6    176             
SEQADV 4FMB GLY A   40  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB PRO A   41  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB LEU A   42  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB GLY A   43  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB SER A   44  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB ALA B   10  UNP  P62820    TYR    10 SEE REMARK 999                 
SEQADV 4FMB GLY C   40  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB PRO C   41  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB LEU C   42  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB GLY C   43  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB SER C   44  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB ALA D   10  UNP  P62820    TYR    10 SEE REMARK 999                 
SEQADV 4FMB GLY E   40  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB PRO E   41  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB LEU E   42  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB GLY E   43  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB SER E   44  UNP  Q7BU69              EXPRESSION TAG                 
SEQADV 4FMB ALA F   10  UNP  P62820    TYR    10 SEE REMARK 999                 
SEQRES   1 A  361  GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU          
SEQRES   2 A  361  ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE          
SEQRES   3 A  361  SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE          
SEQRES   4 A  361  ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS          
SEQRES   5 A  361  LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY          
SEQRES   6 A  361  ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR          
SEQRES   7 A  361  ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN          
SEQRES   8 A  361  LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY          
SEQRES   9 A  361  ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU          
SEQRES  10 A  361  THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP          
SEQRES  11 A  361  ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL          
SEQRES  12 A  361  TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER          
SEQRES  13 A  361  ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO          
SEQRES  14 A  361  LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE          
SEQRES  15 A  361  ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU          
SEQRES  16 A  361  SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE          
SEQRES  17 A  361  PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU          
SEQRES  18 A  361  PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA          
SEQRES  19 A  361  LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER          
SEQRES  20 A  361  SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU          
SEQRES  21 A  361  ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG          
SEQRES  22 A  361  VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA          
SEQRES  23 A  361  VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY          
SEQRES  24 A  361  GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER          
SEQRES  25 A  361  HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU          
SEQRES  26 A  361  THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER          
SEQRES  27 A  361  GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN          
SEQRES  28 A  361  VAL SER PHE ALA ILE ILE SER PRO ASP VAL                      
SEQRES   1 B  171  PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY          
SEQRES   2 B  171  ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE          
SEQRES   3 B  171  ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE          
SEQRES   4 B  171  GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY          
SEQRES   5 B  171  LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN          
SEQRES   6 B  171  GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY          
SEQRES   7 B  171  ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN          
SEQRES   8 B  171  GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE          
SEQRES   9 B  171  ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL          
SEQRES  10 B  171  GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP          
SEQRES  11 B  171  TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE          
SEQRES  12 B  171  PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL          
SEQRES  13 B  171  GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS          
SEQRES  14 B  171  ARG MET                                                      
SEQRES   1 C  361  GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU          
SEQRES   2 C  361  ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE          
SEQRES   3 C  361  SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE          
SEQRES   4 C  361  ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS          
SEQRES   5 C  361  LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY          
SEQRES   6 C  361  ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR          
SEQRES   7 C  361  ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN          
SEQRES   8 C  361  LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY          
SEQRES   9 C  361  ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU          
SEQRES  10 C  361  THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP          
SEQRES  11 C  361  ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL          
SEQRES  12 C  361  TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER          
SEQRES  13 C  361  ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO          
SEQRES  14 C  361  LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE          
SEQRES  15 C  361  ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU          
SEQRES  16 C  361  SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE          
SEQRES  17 C  361  PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU          
SEQRES  18 C  361  PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA          
SEQRES  19 C  361  LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER          
SEQRES  20 C  361  SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU          
SEQRES  21 C  361  ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG          
SEQRES  22 C  361  VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA          
SEQRES  23 C  361  VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY          
SEQRES  24 C  361  GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER          
SEQRES  25 C  361  HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU          
SEQRES  26 C  361  THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER          
SEQRES  27 C  361  GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN          
SEQRES  28 C  361  VAL SER PHE ALA ILE ILE SER PRO ASP VAL                      
SEQRES   1 D  171  PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY          
SEQRES   2 D  171  ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE          
SEQRES   3 D  171  ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE          
SEQRES   4 D  171  GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY          
SEQRES   5 D  171  LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN          
SEQRES   6 D  171  GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY          
SEQRES   7 D  171  ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN          
SEQRES   8 D  171  GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE          
SEQRES   9 D  171  ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL          
SEQRES  10 D  171  GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP          
SEQRES  11 D  171  TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE          
SEQRES  12 D  171  PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL          
SEQRES  13 D  171  GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS          
SEQRES  14 D  171  ARG MET                                                      
SEQRES   1 E  361  GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU          
SEQRES   2 E  361  ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE          
SEQRES   3 E  361  SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE          
SEQRES   4 E  361  ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS          
SEQRES   5 E  361  LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY          
SEQRES   6 E  361  ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR          
SEQRES   7 E  361  ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN          
SEQRES   8 E  361  LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY          
SEQRES   9 E  361  ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU          
SEQRES  10 E  361  THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP          
SEQRES  11 E  361  ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL          
SEQRES  12 E  361  TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER          
SEQRES  13 E  361  ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO          
SEQRES  14 E  361  LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE          
SEQRES  15 E  361  ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU          
SEQRES  16 E  361  SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE          
SEQRES  17 E  361  PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU          
SEQRES  18 E  361  PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA          
SEQRES  19 E  361  LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER          
SEQRES  20 E  361  SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU          
SEQRES  21 E  361  ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG          
SEQRES  22 E  361  VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA          
SEQRES  23 E  361  VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY          
SEQRES  24 E  361  GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER          
SEQRES  25 E  361  HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU          
SEQRES  26 E  361  THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER          
SEQRES  27 E  361  GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN          
SEQRES  28 E  361  VAL SER PHE ALA ILE ILE SER PRO ASP VAL                      
SEQRES   1 F  171  PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY          
SEQRES   2 F  171  ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE          
SEQRES   3 F  171  ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE          
SEQRES   4 F  171  GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY          
SEQRES   5 F  171  LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN          
SEQRES   6 F  171  GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY          
SEQRES   7 F  171  ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN          
SEQRES   8 F  171  GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE          
SEQRES   9 F  171  ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL          
SEQRES  10 F  171  GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP          
SEQRES  11 F  171  TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE          
SEQRES  12 F  171  PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL          
SEQRES  13 F  171  GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS          
SEQRES  14 F  171  ARG MET                                                      
HET    AF3  B 201       4                                                       
HET    GDP  B 202      28                                                       
HET     MG  B 203       1                                                       
HET    AF3  D 201       4                                                       
HET    GDP  D 202      28                                                       
HET     MG  D 203       1                                                       
HET    AF3  F 201       4                                                       
HET    GDP  F 202      28                                                       
HET     MG  F 203       1                                                       
HETNAM     AF3 ALUMINUM FLUORIDE                                                
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   7  AF3    3(AL F3)                                                     
FORMUL   8  GDP    3(C10 H15 N5 O11 P2)                                         
FORMUL   9   MG    3(MG 2+)                                                     
FORMUL  16  HOH   *9(H2 O)                                                      
HELIX    1   1 SER A   47  HIS A   56  1                                  10    
HELIX    2   2 SER A   57  SER A   64  1                                   8    
HELIX    3   3 SER A  113  SER A  123  1                                  11    
HELIX    4   4 ALA A  151  CYS A  161  1                                  11    
HELIX    5   5 SER A  181  ALA A  192  1                                  12    
HELIX    6   6 SER A  193  ASN A  196  5                                   4    
HELIX    7   7 PRO A  208  LEU A  219  1                                  12    
HELIX    8   8 SER A  235  PHE A  247  1                                  13    
HELIX    9   9 PHE A  254  PHE A  265  1                                  12    
HELIX   10  10 ASP A  267  ALA A  277  1                                  11    
HELIX   11  11 SER A  286  MET A  308  1                                  23    
HELIX   12  12 SER A  376  ILE A  384  1                                   9    
HELIX   13  13 PRO A  385  ARG A  389  5                                   5    
HELIX   14  14 GLY B   23  ASP B   33  1                                  11    
HELIX   15  15 GLN B   70  ARG B   72  5                                   3    
HELIX   16  16 PHE B   73  SER B   79  1                                   7    
HELIX   17  17 ASP B   95  ASN B  101  1                                   7    
HELIX   18  18 ASN B  101  ALA B  113  1                                  13    
HELIX   19  19 ASP B  135  SER B  145  1                                  11    
HELIX   20  20 ASN B  160  LYS B  174  1                                  15    
HELIX   21  21 SER C   47  HIS C   56  1                                  10    
HELIX   22  22 SER C   57  SER C   64  1                                   8    
HELIX   23  23 SER C  113  SER C  123  1                                  11    
HELIX   24  24 ALA C  151  CYS C  161  1                                  11    
HELIX   25  25 SER C  181  ALA C  192  1                                  12    
HELIX   26  26 SER C  193  ASN C  196  5                                   4    
HELIX   27  27 PRO C  208  LEU C  219  1                                  12    
HELIX   28  28 SER C  235  PHE C  247  1                                  13    
HELIX   29  29 PHE C  254  PHE C  265  1                                  12    
HELIX   30  30 ASP C  267  ALA C  277  1                                  11    
HELIX   31  31 SER C  286  MET C  308  1                                  23    
HELIX   32  32 SER C  376  ILE C  384  1                                   9    
HELIX   33  33 PRO C  385  ARG C  389  5                                   5    
HELIX   34  34 GLY D   23  ASP D   33  1                                  11    
HELIX   35  35 GLN D   70  ARG D   72  5                                   3    
HELIX   36  36 PHE D   73  SER D   79  1                                   7    
HELIX   37  37 ASP D   95  ASN D  101  1                                   7    
HELIX   38  38 ASN D  101  ALA D  113  1                                  13    
HELIX   39  39 ASP D  135  SER D  145  1                                  11    
HELIX   40  40 ASN D  160  LYS D  174  1                                  15    
HELIX   41  41 SER E   47  HIS E   56  1                                  10    
HELIX   42  42 SER E   57  SER E   64  1                                   8    
HELIX   43  43 SER E  113  SER E  123  1                                  11    
HELIX   44  44 ALA E  151  CYS E  161  1                                  11    
HELIX   45  45 SER E  181  ALA E  192  1                                  12    
HELIX   46  46 SER E  193  ASN E  196  5                                   4    
HELIX   47  47 PRO E  208  LEU E  219  1                                  12    
HELIX   48  48 SER E  235  PHE E  247  1                                  13    
HELIX   49  49 PHE E  254  PHE E  265  1                                  12    
HELIX   50  50 ASP E  267  ALA E  277  1                                  11    
HELIX   51  51 SER E  286  MET E  308  1                                  23    
HELIX   52  52 SER E  376  ILE E  384  1                                   9    
HELIX   53  53 PRO E  385  ARG E  389  5                                   5    
HELIX   54  54 GLY F   23  ASP F   33  1                                  11    
HELIX   55  55 GLN F   70  ARG F   72  5                                   3    
HELIX   56  56 PHE F   73  SER F   79  1                                   7    
HELIX   57  57 ASP F   95  ASN F  101  1                                   7    
HELIX   58  58 ASN F  101  ALA F  113  1                                  13    
HELIX   59  59 ASP F  135  SER F  145  1                                  11    
HELIX   60  60 ASN F  160  LYS F  174  1                                  15    
SHEET    1   A 5 SER A  66  PRO A  67  0                                        
SHEET    2   A 5 GLU A  77  ILE A  83 -1  O  HIS A  80   N  SER A  66           
SHEET    3   A 5 ILE A  86  ASN A  93 -1  O  LEU A  90   N  ALA A  79           
SHEET    4   A 5 ILE A  96  ASP A 103 -1  O  PHE A 100   N  ARG A  89           
SHEET    5   A 5 LYS A 106  GLN A 111 -1  O  THR A 110   N  VAL A  99           
SHEET    1   B 4 GLN A 128  PHE A 129  0                                        
SHEET    2   B 4 THR A 163  ILE A 165  1  O  THR A 163   N  PHE A 129           
SHEET    3   B 4 GLN A 390  ASP A 399 -1  O  PHE A 393   N  SER A 164           
SHEET    4   B 4 THR A 136  SER A 142  1  N  ALA A 139   O  SER A 397           
SHEET    1   C 7 GLN A 128  PHE A 129  0                                        
SHEET    2   C 7 THR A 163  ILE A 165  1  O  THR A 163   N  PHE A 129           
SHEET    3   C 7 GLN A 390  ASP A 399 -1  O  PHE A 393   N  SER A 164           
SHEET    4   C 7 VAL A 358  VAL A 369 -1  N  ILE A 360   O  ILE A 396           
SHEET    5   C 7 TYR A 342  ILE A 353 -1  N  TYR A 342   O  VAL A 369           
SHEET    6   C 7 ASN A 316  ALA A 325 -1  N  ASN A 324   O  GLU A 343           
SHEET    7   C 7 LYS A 199  PHE A 202  1  N  TYR A 201   O  ILE A 323           
SHEET    1   D 6 ASP B  47  ILE B  53  0                                        
SHEET    2   D 6 ILE B  60  ASP B  66 -1  O  ASP B  66   N  ASP B  47           
SHEET    3   D 6 ALA B  10  ILE B  17  1  N  ALA B  10   O  LYS B  61           
SHEET    4   D 6 GLY B  86  ASP B  92  1  O  ILE B  88   N  LEU B  15           
SHEET    5   D 6 ASN B 118  ASN B 124  1  O  ASN B 124   N  TYR B  91           
SHEET    6   D 6 PHE B 150  THR B 153  1  O  LEU B 151   N  GLY B 123           
SHEET    1   E 5 PHE C  65  PRO C  67  0                                        
SHEET    2   E 5 GLU C  77  ILE C  83 -1  O  HIS C  80   N  SER C  66           
SHEET    3   E 5 ILE C  86  ASN C  93 -1  O  LEU C  90   N  PHE C  78           
SHEET    4   E 5 ILE C  96  ASP C 103 -1  O  PHE C 100   N  ARG C  89           
SHEET    5   E 5 LYS C 106  GLN C 111 -1  O  THR C 110   N  VAL C  99           
SHEET    1   F 4 GLN C 128  PHE C 129  0                                        
SHEET    2   F 4 THR C 163  ILE C 165  1  O  THR C 163   N  PHE C 129           
SHEET    3   F 4 GLN C 390  ASP C 399 -1  O  PHE C 393   N  SER C 164           
SHEET    4   F 4 THR C 136  SER C 142  1  N  ALA C 139   O  SER C 397           
SHEET    1   G 7 GLN C 128  PHE C 129  0                                        
SHEET    2   G 7 THR C 163  ILE C 165  1  O  THR C 163   N  PHE C 129           
SHEET    3   G 7 GLN C 390  ASP C 399 -1  O  PHE C 393   N  SER C 164           
SHEET    4   G 7 VAL C 358  VAL C 369 -1  N  ILE C 360   O  ILE C 396           
SHEET    5   G 7 TYR C 342  ILE C 353 -1  N  HIS C 352   O  GLY C 359           
SHEET    6   G 7 ASN C 316  ALA C 325 -1  N  ASN C 324   O  GLU C 343           
SHEET    7   G 7 LYS C 199  PHE C 202  1  N  TYR C 201   O  ILE C 323           
SHEET    1   H 6 ASP D  47  ILE D  53  0                                        
SHEET    2   H 6 ILE D  60  ASP D  66 -1  O  ASP D  66   N  ASP D  47           
SHEET    3   H 6 ALA D  10  ILE D  17  1  N  ALA D  10   O  LYS D  61           
SHEET    4   H 6 GLY D  86  ASP D  92  1  O  VAL D  90   N  ILE D  17           
SHEET    5   H 6 ASN D 118  ASN D 124  1  O  ASN D 124   N  TYR D  91           
SHEET    6   H 6 PHE D 150  THR D 153  1  O  LEU D 151   N  GLY D 123           
SHEET    1   I 5 PHE E  65  PRO E  67  0                                        
SHEET    2   I 5 GLU E  77  ILE E  83 -1  O  HIS E  80   N  SER E  66           
SHEET    3   I 5 ILE E  86  ASN E  93 -1  O  LEU E  90   N  PHE E  78           
SHEET    4   I 5 ILE E  96  ASP E 103 -1  O  PHE E 100   N  ARG E  89           
SHEET    5   I 5 LYS E 106  GLN E 111 -1  O  THR E 110   N  VAL E  99           
SHEET    1   J 4 GLN E 128  PHE E 129  0                                        
SHEET    2   J 4 THR E 163  ILE E 165  1  O  THR E 163   N  PHE E 129           
SHEET    3   J 4 GLN E 390  ASP E 399 -1  O  PHE E 393   N  SER E 164           
SHEET    4   J 4 THR E 136  SER E 142  1  N  ALA E 139   O  SER E 397           
SHEET    1   K 7 GLN E 128  PHE E 129  0                                        
SHEET    2   K 7 THR E 163  ILE E 165  1  O  THR E 163   N  PHE E 129           
SHEET    3   K 7 GLN E 390  ASP E 399 -1  O  PHE E 393   N  SER E 164           
SHEET    4   K 7 VAL E 358  VAL E 369 -1  N  ILE E 360   O  ILE E 396           
SHEET    5   K 7 TYR E 342  ILE E 353 -1  N  TYR E 342   O  VAL E 369           
SHEET    6   K 7 ASN E 316  ALA E 325 -1  N  ASN E 324   O  GLU E 343           
SHEET    7   K 7 LYS E 199  PHE E 202  1  N  TYR E 201   O  ILE E 323           
SHEET    1   L 6 ASP F  47  ILE F  53  0                                        
SHEET    2   L 6 ILE F  60  ASP F  66 -1  O  ASP F  66   N  ASP F  47           
SHEET    3   L 6 ALA F  10  ILE F  17  1  N  ALA F  10   O  LYS F  61           
SHEET    4   L 6 GLY F  86  ASP F  92  1  O  VAL F  90   N  ILE F  17           
SHEET    5   L 6 ASN F 118  ASN F 124  1  O  ASN F 124   N  TYR F  91           
SHEET    6   L 6 PHE F 150  THR F 153  1  O  LEU F 151   N  GLY F 123           
SSBOND   1 CYS A  253    CYS E  355                          1555   1555  2.02  
SSBOND   2 CYS A  355    CYS C  253                          1555   1555  2.00  
SSBOND   3 CYS C  355    CYS E  253                          1555   1555  2.05  
LINK        MG    MG B 203                 O   HOH B 303     1555   1555  1.75  
LINK        MG    MG D 203                 O   HOH D 302     1555   1555  1.92  
LINK        MG    MG F 203                 O   HOH F 302     1555   1555  1.99  
LINK        MG    MG D 203                 O   HOH D 301     1555   1555  2.01  
LINK        MG    MG F 203                 O   HOH F 301     1555   1555  2.02  
LINK        MG    MG B 203                 O   HOH B 302     1555   1555  2.10  
LINK         OG  SER B  25                MG    MG B 203     1555   1555  2.18  
LINK         OG  SER D  25                MG    MG D 203     1555   1555  2.22  
LINK         OG  SER F  25                MG    MG F 203     1555   1555  2.24  
LINK         O3B GDP B 202                MG    MG B 203     1555   1555  2.27  
LINK         OG1 THR F  43                MG    MG F 203     1555   1555  2.42  
LINK         OG1 THR D  43                MG    MG D 203     1555   1555  2.44  
LINK         OG1 THR B  43                MG    MG B 203     1555   1555  2.46  
LINK         O3B GDP D 202                MG    MG D 203     1555   1555  2.52  
LINK         O3B GDP F 202                MG    MG F 203     1555   1555  2.84  
LINK         O1B GDP F 202                MG    MG F 203     1555   1555  2.98  
LINK        AL   AF3 B 201                 O1B GDP B 202     1555   1555  1.93  
LINK        AL   AF3 F 201                 O1B GDP F 202     1555   1555  1.95  
LINK        AL   AF3 D 201                 O1B GDP D 202     1555   1555  1.96  
LINK        AL   AF3 F 201                 O   HOH E 501     1555   1555  2.07  
LINK        AL   AF3 B 201                 O   HOH B 301     1555   1555  2.08  
LINK        AL   AF3 D 201                 O   HOH C 501     1555   1555  2.08  
CISPEP   1 GLY A   40    PRO A   41          0        -0.21                     
CISPEP   2 GLY C   40    PRO C   41          0        -0.04                     
CISPEP   3 GLY E   40    PRO E   41          0        -0.07                     
SITE     1 AC1 13 ARG A 188  GLN A 280  SER B  20  GLY B  21                    
SITE     2 AC1 13 LYS B  24  SER B  42  THR B  43  THR B  67                    
SITE     3 AC1 13 GLY B  69  GDP B 202   MG B 203  HOH B 301                    
SITE     4 AC1 13 HOH B 303                                                     
SITE     1 AC2 21 ARG A 188  ARG A 191  ASP B  19  GLY B  21                    
SITE     2 AC2 21 VAL B  22  GLY B  23  LYS B  24  SER B  25                    
SITE     3 AC2 21 CYS B  26  TYR B  36  ASN B 124  LYS B 125                    
SITE     4 AC2 21 ASP B 127  LEU B 128  SER B 154  ALA B 155                    
SITE     5 AC2 21 LYS B 156  AF3 B 201   MG B 203  HOH B 302                    
SITE     6 AC2 21 HOH B 303                                                     
SITE     1 AC3  6 SER B  25  THR B  43  AF3 B 201  GDP B 202                    
SITE     2 AC3  6 HOH B 302  HOH B 303                                          
SITE     1 AC4 13 ARG C 188  GLN C 280  HOH C 501  SER D  20                    
SITE     2 AC4 13 GLY D  21  LYS D  24  SER D  42  THR D  43                    
SITE     3 AC4 13 THR D  67  GLY D  69  GDP D 202   MG D 203                    
SITE     4 AC4 13 HOH D 302                                                     
SITE     1 AC5 20 ARG C 188  ARG C 191  ASP D  19  GLY D  21                    
SITE     2 AC5 20 VAL D  22  GLY D  23  LYS D  24  SER D  25                    
SITE     3 AC5 20 CYS D  26  TYR D  36  ASN D 124  LYS D 125                    
SITE     4 AC5 20 ASP D 127  LEU D 128  SER D 154  ALA D 155                    
SITE     5 AC5 20 LYS D 156  AF3 D 201   MG D 203  HOH D 302                    
SITE     1 AC6  6 SER D  25  THR D  43  AF3 D 201  GDP D 202                    
SITE     2 AC6  6 HOH D 301  HOH D 302                                          
SITE     1 AC7 11 ARG E 188  GLN E 280  HOH E 501  SER F  20                    
SITE     2 AC7 11 GLY F  21  LYS F  24  THR F  43  THR F  67                    
SITE     3 AC7 11 GLY F  69  GDP F 202   MG F 203                               
SITE     1 AC8 20 ARG E 188  ARG E 191  ASP F  19  GLY F  21                    
SITE     2 AC8 20 VAL F  22  GLY F  23  LYS F  24  SER F  25                    
SITE     3 AC8 20 CYS F  26  TYR F  36  ASN F 124  LYS F 125                    
SITE     4 AC8 20 ASP F 127  LEU F 128  SER F 154  ALA F 155                    
SITE     5 AC8 20 LYS F 156  AF3 F 201   MG F 203  HOH F 302                    
SITE     1 AC9  6 SER F  25  THR F  43  AF3 F 201  GDP F 202                    
SITE     2 AC9  6 HOH F 301  HOH F 302                                          
CRYST1  186.118  127.311  107.325  90.00  94.45  90.00 C 1 2 1      12          
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      0.005373  0.000000  0.000418        0.00000                         
SCALE2      0.000000  0.007855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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