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Database: PDB
Entry: 1HE1
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HEADER    SIGNALING PROTEIN                       18-NOV-00   1HE1              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP DOMAIN OF            
TITLE    2 THE PSEUDOMONAS AERUGINOSA EXOS TOXIN AND HUMAN RAC                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXOENZYME S;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: 96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN);            
COMPND   5 SYNONYM: EXOS;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: 2-184;                                                     
COMPND  11 SYNONYM: P21-RAC1, RAS-LIKE PROTEIN TC25;                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 GENE: EXOS;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    SIGNALING PROTEIN, SIGNALLING COMPLEX, EXOS, RAC,                     
KEYWDS   2 PSEUDOMONAS AERUGINOSA, GAP, TOXIN, VIRULENCE FACTOR,                
KEYWDS   3 TRANSITION STATE, PROTEIN-PROTEIN COMPLEX, GTPASE, SIGNAL            
KEYWDS   4 TRANSDUCTION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WURTELE,E.WOLF,K.J.PEDERSON,G.BUCHWALD,M.R.AHMADIAN,                
AUTHOR   2 J.T.BARBIERI,A.WITTINGHOFER                                          
REVDAT   3   24-FEB-09 1HE1    1       VERSN                                    
REVDAT   2   24-JUL-07 1HE1    1       COMPND                                   
REVDAT   1   02-JAN-01 1HE1    0                                                
JRNL        AUTH   M.WURTELE,E.WOLF,K.J.PEDERSON,G.BUCHWALD,                    
JRNL        AUTH 2 M.R.AHMADIAN,J.T.BARBIERI,A.WITTINGHOFER                     
JRNL        TITL   HOW THE PSEUDOMONAS AERUGINOSA EXOS TOXIN                    
JRNL        TITL 2 DOWNREGULATES RAC                                            
JRNL        REF    NAT.STRUCT.BIOL.              V.   8    23 2001              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11135665                                                     
JRNL        DOI    10.1038/83007                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2288865.96                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53886                          
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) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2739                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8396                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.195                        
REMARK   3   BIN FREE R VALUE                    : 0.252                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.0                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 439                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4742                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 712                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.7                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.5                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.56                                                 
REMARK   3    B22 (A**2) : 0.68                                                 
REMARK   3    B33 (A**2) : -2.23                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.11                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.4                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.5                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.29  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.96  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.29  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.43  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.372576                                             
REMARK   3   BSOL        : 53.2816                                              
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  : GDP.PAR                                        
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : GDP.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HE1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5475.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 527331                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
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: PDB ENTRY 1DS6 CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 40                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 6000, 3MM NICL2,                  
REMARK 280  100 MM TRIS/HCL PH8.5                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.01250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.14200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.54350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.14200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.01250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.54350            
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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    LEU C  19   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    LEU D  19   CA  -  CB  -  CG  ANGL. DEV. =  18.0 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 C  96      -55.98   -129.00                                   
REMARK 500    LYS D  96      -59.85   -125.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR D  72        24.2      L          L   OUTSIDE RANGE           
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                              NI A 230  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 211   ND1                                                    
REMARK 620 2 HOH A2067   O   176.3                                              
REMARK 620 3 HOH A2115   O    99.8  77.6                                        
REMARK 620 4 HOH A2117   O    85.0  97.8  93.6                                  
REMARK 620 5 HOH C2023   O   105.4  71.5  78.0 167.5                            
REMARK 620 6 HOH C2025   O    92.8  89.7 167.3  88.9  97.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI C 203  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 103   NE2                                                    
REMARK 620 2 HOH C2092   O    85.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI D 203  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 103   NE2                                                    
REMARK 620 2 HOH D2091   O    94.9                                              
REMARK 620 3 HOH D2092   O    84.7 117.4                                        
REMARK 620 4 HOH D2093   O    87.5 167.6  74.9                                  
REMARK 620 5 HOH D2143   O   162.7  71.9  91.5 107.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2224   O                                                      
REMARK 620 2 THR C  35   OG1  88.2                                              
REMARK 620 3 GDP C 200   O2B  89.8 176.5                                        
REMARK 620 4 AF3 C 201   F3   90.4  89.1  93.8                                  
REMARK 620 5 HOH C2047   O   178.0  93.6  88.4  90.6                            
REMARK 620 6 THR C  17   OG1  90.0  79.6  97.6 168.7  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AF3 D 201   F1                                                     
REMARK 620 2 THR D  35   OG1  90.3                                              
REMARK 620 3 THR D  17   OG1 170.3  80.3                                        
REMARK 620 4 GDP D 200   O2B  94.0 174.2  95.1                                  
REMARK 620 5 HOH D2224   O    91.6  94.3  91.8  89.5                            
REMARK 620 6 HOH D2046   O    87.9  89.9  89.4  86.4 175.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 C 201  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AF3 C 201   F1                                                     
REMARK 620 2 HOH C2026   O    52.3                                              
REMARK 620 3  MG C 202  MG   134.6  92.7                                        
REMARK 620 4 GDP C 200   O2B 123.7 109.3  33.9                                  
REMARK 620 5 AF3 C 201   F3  123.8  73.9  23.7  56.5                            
REMARK 620 6 HOH C2050   O    83.3  66.8 111.0 144.4  90.1                      
REMARK 620 7 GDP C 200   O3B  88.5 106.8  73.8  41.5  93.1 171.7                
REMARK 620 8 AF3 C 201   F2  110.6 150.0 112.6 100.7 125.0  88.4  96.1          
REMARK 620 N                    1     2     3     4     5     6     7           
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 HOH D2049   O                                                      
REMARK 620 2 GDP D 200   O3B 173.1                                              
REMARK 620 3 AF3 D 201   F1   89.5  91.9                                        
REMARK 620 4 AF3 D 201   F2   82.5  91.0 120.6                                  
REMARK 620 5 HOH D2025   O    66.9 106.9  76.2  46.6                            
REMARK 620 6  MG D 202  MG   109.4  73.3  22.0 130.7  93.0                      
REMARK 620 7 GDP D 200   O2B 142.4  41.5  55.3 124.6 110.7  33.8                
REMARK 620 8 AF3 D 201   F3   87.6  97.0 125.3 113.1 147.6 115.0 101.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI A 230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 201                 
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: 1MH1   RELATED DB: PDB                                   
REMARK 900  SMALL G-PROTEIN                                                     
REMARK 900 RELATED ID: 1HE9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS              
REMARK 900  AERUGINOSA EXOS TOXIN                                               
DBREF  1HE1 A   95   229  UNP    Q51451   Q51451          95    229             
DBREF  1HE1 B   95   229  UNP    Q51451   Q51451          95    229             
DBREF  1HE1 C    1   176  UNP    P15154   RAC1_HUMAN       1    176             
DBREF  1HE1 D    1   176  UNP    P15154   RAC1_HUMAN       1    176             
SEQADV 1HE1 ALA A   95  UNP  Q51451    MET     1 CLONING ARTIFACT               
SEQADV 1HE1 ALA B   95  UNP  Q51451    MET     1 CLONING ARTIFACT               
SEQADV 1HE1 PRO C    1  UNP  P15154    MET     1 CLONING ARTIFACT               
SEQADV 1HE1 PRO D    1  UNP  P15154    MET     1 CLONING ARTIFACT               
SEQRES   1 A  135  ALA SER SER ALA VAL VAL PHE LYS GLN MET VAL LEU GLN          
SEQRES   2 A  135  GLN ALA LEU PRO MET THR LEU LYS GLY LEU ASP LYS ALA          
SEQRES   3 A  135  SER GLU LEU ALA THR LEU THR PRO GLU GLY LEU ALA ARG          
SEQRES   4 A  135  GLU HIS SER ARG LEU ALA SER GLY ASP GLY ALA LEU ARG          
SEQRES   5 A  135  SER LEU SER THR ALA LEU ALA GLY ILE ARG ALA GLY SER          
SEQRES   6 A  135  GLN VAL GLU GLU SER ARG ILE GLN ALA GLY ARG LEU LEU          
SEQRES   7 A  135  GLU ARG SER ILE GLY GLY ILE ALA LEU GLN GLN TRP GLY          
SEQRES   8 A  135  THR THR GLY GLY ALA ALA SER GLN LEU VAL LEU ASP ALA          
SEQRES   9 A  135  SER PRO GLU LEU ARG ARG GLU ILE THR ASP GLN LEU HIS          
SEQRES  10 A  135  GLN VAL MET SER GLU VAL ALA LEU LEU ARG GLN ALA VAL          
SEQRES  11 A  135  GLU SER GLU VAL SER                                          
SEQRES   1 B  135  ALA SER SER ALA VAL VAL PHE LYS GLN MET VAL LEU GLN          
SEQRES   2 B  135  GLN ALA LEU PRO MET THR LEU LYS GLY LEU ASP LYS ALA          
SEQRES   3 B  135  SER GLU LEU ALA THR LEU THR PRO GLU GLY LEU ALA ARG          
SEQRES   4 B  135  GLU HIS SER ARG LEU ALA SER GLY ASP GLY ALA LEU ARG          
SEQRES   5 B  135  SER LEU SER THR ALA LEU ALA GLY ILE ARG ALA GLY SER          
SEQRES   6 B  135  GLN VAL GLU GLU SER ARG ILE GLN ALA GLY ARG LEU LEU          
SEQRES   7 B  135  GLU ARG SER ILE GLY GLY ILE ALA LEU GLN GLN TRP GLY          
SEQRES   8 B  135  THR THR GLY GLY ALA ALA SER GLN LEU VAL LEU ASP ALA          
SEQRES   9 B  135  SER PRO GLU LEU ARG ARG GLU ILE THR ASP GLN LEU HIS          
SEQRES  10 B  135  GLN VAL MET SER GLU VAL ALA LEU LEU ARG GLN ALA VAL          
SEQRES  11 B  135  GLU SER GLU VAL SER                                          
SEQRES   1 C  176  PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 C  176  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 C  176  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 C  176  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 C  176  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 C  176  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 C  176  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 C  176  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 C  176  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 C  176  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 C  176  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 C  176  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 C  176  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 C  176  ASP GLU ALA ILE ARG ALA VAL                                  
SEQRES   1 D  176  PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 D  176  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 D  176  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 D  176  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 D  176  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 D  176  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 D  176  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 D  176  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 D  176  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 D  176  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 D  176  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 D  176  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 D  176  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 D  176  ASP GLU ALA ILE ARG ALA VAL                                  
HET     NI  A 230       1                                                       
HET     MG  C 202       1                                                       
HET     NI  C 203       1                                                       
HET     NI  C 204       2                                                       
HET     MG  D 202       1                                                       
HET     NI  D 203       1                                                       
HET    GDP  C 200      28                                                       
HET    AF3  C 201       4                                                       
HET    GDP  D 200      28                                                       
HET    AF3  D 201       4                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     AF3 ALUMINUM FLUORIDE                                                
FORMUL   5   NI    4(NI 2+)                                                     
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL  11  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL  12  AF3    2()                                                          
FORMUL  15  HOH   *712(H2 O1)                                                   
HELIX    1   1 SER A   96  ALA A  109  1                                  14    
HELIX    2   2 ALA A  109  ALA A  120  1                                  12    
HELIX    3   3 SER A  121  LEU A  126  5                                   6    
HELIX    4   4 THR A  127  HIS A  135  1                                   9    
HELIX    5   5 GLU A  134  ALA A  139  1                                   6    
HELIX    6   6 GLY A  143  SER A  159  1                                  17    
HELIX    7   7 VAL A  161  GLU A  173  1                                  13    
HELIX    8   8 LEU A  181  GLY A  185  1                                   5    
HELIX    9   9 GLY A  189  ALA A  198  1                                  10    
HELIX   10  10 SER A  199  SER A  229  1                                  31    
HELIX   11  11 ALA B   95  ALA B  109  1                                  15    
HELIX   12  12 ALA B  109  ALA B  120  1                                  12    
HELIX   13  13 SER B  121  LEU B  126  5                                   6    
HELIX   14  14 THR B  127  HIS B  135  1                                   9    
HELIX   15  15 GLU B  134  ALA B  139  1                                   6    
HELIX   16  16 GLY B  143  SER B  159  1                                  17    
HELIX   17  17 VAL B  161  ARG B  174  1                                  14    
HELIX   18  18 LEU B  181  GLY B  185  1                                   5    
HELIX   19  19 GLY B  189  ALA B  198  1                                  10    
HELIX   20  20 SER B  199  SER B  229  1                                  31    
HELIX   21  21 GLY C   15  ASN C   26  1                                  12    
HELIX   22  22 GLN C   61  ASP C   65  5                                   5    
HELIX   23  23 LEU C   67  TYR C   72  5                                   6    
HELIX   24  24 SER C   86  LYS C   96  1                                  11    
HELIX   25  25 LYS C   96  CYS C  105  1                                  10    
HELIX   26  26 LYS C  116  ASP C  121  5                                   6    
HELIX   27  27 ASP C  122  LYS C  132  1                                  11    
HELIX   28  28 THR C  138  ILE C  149  1                                  12    
HELIX   29  29 GLY C  164  ALA C  175  1                                  12    
HELIX   30  30 GLY D   15  ASN D   26  1                                  12    
HELIX   31  31 GLN D   61  ASP D   65  5                                   5    
HELIX   32  32 LEU D   67  TYR D   72  5                                   6    
HELIX   33  33 SER D   86  LYS D   96  1                                  11    
HELIX   34  34 LYS D   96  CYS D  105  1                                  10    
HELIX   35  35 LYS D  116  ARG D  120  5                                   5    
HELIX   36  36 ASP D  122  GLU D  131  1                                  10    
HELIX   37  37 THR D  138  GLY D  150  1                                  13    
HELIX   38  38 GLY D  164  ALA D  175  1                                  12    
SHEET    1  AA 2 SER A 175  ILE A 176  0                                        
SHEET    2  AA 2 ILE A 179  ALA A 180 -1  O  ILE A 179   N  ILE A 176           
SHEET    1  BA 2 SER B 175  ILE B 176  0                                        
SHEET    2  BA 2 ILE B 179  ALA B 180 -1  O  ILE B 179   N  ILE B 176           
SHEET    1  CA 6 PHE C  37  VAL C  46  0                                        
SHEET    2  CA 6 LYS C  49  THR C  58 -1  O  LYS C  49   N  VAL C  46           
SHEET    3  CA 6 GLN C   2  GLY C  10  1  O  GLN C   2   N  ASN C  52           
SHEET    4  CA 6 VAL C  77  SER C  83  1  O  VAL C  77   N  VAL C   7           
SHEET    5  CA 6 ILE C 110  THR C 115  1  O  ILE C 111   N  ILE C  80           
SHEET    6  CA 6 LYS C 153  GLU C 156  1  O  LYS C 153   N  LEU C 112           
SHEET    1  DA 6 PHE D  37  VAL D  46  0                                        
SHEET    2  DA 6 LYS D  49  THR D  58 -1  O  LYS D  49   N  VAL D  46           
SHEET    3  DA 6 GLN D   2  VAL D   9  1  O  GLN D   2   N  ASN D  52           
SHEET    4  DA 6 VAL D  77  SER D  83  1  O  VAL D  77   N  VAL D   7           
SHEET    5  DA 6 ILE D 110  THR D 115  1  O  ILE D 111   N  ILE D  80           
SHEET    6  DA 6 LYS D 153  GLU D 156  1  O  LYS D 153   N  LEU D 112           
LINK        NI    NI A 230                 ND1 HIS A 211     1555   1555  2.14  
LINK        NI    NI A 230                 O   HOH A2067     1555   1555  2.36  
LINK        NI    NI A 230                 O   HOH A2115     1555   1555  2.11  
LINK        NI    NI A 230                 O   HOH A2117     1555   1555  2.09  
LINK        NI    NI A 230                 O   HOH C2023     1555   4455  2.11  
LINK        NI    NI A 230                 O   HOH C2025     1555   4455  1.87  
LINK         O2B GDP C 200                MG    MG C 202     1555   1555  2.03  
LINK         O3B GDP C 200                AL   AF3 C 201     1555   1555  2.03  
LINK        AL   AF3 C 201                 O   HOH C2050     1555   1555  2.23  
LINK        AL   AF3 C 201                 O2B GDP C 200     1555   1555  3.51  
LINK        AL   AF3 C 201                 O   HOH C2026     1555   1555  3.55  
LINK         F3  AF3 C 201                MG    MG C 202     1555   1555  1.99  
LINK        AL   AF3 C 201                MG    MG C 202     1555   1555  3.46  
LINK        MG    MG C 202                 O   HOH C2224     1555   1555  2.22  
LINK        MG    MG C 202                 OG1 THR C  35     1555   1555  2.14  
LINK        MG    MG C 202                 O   HOH C2047     1555   1555  2.05  
LINK        MG    MG C 202                 OG1 THR C  17     1555   1555  2.03  
LINK        NI    NI C 203                 NE2 HIS C 103     1555   1555  2.17  
LINK        NI    NI C 203                 O   HOH C2092     1555   1555  2.04  
LINK        NI  B NI C 204                 OD1 ASP D  76     1555   1555  2.12  
LINK        NI  A NI C 204                 OD1 ASP C  76     1555   1555  2.08  
LINK         O3B GDP D 200                AL   AF3 D 201     1555   1555  2.04  
LINK         O2B GDP D 200                MG    MG D 202     1555   1555  2.04  
LINK        AL   AF3 D 201                 O2B GDP D 200     1555   1555  3.51  
LINK         F1  AF3 D 201                MG    MG D 202     1555   1555  1.91  
LINK        AL   AF3 D 201                 O   HOH D2049     1555   1555  2.21  
LINK        AL   AF3 D 201                 O   HOH D2025     1555   1555  3.50  
LINK        AL   AF3 D 201                MG    MG D 202     1555   1555  3.49  
LINK        MG    MG D 202                 O   HOH D2046     1555   1555  2.13  
LINK        MG    MG D 202                 O   HOH D2224     1555   1555  2.06  
LINK        MG    MG D 202                 OG1 THR D  17     1555   1555  2.06  
LINK        MG    MG D 202                 OG1 THR D  35     1555   1555  2.11  
LINK        NI    NI D 203                 O   HOH D2143     1555   1555  2.21  
LINK        NI    NI D 203                 O   HOH D2093     1555   1555  2.30  
LINK        NI    NI D 203                 O   HOH D2092     1555   1555  1.83  
LINK        NI    NI D 203                 O   HOH D2091     1555   1555  1.99  
LINK        NI    NI D 203                 NE2 HIS D 103     1555   1555  2.07  
SITE     1 AC1  6 HIS A 211  HOH A2067  HOH A2115  HOH A2117                    
SITE     2 AC1  6 HOH C2023  HOH C2025                                          
SITE     1 AC2  6 THR C  17  THR C  35  GDP C 200  AF3 C 201                    
SITE     2 AC2  6 HOH C2047  HOH C2224                                          
SITE     1 AC3  2 HIS C 103  HOH C2092                                          
SITE     1 AC4  2 ASP C  76  ASP D  76                                          
SITE     1 AC5  6 THR D  17  THR D  35  GDP D 200  AF3 D 201                    
SITE     2 AC5  6 HOH D2046  HOH D2224                                          
SITE     1 AC6  5 HIS D 103  HOH D2091  HOH D2092  HOH D2093                    
SITE     2 AC6  5 HOH D2143                                                     
SITE     1 AC7 27 ARG A 146  THR A 186  THR A 187  GLY A 188                    
SITE     2 AC7 27 HOH A2094  ALA C  13  VAL C  14  GLY C  15                    
SITE     3 AC7 27 LYS C  16  THR C  17  CYS C  18  TYR C  32                    
SITE     4 AC7 27 LYS C 116  ASP C 118  LEU C 119  SER C 158                    
SITE     5 AC7 27 ALA C 159  LEU C 160  AF3 C 201   MG C 202                    
SITE     6 AC7 27 HOH C2006  HOH C2047  HOH C2224  HOH C2225                    
SITE     7 AC7 27 HOH C2226  HOH C2227  HOH C2228                               
SITE     1 AC8 15 ARG A 146  GLY C  12  ALA C  13  LYS C  16                    
SITE     2 AC8 15 THR C  35  THR C  58  ALA C  59  GLY C  60                    
SITE     3 AC8 15 GLN C  61  GDP C 200   MG C 202  HOH C2026                    
SITE     4 AC8 15 HOH C2047  HOH C2050  HOH C2224                               
SITE     1 AC9 25 ARG B 146  THR B 186  THR B 187  GLY B 188                    
SITE     2 AC9 25 ALA D  13  VAL D  14  GLY D  15  LYS D  16                    
SITE     3 AC9 25 THR D  17  CYS D  18  TYR D  32  LYS D 116                    
SITE     4 AC9 25 ASP D 118  LEU D 119  SER D 158  ALA D 159                    
SITE     5 AC9 25 LEU D 160  AF3 D 201   MG D 202  HOH D2046                    
SITE     6 AC9 25 HOH D2221  HOH D2223  HOH D2224  HOH D2225                    
SITE     7 AC9 25 HOH D2226                                                     
SITE     1 BC1 13 ARG B 146  GLY D  12  ALA D  13  LYS D  16                    
SITE     2 BC1 13 THR D  35  GLY D  60  GLN D  61  GDP D 200                    
SITE     3 BC1 13  MG D 202  HOH D2025  HOH D2046  HOH D2049                    
SITE     4 BC1 13 HOH D2224                                                     
CRYST1   46.025  125.087  136.284  90.00  90.00  90.00 P 21 21 21    8          
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      0.021727  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007994  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007338        0.00000                         
MTRIX1   1 -0.117000  0.849200  0.514900      -49.90880    1                    
MTRIX2   1  0.860200 -0.172500  0.480000       25.66220    1                    
MTRIX3   1  0.496400  0.499000 -0.710300       43.16680    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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