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Database: PDB
Entry: 1JR0
LinkDB: 1JR0
Original site: 1JR0 
HEADER    TOXIN                                   09-AUG-01   1JR0              
TITLE     CHOLERA TOXIN B-PENTAMER WITH LIGAND BMSC-0011                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B SUBUNIT;                                   
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CTXB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENTEROTOXIN, RECEPTOR, B-PENTAMER, TOXIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   4   13-JUL-11 1JR0    1       VERSN                                    
REVDAT   3   24-FEB-09 1JR0    1       VERSN                                    
REVDAT   2   01-APR-03 1JR0    1       JRNL                                     
REVDAT   1   08-MAY-02 1JR0    0                                                
JRNL        AUTH   J.C.PICKENS,E.A.MERRITT,M.AHN,C.L.VERLINDE,W.G.HOL,E.FAN     
JRNL        TITL   ANCHOR-BASED DESIGN OF IMPROVED CHOLERA TOXIN AND E. COLI    
JRNL        TITL 2 HEAT-LABILE ENTEROTOXIN RECEPTOR BINDING ANTAGONISTS THAT    
JRNL        TITL 3 DISPLAY MULTIPLE BINDING MODES.                              
JRNL        REF    CHEM.BIOL.                    V.   9   215 2002              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   11880036                                                     
JRNL        DOI    10.1016/S1074-5521(02)00097-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.131                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.183                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5513                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.115                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.164                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 4511                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 4070                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 160                                           
REMARK   3   SOLVENT ATOMS      : 695                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 4925.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 4085.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 12                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 44038                   
REMARK   3   NUMBER OF RESTRAINTS                     : 52704                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.012                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.031                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.037                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.061                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.067                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.054                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.041                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.083                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228        
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014088.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110275                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, NACL, MGCL2, TRIS HCL, PH      
REMARK 280  7.5, VAPOR DIFFUSION, SITTING DROP                                  
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       51.04900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.04900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.03200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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    ARG D  35   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG D  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    HIS D  57   CG  -  ND1 -  CE1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    HIS D  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG D  73   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH2 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    HIS D  94   CG  -  ND1 -  CE1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASN D 103   C   -  N   -  CA  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    THR E   1   CA  -  CB  -  CG2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    GLY E  54   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    GLN E  56   C   -  N   -  CA  ANGL. DEV. =  20.5 DEGREES          
REMARK 500    HIS E  57   CG  -  ND1 -  CE1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG E  73   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    LYS E  81   CD  -  CE  -  NZ  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ARG F  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG F  73   NE  -  CZ  -  NH2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    HIS F  94   CG  -  ND1 -  CE1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    HIS G  57   CG  -  ND1 -  CE1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    HIS G  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG G  73   CD  -  NE  -  CZ  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    HIS H  57   CG  -  ND1 -  CE1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    HIS H  57   ND1 -  CE1 -  NE2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG H  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG H  73   CD  -  NE  -  CZ  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG H  73   NE  -  CZ  -  NH2 ANGL. DEV. =   8.5 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 H  34       -0.52     76.38                                   
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 D 226        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH D 228        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH E 217        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH E 232        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH E 242        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH G 140        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH H 226        DISTANCE =  5.08 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A24 D 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A24 E 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A24 F 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A24 G 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A24 H 104                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LTS   RELATED DB: PDB                                   
REMARK 900 1LTS CONTAINS THE AB5 HOLOTOXIN                                      
REMARK 900 RELATED ID: 1LTA   RELATED DB: PDB                                   
REMARK 900 1LTA CONTAINS THE AB5 HOLOTOXIN COMPLEXED WITH GALACTOSE.            
REMARK 900 RELATED ID: 1LT6   RELATED DB: PDB                                   
REMARK 900 1LT6 CONTAINS THE CHOLERA TOXIN B-PENTAMER COMPLEXED WITH            
REMARK 900 METANITROPHENYL.                                                     
REMARK 900 RELATED ID: 1FD7   RELATED DB: PDB                                   
REMARK 900 1FD7 CONTAINS THE HEAT-LABILE ENTEROTOXIN B CHAIN COMPLEXED          
REMARK 900 WITH N-BENZYL-3-(ALPHA-D-GALACTOS-1-YL)-BENZAMIDE                    
REMARK 900 RELATED ID: 1JQY   RELATED DB: PDB                                   
REMARK 900 1JQY CONTAINS THE HEAT-LABILE ENTEROTOXIN B CHAIN COMPLEXED          
REMARK 900 WITH (3-NITRO-5-(3-MORPHOLIN-4-YL-PROPYLAMINOCARBONYL)               
REMARK 900 PHENYL)-GALACTOPYRANOSIDE                                            
DBREF  1JR0 D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1JR0 E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1JR0 F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1JR0 G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1JR0 H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
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 GLY 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 GLY 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 GLY 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 GLY 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 GLY 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    A24  D 104      32                                                       
HET    A24  E 104      52                                                       
HET    A24  F 104      52                                                       
HET    A24  G 104      52                                                       
HET    A24  H 104      32                                                       
HETNAM     A24 (3-NITRO-5-(2-MORPHOLIN-4-YL-ETHYLAMINOCARBONYL)                 
HETNAM   2 A24  PHENYL)-GALACTOPYRANOSIDE                                       
HETSYN     A24 BMSC-0011                                                        
FORMUL   6  A24    5(C19 H27 N3 O10)                                            
FORMUL  11  HOH   *695(H2 O)                                                    
HELIX    1   1 ASN D    4  ALA D   10  1                                   7    
HELIX    2   2 ILE D   58  GLU D   79  1                                  22    
HELIX    3   3 ASN E    4  ALA E   10  1                                   7    
HELIX    4   4 SER E   60  GLU E   79  1                                  20    
HELIX    5   5 ASN F    4  GLU F   11  1                                   8    
HELIX    6   6 SER F   60  GLU F   79  1                                  20    
HELIX    7   7 ASN G    4  ALA G   10  1                                   7    
HELIX    8   8 SER G   60  GLU G   79  1                                  20    
HELIX    9   9 ASN H    4  GLU H   11  1                                   8    
HELIX   10  10 SER H   60  GLU H   79  1                                  20    
SHEET    1   A39 THR D  15  ASP D  22  0                                        
SHEET    2   A39 VAL D  82  TRP D  88 -1  N  VAL D  82   O  ASP D  22           
SHEET    3   A39 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET    4   A39 THR D  47  VAL D  50  1  O  THR D  47   N  HIS D  94           
SHEET    5   A39 MET D  37  THR D  41 -1  O  ALA D  38   N  VAL D  50           
SHEET    6   A39 SER D  26  SER D  30 -1  O  SER D  26   N  THR D  41           
SHEET    7   A39 HIS H  94  ALA H 102 -1  N  ILE H  99   O  GLU D  29           
SHEET    8   A39 VAL H  82  TRP H  88 -1  N  GLU H  83   O  SER H 100           
SHEET    9   A39 THR H  15  ASP H  22 -1  O  GLN H  16   N  VAL H  87           
SHEET   10   A39 VAL H  82  TRP H  88 -1  N  VAL H  82   O  ASP H  22           
SHEET   11   A39 HIS H  94  ALA H 102 -1  O  ALA H  95   N  TRP H  88           
SHEET   12   A39 THR H  47  VAL H  50  1  O  THR H  47   N  HIS H  94           
SHEET   13   A39 MET H  37  THR H  41 -1  O  ALA H  38   N  VAL H  50           
SHEET   14   A39 SER H  26  SER H  30 -1  O  SER H  26   N  THR H  41           
SHEET   15   A39 HIS G  94  ALA G 102 -1  N  ILE G  99   O  GLU H  29           
SHEET   16   A39 VAL G  82  TRP G  88 -1  N  GLU G  83   O  SER G 100           
SHEET   17   A39 THR G  15  ASP G  22 -1  O  GLN G  16   N  VAL G  87           
SHEET   18   A39 VAL G  82  TRP G  88 -1  N  VAL G  82   O  ASP G  22           
SHEET   19   A39 HIS G  94  ALA G 102 -1  O  ALA G  95   N  TRP G  88           
SHEET   20   A39 THR G  47  VAL G  50  1  O  THR G  47   N  HIS G  94           
SHEET   21   A39 MET G  37  THR G  41 -1  O  ALA G  38   N  VAL G  50           
SHEET   22   A39 SER G  26  SER G  30 -1  N  SER G  26   O  THR G  41           
SHEET   23   A39 HIS F  94  ALA F 102 -1  O  ILE F  99   N  GLU G  29           
SHEET   24   A39 VAL F  82  TRP F  88 -1  N  GLU F  83   O  SER F 100           
SHEET   25   A39 THR F  15  ASP F  22 -1  O  GLN F  16   N  VAL F  87           
SHEET   26   A39 VAL F  82  TRP F  88 -1  N  VAL F  82   O  ASP F  22           
SHEET   27   A39 HIS F  94  ALA F 102 -1  O  ALA F  95   N  TRP F  88           
SHEET   28   A39 THR F  47  VAL F  50  1  O  THR F  47   N  HIS F  94           
SHEET   29   A39 MET F  37  THR F  41 -1  O  ALA F  38   N  VAL F  50           
SHEET   30   A39 SER F  26  SER F  30 -1  O  SER F  26   N  THR F  41           
SHEET   31   A39 HIS E  94  ALA E 102 -1  N  ILE E  99   O  GLU F  29           
SHEET   32   A39 VAL E  82  TRP E  88 -1  N  GLU E  83   O  SER E 100           
SHEET   33   A39 THR E  15  ASP E  22 -1  O  GLN E  16   N  VAL E  87           
SHEET   34   A39 VAL E  82  TRP E  88 -1  N  VAL E  82   O  ASP E  22           
SHEET   35   A39 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET   36   A39 THR E  47  VAL E  50  1  O  THR E  47   N  HIS E  94           
SHEET   37   A39 ALA E  38  THR E  41 -1  O  ALA E  38   N  VAL E  50           
SHEET   38   A39 SER E  26  SER E  30 -1  O  SER E  26   N  THR E  41           
SHEET   39   A39 HIS D  94  ALA D 102  1  O  ILE D  99   N  GLU E  29           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.05  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.05  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.05  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.05  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.06  
CISPEP   1 THR D   92    PRO D   93          0       -14.92                     
CISPEP   2 THR E   92    PRO E   93          0        -9.79                     
CISPEP   3 THR F   92    PRO F   93          0       -11.08                     
CISPEP   4 THR G   92    PRO G   93          0       -10.12                     
CISPEP   5 THR H   92    PRO H   93          0       -11.82                     
SITE     1 AC1 14 GLU D  51  GLN D  56  HIS D  57  ILE D  58                    
SITE     2 AC1 14 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     3 AC1 14 HOH D 179  HOH D 231  GLY E  33  LYS E  34                    
SITE     4 AC1 14 ASP H  59  HOH H 221                                          
SITE     1 AC2 15 GLU E  11  TYR E  12  GLU E  51  GLN E  56                    
SITE     2 AC2 15 HIS E  57  ILE E  58  GLN E  61  TRP E  88                    
SITE     3 AC2 15 ASN E  90  LYS E  91  HOH E 142  HOH E 147                    
SITE     4 AC2 15 HOH E 155  HOH E 209  GLY F  33                               
SITE     1 AC3 14 GLU F  11  TYR F  12  GLU F  51  GLN F  56                    
SITE     2 AC3 14 HIS F  57  GLN F  61  TRP F  88  ASN F  90                    
SITE     3 AC3 14 LYS F  91  HOH F 160  HOH F 207  HOH F 209                    
SITE     4 AC3 14 GLY G  33  LYS G  34                                          
SITE     1 AC4 17 GLU G  11  TYR G  12  HIS G  13  GLU G  51                    
SITE     2 AC4 17 GLN G  56  HIS G  57  GLN G  61  TRP G  88                    
SITE     3 AC4 17 ASN G  90  LYS G  91  HOH G 109  HOH G 117                    
SITE     4 AC4 17 HOH G 138  HOH G 146  HOH G 236  GLY H  33                    
SITE     5 AC4 17 LYS H  34                                                     
SITE     1 AC5 13 GLY D  33  TYR H  12  GLU H  51  GLN H  56                    
SITE     2 AC5 13 HIS H  57  ILE H  58  GLN H  61  TRP H  88                    
SITE     3 AC5 13 ASN H  90  LYS H  91  HOH H 149  HOH H 222                    
SITE     4 AC5 13 HOH H 232                                                     
CRYST1  102.098   66.064   78.565  90.00 105.74  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      0.009795  0.000000  0.002760        0.00000                         
SCALE2      0.000000  0.015137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013224        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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