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Database: PDB
Entry: 2VK6
LinkDB: 2VK6
Original site: 2VK6 
HEADER    HYDROLASE                               17-DEC-07   2VK6              
TITLE     THE STRUCTURE OF CLOSTRIDIUM PERFRINGENS NANI SIALIDASE AND           
TITLE    2 ITS CATALYTIC INTERMEDIATES                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXO-ALPHA-SIALIDASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 243-694;                        
COMPND   5 SYNONYM: SIALIDASE;                                                  
COMPND   6 EC: 3.2.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;                        
SOURCE   3 ORGANISM_TAXID: 1502;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, SIALIDASE, GLYCOSIDASE, SIALIC ACID, CLOSTRIDIUM           
KEYWDS   2 PERFRINGENS                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.L.NEWSTEAD,J.A.POTTER,J.C.WILSON,G.XU,C.H.CHIEN,A.G.WATTS,          
AUTHOR   2 S.G.WITHERS,G.L.TAYLOR                                               
REVDAT   3   24-FEB-09 2VK6    1       VERSN                                    
REVDAT   2   08-APR-08 2VK6    1       JRNL   REMARK                            
REVDAT   1   22-JAN-08 2VK6    0                                                
JRNL        AUTH   S.L.NEWSTEAD,J.A.POTTER,J.C.WILSON,G.XU,C.H.CHIEN,           
JRNL        AUTH 2 A.G.WATTS,S.G.WITHERS,G.L.TAYLOR                             
JRNL        TITL   THE STRUCTURE OF CLOSTRIDIUM PERFRINGENS NANI                
JRNL        TITL 2 SIALIDASE AND ITS CATALYTIC INTERMEDIATES.                   
JRNL        REF    J.BIOL.CHEM.                  V. 283  9080 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18218621                                                     
JRNL        DOI    10.1074/JBC.M710247200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 69514                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3675                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4895                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 243                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3657                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 396                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3778 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5136 ; 1.713 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   477 ; 7.061 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   188 ;36.546 ;25.745       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   664 ;11.941 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;12.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   556 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2911 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1701 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2609 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   342 ; 0.121 ; 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):    43 ; 0.115 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.128 ; 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):  2352 ; 1.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3721 ; 1.700 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1639 ; 2.598 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1402 ; 3.614 ; 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   : 1.20                                          
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 2VK6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34808.                                       
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                             : 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) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73189                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.40                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.29                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.60                               
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: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.33                      
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       34.68500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.45000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.52300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.45000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.68500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.52300            
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     ALA A  1692                                                      
REMARK 465     ASN A  1693                                                      
REMARK 465     LYS A  1694                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY A1691    CA   C    O                                         
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    ILE A1267       76.78     76.86                                   
REMARK 500    ASN A1294       46.42    -87.41                                   
REMARK 500    ASP A1328       95.36     77.54                                   
REMARK 500    LYS A1350       -5.10     85.83                                   
REMARK 500    ASP A1414     -158.07   -172.31                                   
REMARK 500    LYS A1459      -70.16    -93.60                                   
REMARK 500    THR A1538     -122.73   -123.08                                   
REMARK 500    TYR A1587       61.59     76.06                                   
REMARK 500    ALA A1654     -113.76   -124.20                                   
REMARK 500    SER A1675       29.45   -157.45                                   
REMARK 500    GLU A1676      -95.95   -123.08                                   
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 A2691  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2096   O                                                      
REMARK 620 2 ASP A1298   OD1  69.9                                              
REMARK 620 3 ASP A1319   OD1 106.1  81.7                                        
REMARK 620 4 TYR A1320   O    73.9 133.1  80.7                                  
REMARK 620 5 HOH A2068   O   141.3 148.2  91.1  75.1                            
REMARK 620 6 HOH A2070   O   141.4  76.1  86.2 144.7  72.5                      
REMARK 620 7 ASP A1296   OD1  82.4 101.9 171.5 101.8  81.7  87.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2693  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2163   O                                                      
REMARK 620 2 HOH A2170   O   110.4                                              
REMARK 620 3 HOH A2387   O   131.3 115.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2694  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP A1573   O                                                      
REMARK 620 2 HOH A2237   O    88.1                                              
REMARK 620 3 HOH A2239   O    82.6 101.1                                        
REMARK 620 4 HOH A2236   O   106.2  78.5 171.1                                  
REMARK 620 5 HOH A2241   O    89.2 165.5  92.6  88.7                            
REMARK 620 6 ASP A1515   O   167.9  87.2  87.4  83.7  98.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2695  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2076   O                                                      
REMARK 620 2 HOH A2075   O   107.9                                              
REMARK 620 3 HOH A2384   O   111.5 123.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2696  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2095   O                                                      
REMARK 620 2 HOH A2033   O   104.4                                              
REMARK 620 3 HOH A2167   O   110.9 114.9                                        
REMARK 620 4 HOH A2251   O   105.6  96.4 122.3                                  
REMARK 620 N                    1     2     3                                   
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  CA A2691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A2692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A2696                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A2697                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BF6   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF THE BACTERIAL                        
REMARK 900  SIALIDASE NANI FROM CLOSTRIDIUM PERFRINGENS IN                      
REMARK 900   COMPLEX WITH ALPHA-SIALIC ACID (NEU5AC).                           
REMARK 900 RELATED ID: 2VK5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF CLOSTRIDIUM PERFRINGENS NANI                       
REMARK 900   SIALIDASE AND ITS CATALYTIC INTERMEDIATES                          
REMARK 900 RELATED ID: 2VK7   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF CLOSTRIDIUM PERFRINGENS NANI                       
REMARK 900   SIALIDASE AND ITS CATALYTIC INTERMEDIATE                           
DBREF  2VK6 A 1243  1694  UNP    Q59310   Q59310_CLOPE   243    694             
SEQADV 2VK6 SER A 1393  UNP  Q59310    GLY   393 CONFLICT                       
SEQRES   1 A  452  VAL GLU GLY ALA VAL LYS THR GLU PRO VAL ASP LEU PHE          
SEQRES   2 A  452  HIS PRO GLY PHE LEU ASN SER SER ASN TYR ARG ILE PRO          
SEQRES   3 A  452  ALA LEU PHE LYS THR LYS GLU GLY THR LEU ILE ALA SER          
SEQRES   4 A  452  ILE ASP ALA ARG ARG HIS GLY GLY ALA ASP ALA PRO ASN          
SEQRES   5 A  452  ASN ASP ILE ASP THR ALA VAL ARG ARG SER GLU ASP GLY          
SEQRES   6 A  452  GLY LYS THR TRP ASP GLU GLY GLN ILE ILE MET ASP TYR          
SEQRES   7 A  452  PRO ASP LYS SER SER VAL ILE ASP THR THR LEU ILE GLN          
SEQRES   8 A  452  ASP ASP GLU THR GLY ARG ILE PHE LEU LEU VAL THR HIS          
SEQRES   9 A  452  PHE PRO SER LYS TYR GLY PHE TRP ASN ALA GLY LEU GLY          
SEQRES  10 A  452  SER GLY PHE LYS ASN ILE ASP GLY LYS GLU TYR LEU CYS          
SEQRES  11 A  452  LEU TYR ASP SER SER GLY LYS GLU PHE THR VAL ARG GLU          
SEQRES  12 A  452  ASN VAL VAL TYR ASP LYS ASP SER ASN LYS THR GLU TYR          
SEQRES  13 A  452  THR THR ASN ALA LEU GLY ASP LEU PHE LYS ASN GLY THR          
SEQRES  14 A  452  LYS ILE ASP ASN ILE ASN SER SER THR ALA PRO LEU LYS          
SEQRES  15 A  452  ALA LYS GLY THR SER TYR ILE ASN LEU VAL TYR SER ASP          
SEQRES  16 A  452  ASP ASP GLY LYS THR TRP SER GLU PRO GLN ASN ILE ASN          
SEQRES  17 A  452  PHE GLN VAL LYS LYS ASP TRP MET LYS PHE LEU GLY ILE          
SEQRES  18 A  452  ALA PRO GLY ARG GLY ILE GLN ILE LYS ASN GLY GLU HIS          
SEQRES  19 A  452  LYS GLY ARG ILE VAL VAL PRO VAL TYR TYR THR ASN GLU          
SEQRES  20 A  452  LYS GLY LYS GLN SER SER ALA VAL ILE TYR SER ASP ASP          
SEQRES  21 A  452  SER GLY LYS ASN TRP THR ILE GLY GLU SER PRO ASN ASP          
SEQRES  22 A  452  ASN ARG LYS LEU GLU ASN GLY LYS ILE ILE ASN SER LYS          
SEQRES  23 A  452  THR LEU SER ASP ASP ALA PRO GLN LEU THR GLU CYS GLN          
SEQRES  24 A  452  VAL VAL GLU MET PRO ASN GLY GLN LEU LYS LEU PHE MET          
SEQRES  25 A  452  ARG ASN LEU SER GLY TYR LEU ASN ILE ALA THR SER PHE          
SEQRES  26 A  452  ASP GLY GLY ALA THR TRP ASP GLU THR VAL GLU LYS ASP          
SEQRES  27 A  452  THR ASN VAL LEU GLU PRO TYR CYS GLN LEU SER VAL ILE          
SEQRES  28 A  452  ASN TYR SER GLN LYS VAL ASP GLY LYS ASP ALA VAL ILE          
SEQRES  29 A  452  PHE SER ASN PRO ASN ALA ARG SER ARG SER ASN GLY THR          
SEQRES  30 A  452  VAL ARG ILE GLY LEU ILE ASN GLN VAL GLY THR TYR GLU          
SEQRES  31 A  452  ASN GLY GLU PRO LYS TYR GLU PHE ASP TRP LYS TYR ASN          
SEQRES  32 A  452  LYS LEU VAL LYS PRO GLY TYR TYR ALA TYR SER CYS LEU          
SEQRES  33 A  452  THR GLU LEU SER ASN GLY ASN ILE GLY LEU LEU TYR GLU          
SEQRES  34 A  452  GLY THR PRO SER GLU GLU MET SER TYR ILE GLU MET ASN          
SEQRES  35 A  452  LEU LYS TYR LEU GLU SER GLY ALA ASN LYS                      
HET     CA  A2691       1                                                       
HET    DAN  A2692      20                                                       
HET     MG  A2693       1                                                       
HET     MG  A2694       1                                                       
HET     MG  A2695       1                                                       
HET     MG  A2696       1                                                       
HET    PG4  A2697      13                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID                     
FORMUL   2  PG4    C8 H18 O5                                                    
FORMUL   3   CA    CA 2+                                                        
FORMUL   4   MG    4(MG 2+)                                                     
FORMUL   5  DAN    C11 H17 N O8                                                 
FORMUL   6  HOH   *396(H2 O1)                                                   
HELIX    1   1 GLY A 1258  SER A 1262  5                                   5    
HELIX    2   2 ILE A 1449  LYS A 1454  1                                   6    
HELIX    3   3 ASN A 1684  GLU A 1689  1                                   6    
SHEET    1  AA 4 VAL A1252  PHE A1255  0                                        
SHEET    2  AA 4 MET A1678  MET A1683 -1  O  MET A1678   N  LEU A1254           
SHEET    3  AA 4 ILE A1666  GLU A1671 -1  O  ILE A1666   N  MET A1683           
SHEET    4  AA 4 SER A1656  GLU A1660 -1  O  CYS A1657   N  LEU A1669           
SHEET    1  AB 4 ASN A1264  LYS A1272  0                                        
SHEET    2  AB 4 LEU A1278  ARG A1285 -1  O  ILE A1279   N  PHE A1271           
SHEET    3  AB 4 ILE A1297  SER A1304 -1  O  ASP A1298   N  ALA A1284           
SHEET    4  AB 4 GLN A1315  MET A1318 -1  O  GLN A1315   N  VAL A1301           
SHEET    1  AC 5 GLN A1447  ASN A1448  0                                        
SHEET    2  AC 5 TYR A1430  SER A1436 -1  O  LEU A1433   N  GLN A1447           
SHEET    3  AC 5 ILE A1340  PHE A1347 -1  O  ILE A1340   N  SER A1436           
SHEET    4  AC 5 SER A1325  GLN A1333 -1  O  SER A1325   N  PHE A1347           
SHEET    5  AC 5 GLY A1466  ARG A1467  1  O  GLY A1466   N  LEU A1331           
SHEET    1  AD 7 PHE A1362  ILE A1365  0                                        
SHEET    2  AD 7 LYS A1368  TYR A1374 -1  O  LYS A1368   N  ILE A1365           
SHEET    3  AD 7 GLU A1380  ARG A1384 -1  O  PHE A1381   N  LEU A1373           
SHEET    4  AD 7 VAL A1387  TYR A1389 -1  O  VAL A1387   N  ARG A1384           
SHEET    5  AD 7 LYS A1395  THR A1400 -1  N  THR A1396   O  VAL A1388           
SHEET    6  AD 7 ASP A1405  LYS A1408 -1  O  PHE A1407   N  THR A1399           
SHEET    7  AD 7 THR A1411  ASN A1415 -1  O  THR A1411   N  LYS A1408           
SHEET    1  AE 3 PHE A1362  ILE A1365  0                                        
SHEET    2  AE 3 LYS A1368  TYR A1374 -1  O  LYS A1368   N  ILE A1365           
SHEET    3  AE 3 LYS A1424  ALA A1425 -1  O  LYS A1424   N  TYR A1374           
SHEET    1  AF 3 LEU A1461  ILE A1463  0                                        
SHEET    2  AF 3 ILE A1480  THR A1487 -1  O  TYR A1485   N  GLY A1462           
SHEET    3  AF 3 ILE A1469  GLN A1470 -1  O  ILE A1469   N  VAL A1481           
SHEET    1  AG 4 LEU A1461  ILE A1463  0                                        
SHEET    2  AG 4 ILE A1480  THR A1487 -1  O  TYR A1485   N  GLY A1462           
SHEET    3  AG 4 GLN A1493  SER A1500 -1  O  SER A1494   N  TYR A1486           
SHEET    4  AG 4 THR A1508  ILE A1509 -1  O  THR A1508   N  TYR A1499           
SHEET    1  AH 2 ARG A1517  LYS A1518  0                                        
SHEET    2  AH 2 ILE A1524  ILE A1525 -1  N  ILE A1525   O  ARG A1517           
SHEET    1  AI 4 LEU A1537  GLU A1544  0                                        
SHEET    2  AI 4 LEU A1550  ASN A1556 -1  O  LYS A1551   N  VAL A1543           
SHEET    3  AI 4 TYR A1560  SER A1566 -1  O  ASN A1562   N  MET A1554           
SHEET    4  AI 4 GLU A1578  LEU A1584 -1  O  GLU A1578   N  ILE A1563           
SHEET    1  AJ 4 SER A1591  ASN A1594  0                                        
SHEET    2  AJ 4 ALA A1604  PRO A1610 -1  O  ILE A1606   N  ILE A1593           
SHEET    3  AJ 4 SER A1616  THR A1630 -1  O  THR A1619   N  ASN A1609           
SHEET    4  AJ 4 PRO A1636  TYR A1652 -1  O  LYS A1637   N  VAL A1628           
LINK        CA    CA A2691                 O   HOH A2096     1555   1555  2.54  
LINK        CA    CA A2691                 OD1 ASP A1298     1555   1555  2.45  
LINK        CA    CA A2691                 OD1 ASP A1319     1555   1555  2.39  
LINK        CA    CA A2691                 O   TYR A1320     1555   1555  2.36  
LINK        CA    CA A2691                 O   HOH A2068     1555   1555  2.48  
LINK        CA    CA A2691                 O   HOH A2070     1555   1555  2.47  
LINK        CA    CA A2691                 OD1 ASP A1296     1555   1555  2.35  
LINK        MG    MG A2693                 O   HOH A2163     1555   1555  2.28  
LINK        MG    MG A2693                 O   HOH A2170     1555   1555  2.67  
LINK        MG    MG A2693                 O   HOH A2387     1555   1555  2.75  
LINK        MG    MG A2694                 O   HOH A2236     1555   1555  2.64  
LINK        MG    MG A2694                 O   HOH A2237     1555   1555  2.54  
LINK        MG    MG A2694                 O   HOH A2239     1555   1555  2.37  
LINK        MG    MG A2694                 O   HOH A2241     1555   1555  2.35  
LINK        MG    MG A2694                 O   ASP A1515     1555   1555  2.36  
LINK        MG    MG A2694                 O   TRP A1573     1555   1555  2.50  
LINK        MG    MG A2695                 O   HOH A2075     1555   1555  2.65  
LINK        MG    MG A2695                 O   HOH A2384     1555   1555  2.76  
LINK        MG    MG A2695                 O   HOH A2076     1555   1555  2.77  
LINK        MG    MG A2696                 O   HOH A2033     1555   2565  2.84  
LINK        MG    MG A2696                 O   HOH A2167     1555   1555  2.74  
LINK        MG    MG A2696                 O   HOH A2251     1555   2565  2.74  
LINK        MG    MG A2696                 O   HOH A2095     1555   1555  2.68  
CISPEP   1 ALA A 1292    PRO A 1293          0         7.40                     
SITE     1 AC1  7 ASP A1296  ASP A1298  ASP A1319  TYR A1320                    
SITE     2 AC1  7 HOH A2068  HOH A2070  HOH A2096                               
SITE     1 AC2 17 ARG A1266  ILE A1267  ARG A1285  ASP A1291                    
SITE     2 AC2 17 ILE A1327  ASP A1328  PHE A1353  TYR A1485                    
SITE     3 AC2 17 GLN A1493  ARG A1555  TYR A1587  ARG A1615                    
SITE     4 AC2 17 TYR A1655  HOH A2263  HOH A2298  HOH A2392                    
SITE     5 AC2 17 HOH A2393                                                     
SITE     1 AC3  4 ASP A1322  HOH A2163  HOH A2170  HOH A2387                    
SITE     1 AC4  6 ASP A1515  TRP A1573  HOH A2236  HOH A2237                    
SITE     2 AC4  6 HOH A2239  HOH A2241                                          
SITE     1 AC5  4 VAL A1252  HOH A2075  HOH A2076  HOH A2384                    
SITE     1 AC6  5 ILE A1524  HOH A2033  HOH A2095  HOH A2167                    
SITE     2 AC6  5 HOH A2251                                                     
SITE     1 AC7  6 ASP A1312  GLY A1314  GLN A1315  TRP A1354                    
SITE     2 AC7  6 HOH A2079  HOH A2395                                          
CRYST1   69.370   71.046   98.900  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      0.014415  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014075  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010111        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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