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Database: PDB
Entry: 2BF6
LinkDB: 2BF6
Original site: 2BF6 
HEADER    HYDROLASE                               04-DEC-04   2BF6              
TITLE     ATOMIC RESOLUTION STRUCTURE OF THE BACTERIAL SIALIDASE NANI           
TITLE    2 FROM CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH ALPHA-SIALIC            
TITLE    3 ACID (NEU5AC).                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXO-ALPHA-SIALIDASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 243-691;                                          
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 ATCC: 10543;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PMAL-C2                                    
KEYWDS    SIALIDASE, CLOSTRIDIUM PERFRINGENS, SIALIC ACID, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.NEWSTEAD,G.L.TAYLOR                                                 
REVDAT   2   24-FEB-09 2BF6    1       VERSN                                    
REVDAT   1   09-MAR-06 2BF6    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.    0.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1133                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1134                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.1331                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.9                    
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 13089                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 264777                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.1103                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.1104                 
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.1296                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.0                    
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 12074                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 243689                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3569                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 35                                            
REMARK   3   SOLVENT ATOMS      : 485                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 4037.50                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 3285.20                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 11                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 36804                   
REMARK   3   NUMBER OF RESTRAINTS                     : 44962                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.016                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.0348                  
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.103                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.110                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.081                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.032                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.092                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE       
REMARK   3  R (NO CUTOFF) BY 2.0                                                
REMARK   4                                                                      
REMARK   4 2BF6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-DEC-04.                 
REMARK 100 THE PDBE ID CODE IS EBI-21867.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 290992                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1SLL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.2M POTASSIUM            
REMARK 280  NITRATE                                                             
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       48.49050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.34700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.70650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.34700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.49050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.70650            
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 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 A 691    CA   C    O                                         
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     GLU A 336   OE2                                                  
REMARK 480     LYS A 528    NZ                                                  
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    ASP A 253   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    LYS A 274   CB  -  CG  -  CD  ANGL. DEV. =  21.5 DEGREES          
REMARK 500    GLU A 313   CG  -  CD  -  OE1 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    GLU A 313   OE1 -  CD  -  OE2 ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASP A 392   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP A 392   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    GLU A 397   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ASP A 456   CB  -  CG  -  OD2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG A 613   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR A 655   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR A 655   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 267       73.76     78.95                                   
REMARK 500    ASN A 294       49.05    -89.69                                   
REMARK 500    ASN A 295     -177.23   -171.04                                   
REMARK 500    ASP A 328       89.33     78.90                                   
REMARK 500    LYS A 350       -6.15     87.93                                   
REMARK 500    ASP A 414     -162.32   -174.15                                   
REMARK 500    LYS A 459      -71.94    -92.98                                   
REMARK 500    THR A 538     -124.18   -124.08                                   
REMARK 500    TYR A 587       65.13     78.42                                   
REMARK 500    ALA A 654     -114.46   -123.65                                   
REMARK 500    SER A 675       26.31   -160.05                                   
REMARK 500    GLU A 676      -97.58   -120.06                                   
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 A1693  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2039   O                                                      
REMARK 620 2 HOH A2042   O    70.8                                              
REMARK 620 3 ASP A 319   OD1  89.7  85.3                                        
REMARK 620 4 ASP A 296   OD1  79.7  87.0 168.5                                  
REMARK 620 5 ASP A 298   OD1 146.9  76.7  81.2 105.3                            
REMARK 620 6 TYR A 320   O    74.5 143.2  82.7  98.7 134.8                      
REMARK 620 7 HOH A2071   O   142.5 141.4 108.0  83.4  70.1  75.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1694  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 515   O                                                      
REMARK 620 2 HOH A2306   O    81.8                                              
REMARK 620 3 HOH A2309   O    83.6  92.0                                        
REMARK 620 4 TRP A 573   O   154.8  81.3  78.5                                  
REMARK 620 5 HOH A2193   O   116.8 147.0 115.9  87.2                            
REMARK 620 6 HOH A2303   O    79.1  79.6 161.6 115.8  77.9                      
REMARK 620 N                    1     2     3     4     5                       
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 A1692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1696                 
DBREF  2BF6 A  243   691  UNP    Q59310   Q59310         243    691             
SEQRES   1 A  449  VAL GLU GLY ALA VAL LYS THR GLU PRO VAL ASP LEU PHE          
SEQRES   2 A  449  HIS PRO GLY PHE LEU ASN SER SER ASN TYR ARG ILE PRO          
SEQRES   3 A  449  ALA LEU PHE LYS THR LYS GLU GLY THR LEU ILE ALA SER          
SEQRES   4 A  449  ILE ASP ALA ARG ARG HIS GLY GLY ALA ASP ALA PRO ASN          
SEQRES   5 A  449  ASN ASP ILE ASP THR ALA VAL ARG ARG SER GLU ASP GLY          
SEQRES   6 A  449  GLY LYS THR TRP ASP GLU GLY GLN ILE ILE MET ASP TYR          
SEQRES   7 A  449  PRO ASP LYS SER SER VAL ILE ASP THR THR LEU ILE GLN          
SEQRES   8 A  449  ASP ASP GLU THR GLY ARG ILE PHE LEU LEU VAL THR HIS          
SEQRES   9 A  449  PHE PRO SER LYS TYR GLY PHE TRP ASN ALA GLY LEU GLY          
SEQRES  10 A  449  SER GLY PHE LYS ASN ILE ASP GLY LYS GLU TYR LEU CYS          
SEQRES  11 A  449  LEU TYR ASP SER SER GLY LYS GLU PHE THR VAL ARG GLU          
SEQRES  12 A  449  ASN VAL VAL TYR ASP LYS ASP SER ASN LYS THR GLU TYR          
SEQRES  13 A  449  THR THR ASN ALA LEU GLY ASP LEU PHE LYS ASN GLY THR          
SEQRES  14 A  449  LYS ILE ASP ASN ILE ASN SER SER THR ALA PRO LEU LYS          
SEQRES  15 A  449  ALA LYS GLY THR SER TYR ILE ASN LEU VAL TYR SER ASP          
SEQRES  16 A  449  ASP ASP GLY LYS THR TRP SER GLU PRO GLN ASN ILE ASN          
SEQRES  17 A  449  PHE GLN VAL LYS LYS ASP TRP MET LYS PHE LEU GLY ILE          
SEQRES  18 A  449  ALA PRO GLY ARG GLY ILE GLN ILE LYS ASN GLY GLU HIS          
SEQRES  19 A  449  LYS GLY ARG ILE VAL VAL PRO VAL TYR TYR THR ASN GLU          
SEQRES  20 A  449  LYS GLY LYS GLN SER SER ALA VAL ILE TYR SER ASP ASP          
SEQRES  21 A  449  SER GLY LYS ASN TRP THR ILE GLY GLU SER PRO ASN ASP          
SEQRES  22 A  449  ASN ARG LYS LEU GLU ASN GLY LYS ILE ILE ASN SER LYS          
SEQRES  23 A  449  THR LEU SER ASP ASP ALA PRO GLN LEU THR GLU CYS GLN          
SEQRES  24 A  449  VAL VAL GLU MET PRO ASN GLY GLN LEU LYS LEU PHE MET          
SEQRES  25 A  449  ARG ASN LEU SER GLY TYR LEU ASN ILE ALA THR SER PHE          
SEQRES  26 A  449  ASP GLY GLY ALA THR TRP ASP GLU THR VAL GLU LYS ASP          
SEQRES  27 A  449  THR ASN VAL LEU GLU PRO TYR CYS GLN LEU SER VAL ILE          
SEQRES  28 A  449  ASN TYR SER GLN LYS VAL ASP GLY LYS ASP ALA VAL ILE          
SEQRES  29 A  449  PHE SER ASN PRO ASN ALA ARG SER ARG SER ASN GLY THR          
SEQRES  30 A  449  VAL ARG ILE GLY LEU ILE ASN GLN VAL GLY THR TYR GLU          
SEQRES  31 A  449  ASN GLY GLU PRO LYS TYR GLU PHE ASP TRP LYS TYR ASN          
SEQRES  32 A  449  LYS LEU VAL LYS PRO GLY TYR TYR ALA TYR SER CYS LEU          
SEQRES  33 A  449  THR GLU LEU SER ASN GLY ASN ILE GLY LEU LEU TYR GLU          
SEQRES  34 A  449  GLY THR PRO SER GLU GLU MET SER TYR ILE GLU MET ASN          
SEQRES  35 A  449  LEU LYS TYR LEU GLU SER GLY                                  
HET    SIA  A1692      21                                                       
HET     CA  A1693       1                                                       
HET     CA  A1694       1                                                       
HET    GOL  A1695       6                                                       
HET    GOL  A1696       6                                                       
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
FORMUL   2  SIA    C11 H19 N O9                                                 
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   7  HOH   *485(H2 O1)                                                   
HELIX    1   1 GLY A  258  SER A  262  5                                   5    
HELIX    2   2 ILE A  449  LYS A  454  1                                   6    
HELIX    3   3 ASN A  684  GLU A  689  1                                   6    
SHEET    1  AA 4 VAL A 252  PHE A 255  0                                        
SHEET    2  AA 4 MET A 678  MET A 683 -1  O  MET A 678   N  LEU A 254           
SHEET    3  AA 4 ILE A 666  TYR A 670 -1  O  ILE A 666   N  MET A 683           
SHEET    4  AA 4 SER A 656  GLU A 660 -1  O  CYS A 657   N  LEU A 669           
SHEET    1  AB 4 ASN A 264  LYS A 272  0                                        
SHEET    2  AB 4 LEU A 278  ARG A 285 -1  O  ILE A 279   N  PHE A 271           
SHEET    3  AB 4 ILE A 297  SER A 304 -1  O  ASP A 298   N  ALA A 284           
SHEET    4  AB 4 GLN A 315  MET A 318 -1  O  GLN A 315   N  VAL A 301           
SHEET    1  AC 5 GLN A 447  ASN A 448  0                                        
SHEET    2  AC 5 TYR A 430  SER A 436 -1  O  LEU A 433   N  GLN A 447           
SHEET    3  AC 5 ILE A 340  PHE A 347 -1  O  ILE A 340   N  SER A 436           
SHEET    4  AC 5 SER A 325  GLN A 333 -1  O  SER A 325   N  PHE A 347           
SHEET    5  AC 5 GLY A 466  ARG A 467  1  O  GLY A 466   N  LEU A 331           
SHEET    1  AD 7 PHE A 362  ILE A 365  0                                        
SHEET    2  AD 7 LYS A 368  TYR A 374 -1  O  LYS A 368   N  ILE A 365           
SHEET    3  AD 7 GLU A 380  ARG A 384 -1  O  PHE A 381   N  LEU A 373           
SHEET    4  AD 7 VAL A 387  TYR A 389 -1  O  VAL A 387   N  ARG A 384           
SHEET    5  AD 7 LYS A 395  THR A 400 -1  N  THR A 396   O  VAL A 388           
SHEET    6  AD 7 ASP A 405  LYS A 408 -1  O  PHE A 407   N  THR A 399           
SHEET    7  AD 7 THR A 411  ASN A 415 -1  O  THR A 411   N  LYS A 408           
SHEET    1  AE 3 PHE A 362  ILE A 365  0                                        
SHEET    2  AE 3 LYS A 368  TYR A 374 -1  O  LYS A 368   N  ILE A 365           
SHEET    3  AE 3 LYS A 424  ALA A 425 -1  O  LYS A 424   N  TYR A 374           
SHEET    1  AF 3 LEU A 461  ILE A 463  0                                        
SHEET    2  AF 3 ILE A 480  THR A 487 -1  O  TYR A 485   N  GLY A 462           
SHEET    3  AF 3 ILE A 469  GLN A 470 -1  O  ILE A 469   N  VAL A 481           
SHEET    1  AG 4 LEU A 461  ILE A 463  0                                        
SHEET    2  AG 4 ILE A 480  THR A 487 -1  O  TYR A 485   N  GLY A 462           
SHEET    3  AG 4 GLN A 493  SER A 500 -1  O  SER A 494   N  TYR A 486           
SHEET    4  AG 4 THR A 508  ILE A 509 -1  O  THR A 508   N  TYR A 499           
SHEET    1  AH 2 ARG A 517  LYS A 518  0                                        
SHEET    2  AH 2 ILE A 524  ILE A 525 -1  N  ILE A 525   O  ARG A 517           
SHEET    1  AI 4 LEU A 537  GLU A 544  0                                        
SHEET    2  AI 4 LEU A 550  ASN A 556 -1  O  LYS A 551   N  VAL A 543           
SHEET    3  AI 4 TYR A 560  SER A 566 -1  O  ASN A 562   N  MET A 554           
SHEET    4  AI 4 GLU A 578  LEU A 584 -1  O  GLU A 578   N  ILE A 563           
SHEET    1  AJ 4 SER A 591  ASN A 594  0                                        
SHEET    2  AJ 4 ALA A 604  PRO A 610 -1  O  ILE A 606   N  ILE A 593           
SHEET    3  AJ 4 SER A 616  THR A 630 -1  O  THR A 619   N  ASN A 609           
SHEET    4  AJ 4 PRO A 636  TYR A 652 -1  O  LYS A 637   N  VAL A 628           
LINK        CA    CA A1693                 O   HOH A2039     1555   1555  2.49  
LINK        CA    CA A1693                 O   HOH A2042     1555   1555  2.43  
LINK        CA    CA A1693                 OD1 ASP A 319     1555   1555  2.33  
LINK        CA    CA A1693                 OD1 ASP A 296     1555   1555  2.31  
LINK        CA    CA A1693                 OD1 ASP A 298     1555   1555  2.40  
LINK        CA    CA A1693                 O   TYR A 320     1555   1555  2.37  
LINK        CA    CA A1693                 O   HOH A2071     1555   1555  2.45  
LINK        CA    CA A1694                 O   HOH A2306     1555   1555  2.79  
LINK        CA    CA A1694                 O   HOH A2309     1555   1555  2.64  
LINK        CA    CA A1694                 O   TRP A 573     1555   1555  2.63  
LINK        CA    CA A1694                 O   HOH A2193     1555   1555  2.74  
LINK        CA    CA A1694                 O   HOH A2303     1555   1555  2.78  
LINK        CA    CA A1694                 O   ASP A 515     1555   1555  2.58  
CISPEP   1 ALA A  292    PRO A  293          0        11.36                     
SITE     1 AC1 16 ARG A 266  ILE A 267  ARG A 285  ASP A 291                    
SITE     2 AC1 16 ILE A 327  ASP A 328  PHE A 353  TYR A 485                    
SITE     3 AC1 16 GLN A 493  ARG A 555  TYR A 587  ARG A 615                    
SITE     4 AC1 16 TYR A 655  HOH A2032  HOH A2337  HOH A2481                    
SITE     1 AC2  7 ASP A 296  ASP A 298  ASP A 319  TYR A 320                    
SITE     2 AC2  7 HOH A2039  HOH A2042  HOH A2071                               
SITE     1 AC3  6 ASP A 515  TRP A 573  HOH A2193  HOH A2303                    
SITE     2 AC3  6 HOH A2306  HOH A2309                                          
SITE     1 AC4  8 LYS A 551  GLU A 578  TYR A 631  GLU A 639                    
SITE     2 AC4  8 HOH A2353  HOH A2482  HOH A2483  HOH A2484                    
SITE     1 AC5  8 GLU A 578  LYS A 579  ASP A 580  THR A 581                    
SITE     2 AC5  8 ASN A 582  GLU A 639  HOH A2431  HOH A2485                    
CRYST1   96.981   69.413   72.694  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      0.010311  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014407  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013756        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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