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Database: PDB
Entry: 1CT1
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Original site: 1CT1 
HEADER    ENTEROTOXIN                             03-JUN-97   1CT1              
TITLE     CHOLERA TOXIN B-PENTAMER MUTANT G33R BOUND TO RECEPTOR                
TITLE    2 PENTASACCHARIDE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN;                                             
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 FRAGMENT: B-PENTAMER;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 STRAIN: OGAWA 41 (CLASSICAL BIOTYPE);                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENTEROTOXIN, TOXIN/RECEPTOR COMPLEX, OLIGOSACCHARIDE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   3   04-AUG-09 1CT1    1       ATOM   COMPND CONECT HET                 
REVDAT   3 2                   1       HETATM HETNAM LINK   SITE                
REVDAT   2   24-FEB-09 1CT1    1       VERSN                                    
REVDAT   1   15-OCT-97 1CT1    0                                                
JRNL        AUTH   E.A.MERRITT,S.SARFATY,M.G.JOBLING,T.CHANG,                   
JRNL        AUTH 2 R.K.HOLMES,T.R.HIRST,W.G.HOL                                 
JRNL        TITL   STRUCTURAL STUDIES OF RECEPTOR BINDING BY CHOLERA            
JRNL        TITL 2 TOXIN MUTANTS.                                               
JRNL        REF    PROTEIN SCI.                  V.   6  1516 1997              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9232653                                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21343                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 272                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2277                       
REMARK   3   BIN FREE R VALUE                    : 0.2620                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 21                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4105                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 137                                     
REMARK   3   SOLVENT ATOMS            : 151                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20300                                             
REMARK   3    B22 (A**2) : -3.33020                                             
REMARK   3    B33 (A**2) : 3.53320                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.20290                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.57                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.000 ; 2.300                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.000 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.300                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.000 ; 4.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM1.CHO (MODIFIED)                          
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH1.CHO (MODIFIED)                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BABINET BULK SOLVENT MODEL KSOL =         
REMARK   3  0.8 BSOL = 50.0                                                     
REMARK   4                                                                      
REMARK   4 1CT1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : DEC-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.2-7.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : MACRO                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22182                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1CHP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN, 20 MM TRIS, 1 MM GM1-OS,        
REMARK 280  PH 7.5 200 MM MGCL2, 100 MM CACODYLATE, 19% PEG 1000, 0.2%          
REMARK 280  AGAROSE, PH 7.2                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.70000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.80500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.70000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.80500            
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 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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 EACH CHAIN CONTAINS AN INTRODUCED MUTATION GLY->ARG AT               
REMARK 400 RESIDUE 33 OF THE RECEPTOR BINDING SITE.                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET F  68   SD    MET F  68   CE      0.398                       
REMARK 500    MET G  68   CG    MET G  68   SD     -0.319                       
REMARK 500    MET H  68   CG    MET H  68   SD     -0.169                       
REMARK 500    MET H  68   SD    MET H  68   CE      0.409                       
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    LEU F  31   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    MET F  68   CG  -  SD  -  CE  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LEU G  31   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU H  31   CA  -  CB  -  CG  ANGL. DEV. =  15.2 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                                                                      
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    LYS D  34       -2.04     75.38                                   
REMARK 500    GLN E  16      139.23   -173.27                                   
REMARK 500    LYS F  34       -1.42     78.52                                   
REMARK 500    ARG G  35       30.31   -141.12                                   
REMARK 500    GLN H  16      142.29   -173.64                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 129        DISTANCE =  8.04 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA F 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC F 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA F 108                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 104                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGA G 105                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 106                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC G 107                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA G 108                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 104                  
DBREF  1CT1 D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1CT1 E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1CT1 F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1CT1 G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1CT1 H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1CT1 HIS D   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1CT1 ARG D   33  UNP  P01556    GLY    54 ENGINEERED                     
SEQADV 1CT1 THR D   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1CT1 HIS E   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1CT1 ARG E   33  UNP  P01556    GLY    54 ENGINEERED                     
SEQADV 1CT1 THR E   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1CT1 HIS F   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1CT1 ARG F   33  UNP  P01556    GLY    54 ENGINEERED                     
SEQADV 1CT1 THR F   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1CT1 HIS G   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1CT1 ARG G   33  UNP  P01556    GLY    54 ENGINEERED                     
SEQADV 1CT1 THR G   47  UNP  P01556    ILE    68 CONFLICT                       
SEQADV 1CT1 HIS H   18  UNP  P01556    TYR    39 CONFLICT                       
SEQADV 1CT1 ARG H   33  UNP  P01556    GLY    54 ENGINEERED                     
SEQADV 1CT1 THR H   47  UNP  P01556    ILE    68 CONFLICT                       
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET    GAL  F 104      11                                                       
HET    NGA  F 105      14                                                       
HET    GAL  F 106      11                                                       
HET    BGC  F 107      12                                                       
HET    SIA  F 108      20                                                       
HET    GAL  G 104      11                                                       
HET    NGA  G 105      14                                                       
HET    GAL  G 106      11                                                       
HET    BGC  G 107      12                                                       
HET    SIA  G 108      20                                                       
HET     CL  H 104       1                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NGA N-ACETYL-D-GALACTOSAMINE                                         
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   6  GAL    4(C6 H12 O6)                                                 
FORMUL   6  NGA    2(C8 H15 N O6)                                               
FORMUL   6  BGC    2(C6 H12 O6)                                                 
FORMUL   6  SIA    2(C11 H19 N O9)                                              
FORMUL   8   CL    CL 1-                                                        
FORMUL   9  HOH   *151(H2 O)                                                    
HELIX    1 DA1 ILE D    5  CYS D    9  1                                   5    
HELIX    2 DA2 ASP D   59  THR D   78  1                                  20    
HELIX    3 EA1 ILE E    5  CYS E    9  1                                   5    
HELIX    4 EA2 LYS E   62  THR E   78  1                                  17    
HELIX    5 FA1 ILE F    5  CYS F    9  1                                   5    
HELIX    6 FA2 ASP F   59  THR F   78  1                                  20    
HELIX    7 GA1 ILE G    5  CYS G    9  1                                   5    
HELIX    8 GA2 GLN G   61  THR G   78  1                                  18    
HELIX    9 HA1 ILE H    5  CYS H    9  1                                   5    
HELIX   10 HA2 SER H   60  THR H   78  1                                  19    
SHEET    1 BB1 6 THR D  15  ASP D  22  0                                        
SHEET    2 BB1 6 VAL D  82  TRP D  88 -1                                        
SHEET    3 BB1 6 HIS D  94  ALA D 102 -1                                        
SHEET    4 BB1 6 SER E  26  SER E  30 -1                                        
SHEET    5 BB1 6 MET E  37  THR E  41 -1                                        
SHEET    6 BB1 6 THR E  47  VAL E  50 -1                                        
SHEET    1 BB2 6 THR E  15  ASP E  22  0                                        
SHEET    2 BB2 6 VAL E  82  TRP E  88 -1                                        
SHEET    3 BB2 6 HIS E  94  ALA E 102 -1                                        
SHEET    4 BB2 6 SER F  26  SER F  30 -1                                        
SHEET    5 BB2 6 MET F  37  THR F  41 -1                                        
SHEET    6 BB2 6 THR F  47  VAL F  50 -1                                        
SHEET    1 BB3 6 THR F  15  ASP F  22  0                                        
SHEET    2 BB3 6 VAL F  82  TRP F  88 -1                                        
SHEET    3 BB3 6 HIS F  94  ALA F 102 -1                                        
SHEET    4 BB3 6 SER G  26  SER G  30 -1                                        
SHEET    5 BB3 6 MET G  37  THR G  41 -1                                        
SHEET    6 BB3 6 THR G  47  VAL G  50 -1                                        
SHEET    1 BB4 6 THR G  15  ASP G  22  0                                        
SHEET    2 BB4 6 VAL G  82  TRP G  88 -1                                        
SHEET    3 BB4 6 HIS G  94  ALA G 102 -1                                        
SHEET    4 BB4 6 SER H  26  SER H  30 -1                                        
SHEET    5 BB4 6 MET H  37  THR H  41 -1                                        
SHEET    6 BB4 6 THR H  47  VAL H  50 -1                                        
SHEET    1 BB5 6 THR H  15  ASP H  22  0                                        
SHEET    2 BB5 6 VAL H  82  TRP H  88 -1                                        
SHEET    3 BB5 6 HIS H  94  ALA H 102 -1                                        
SHEET    4 BB5 6 SER D  26  SER D  30 -1                                        
SHEET    5 BB5 6 MET D  37  THR D  41 -1                                        
SHEET    6 BB5 6 THR D  47  VAL D  50 -1                                        
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.03  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.03  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.03  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.01  
LINK         C1  GAL F 104                 O3  NGA F 105     1555   1555  1.40  
LINK         C1  NGA F 105                 O4  GAL F 106     1555   1555  1.43  
LINK         O3  GAL F 106                 C2  SIA F 108     1555   1555  1.42  
LINK         C1  GAL G 104                 O3  NGA G 105     1555   1555  1.43  
LINK         C1  NGA G 105                 O4  GAL G 106     1555   1555  1.43  
LINK         O3  GAL G 106                 C2  SIA G 108     1555   1555  1.43  
LINK         C1  GAL F 106                 O4  BGC F 107     1555   1555  1.40  
LINK         C1  GAL G 106                 O4  BGC G 107     1555   1555  1.41  
CISPEP   1 THR D   92    PRO D   93          0        -0.29                     
CISPEP   2 THR E   92    PRO E   93          0         0.37                     
CISPEP   3 THR F   92    PRO F   93          0        -1.49                     
CISPEP   4 THR G   92    PRO G   93          0        -0.27                     
CISPEP   5 THR H   92    PRO H   93          0         1.13                     
SITE     1 AC1 11 GLU F  51  GLN F  56  HIS F  57  GLN F  61                    
SITE     2 AC1 11 TRP F  88  ASN F  90  LYS F  91  NGA F 105                    
SITE     3 AC1 11 SIA F 108  HOH F 141  HOH F 143                               
SITE     1 AC2  8 GLN F  56  GAL F 104  GAL F 106  SIA F 108                    
SITE     2 AC2  8 HOH F 141  ARG G  33  GLN H  16  HIS H  18                    
SITE     1 AC3  5 NGA F 105  BGC F 107  SIA F 108  GLN H  16                    
SITE     2 AC3  5 HIS H  94                                                     
SITE     1 AC4  6 GAL F 106  HIS H  18  THR H  47  PRO H  93                    
SITE     2 AC4  6 HIS H  94  HOH H 121                                          
SITE     1 AC5  8 HIS F  13  GLN F  56  GAL F 104  NGA F 105                    
SITE     2 AC5  8 GAL F 106  HOH F 143  ARG G  33  LYS G  34                    
SITE     1 AC6 11 GLU G  51  GLN G  56  HIS G  57  GLN G  61                    
SITE     2 AC6 11 TRP G  88  ASN G  90  LYS G  91  NGA G 105                    
SITE     3 AC6 11 SIA G 108  HOH G 112  HOH G 145                               
SITE     1 AC7  7 HIS D  18  GLN G  56  GAL G 104  GAL G 106                    
SITE     2 AC7  7 SIA G 108  HOH G 112  ARG H  33                               
SITE     1 AC8  4 GLN D  16  NGA G 105  BGC G 107  SIA G 108                    
SITE     1 AC9  5 HIS D  18  ALA D  46  THR D  47  HIS D  94                    
SITE     2 AC9  5 GAL G 106                                                     
SITE     1 BC1  8 HIS G  13  GLN G  56  GAL G 104  NGA G 105                    
SITE     2 BC1  8 GAL G 106  HOH G 145  ARG H  33  LYS H  34                    
SITE     1 BC2  4 TYR D  12  HIS D  13  TYR H  12  HIS H  13                    
CRYST1  103.400   67.610  101.700  90.00 131.66  90.00 C 1 2 1      20          
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      0.009671  0.000000  0.008605        0.00000                         
SCALE2      0.000000  0.014791  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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