GenomeNet

Database: PDB
Entry: 2W68
LinkDB: 2W68
Original site: 2W68 
HEADER    HYDROLASE                               17-DEC-08   2W68              
TITLE     ENHANCING THE RECEPTOR AFFINITY OF THE SIALIC ACID-BINDING            
TITLE    2 DOMAIN OF VIBRIO CHOLERAE SIALIDASE THROUGH MULTIVALENCY             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CBM40 DOMAIN, RESIDUES 25-216;                             
COMPND   5 SYNONYM: SIALIC ACID BINDING DOMAIN FROM V.                          
COMPND   6  CHOLERAESIALIDASE, NANASE, NEURAMINIDASE;                           
COMPND   7 EC: 3.2.1.18;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CBM, CALCIUM, SECRETED, HYDROLASE, GLYCOSIDASE, SIALIC                
KEYWDS   2 ACID, CARBOHYDRATE-BINDING-DOMAIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.CONNARIS,P.R.CROCKER,G.L.TAYLOR                                     
REVDAT   4   10-NOV-09 2W68    1       REMARK                                   
REVDAT   3   24-MAR-09 2W68    1       JRNL   REMARK                            
REVDAT   2   20-JAN-09 2W68    1       JRNL                                     
REVDAT   1   30-DEC-08 2W68    0                                                
JRNL        AUTH   H.CONNARIS,P.R.CROCKER,G.L.TAYLOR                            
JRNL        TITL   ENHANCING THE RECEPTOR AFFINITY OF THE SIALIC ACID-          
JRNL        TITL 2 BINDING DOMAIN OF VIBRIO CHOLERAE SIALIDASE                  
JRNL        TITL 3 THROUGH MULTIVALENCY                                         
JRNL        REF    J.BIOL.CHEM.                  V. 284  7339 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19124471                                                     
JRNL        DOI    10.1074/JBC.M807398200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 35893                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1911                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2439                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4433                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 130                                     
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 1.05000                                              
REMARK   3    B33 (A**2) : -1.13000                                             
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): 0.291         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.401         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4669 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6354 ; 2.020 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   579 ; 7.941 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   215 ;37.244 ;25.116       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   695 ;18.285 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.709 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   707 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3560 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1969 ; 0.247 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3149 ; 0.326 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   230 ; 0.166 ; 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):    60 ; 0.390 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.246 ; 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):  2930 ; 0.914 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4557 ; 1.557 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2029 ; 2.185 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1795 ; 3.559 ; 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 2W68 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-38364.                                       
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37806                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
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     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 4.9                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.41                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 71.31                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.49000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.49000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       69.30013            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       98.81000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       69.30019            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       98.81006            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.49000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       69.30019            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       98.81006            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.49000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       69.30013            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       98.81000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  3                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     ASP C   216                                                      
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     ALA A  22    CB                                                  
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   CG   MET B    24  -  O    HOH B  2042              1.79            
REMARK 500   NH1  ARG B    74  -  O1   3SL B  1217              1.98            
REMARK 500   O    ALA C    60  -  N    GLY C    62              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   N    GLY A    22     N    ASP A    28     3554      2.01           
REMARK 500   N    ASP A    28     N    GLY A    22     3554      2.01           
REMARK 500   CE   MET B    24     O    HOH C  2002     3555      1.98           
REMARK 500   O    HOH C  2002     CE   MET B    24     3555      1.98           
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 121   C   -  N   -  CA  ANGL. DEV. =  -9.0 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    ASP A  34      131.77    -36.69                                   
REMARK 500    ASN A  51     -126.16     58.39                                   
REMARK 500    ALA A  60      -77.41   -117.29                                   
REMARK 500    SER A 186      139.83   -175.05                                   
REMARK 500    ASN A 189       39.71   -147.77                                   
REMARK 500    SER A 197      126.66   -171.51                                   
REMARK 500    ASP B  34      137.35    -38.44                                   
REMARK 500    ASP B  48       56.75   -140.17                                   
REMARK 500    ASN B  51     -118.87     40.10                                   
REMARK 500    VAL B  56      142.96   -172.93                                   
REMARK 500    THR B 116      -52.60    176.62                                   
REMARK 500    ALA B 150       -8.56    -56.73                                   
REMARK 500    ASN B 165       78.75   -113.29                                   
REMARK 500    MET B 190      148.93   -175.88                                   
REMARK 500    ASP C  34      100.77    -24.67                                   
REMARK 500    THR C  35      -52.60    -26.38                                   
REMARK 500    ASN C  51     -125.20     55.36                                   
REMARK 500    ALA C  60     -107.35   -151.37                                   
REMARK 500    SER C  91      -84.23    -52.90                                   
REMARK 500    THR C 116      -33.45   -131.15                                   
REMARK 500    MET C 190      150.56    163.76                                   
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  CA A1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A1217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A1219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A1220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B1217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B1219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B1220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA C1216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL C1219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC C1220                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W0P   RELATED DB: PDB                                   
REMARK 900  VIBRIO CHOLERAE SIALIDASE WITH ALPHA-2,6-                           
REMARK 900  SIALYLLACTOSE                                                       
REMARK 900 RELATED ID: 1KIT   RELATED DB: PDB                                   
REMARK 900  VIBRIO CHOLERAE NEURAMINIDASE                                       
REMARK 900 RELATED ID: 1W0O   RELATED DB: PDB                                   
REMARK 900  VIBRIO CHOLERAE SIALIDASE                                           
DBREF  2W68 A   22    24  PDB    2W68     2W68            22     24             
DBREF  2W68 A   25   216  UNP    P0C6E9   NANH_VIBCH      25    216             
DBREF  2W68 B   22    24  PDB    2W68     2W68            22     24             
DBREF  2W68 B   25   216  UNP    P0C6E9   NANH_VIBCH      25    216             
DBREF  2W68 C   22    24  PDB    2W68     2W68            22     24             
DBREF  2W68 C   25   216  UNP    P0C6E9   NANH_VIBCH      25    216             
SEQRES   1 A  195  ALA ALA MET ALA LEU PHE ASP TYR ASN ALA THR GLY ASP          
SEQRES   2 A  195  THR GLU PHE ASP SER PRO ALA LYS GLN GLY TRP MET GLN          
SEQRES   3 A  195  ASP ASN THR ASN ASN GLY SER GLY VAL LEU THR ASN ALA          
SEQRES   4 A  195  ASP GLY MET PRO ALA TRP LEU VAL GLN GLY ILE GLY GLY          
SEQRES   5 A  195  ARG ALA GLN TRP THR TYR SER LEU SER THR ASN GLN HIS          
SEQRES   6 A  195  ALA GLN ALA SER SER PHE GLY TRP ARG MET THR THR GLU          
SEQRES   7 A  195  MET LYS VAL LEU SER GLY GLY MET ILE THR ASN TYR TYR          
SEQRES   8 A  195  ALA ASN GLY THR GLN ARG VAL LEU PRO ILE ILE SER LEU          
SEQRES   9 A  195  ASP SER SER GLY ASN LEU VAL VAL GLU PHE GLU GLY GLN          
SEQRES  10 A  195  THR GLY ARG THR VAL LEU ALA THR GLY THR ALA ALA THR          
SEQRES  11 A  195  GLU TYR HIS LYS PHE GLU LEU VAL PHE LEU PRO GLY SER          
SEQRES  12 A  195  ASN PRO SER ALA SER PHE TYR PHE ASP GLY LYS LEU ILE          
SEQRES  13 A  195  ARG ASP ASN ILE GLN PRO THR ALA SER LYS GLN ASN MET          
SEQRES  14 A  195  ILE VAL TRP GLY ASN GLY SER SER ASN THR ASP GLY VAL          
SEQRES  15 A  195  ALA ALA TYR ARG ASP ILE LYS PHE GLU ILE GLN GLY ASP          
SEQRES   1 B  195  ALA ALA MET ALA LEU PHE ASP TYR ASN ALA THR GLY ASP          
SEQRES   2 B  195  THR GLU PHE ASP SER PRO ALA LYS GLN GLY TRP MET GLN          
SEQRES   3 B  195  ASP ASN THR ASN ASN GLY SER GLY VAL LEU THR ASN ALA          
SEQRES   4 B  195  ASP GLY MET PRO ALA TRP LEU VAL GLN GLY ILE GLY GLY          
SEQRES   5 B  195  ARG ALA GLN TRP THR TYR SER LEU SER THR ASN GLN HIS          
SEQRES   6 B  195  ALA GLN ALA SER SER PHE GLY TRP ARG MET THR THR GLU          
SEQRES   7 B  195  MET LYS VAL LEU SER GLY GLY MET ILE THR ASN TYR TYR          
SEQRES   8 B  195  ALA ASN GLY THR GLN ARG VAL LEU PRO ILE ILE SER LEU          
SEQRES   9 B  195  ASP SER SER GLY ASN LEU VAL VAL GLU PHE GLU GLY GLN          
SEQRES  10 B  195  THR GLY ARG THR VAL LEU ALA THR GLY THR ALA ALA THR          
SEQRES  11 B  195  GLU TYR HIS LYS PHE GLU LEU VAL PHE LEU PRO GLY SER          
SEQRES  12 B  195  ASN PRO SER ALA SER PHE TYR PHE ASP GLY LYS LEU ILE          
SEQRES  13 B  195  ARG ASP ASN ILE GLN PRO THR ALA SER LYS GLN ASN MET          
SEQRES  14 B  195  ILE VAL TRP GLY ASN GLY SER SER ASN THR ASP GLY VAL          
SEQRES  15 B  195  ALA ALA TYR ARG ASP ILE LYS PHE GLU ILE GLN GLY ASP          
SEQRES   1 C  195  ALA ALA MET ALA LEU PHE ASP TYR ASN ALA THR GLY ASP          
SEQRES   2 C  195  THR GLU PHE ASP SER PRO ALA LYS GLN GLY TRP MET GLN          
SEQRES   3 C  195  ASP ASN THR ASN ASN GLY SER GLY VAL LEU THR ASN ALA          
SEQRES   4 C  195  ASP GLY MET PRO ALA TRP LEU VAL GLN GLY ILE GLY GLY          
SEQRES   5 C  195  ARG ALA GLN TRP THR TYR SER LEU SER THR ASN GLN HIS          
SEQRES   6 C  195  ALA GLN ALA SER SER PHE GLY TRP ARG MET THR THR GLU          
SEQRES   7 C  195  MET LYS VAL LEU SER GLY GLY MET ILE THR ASN TYR TYR          
SEQRES   8 C  195  ALA ASN GLY THR GLN ARG VAL LEU PRO ILE ILE SER LEU          
SEQRES   9 C  195  ASP SER SER GLY ASN LEU VAL VAL GLU PHE GLU GLY GLN          
SEQRES  10 C  195  THR GLY ARG THR VAL LEU ALA THR GLY THR ALA ALA THR          
SEQRES  11 C  195  GLU TYR HIS LYS PHE GLU LEU VAL PHE LEU PRO GLY SER          
SEQRES  12 C  195  ASN PRO SER ALA SER PHE TYR PHE ASP GLY LYS LEU ILE          
SEQRES  13 C  195  ARG ASP ASN ILE GLN PRO THR ALA SER LYS GLN ASN MET          
SEQRES  14 C  195  ILE VAL TRP GLY ASN GLY SER SER ASN THR ASP GLY VAL          
SEQRES  15 C  195  ALA ALA TYR ARG ASP ILE LYS PHE GLU ILE GLN GLY ASP          
HET     CA  A1211       1                                                       
HET    SIA  A1217      20                                                       
HET    GAL  A1219      11                                                       
HET    BGC  A1220      12                                                       
HET    SIA  B1217      20                                                       
HET    GAL  B1219      11                                                       
HET    BGC  B1220      12                                                       
HET    SIA  C1216      20                                                       
HET    GAL  C1219      11                                                       
HET    BGC  C1220      12                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   4  GAL    3(C6 H12 O6)                                                 
FORMUL   5  BGC    3(C6 H12 O6)                                                 
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  HOH   *133(H2 O1)                                                   
HELIX    1   1 ASP A   34  ASP A   38  5                                   5    
HELIX    2   2 PRO A   40  GLY A   44  5                                   5    
HELIX    3   3 SER A   82  GLY A   93  1                                  12    
HELIX    4   4 THR A  146  GLU A  152  5                                   7    
HELIX    5   5 ASP B   34  ASP B   38  5                                   5    
HELIX    6   6 PRO B   40  GLY B   44  5                                   5    
HELIX    7   7 SER B   82  GLY B   93  1                                  12    
HELIX    8   8 THR B  146  GLU B  152  5                                   7    
HELIX    9   9 ASP C   34  ASP C   38  5                                   5    
HELIX   10  10 SER C   39  GLY C   44  5                                   6    
HELIX   11  11 SER C   82  GLY C   93  1                                  12    
HELIX   12  12 THR C  146  THR C  151  5                                   6    
SHEET    1  AA 4 ALA A  25  ASN A  30  0                                        
SHEET    2  AA 4 GLY A 202  ILE A 213 -1  O  ILE A 209   N  TYR A  29           
SHEET    3  AA 4 PRO A  64  GLY A  70 -1  O  TRP A  66   N  TYR A 206           
SHEET    4  AA 4 SER A  54  ASN A  59 -1  O  SER A  54   N  GLN A  69           
SHEET    1  AB 6 ALA A  25  ASN A  30  0                                        
SHEET    2  AB 6 GLY A 202  ILE A 213 -1  O  ILE A 209   N  TYR A  29           
SHEET    3  AB 6 TRP A  94  GLY A 105 -1  O  ARG A  95   N  GLU A 212           
SHEET    4  AB 6 HIS A 154  LEU A 161 -1  O  HIS A 154   N  MET A 100           
SHEET    5  AB 6 SER A 167  PHE A 172 -1  O  SER A 167   N  LEU A 161           
SHEET    6  AB 6 LYS A 175  ILE A 181 -1  O  LYS A 175   N  PHE A 172           
SHEET    1  AC 6 MET A  46  GLN A  47  0                                        
SHEET    2  AC 6 ALA A  75  TYR A  79 -1  O  THR A  78   N  MET A  46           
SHEET    3  AC 6 ILE A 191  ASN A 195 -1  O  ILE A 191   N  TYR A  79           
SHEET    4  AC 6 TYR A 111  ALA A 113 -1  O  TYR A 111   N  VAL A 192           
SHEET    5  AC 6 GLN A 117  VAL A 119 -1  O  VAL A 119   N  TYR A 112           
SHEET    6  AC 6 THR A 184  ALA A 185 -1  O  THR A 184   N  ARG A 118           
SHEET    1  AD 4 ILE A 108  THR A 109  0                                        
SHEET    2  AD 4 PRO A 121  LEU A 125 -1  O  ILE A 123   N  ILE A 108           
SHEET    3  AD 4 LEU A 131  PHE A 135 -1  O  VAL A 132   N  SER A 124           
SHEET    4  AD 4 THR A 142  ALA A 145 -1  O  THR A 142   N  VAL A 133           
SHEET    1  BA 4 ALA B  25  ASN B  30  0                                        
SHEET    2  BA 4 GLY B 202  ILE B 213 -1  O  ILE B 209   N  TYR B  29           
SHEET    3  BA 4 ALA B  65  GLY B  70 -1  O  TRP B  66   N  TYR B 206           
SHEET    4  BA 4 SER B  54  THR B  58 -1  O  SER B  54   N  GLN B  69           
SHEET    1  BB 6 ALA B  25  ASN B  30  0                                        
SHEET    2  BB 6 GLY B 202  ILE B 213 -1  O  ILE B 209   N  TYR B  29           
SHEET    3  BB 6 TRP B  94  GLY B 105 -1  O  ARG B  95   N  GLU B 212           
SHEET    4  BB 6 HIS B 154  LEU B 161 -1  O  HIS B 154   N  MET B 100           
SHEET    5  BB 6 SER B 167  PHE B 172 -1  O  SER B 167   N  LEU B 161           
SHEET    6  BB 6 LYS B 175  ILE B 181 -1  O  LYS B 175   N  PHE B 172           
SHEET    1  BC 4 MET B  46  GLN B  47  0                                        
SHEET    2  BC 4 ALA B  75  TYR B  79 -1  O  THR B  78   N  MET B  46           
SHEET    3  BC 4 THR B 184  ASN B 195 -1  O  ILE B 191   N  TYR B  79           
SHEET    4  BC 4 TYR B 111  ARG B 118 -1  O  TYR B 111   N  VAL B 192           
SHEET    1  BD 4 ILE B 108  THR B 109  0                                        
SHEET    2  BD 4 PRO B 121  LEU B 125 -1  O  ILE B 123   N  ILE B 108           
SHEET    3  BD 4 LEU B 131  PHE B 135 -1  O  VAL B 132   N  SER B 124           
SHEET    4  BD 4 THR B 142  ALA B 145 -1  O  THR B 142   N  VAL B 133           
SHEET    1  CA 4 ALA C  25  ASN C  30  0                                        
SHEET    2  CA 4 GLY C 202  ILE C 213 -1  O  ILE C 209   N  TYR C  29           
SHEET    3  CA 4 PRO C  64  GLN C  69 -1  O  TRP C  66   N  TYR C 206           
SHEET    4  CA 4 SER C  54  ASN C  59 -1  O  SER C  54   N  GLN C  69           
SHEET    1  CB 6 ALA C  25  ASN C  30  0                                        
SHEET    2  CB 6 GLY C 202  ILE C 213 -1  O  ILE C 209   N  TYR C  29           
SHEET    3  CB 6 TRP C  94  GLY C 105 -1  O  ARG C  95   N  GLU C 212           
SHEET    4  CB 6 TYR C 153  LEU C 161 -1  O  HIS C 154   N  MET C 100           
SHEET    5  CB 6 SER C 167  PHE C 172 -1  O  SER C 167   N  LEU C 161           
SHEET    6  CB 6 LEU C 176  ILE C 181 -1  N  ILE C 177   O  PHE C 170           
SHEET    1  CC 6 MET C  46  GLN C  47  0                                        
SHEET    2  CC 6 ALA C  75  TYR C  79 -1  O  THR C  78   N  MET C  46           
SHEET    3  CC 6 ASN C 189  ASN C 195 -1  O  ILE C 191   N  TYR C  79           
SHEET    4  CC 6 TYR C 111  ASN C 114 -1  O  TYR C 111   N  VAL C 192           
SHEET    5  CC 6 GLN C 117  VAL C 119 -1  O  GLN C 117   N  ASN C 114           
SHEET    6  CC 6 THR C 184  ALA C 185 -1  O  THR C 184   N  ARG C 118           
SHEET    1  CD 3 PRO C 121  LEU C 125  0                                        
SHEET    2  CD 3 LEU C 131  PHE C 135 -1  O  VAL C 132   N  SER C 124           
SHEET    3  CD 3 THR C 142  ALA C 145 -1  O  THR C 142   N  VAL C 133           
LINK         C2  SIA A1217                 O3  GAL A1219     1555   1555  1.44  
LINK         C1  GAL A1219                 O4  BGC A1220     1555   1555  1.42  
LINK         C2  SIA B1217                 O3  GAL B1219     1555   1555  1.43  
LINK         C1  GAL B1219                 O4  BGC B1220     1555   1555  1.42  
LINK         C2  SIA C1216                 O3  GAL C1219     1555   1555  1.45  
LINK         C1  GAL C1219                 O4  BGC C1220     1555   1555  1.43  
CISPEP   1 ALA A   22    ALA A   23          0        -0.80                     
SITE     1 AC1  1 SER A  82                                                     
SITE     1 AC2 10 ARG A  74  ARG A 118  GLN A 188  GLY A 196                    
SITE     2 AC2 10 SER A 197  SER A 198  GAL A1219  HOH A2009                    
SITE     3 AC2 10 THR C 139  GLY C 140                                          
SITE     1 AC3  2 SIA A1217  BGC A1220                                          
SITE     1 AC4  1 GAL A1219                                                     
SITE     1 AC5 11 ARG B  74  TYR B 111  ARG B 118  GLY B 140                    
SITE     2 AC5 11 GLN B 188  GLY B 196  SER B 197  SER B 198                    
SITE     3 AC5 11 ASN B 199  GAL B1219  HOH B2044                               
SITE     1 AC6  3 SER B 198  SIA B1217  BGC B1220                               
SITE     1 AC7  1 GAL B1219                                                     
SITE     1 AC8 10 GLY A 140  ARG C  74  ARG C 118  GLN C 188                    
SITE     2 AC8 10 GLY C 196  SER C 197  SER C 198  GAL C1219                    
SITE     3 AC8 10 HOH C2048  HOH C2049                                          
SITE     1 AC9  2 SIA C1216  BGC C1220                                          
SITE     1 BC1  2 ARG A 141  GAL C1219                                          
CRYST1  138.600  197.620   82.980  90.00  90.00  90.00 C 2 2 21     24          
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      0.007215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system