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Database: PDB
Entry: 2VW1
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HEADER    HYDROLASE                               13-JUN-08   2VW1              
TITLE     CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS            
TITLE    2 PNEUMONIAE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE B;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NANB SIALIDASE, NEURAMINIDASE B;                            
COMPND   5 EC: 3.2.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: TIGR;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    HYDROLASE, SIALIDASE, NEURAMINIDASE, VIRULENCE FACTOR, DRUG           
KEYWDS   2 DESIGN                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,P.W.ANDREW,                 
AUTHOR   2 G.L.TAYLOR                                                           
REVDAT   3   24-FEB-09 2VW1    1       VERSN                                    
REVDAT   2   18-NOV-08 2VW1    1       SOURCE JRNL   REMARK                     
REVDAT   1   24-JUN-08 2VW1    0                                                
JRNL        AUTH   G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,                   
JRNL        AUTH 2 P.W.ANDREW,G.L.TAYLOR                                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                 
JRNL        TITL 2 STREPTOCOCCUS PNEUMONIAE                                     
JRNL        REF    J.MOL.BIOL.                   V. 384   436 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18835278                                                     
JRNL        DOI    10.1016/J.JMB.2008.09.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 28251                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1511                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.39                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1902                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5189                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 463                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.44000                                             
REMARK   3    B22 (A**2) : 0.33000                                              
REMARK   3    B33 (A**2) : 1.11000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.475         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.211         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.854                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5323 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7198 ; 1.514 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   657 ; 8.319 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;37.757 ;25.020       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   922 ;15.934 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;16.509 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   786 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4033 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2590 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3531 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   501 ; 0.191 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    24 ; 0.181 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3336 ; 0.594 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5260 ; 1.058 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2267 ; 1.472 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1938 ; 2.269 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VW1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-36564.                                       
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                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (SATURN 944)                   
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29767                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.30                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.35                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
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 1SLI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1M IMIDAZOLE PH           
REMARK 280  8                                                                   
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       38.29850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.71150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.34950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.71150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.29850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.34950            
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     ASN A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     MET A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     HIS A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     LEU A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     LYS A   697                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A   125  -  O    THR A   173              2.20            
REMARK 500   NE1  TRP A   526  -  O    HOH A  2354              2.19            
REMARK 500   O    HOH A  2058  -  O    HOH A  2428              2.06            
REMARK 500   O    HOH A  2058  -  O    HOH A  2331              1.97            
REMARK 500   O    HOH A  2079  -  O    HOH A  2211              2.02            
REMARK 500   O    HOH A  2161  -  O    HOH A  2434              2.12            
REMARK 500   O    HOH A  2172  -  O    HOH A  2451              2.11            
REMARK 500   O    HOH A  2172  -  O    HOH A  2452              2.06            
REMARK 500   O    HOH A  2188  -  O    HOH A  2265              2.17            
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    PRO A 309   C   -  N   -  CA  ANGL. DEV. =  27.3 DEGREES          
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    SER A  47       70.29     45.72                                   
REMARK 500    ASN A  51       57.96   -118.15                                   
REMARK 500    ALA A  78       93.49   -163.09                                   
REMARK 500    ASP A 108        0.64    -69.32                                   
REMARK 500    LYS A 213      137.70   -170.18                                   
REMARK 500    SER A 226       78.05   -105.58                                   
REMARK 500    ASP A 237     -173.86    -65.42                                   
REMARK 500    ILE A 246       67.77     67.56                                   
REMARK 500    PRO A 309       87.10     26.71                                   
REMARK 500    ASP A 327       89.93     63.48                                   
REMARK 500    ASN A 356       95.64    -64.08                                   
REMARK 500    ARG A 386     -160.28    -75.84                                   
REMARK 500    PRO A 534       42.19    -77.84                                   
REMARK 500    ASP A 634       -0.50     76.64                                   
REMARK 500    ALA A 652     -124.00   -129.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TRP A  308     PRO A  309                   99.83                    
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 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 DAN A1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1698                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VW0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                        
REMARK 900   STREPTOCOCCUS PNEUMONIAE                                           
REMARK 900 RELATED ID: 2VW2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                        
REMARK 900   STREPTOCOCCUS PNEUMONIAE                                           
DBREF  2VW1 A    1   697  UNP    Q54727   NANB_STRPN       1    697             
SEQRES   1 A  697  MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER          
SEQRES   2 A  697  VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU          
SEQRES   3 A  697  ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE          
SEQRES   4 A  697  SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN          
SEQRES   5 A  697  LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU          
SEQRES   6 A  697  SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA          
SEQRES   7 A  697  ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER          
SEQRES   8 A  697  ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE          
SEQRES   9 A  697  PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG          
SEQRES  10 A  697  ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO          
SEQRES  11 A  697  ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU          
SEQRES  12 A  697  ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR          
SEQRES  13 A  697  TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU          
SEQRES  14 A  697  THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY          
SEQRES  15 A  697  ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY          
SEQRES  16 A  697  LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE          
SEQRES  17 A  697  SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER          
SEQRES  18 A  697  THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN          
SEQRES  19 A  697  SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO          
SEQRES  20 A  697  THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER          
SEQRES  21 A  697  ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER          
SEQRES  22 A  697  LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY          
SEQRES  23 A  697  LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN          
SEQRES  24 A  697  ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN          
SEQRES  25 A  697  LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE          
SEQRES  26 A  697  ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS          
SEQRES  27 A  697  THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY          
SEQRES  28 A  697  ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU          
SEQRES  29 A  697  ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY          
SEQRES  30 A  697  ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL          
SEQRES  31 A  697  VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR          
SEQRES  32 A  697  ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER          
SEQRES  33 A  697  LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY          
SEQRES  34 A  697  SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET          
SEQRES  35 A  697  ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO          
SEQRES  36 A  697  THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY          
SEQRES  37 A  697  GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU          
SEQRES  38 A  697  GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN          
SEQRES  39 A  697  GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA          
SEQRES  40 A  697  THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP          
SEQRES  41 A  697  ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE          
SEQRES  42 A  697  PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU          
SEQRES  43 A  697  LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR          
SEQRES  44 A  697  THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY          
SEQRES  45 A  697  GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN          
SEQRES  46 A  697  GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR          
SEQRES  47 A  697  SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER          
SEQRES  48 A  697  THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU          
SEQRES  49 A  697  VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP          
SEQRES  50 A  697  TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY          
SEQRES  51 A  697  TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS          
SEQRES  52 A  697  ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG          
SEQRES  53 A  697  ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP          
SEQRES  54 A  697  LEU GLU ILE ASN ASP LEU THR LYS                              
HET    DAN  A1000      20                                                       
HET    GOL  A1698       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   2  GOL    C3 H8 O3                                                     
FORMUL   3  DAN    C11 H17 N O8                                                 
FORMUL   4  HOH   *463(H2 O1)                                                   
HELIX    1   1 ILE A   57  LEU A   62  1                                   6    
HELIX    2   2 SER A  216  SER A  221  1                                   6    
HELIX    3   3 GLU A  691  THR A  696  1                                   6    
SHEET    1  AA 6 PHE A  43  ASN A  51  0                                        
SHEET    2  AA 6 LYS A 202  PHE A 211 -1  O  GLY A 203   N  LEU A  50           
SHEET    3  AA 6 GLN A  70  LYS A  77 -1  O  THR A  71   N  PHE A 211           
SHEET    4  AA 6 ASN A 144  ASP A 151 -1  O  ASN A 144   N  PHE A  76           
SHEET    5  AA 6 THR A 156  VAL A 161 -1  O  THR A 156   N  ASP A 151           
SHEET    6  AA 6 ILE A 164  THR A 170 -1  O  ILE A 164   N  VAL A 161           
SHEET    1  AB 6 ILE A  55  ASP A  56  0                                        
SHEET    2  AB 6 LYS A 185  LEU A 188 -1  O  LEU A 188   N  ILE A  55           
SHEET    3  AB 6 LEU A  84  SER A  91 -1  O  GLY A  89   N  THR A 187           
SHEET    4  AB 6 TYR A 101  ARG A 107 -1  O  PHE A 102   N  LEU A  90           
SHEET    5  AB 6 ILE A 112  ASP A 118 -1  O  GLY A 113   N  PHE A 105           
SHEET    6  AB 6 ILE A 123  ARG A 129 -1  O  ILE A 123   N  ASP A 118           
SHEET    1  AC 2 VAL A 191  ARG A 193  0                                        
SHEET    2  AC 2 LYS A 196  HIS A 198 -1  O  LYS A 196   N  ARG A 193           
SHEET    1  AD 3 TYR A 243  ARG A 245  0                                        
SHEET    2  AD 3 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3  AD 3 TYR A 250  THR A 251 -1  O  TYR A 250   N  LEU A 258           
SHEET    1  AE 4 TYR A 243  ARG A 245  0                                        
SHEET    2  AE 4 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3  AE 4 ILE A 275  SER A 282 -1  O  ASN A 276   N  ALA A 263           
SHEET    4  AE 4 ILE A 293  MET A 296 -1  O  ILE A 293   N  THR A 279           
SHEET    1  AF 5 LYS A 475  LEU A 476  0                                        
SHEET    2  AF 5 TYR A 458  SER A 464 -1  O  MET A 461   N  LYS A 475           
SHEET    3  AF 5 THR A 339  MET A 346 -1  O  THR A 339   N  SER A 464           
SHEET    4  AF 5 SER A 324  GLU A 332 -1  O  SER A 324   N  MET A 346           
SHEET    5  AF 5 GLY A 493  GLN A 494  1  O  GLY A 493   N  ILE A 330           
SHEET    1  AG 7 PHE A 362  ILE A 365  0                                        
SHEET    2  AG 7 HIS A 368  LYS A 375 -1  O  HIS A 368   N  ILE A 365           
SHEET    3  AG 7 TYR A 383  VAL A 385 -1  O  TYR A 383   N  LEU A 373           
SHEET    4  AG 7 VAL A 390  ASN A 393 -1  O  TYR A 392   N  THR A 384           
SHEET    5  AG 7 LYS A 398  ILE A 404 -1  O  LYS A 398   N  ASN A 393           
SHEET    6  AG 7 VAL A 410  GLU A 412 -1  O  LEU A 411   N  THR A 403           
SHEET    7  AG 7 LYS A 415  SER A 416 -1  O  LYS A 415   N  GLU A 412           
SHEET    1  AH 3 PHE A 362  ILE A 365  0                                        
SHEET    2  AH 3 HIS A 368  LYS A 375 -1  O  HIS A 368   N  ILE A 365           
SHEET    3  AH 3 PHE A 451  LYS A 452 -1  O  LYS A 452   N  LYS A 374           
SHEET    1  AI 2 THR A 418  ASP A 425  0                                        
SHEET    2  AI 2 ARG A 432  PRO A 441 -1  O  ARG A 432   N  ASP A 425           
SHEET    1  AJ 3 TYR A 489  LEU A 490  0                                        
SHEET    2  AJ 3 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3  AJ 3 LEU A 496  ALA A 497 -1  O  LEU A 496   N  ILE A 505           
SHEET    1  AK 4 TYR A 489  LEU A 490  0                                        
SHEET    2  AK 4 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3  AK 4 GLU A 513  SER A 519 -1  O  GLU A 513   N  THR A 510           
SHEET    4  AK 4 LYS A 527  SER A 532 -1  O  LYS A 527   N  ILE A 518           
SHEET    1  AL 4 ALA A 542  ARG A 548  0                                        
SHEET    2  AL 4 VAL A 551  PHE A 556 -1  O  VAL A 551   N  LEU A 547           
SHEET    3  AL 4 ALA A 564  SER A 568 -1  O  ALA A 564   N  PHE A 556           
SHEET    4  AL 4 SER A 579  TYR A 580 -1  O  SER A 579   N  TYR A 565           
SHEET    1  AM 4 SER A 594  ILE A 602  0                                        
SHEET    2  AM 4 LYS A 605  PRO A 613 -1  O  LYS A 605   N  ILE A 602           
SHEET    3  AM 4 GLY A 622  VAL A 629 -1  O  GLN A 623   N  THR A 612           
SHEET    4  AM 4 ILE A 636  ASP A 643 -1  O  ASP A 637   N  LEU A 628           
SHEET    1  AN 3 SER A 654  GLU A 658  0                                        
SHEET    2  AN 3 ILE A 664  GLU A 669 -1  O  GLY A 665   N  THR A 657           
SHEET    3  AN 3 VAL A 685  LEU A 690 -1  O  GLN A 686   N  PHE A 668           
CISPEP   1 SER A  271    LYS A  272          0         8.43                     
SITE     1 AC1 15 ARG A 245  ILE A 246  ARG A 264  ASP A 270                    
SITE     2 AC1 15 ILE A 326  ASP A 327  ASP A 344  ASN A 352                    
SITE     3 AC1 15 THR A 539  ARG A 557  ARG A 619  TYR A 653                    
SITE     4 AC1 15 TRP A 674  HOH A2159  HOH A2462                               
SITE     1 AC2  5 LEU A 252  SER A 253  LYS A 315  ARG A 676                    
SITE     2 AC2  5 HOH A2213                                                     
CRYST1   76.597   82.699  117.423  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      0.013055  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008516        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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