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Database: PDB
Entry: 1W0O
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Original site: 1W0O 
HEADER    HYDROLASE                               09-JUN-04   1W0O              
TITLE     VIBRIO CHOLERAE SIALIDASE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NEURAMINIDASE, NANASE;                                      
COMPND   5 EC: 3.2.1.18                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666                                                  
KEYWDS    VIBRIO CHOLERAE, SIALIDASE, GLYCOSIDASE, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV,J.C.WILSON,                  
AUTHOR   2 M.J.KIEFEL,M.VON-ITZSTEIN,G.TAYLOR                                   
REVDAT   3   24-FEB-09 1W0O    1       VERSN                                    
REVDAT   2   24-SEP-04 1W0O    1       JRNL                                     
REVDAT   1   08-JUL-04 1W0O    0                                                
JRNL        AUTH   I.MOUSTAFA,H.CONNARIS,M.TAYLOR,V.ZAITSEV,                    
JRNL        AUTH 2 J.C.WILSONM.J.KIEFEL,M.VON-ITZSTEIN,G.TAYLOR                 
JRNL        TITL   SIALIC ACID RECOGNITION BY VIBRIO CHOLERAE                   
JRNL        TITL 2 NEURAMINIDASE                                                
JRNL        REF    J.BIOL.CHEM.                  V. 279 40819 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15226294                                                     
JRNL        DOI    10.1074/JBC.M404965200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.9  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) : 1.9                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100                            
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58159                          
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) : 0.1794                          
REMARK   3   FREE R VALUE                     : 0.2178                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.3                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5918                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5827                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 920                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.717                                                
REMARK   3    B22 (A**2) : 0.484                                                
REMARK   3    B33 (A**2) : -1.201                                               
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.000                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005065                        
REMARK   3   BOND ANGLES            (DEGREES) : 1.31648                         
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.378267                                             
REMARK   3   BSOL        : 57.0826                                              
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  : DANA.PARAM                                     
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DANA.TOP                                       
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1W0O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-20132.                                       
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                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63699                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       35.15500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.80750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.45500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.80750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.15500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.45500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     PHE A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     LEU A   778                                                      
REMARK 465     SER A   779                                                      
REMARK 465     GLN A   780                                                      
REMARK 465     ASN A   781                                                      
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    ASN A  51     -124.62     45.81                                   
REMARK 500    ALA A  60      -16.15    -49.52                                   
REMARK 500    MET A 190      159.11    174.25                                   
REMARK 500    ILE A 225       72.29     62.47                                   
REMARK 500    ASN A 283       44.54   -144.73                                   
REMARK 500    ASP A 292       73.29     48.13                                   
REMARK 500    ALA A 316     -157.73   -145.72                                   
REMARK 500    PRO A 327       25.82    -62.64                                   
REMARK 500    SER A 402      -40.86   -131.74                                   
REMARK 500    PRO A 516       -9.24    -58.41                                   
REMARK 500    ARG A 577      -58.29   -152.69                                   
REMARK 500    SER A 610      -31.23   -154.60                                   
REMARK 500    SER A 618      -98.82   -133.52                                   
REMARK 500    PHE A 638     -134.59     57.78                                   
REMARK 500    SER A 648     -179.63     71.11                                   
REMARK 500    ALA A 667       12.89     58.70                                   
REMARK 500    ASN A 668       78.27   -110.35                                   
REMARK 500    ASN A 669     -147.23   -129.71                                   
REMARK 500    ASN A 714       80.32     43.01                                   
REMARK 500    ALA A 739     -117.11   -116.07                                   
REMARK 500    THR A 757     -127.79   -127.84                                   
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                              CA A1779  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 313   OG1                                                    
REMARK 620 2 ASP A 289   OD1  83.0                                              
REMARK 620 3 ASP A 289   OD2 102.7  53.1                                        
REMARK 620 4 THR A 313   O    71.6 119.4  79.9                                  
REMARK 620 5 ALA A 253   O   107.2 167.2 129.1  72.1                            
REMARK 620 6 ASN A 256   OD1 150.1  87.7  94.0 136.5  79.6                      
REMARK 620 7 ASN A 256   O    78.3  85.1 137.1 137.3  89.4  72.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1780  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 548   O                                                      
REMARK 620 2 ASP A 621   OD1 111.0                                              
REMARK 620 3 ASP A 621   OD2  89.9  52.9                                        
REMARK 620 4 ASP A 682   OD1  94.0  87.9 138.8                                  
REMARK 620 5 ASP A 682   OD2  87.9 139.8 166.6  54.6                            
REMARK 620 6 ALA A 683   O   174.2  74.5  92.3  87.8  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1781  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 320   OD1                                                    
REMARK 620 2 PHE A 578   O    87.8                                              
REMARK 620 3 ASP A 320   OD2  50.7 102.4                                        
REMARK 620 4 HOH A2466   O   107.2 161.3  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1782  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2367   O                                                      
REMARK 620 2 HOH A2426   O    74.5                                              
REMARK 620 3 ASP A 286   OD1  81.8  87.8                                        
REMARK 620 4 HOH A2433   O    84.9 159.4  88.4                                  
REMARK 620 5 HOH A2434   O   142.6 134.9  77.8  63.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A1783                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1779                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1780                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1781                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1782                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1778                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KIT   RELATED DB: PDB                                   
REMARK 900  VIBRIO CHOLERAE NEURAMINIDASE                                       
REMARK 900 RELATED ID: 1W0P   RELATED DB: PDB                                   
REMARK 900  VIBRIO CHOLERAE SIALIDASE                                           
DBREF  1W0O A    1   781  UNP    P37060   NANH_VIBCH       1    781             
SEQRES   1 A  781  MET ARG PHE LYS ASN VAL LYS LYS THR ALA LEU MET LEU          
SEQRES   2 A  781  ALA MET PHE GLY MET ALA THR SER SER ASN ALA ALA LEU          
SEQRES   3 A  781  PHE ASP TYR ASN ALA THR GLY ASP THR GLU PHE ASP SER          
SEQRES   4 A  781  PRO ALA LYS GLN GLY TRP MET GLN ASP ASN THR ASN ASN          
SEQRES   5 A  781  GLY SER GLY VAL LEU THR ASN ALA ASP GLY MET PRO ALA          
SEQRES   6 A  781  TRP LEU VAL GLN GLY ILE GLY GLY ARG ALA GLN TRP THR          
SEQRES   7 A  781  TYR SER LEU SER THR ASN GLN HIS ALA GLN ALA SER SER          
SEQRES   8 A  781  PHE GLY TRP ARG MET THR THR GLU MET LYS VAL LEU SER          
SEQRES   9 A  781  GLY GLY MET ILE THR ASN TYR TYR ALA ASN GLY THR GLN          
SEQRES  10 A  781  ARG VAL LEU PRO ILE ILE SER LEU ASP SER SER GLY ASN          
SEQRES  11 A  781  LEU VAL VAL GLU PHE GLU GLY GLN THR GLY ARG THR VAL          
SEQRES  12 A  781  LEU ALA THR GLY THR ALA ALA THR GLU TYR HIS LYS PHE          
SEQRES  13 A  781  GLU LEU VAL PHE LEU PRO GLY SER ASN PRO SER ALA SER          
SEQRES  14 A  781  PHE TYR PHE ASP GLY LYS LEU ILE ARG ASP ASN ILE GLN          
SEQRES  15 A  781  PRO THR ALA SER LYS GLN ASN MET ILE VAL TRP GLY ASN          
SEQRES  16 A  781  GLY SER SER ASN THR ASP GLY VAL ALA ALA TYR ARG ASP          
SEQRES  17 A  781  ILE LYS PHE GLU ILE GLN GLY ASP VAL ILE PHE ARG GLY          
SEQRES  18 A  781  PRO ASP ARG ILE PRO SER ILE VAL ALA SER SER VAL THR          
SEQRES  19 A  781  PRO GLY VAL VAL THR ALA PHE ALA GLU LYS ARG VAL GLY          
SEQRES  20 A  781  GLY GLY ASP PRO GLY ALA LEU SER ASN THR ASN ASP ILE          
SEQRES  21 A  781  ILE THR ARG THR SER ARG ASP GLY GLY ILE THR TRP ASP          
SEQRES  22 A  781  THR GLU LEU ASN LEU THR GLU GLN ILE ASN VAL SER ASP          
SEQRES  23 A  781  GLU PHE ASP PHE SER ASP PRO ARG PRO ILE TYR ASP PRO          
SEQRES  24 A  781  SER SER ASN THR VAL LEU VAL SER TYR ALA ARG TRP PRO          
SEQRES  25 A  781  THR ASP ALA ALA GLN ASN GLY ASP ARG ILE LYS PRO TRP          
SEQRES  26 A  781  MET PRO ASN GLY ILE PHE TYR SER VAL TYR ASP VAL ALA          
SEQRES  27 A  781  SER GLY ASN TRP GLN ALA PRO ILE ASP VAL THR ASP GLN          
SEQRES  28 A  781  VAL LYS GLU ARG SER PHE GLN ILE ALA GLY TRP GLY GLY          
SEQRES  29 A  781  SER GLU LEU TYR ARG ARG ASN THR SER LEU ASN SER GLN          
SEQRES  30 A  781  GLN ASP TRP GLN SER ASN ALA LYS ILE ARG ILE VAL ASP          
SEQRES  31 A  781  GLY ALA ALA ASN GLN ILE GLN VAL ALA ASP GLY SER ARG          
SEQRES  32 A  781  LYS TYR VAL VAL THR LEU SER ILE ASP GLU SER GLY GLY          
SEQRES  33 A  781  LEU VAL ALA ASN LEU ASN GLY VAL SER ALA PRO ILE ILE          
SEQRES  34 A  781  LEU GLN SER GLU HIS ALA LYS VAL HIS SER PHE HIS ASP          
SEQRES  35 A  781  TYR GLU LEU GLN TYR SER ALA LEU ASN HIS THR THR THR          
SEQRES  36 A  781  LEU PHE VAL ASP GLY GLN GLN ILE THR THR TRP ALA GLY          
SEQRES  37 A  781  GLU VAL SER GLN GLU ASN ASN ILE GLN PHE GLY ASN ALA          
SEQRES  38 A  781  ASP ALA GLN ILE ASP GLY ARG LEU HIS VAL GLN LYS ILE          
SEQRES  39 A  781  VAL LEU THR GLN GLN GLY HIS ASN LEU VAL GLU PHE ASP          
SEQRES  40 A  781  ALA PHE TYR LEU ALA GLN GLN THR PRO GLU VAL GLU LYS          
SEQRES  41 A  781  ASP LEU GLU LYS LEU GLY TRP THR LYS ILE LYS THR GLY          
SEQRES  42 A  781  ASN THR MET SER LEU TYR GLY ASN ALA SER VAL ASN PRO          
SEQRES  43 A  781  GLY PRO GLY HIS GLY ILE THR LEU THR ARG GLN GLN ASN          
SEQRES  44 A  781  ILE SER GLY SER GLN ASN GLY ARG LEU ILE TYR PRO ALA          
SEQRES  45 A  781  ILE VAL LEU ASP ARG PHE PHE LEU ASN VAL MET SER ILE          
SEQRES  46 A  781  TYR SER ASP ASP GLY GLY SER ASN TRP GLN THR GLY SER          
SEQRES  47 A  781  THR LEU PRO ILE PRO PHE ARG TRP LYS SER SER SER ILE          
SEQRES  48 A  781  LEU GLU THR LEU GLU PRO SER GLU ALA ASP MET VAL GLU          
SEQRES  49 A  781  LEU GLN ASN GLY ASP LEU LEU LEU THR ALA ARG LEU ASP          
SEQRES  50 A  781  PHE ASN GLN ILE VAL ASN GLY VAL ASN TYR SER PRO ARG          
SEQRES  51 A  781  GLN GLN PHE LEU SER LYS ASP GLY GLY ILE THR TRP SER          
SEQRES  52 A  781  LEU LEU GLU ALA ASN ASN ALA ASN VAL PHE SER ASN ILE          
SEQRES  53 A  781  SER THR GLY THR VAL ASP ALA SER ILE THR ARG PHE GLU          
SEQRES  54 A  781  GLN SER ASP GLY SER HIS PHE LEU LEU PHE THR ASN PRO          
SEQRES  55 A  781  GLN GLY ASN PRO ALA GLY THR ASN GLY ARG GLN ASN LEU          
SEQRES  56 A  781  GLY LEU TRP PHE SER PHE ASP GLU GLY VAL THR TRP LYS          
SEQRES  57 A  781  GLY PRO ILE GLN LEU VAL ASN GLY ALA SER ALA TYR SER          
SEQRES  58 A  781  ASP ILE TYR GLN LEU ASP SER GLU ASN ALA ILE VAL ILE          
SEQRES  59 A  781  VAL GLU THR ASP ASN SER ASN MET ARG ILE LEU ARG MET          
SEQRES  60 A  781  PRO ILE THR LEU LEU LYS GLN LYS LEU THR LEU SER GLN          
SEQRES  61 A  781  ASN                                                          
HET    SIA  A1783      21                                                       
HET     CA  A1779       1                                                       
HET     CA  A1780       1                                                       
HET     CA  A1781       1                                                       
HET     CA  A1782       1                                                       
HET    DAN  A1778      20                                                       
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   2  SIA    C11 H19 N O9                                                 
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  DAN    C11 H17 N O8                                                 
FORMUL   8  HOH   *920(H2 O1)                                                   
HELIX    1   1 ASP A   34  ASP A   38  5                                   5    
HELIX    2   2 SER A   39  GLY A   44  5                                   6    
HELIX    3   3 SER A   82  GLY A   93  1                                  12    
HELIX    4   4 THR A  146  GLU A  152  5                                   7    
HELIX    5   5 THR A  279  ASN A  283  5                                   5    
HELIX    6   6 GLN A  317  ARG A  321  5                                   5    
HELIX    7   7 VAL A  348  LYS A  353  1                                   6    
HELIX    8   8 GLU A  433  HIS A  438  1                                   6    
HELIX    9   9 ALA A  508  GLN A  513  1                                   6    
HELIX   10  10 SER A  608  SER A  610  5                                   3    
HELIX   11  11 ASN A  671  PHE A  673  5                                   3    
HELIX   12  12 ASP A  758  SER A  760  5                                   3    
HELIX   13  13 ILE A  769  LYS A  773  1                                   5    
HELIX   14  14 GLN A  774  LEU A  776  5                                   3    
SHEET    1  AA 4 LEU A  26  ASN A  30  0                                        
SHEET    2  AA 4 GLY A 202  ILE A 213 -1  O  ILE A 209   N  TYR A  29           
SHEET    3  AA 4 ALA A  65  GLY A  70 -1  O  TRP A  66   N  TYR A 206           
SHEET    4  AA 4 SER A  54  THR A  58 -1  O  SER A  54   N  GLN A  69           
SHEET    1  AB 6 LEU A  26  ASN A  30  0                                        
SHEET    2  AB 6 GLY A 202  ILE A 213 -1  O  ILE A 209   N  TYR A  29           
SHEET    3  AB 6 TRP A  94  GLY A 105 -1  O  ARG A  95   N  GLU A 212           
SHEET    4  AB 6 HIS A 154  LEU A 161 -1  O  HIS A 154   N  MET A 100           
SHEET    5  AB 6 SER A 167  PHE A 172 -1  O  SER A 167   N  LEU A 161           
SHEET    6  AB 6 LYS A 175  ILE A 181 -1  O  LYS A 175   N  PHE A 172           
SHEET    1  AC 6 MET A  46  GLN A  47  0                                        
SHEET    2  AC 6 ALA A  75  TYR A  79 -1  O  THR A  78   N  MET A  46           
SHEET    3  AC 6 ASN A 189  ASN A 195 -1  O  ILE A 191   N  TYR A  79           
SHEET    4  AC 6 TYR A 111  ASN A 114 -1  O  TYR A 111   N  VAL A 192           
SHEET    5  AC 6 GLN A 117  VAL A 119 -1  O  GLN A 117   N  ASN A 114           
SHEET    6  AC 6 THR A 184  ALA A 185 -1  O  THR A 184   N  ARG A 118           
SHEET    1  AD 4 ILE A 108  THR A 109  0                                        
SHEET    2  AD 4 PRO A 121  LEU A 125 -1  O  ILE A 123   N  ILE A 108           
SHEET    3  AD 4 LEU A 131  PHE A 135 -1  O  VAL A 132   N  SER A 124           
SHEET    4  AD 4 THR A 142  ALA A 145 -1  O  THR A 142   N  VAL A 133           
SHEET    1  AE 4 ASP A 216  PHE A 219  0                                        
SHEET    2  AE 4 MET A 762  PRO A 768 -1  O  MET A 762   N  ILE A 218           
SHEET    3  AE 4 ASN A 750  GLU A 756 -1  O  ALA A 751   N  MET A 767           
SHEET    4  AE 4 SER A 741  GLN A 745 -1  O  ASP A 742   N  ILE A 754           
SHEET    1  AF 4 ARG A 224  ALA A 230  0                                        
SHEET    2  AF 4 VAL A 238  VAL A 246 -1  O  THR A 239   N  VAL A 229           
SHEET    3  AF 4 THR A 257  SER A 265 -1  O  THR A 257   N  VAL A 246           
SHEET    4  AF 4 LEU A 276  ASN A 277 -1  O  LEU A 276   N  THR A 262           
SHEET    1  AG 4 PHE A 288  ASP A 298  0                                        
SHEET    2  AG 4 THR A 303  PRO A 312 -1  O  THR A 303   N  ASP A 298           
SHEET    3  AG 4 GLY A 329  ASP A 336 -1  O  GLY A 329   N  ARG A 310           
SHEET    4  AG 4 ILE A 346  ASP A 347 -1  O  ILE A 346   N  TYR A 332           
SHEET    1  AH 4 PHE A 288  ASP A 298  0                                        
SHEET    2  AH 4 THR A 303  PRO A 312 -1  O  THR A 303   N  ASP A 298           
SHEET    3  AH 4 GLY A 329  ASP A 336 -1  O  GLY A 329   N  ARG A 310           
SHEET    4  AH 4 ASN A 341  TRP A 342 -1  O  ASN A 341   N  ASP A 336           
SHEET    1  AI 7 GLN A 461  TRP A 466  0                                        
SHEET    2  AI 7 THR A 453  VAL A 458 -1  O  THR A 454   N  TRP A 466           
SHEET    3  AI 7 HIS A 441  SER A 448 -1  O  GLU A 444   N  PHE A 457           
SHEET    4  AI 7 TRP A 380  GLY A 391 -1  O  TRP A 380   N  TYR A 447           
SHEET    5  AI 7 GLY A 487  GLN A 498 -1  O  ARG A 488   N  VAL A 389           
SHEET    6  AI 7 PHE A 357  GLY A 361 -1  O  PHE A 357   N  VAL A 491           
SHEET    7  AI 7 MET A 536  TYR A 539 -1  O  MET A 536   N  ALA A 360           
SHEET    1  AJ 6 GLN A 461  TRP A 466  0                                        
SHEET    2  AJ 6 THR A 453  VAL A 458 -1  O  THR A 454   N  TRP A 466           
SHEET    3  AJ 6 HIS A 441  SER A 448 -1  O  GLU A 444   N  PHE A 457           
SHEET    4  AJ 6 TRP A 380  GLY A 391 -1  O  TRP A 380   N  TYR A 447           
SHEET    5  AJ 6 GLY A 487  GLN A 498 -1  O  ARG A 488   N  VAL A 389           
SHEET    6  AJ 6 HIS A 501  ASP A 507 -1  O  HIS A 501   N  GLN A 498           
SHEET    1  AK10 ILE A 428  GLN A 431  0                                        
SHEET    2  AK10 LEU A 417  LEU A 421 -1  O  LEU A 417   N  LEU A 430           
SHEET    3  AK10 ARG A 403  ILE A 411 -1  O  THR A 408   N  ASN A 420           
SHEET    4  AK10 GLU A 469  VAL A 470 -1  O  GLU A 469   N  LYS A 404           
SHEET    5  AK10 ARG A 403  ILE A 411 -1  O  LYS A 404   N  GLU A 469           
SHEET    6  AK10 THR A 528  GLY A 533                                           
SHEET    7  AK10 GLY A 364  ASN A 371 -1  O  SER A 365   N  THR A 532           
SHEET    8  AK10 ASN A 474  ASN A 480 -1  O  ILE A 476   N  ARG A 370           
SHEET    9  AK10 ASN A 394  ASP A 400 -1  O  GLN A 395   N  GLY A 479           
SHEET   10  AK10 ARG A 403  ILE A 411 -1  O  ARG A 403   N  ASP A 400           
SHEET    1  AL 7 SER A 543  ASN A 545  0                                        
SHEET    2  AL 7 LEU A 568  LEU A 575 -1  O  ILE A 573   N  ASN A 545           
SHEET    3  AL 7 ILE A 552  THR A 553 -1  O  ILE A 552   N  ILE A 569           
SHEET    4  AL 7 LEU A 568  LEU A 575 -1  O  ILE A 569   N  ILE A 552           
SHEET    5  AL 7 GLN A 595  THR A 599                                           
SHEET    6  AL 7 LEU A 580  SER A 587 -1  O  SER A 584   N  GLY A 597           
SHEET    7  AL 7 LEU A 568  LEU A 575 -1  O  LEU A 568   N  SER A 587           
SHEET    1  AM 2 PHE A 604  LYS A 607  0                                        
SHEET    2  AM 2 ILE A 611  THR A 614 -1  O  ILE A 611   N  LYS A 607           
SHEET    1  AN 4 GLU A 616  GLU A 624  0                                        
SHEET    2  AN 4 LEU A 630  ASP A 637 -1  O  LEU A 631   N  VAL A 623           
SHEET    3  AN 4 ARG A 650  SER A 655 -1  O  GLN A 651   N  ALA A 634           
SHEET    4  AN 4 SER A 663  ASN A 669 -1  O  SER A 663   N  LEU A 654           
SHEET    1  AO 2 ILE A 641  VAL A 642  0                                        
SHEET    2  AO 2 VAL A 645  ASN A 646 -1  O  VAL A 645   N  VAL A 642           
SHEET    1  AP 4 SER A 684  GLU A 689  0                                        
SHEET    2  AP 4 HIS A 695  PRO A 702 -1  O  PHE A 696   N  PHE A 688           
SHEET    3  AP 4 LEU A 715  SER A 720 -1  O  GLY A 716   N  ASN A 701           
SHEET    4  AP 4 LYS A 728  GLN A 732 -1  O  LYS A 728   N  PHE A 719           
LINK        CA    CA A1779                 OG1 THR A 313     1555   1555  2.35  
LINK        CA    CA A1779                 OD1 ASP A 289     1555   1555  2.61  
LINK        CA    CA A1779                 OD2 ASP A 289     1555   1555  2.26  
LINK        CA    CA A1779                 O   THR A 313     1555   1555  2.52  
LINK        CA    CA A1779                 O   ALA A 253     1555   1555  2.26  
LINK        CA    CA A1779                 OD1 ASN A 256     1555   1555  2.31  
LINK        CA    CA A1779                 O   ASN A 256     1555   1555  2.28  
LINK        CA    CA A1780                 O   PRO A 548     1555   1555  2.37  
LINK        CA    CA A1780                 OD1 ASP A 621     1555   1555  2.50  
LINK        CA    CA A1780                 OD2 ASP A 621     1555   1555  2.41  
LINK        CA    CA A1780                 OD1 ASP A 682     1555   1555  2.36  
LINK        CA    CA A1780                 OD2 ASP A 682     1555   1555  2.43  
LINK        CA    CA A1780                 O   ALA A 683     1555   1555  2.34  
LINK        CA    CA A1781                 O   PHE A 578     1555   1555  2.32  
LINK        CA    CA A1781                 OD2 ASP A 320     1555   1555  2.41  
LINK        CA    CA A1781                 O   HOH A2466     1555   1555  2.32  
LINK        CA    CA A1781                 OD1 ASP A 320     1555   1555  2.67  
LINK        CA    CA A1782                 O   HOH A2426     1555   1555  2.28  
LINK        CA    CA A1782                 OD1 ASP A 286     1555   1555  2.35  
LINK        CA    CA A1782                 O   HOH A2433     1555   1555  2.55  
LINK        CA    CA A1782                 O   HOH A2434     1555   1555  2.70  
LINK        CA    CA A1782                 O   HOH A2367     1555   1555  2.43  
CISPEP   1 GLY A  221    PRO A  222          0         0.36                     
CISPEP   2 ASN A  705    PRO A  706          0        -0.20                     
CISPEP   3 GLY A  729    PRO A  730          0         0.33                     
SITE     1 AC1 12 ARG A  74  MET A 107  TYR A 111  ARG A 118                    
SITE     2 AC1 12 GLN A 188  GLY A 196  SER A 197  SER A 198                    
SITE     3 AC1 12 ASN A 199  HOH A2147  HOH A2919  HOH A2920                    
SITE     1 AC2  4 ALA A 253  ASN A 256  ASP A 289  THR A 313                    
SITE     1 AC3  4 PRO A 548  ASP A 621  ASP A 682  ALA A 683                    
SITE     1 AC4  3 ASP A 320  PHE A 578  HOH A2466                               
SITE     1 AC5  5 ASP A 286  HOH A2367  HOH A2426  HOH A2433                    
SITE     2 AC5  5 HOH A2434                                                     
SITE     1 AC6 17 ARG A 224  ARG A 245  ASP A 250  ASP A 292                    
SITE     2 AC6 17 ASN A 318  ASN A 545  LEU A 580  GLU A 619                    
SITE     3 AC6 17 ARG A 635  ASP A 637  ARG A 712  TYR A 740                    
SITE     4 AC6 17 HOH A2347  HOH A2462  HOH A2915  HOH A2916                    
SITE     5 AC6 17 HOH A2917                                                     
CRYST1   70.310   74.910  151.615  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014223  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006596        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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