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Database: PDB
Entry: 1HH4
LinkDB: 1HH4
Original site: 1HH4 
HEADER    SIGNALING PROTEIN/INHIBITOR             20-DEC-00   1HH4              
TITLE     RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: P21-RAC1, RAS-LIKE PROTEIN TC25;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RHO GDP-DISSOCIATION INHIBITOR 1;                          
COMPND   8 CHAIN: D, E;                                                         
COMPND   9 SYNONYM: RHO GDI 1, RHO-GDI ALPHA;                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    SIGNALING PROTEIN/INHIBITOR, SINGAL PROTEIN INHIBITOR                 
KEYWDS   2 COMPLEX, SMALL G PROTEIN, GTPASE ACTIVATION, GTP-BINDING,            
KEYWDS   3 PRENYLATION, LIPOPROTEIN                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GRIZOT,J.FAURE,F.FIESCHI,P.V.VIGNAIS,M.-C.DAGHER,                   
AUTHOR   2 E.PEBAY-PEYROULA                                                     
REVDAT   2   24-FEB-09 1HH4    1       VERSN                                    
REVDAT   1   28-AUG-01 1HH4    0                                                
JRNL        AUTH   S.GRIZOT,J.FAURE,F.FIESCHI,P.V.VIGNAIS,M.-C.DAGHER,          
JRNL        AUTH 2 E.PEBAY-PEYROULA                                             
JRNL        TITL   CRYSTAL STRUCTURE OF THE RAC1-RHOGDI COMPLEX                 
JRNL        TITL 2 INVOLVED IN NADPH OXIDASE ACTIVATION                         
JRNL        REF    BIOCHEMISTRY                  V.  40 10007 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11513578                                                     
JRNL        DOI    10.1021/BI010288K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.7  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
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) : 2.7                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.8                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20669                          
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 SET) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.28                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1062                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.5                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3068                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.378                        
REMARK   3   BIN FREE R VALUE                    : 0.449                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5                            
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 165                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5780                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 98                                      
REMARK   3   SOLVENT ATOMS            : 30                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.7                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.4                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.18                                                 
REMARK   3    B22 (A**2) : -4.29                                                
REMARK   3    B33 (A**2) : 0.11                                                 
REMARK   3    B12 (A**2) : 0.0                                                  
REMARK   3    B13 (A**2) : 0.0                                                  
REMARK   3    B23 (A**2) : 0.0                                                  
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.40                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.50                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.60                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.5                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.0                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.94                            
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) : 11.17 ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 17.32 ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 14.59 ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 20.81 ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.29                                                 
REMARK   3   BSOL        : 36.5                                                 
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER-REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : LIG.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TWO GROUPS WERE DEFINED FOR NCS           
REMARK   3  RESTRAINTS, GROUP 1 BETWEEN CHAIN ID A AND B (ALL RESIDUES          
REMARK   3  EXCEPT 28 - 40 AND 178 - 189), GROUP2 BETWEEN CHAIN ID D AND E      
REMARK   3  (RESIDUES 330 - 353 AND 390 - 500)                                  
REMARK   4                                                                      
REMARK   4 1HH4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5664.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21165                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1DOA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 43                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP AT 20C WITH                 
REMARK 280  RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6,                  
REMARK 280  5 MM MGCL2, 200 MM AMMONIUM ACETATE                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       77.35000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       77.35000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.35000            
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                                                    
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 300 DETAILS:THE ASYMMETRIC UNIT CONTAINS TWO HETERODIMERS                
REMARK 300  RAC-RHOGDI,RELATED BY NCS. THE CHAIN IDENTIFIERS                    
REMARK 300  ARE A AND D FOR DIMER1,AND B AND E FOR                              
REMARK 300 DIMER 2.                                                             
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  RACS ARE GTP-BINDING PROTEINS ASSOCIATED WITH PLASMA MEMBRANE       
REMARK 400  WHICH COULD REGULATE SECRETORY PROCESSES.                           
REMARK 400  RHO GDI 1 REGULATES THE GDP/GTP EXCHANGE REACTION OF THE RHO        
REMARK 400  PROTEINS BY INHIBITING THE DISSOCIATION OF GDP FROM THEM.           
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     LEU A   190                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     LEU B   190                                                      
REMARK 465     LEU B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     MET D   301                                                      
REMARK 465     ALA D   302                                                      
REMARK 465     GLU D   303                                                      
REMARK 465     GLN D   304                                                      
REMARK 465     GLU D   305                                                      
REMARK 465     PRO D   306                                                      
REMARK 465     THR D   307                                                      
REMARK 465     ALA D   308                                                      
REMARK 465     VAL D   359                                                      
REMARK 465     ALA D   360                                                      
REMARK 465     VAL D   361                                                      
REMARK 465     SER D   362                                                      
REMARK 465     ALA D   363                                                      
REMARK 465     ASP D   364                                                      
REMARK 465     PRO D   365                                                      
REMARK 465     TRP D   502                                                      
REMARK 465     LYS D   503                                                      
REMARK 465     ASP D   504                                                      
REMARK 465     MET E   301                                                      
REMARK 465     ALA E   302                                                      
REMARK 465     GLU E   303                                                      
REMARK 465     GLN E   304                                                      
REMARK 465     GLU E   305                                                      
REMARK 465     PRO E   306                                                      
REMARK 465     THR E   307                                                      
REMARK 465     ALA E   308                                                      
REMARK 465     GLU E   309                                                      
REMARK 465     GLN E   310                                                      
REMARK 465     LEU E   311                                                      
REMARK 465     ALA E   312                                                      
REMARK 465     GLN E   313                                                      
REMARK 465     ILE E   314                                                      
REMARK 465     ALA E   315                                                      
REMARK 465     ALA E   316                                                      
REMARK 465     GLU E   317                                                      
REMARK 465     ASN E   318                                                      
REMARK 465     GLU E   319                                                      
REMARK 465     GLU E   320                                                      
REMARK 465     ASP E   321                                                      
REMARK 465     GLU E   322                                                      
REMARK 465     LYS E   503                                                      
REMARK 465     ASP E   504                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 128    CG   CD   CE   NZ                                   
REMARK 470     GLU A 131    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 185    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 128    CG   CD   CE   NZ                                   
REMARK 470     LYS B 130    CG   CD   CE   NZ                                   
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     ARG B 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 188    CG   CD   CE   NZ                                   
REMARK 470     GLU D 309    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 310    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 311    CG   CD1  CD2                                       
REMARK 470     GLN D 313    CG   CD   OE1  NE2                                  
REMARK 470     ILE D 314    CG1  CG2  CD1                                       
REMARK 470     GLU D 317    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 319    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 321    CG   OD1  OD2                                       
REMARK 470     GLU D 322    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 420    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 438    CG   CD   CE   NZ                                   
REMARK 470     LYS D 467    CG   CD   CE   NZ                                   
REMARK 470     MET D 469    CG   SD   CE                                        
REMARK 470     LEU D 470    CG   CD1  CD2                                       
REMARK 470     LYS E 438    CG   CD   CE   NZ                                   
REMARK 470     VAL E 462    CG1  CG2                                            
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    THR A    35  -  O    HOH A  2002              2.05            
REMARK 500   O    THR B    35  -  O    HOH B  2001              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 178   CB  -  CA  -  C   ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ALA D 316   N   -  CA  -  CB  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG E 358   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 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 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  96      -58.84   -123.26                                   
REMARK 500    ILE A 126       24.95    -73.88                                   
REMARK 500    GLU A 127      -59.53   -124.56                                   
REMARK 500    CYS A 178       34.23     79.66                                   
REMARK 500    ARG A 185      177.58    -59.32                                   
REMARK 500    LYS A 186       18.06     52.10                                   
REMARK 500    LYS A 188      129.32    -25.87                                   
REMARK 500    ASN B  39       94.03    -58.16                                   
REMARK 500    SER B  41      107.56    175.19                                   
REMARK 500    GLU B  62        3.83    -67.51                                   
REMARK 500    PRO B  69       -7.84    -53.12                                   
REMARK 500    LYS B  96      -56.92   -125.75                                   
REMARK 500    ILE B 126       30.44    -81.99                                   
REMARK 500    GLU B 127      -59.65   -131.64                                   
REMARK 500    CYS B 178        6.68     86.59                                   
REMARK 500    PRO B 180       91.70    -62.22                                   
REMARK 500    PRO B 181        0.98    -69.45                                   
REMARK 500    LYS B 183      -41.66   -134.72                                   
REMARK 500    LYS B 184      117.57   -173.42                                   
REMARK 500    LYS B 186       94.77    -63.51                                   
REMARK 500    ARG B 187       22.13   -148.08                                   
REMARK 500    LYS B 188      -75.22   -118.55                                   
REMARK 500    ILE D 314       91.02    -55.62                                   
REMARK 500    ALA D 315       24.24   -164.50                                   
REMARK 500    ALA D 316       76.26   -167.14                                   
REMARK 500    ASN D 318     -169.38     57.35                                   
REMARK 500    HIS D 323       44.05   -155.74                                   
REMARK 500    ASN D 326       92.61    -62.66                                   
REMARK 500    LEU D 341      -81.54    -63.13                                   
REMARK 500    ASP D 342       72.72   -117.26                                   
REMARK 500    SER D 380       43.30    -90.56                                   
REMARK 500    SER D 381      -62.05   -138.98                                   
REMARK 500    PRO D 385     -159.90    -68.46                                   
REMARK 500    LEU D 386       93.39   -163.65                                   
REMARK 500    LEU D 390       26.03    -62.97                                   
REMARK 500    ASN D 419      -72.04   -104.97                                   
REMARK 500    ARG D 420      -65.56    -94.55                                   
REMARK 500    LYS D 438      106.79    -59.06                                   
REMARK 500    ASP D 440      143.59    172.01                                   
REMARK 500    PRO D 466      173.84    -59.56                                   
REMARK 500    LEU D 470      -63.46   -137.69                                   
REMARK 500    ASP D 483     -165.21   -160.97                                   
REMARK 500    SER D 491      142.47   -179.63                                   
REMARK 500    SER E 324      101.30   -166.58                                   
REMARK 500    ASN E 326       92.83    -68.89                                   
REMARK 500    ALA E 331      155.98    -49.57                                   
REMARK 500    LEU E 341      -99.90    -71.06                                   
REMARK 500    VAL E 359       96.61     77.41                                   
REMARK 500    ALA E 360      136.50    -33.20                                   
REMARK 500    SER E 362      -97.33    -62.80                                   
REMARK 500    ASP E 364      -42.63   -134.63                                   
REMARK 500    PRO E 365      -81.97    -61.81                                   
REMARK 500    ASN E 366      -98.44    -55.12                                   
REMARK 500    VAL E 367      105.13    -14.84                                   
REMARK 500    LEU E 390       36.93    -71.22                                   
REMARK 500    ARG E 420      -67.61    -93.61                                   
REMARK 500    GLU E 421     -161.74   -105.99                                   
REMARK 500    LYS E 438      104.32    -55.83                                   
REMARK 500    ASP E 440      125.55   -175.69                                   
REMARK 500    ARG E 452      168.94    177.60                                   
REMARK 500    PRO E 466     -178.58    -63.18                                   
REMARK 500    LEU E 470      -58.34   -145.96                                   
REMARK 500    ALA E 471       41.71    -87.27                                   
REMARK 500    LYS E 486       16.30     53.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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 A1191  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  35   O                                                      
REMARK 620 2 THR A  17   OG1  69.3                                              
REMARK 620 3 LYS A  16   NZ  147.2 142.7                                        
REMARK 620 4 GDP A1190   O2B  96.3  63.8  95.7                                  
REMARK 620 5 HOH A2002   O    43.5  60.3 133.2  53.4                            
REMARK 620 6 ASP A  57   OD2  85.8  65.8 111.6 124.8 115.0                      
REMARK 620 7 ASP A  57   OD1 124.1 101.9  66.6 130.3 159.7  44.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1191  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  17   OG1                                                    
REMARK 620 2 GDP B1190   O2B  66.1                                              
REMARK 620 3 HOH B2001   O    81.4  51.2                                        
REMARK 620 4 ASP B  57   OD1  99.8 150.2 156.6                                  
REMARK 620 5 ASP B  57   OD2  57.2 122.5 123.0  45.8                            
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  MG A1191                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1191                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A1190                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B1190                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GER D1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GER E1503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E96   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RAC/P67PHOX COMPLEX                                
REMARK 900 RELATED ID: 1HE1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP DOMAIN             
REMARK 900  OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN AND HUMAN RAC              
REMARK 900 RELATED ID: 1MH1   RELATED DB: PDB                                   
REMARK 900  SMALL G-PROTEIN                                                     
REMARK 900 RELATED ID: 1CC0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX                    
REMARK 900 RELATED ID: 1RHO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RHO GUANINE NUCLEOTIDE DISSOCIATION                    
REMARK 900  INHIBITOR                                                           
DBREF  1HH4 A    1   192  UNP    P15154   RAC1_HUMAN       1    192             
DBREF  1HH4 B    1   192  UNP    P15154   RAC1_HUMAN       1    192             
DBREF  1HH4 D  301   504  UNP    P52565   GDIR_HUMAN       1    204             
DBREF  1HH4 E  301   504  UNP    P52565   GDIR_HUMAN       1    204             
SEQADV 1HH4 SER A   78  UNP  P15154    PHE    78 CLONING ARTIFACT               
SEQADV 1HH4 PRO A    1  UNP  P15154    MET     1 CLONING ARTIFACT               
SEQADV 1HH4 SER B   78  UNP  P15154    PHE    78 CLONING ARTIFACT               
SEQADV 1HH4 PRO B    1  UNP  P15154    MET     1 CLONING ARTIFACT               
SEQRES   1 A  192  PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  192  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  192  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  192  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  192  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 A  192  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER          
SEQRES   7 A  192  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  192  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  192  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  192  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  192  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  192  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  192  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  192  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 A  192  LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU                      
SEQRES   1 B  192  PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 B  192  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 B  192  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 B  192  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 B  192  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 B  192  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER          
SEQRES   7 B  192  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 B  192  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 B  192  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 B  192  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 B  192  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 B  192  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 B  192  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 B  192  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 B  192  LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU                      
SEQRES   1 D  204  MET ALA GLU GLN GLU PRO THR ALA GLU GLN LEU ALA GLN          
SEQRES   2 D  204  ILE ALA ALA GLU ASN GLU GLU ASP GLU HIS SER VAL ASN          
SEQRES   3 D  204  TYR LYS PRO PRO ALA GLN LYS SER ILE GLN GLU ILE GLN          
SEQRES   4 D  204  GLU LEU ASP LYS ASP ASP GLU SER LEU ARG LYS TYR LYS          
SEQRES   5 D  204  GLU ALA LEU LEU GLY ARG VAL ALA VAL SER ALA ASP PRO          
SEQRES   6 D  204  ASN VAL PRO ASN VAL VAL VAL THR GLY LEU THR LEU VAL          
SEQRES   7 D  204  CYS SER SER ALA PRO GLY PRO LEU GLU LEU ASP LEU THR          
SEQRES   8 D  204  GLY ASP LEU GLU SER PHE LYS LYS GLN SER PHE VAL LEU          
SEQRES   9 D  204  LYS GLU GLY VAL GLU TYR ARG ILE LYS ILE SER PHE ARG          
SEQRES  10 D  204  VAL ASN ARG GLU ILE VAL SER GLY MET LYS TYR ILE GLN          
SEQRES  11 D  204  HIS THR TYR ARG LYS GLY VAL LYS ILE ASP LYS THR ASP          
SEQRES  12 D  204  TYR MET VAL GLY SER TYR GLY PRO ARG ALA GLU GLU TYR          
SEQRES  13 D  204  GLU PHE LEU THR PRO VAL GLU GLU ALA PRO LYS GLY MET          
SEQRES  14 D  204  LEU ALA ARG GLY SER TYR SER ILE LYS SER ARG PHE THR          
SEQRES  15 D  204  ASP ASP ASP LYS THR ASP HIS LEU SER TRP GLU TRP ASN          
SEQRES  16 D  204  LEU THR ILE LYS LYS ASP TRP LYS ASP                          
SEQRES   1 E  204  MET ALA GLU GLN GLU PRO THR ALA GLU GLN LEU ALA GLN          
SEQRES   2 E  204  ILE ALA ALA GLU ASN GLU GLU ASP GLU HIS SER VAL ASN          
SEQRES   3 E  204  TYR LYS PRO PRO ALA GLN LYS SER ILE GLN GLU ILE GLN          
SEQRES   4 E  204  GLU LEU ASP LYS ASP ASP GLU SER LEU ARG LYS TYR LYS          
SEQRES   5 E  204  GLU ALA LEU LEU GLY ARG VAL ALA VAL SER ALA ASP PRO          
SEQRES   6 E  204  ASN VAL PRO ASN VAL VAL VAL THR GLY LEU THR LEU VAL          
SEQRES   7 E  204  CYS SER SER ALA PRO GLY PRO LEU GLU LEU ASP LEU THR          
SEQRES   8 E  204  GLY ASP LEU GLU SER PHE LYS LYS GLN SER PHE VAL LEU          
SEQRES   9 E  204  LYS GLU GLY VAL GLU TYR ARG ILE LYS ILE SER PHE ARG          
SEQRES  10 E  204  VAL ASN ARG GLU ILE VAL SER GLY MET LYS TYR ILE GLN          
SEQRES  11 E  204  HIS THR TYR ARG LYS GLY VAL LYS ILE ASP LYS THR ASP          
SEQRES  12 E  204  TYR MET VAL GLY SER TYR GLY PRO ARG ALA GLU GLU TYR          
SEQRES  13 E  204  GLU PHE LEU THR PRO VAL GLU GLU ALA PRO LYS GLY MET          
SEQRES  14 E  204  LEU ALA ARG GLY SER TYR SER ILE LYS SER ARG PHE THR          
SEQRES  15 E  204  ASP ASP ASP LYS THR ASP HIS LEU SER TRP GLU TRP ASN          
SEQRES  16 E  204  LEU THR ILE LYS LYS ASP TRP LYS ASP                          
HET     MG  A1191       1                                                       
HET     MG  B1191       1                                                       
HET    GDP  A1190      28                                                       
HET    GDP  B1190      28                                                       
HET    GER  D1502      20                                                       
HET    GER  E1503      20                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     GER GERAN-8-YL GERAN                                                 
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   9  GER    2(C20 H34)                                                   
FORMUL  11  HOH   *30(H2 O1)                                                    
HELIX    1   1 GLY A   15  THR A   25  1                                  11    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 LYS A  116  ARG A  120  5                                   5    
HELIX    7   7 ASP A  124  LEU A  129  1                                   6    
HELIX    8   8 THR A  138  GLY A  150  1                                  13    
HELIX    9   9 GLY A  164  LEU A  177  1                                  14    
HELIX   10  10 GLY B   15  THR B   25  1                                  11    
HELIX   11  11 LEU B   67  TYR B   72  5                                   6    
HELIX   12  12 SER B   86  LYS B   96  1                                  11    
HELIX   13  13 LYS B   96  CYS B  105  1                                  10    
HELIX   14  14 LYS B  116  ARG B  120  5                                   5    
HELIX   15  15 ASP B  124  LEU B  129  1                                   6    
HELIX   16  16 LYS B  130  LYS B  133  5                                   4    
HELIX   17  17 THR B  138  GLY B  150  1                                  13    
HELIX   18  18 GLY B  164  LEU B  177  1                                  14    
HELIX   19  19 SER D  334  GLU D  340  1                                   7    
HELIX   20  20 ASP D  345  GLY D  357  1                                  13    
HELIX   21  21 LEU D  394  LYS D  399  5                                   6    
HELIX   22  22 SER E  334  GLU E  340  1                                   7    
HELIX   23  23 ASP E  345  GLY E  357  1                                  13    
HELIX   24  24 LEU E  394  LYS E  399  5                                   6    
HELIX   25  25 LYS E  467  ARG E  472  1                                   6    
SHEET    1  AA 6 TYR A  40  MET A  45  0                                        
SHEET    2  AA 6 PRO A  50  ASP A  57 -1  O  VAL A  51   N  VAL A  44           
SHEET    3  AA 6 LYS A   5  GLY A  10  1  O  CYS A   6   N  TRP A  56           
SHEET    4  AA 6 VAL A  77  SER A  83  1  O  VAL A  77   N  VAL A   7           
SHEET    5  AA 6 ILE A 110  THR A 115  1  O  ILE A 111   N  ILE A  80           
SHEET    6  AA 6 LYS A 153  GLU A 156  1  O  LYS A 153   N  LEU A 112           
SHEET    1  BA 6 ALA B  42  MET B  45  0                                        
SHEET    2  BA 6 PRO B  50  ASP B  57 -1  O  VAL B  51   N  VAL B  44           
SHEET    3  BA 6 GLN B   2  GLY B  10  1  O  GLN B   2   N  ASN B  52           
SHEET    4  BA 6 VAL B  77  SER B  83  1  O  VAL B  77   N  VAL B   7           
SHEET    5  BA 6 ILE B 110  THR B 115  1  O  ILE B 111   N  ILE B  80           
SHEET    6  BA 6 LYS B 153  GLU B 156  1  O  LYS B 153   N  LEU B 112           
SHEET    1  DA 4 GLU D 387  ASP D 389  0                                        
SHEET    2  DA 4 VAL D 370  CYS D 379 -1  O  LEU D 375   N  LEU D 388           
SHEET    3  DA 4 GLU D 409  VAL D 418 -1  O  ARG D 411   N  VAL D 378           
SHEET    4  DA 4 GLU D 463  GLU D 464 -1  O  GLU D 463   N  TYR D 410           
SHEET    1  DB 4 GLU D 387  ASP D 389  0                                        
SHEET    2  DB 4 VAL D 370  CYS D 379 -1  O  LEU D 375   N  LEU D 388           
SHEET    3  DB 4 GLU D 409  VAL D 418 -1  O  ARG D 411   N  VAL D 378           
SHEET    4  DB 4 TYR D 456  LEU D 459 -1  O  TYR D 456   N  PHE D 416           
SHEET    1  DC 5 SER D 401  LEU D 404  0                                        
SHEET    2  DC 5 LEU D 490  ILE D 498  1  O  ASN D 495   N  PHE D 402           
SHEET    3  DC 5 SER D 474  THR D 482 -1  O  TYR D 475   N  LEU D 496           
SHEET    4  DC 5 VAL D 423  TYR D 433 -1  O  LYS D 427   N  THR D 482           
SHEET    5  DC 5 LYS D 438  TYR D 449 -1  N  ILE D 439   O  THR D 432           
SHEET    1  EA 4 LEU E 386  ASP E 389  0                                        
SHEET    2  EA 4 VAL E 370  CYS E 379 -1  O  LEU E 375   N  LEU E 388           
SHEET    3  EA 4 GLU E 409  VAL E 418 -1  O  ARG E 411   N  VAL E 378           
SHEET    4  EA 4 GLU E 463  GLU E 464 -1  O  GLU E 463   N  TYR E 410           
SHEET    1  EB 4 LEU E 386  ASP E 389  0                                        
SHEET    2  EB 4 VAL E 370  CYS E 379 -1  O  LEU E 375   N  LEU E 388           
SHEET    3  EB 4 GLU E 409  VAL E 418 -1  O  ARG E 411   N  VAL E 378           
SHEET    4  EB 4 TYR E 456  LEU E 459 -1  O  TYR E 456   N  PHE E 416           
SHEET    1  EC 5 SER E 401  LYS E 405  0                                        
SHEET    2  EC 5 LEU E 490  LYS E 499  1  O  ASN E 495   N  PHE E 402           
SHEET    3  EC 5 SER E 474  THR E 482 -1  O  TYR E 475   N  LEU E 496           
SHEET    4  EC 5 VAL E 423  TYR E 433 -1  O  LYS E 427   N  THR E 482           
SHEET    5  EC 5 LYS E 438  TYR E 449 -1  N  ILE E 439   O  THR E 432           
LINK        MG    MG A1191                 O   THR A  35     1555   1555  2.89  
LINK        MG    MG A1191                 OG1 THR A  17     1555   1555  2.38  
LINK        MG    MG A1191                 NZ  LYS A  16     1555   1555  2.97  
LINK        MG    MG A1191                 O2B GDP A1190     1555   1555  2.79  
LINK        MG    MG A1191                 O   HOH A2002     1555   1555  2.59  
LINK        MG    MG A1191                 OD2 ASP A  57     1555   1555  2.74  
LINK        MG    MG A1191                 OD1 ASP A  57     1555   1555  2.97  
LINK        MG    MG B1191                 O2B GDP B1190     1555   1555  2.77  
LINK        MG    MG B1191                 O   HOH B2001     1555   1555  2.48  
LINK        MG    MG B1191                 OD1 ASP B  57     1555   1555  2.78  
LINK        MG    MG B1191                 OD2 ASP B  57     1555   1555  2.90  
LINK        MG    MG B1191                 OG1 THR B  17     1555   1555  2.63  
SITE     1 AC1  7 LYS A  16  THR A  17  THR A  35  ASP A  57                    
SITE     2 AC1  7 THR A  58  GDP A1190  HOH A2002                               
SITE     1 AC2  7 LYS B  16  THR B  17  THR B  35  ASP B  57                    
SITE     2 AC2  7 THR B  58  GDP B1190  HOH B2001                               
SITE     1 AC3 16 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC3 16 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC3 16 ILE A  33  LYS A 116  ASP A 118  LEU A 119                    
SITE     4 AC3 16 ALA A 159  LEU A 160   MG A1191  HOH A2002                    
SITE     1 AC4 17 GLY B  12  ALA B  13  VAL B  14  GLY B  15                    
SITE     2 AC4 17 LYS B  16  THR B  17  CYS B  18  PHE B  28                    
SITE     3 AC4 17 ILE B  33  LYS B 116  ASP B 118  LEU B 119                    
SITE     4 AC4 17 ALA B 159  LEU B 160   MG B1191  HOH B2001                    
SITE     5 AC4 17 HOH B2006                                                     
SITE     1 AC5  9 LEU D 377  TYR D 410  GLN D 430  THR D 432                    
SITE     2 AC5  9 ILE D 439  PRO D 466  ALA D 471  TRP D 494                    
SITE     3 AC5  9 LEU D 496                                                     
SITE     1 AC6 12 ARG B 187  LYS B 188  CYS B 189  LEU E 377                    
SITE     2 AC6 12 TYR E 410  GLN E 430  THR E 432  ILE E 439                    
SITE     3 AC6 12 PRO E 466  ALA E 471  TRP E 494  LEU E 496                    
CRYST1  154.700   88.700   62.600  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006464  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015974        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system