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Database: PDB
Entry: 1MD2
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Original site: 1MD2 
HEADER    TOXIN                                   06-AUG-02   1MD2              
TITLE     CHOLERA TOXIN B-PENTAMER WITH DECAVALENT LIGAND BMSC-0013             
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    MULTIVALENT INHIBITOR TOXIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ZHANG,E.A.MERRITT,M.AHN,C.ROACH,W.G.J.HOL,E.FAN                     
REVDAT   2   24-FEB-09 1MD2    1       VERSN                                    
REVDAT   1   11-DEC-02 1MD2    0                                                
JRNL        AUTH   Z.ZHANG,E.A.MERRITT,M.AHN,C.ROACH,Z.HOU,                     
JRNL        AUTH 2 C.L.VERLINDE,W.G.HOL,E.FAN                                   
JRNL        TITL   SOLUTION AND CRYSTALLOGRAPHIC STUDIES OF BRANCHED            
JRNL        TITL 2 MULTIVALENT LIGANDS THAT INHIBIT THE                         
JRNL        TITL 3 RECEPTOR-BINDING OF CHOLERA TOXIN.                           
JRNL        REF    J.AM.CHEM.SOC.                V. 124 12991 2002              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   12405825                                                     
JRNL        DOI    10.1021/JA027584K                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 77338                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.125                           
REMARK   3   FREE R VALUE                     : 0.164                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4085                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4100                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 193                                     
REMARK   3   SOLVENT ATOMS            : 674                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.074         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.063         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.035 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MD2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016825.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-00                          
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-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84651                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 32.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS TO 3CHB          
REMARK 200 SOFTWARE USED: ISOMORPHOUS WITH 3CHB                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3CHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, PH 7.5, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE RTK                                       
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       51.06200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.08800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.06200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.08800            
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 300 REMARK: THE CRYSTALLIZED COMPLEX CONTAINS TWO CTB PENTAMERS          
REMARK 300 SANDWICHING A SINGLE DECAVALENT LIGAND. THIS SANDWICH SPANS 2        
REMARK 300 ASYMMETRIC UNITS.                                                    
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 C    CYN F1208  LIES ON A SPECIAL POSITION.                          
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   C    CYN F  1208     C17  233 F  1207              1.51            
REMARK 500   O    HOH D  2287     O    HOH D  2289              1.61            
REMARK 500   O    HOH D  2320     O    HOH H   235              2.04            
REMARK 500   SG   CSS D     9     SG   CYS D    86              2.04            
REMARK 500   SG   CSS G     9     SG   CYS G    86              2.05            
REMARK 500   SG   CSS F     9     SG   CYS F    86              2.06            
REMARK 500   SG   CSS H     9     SG   CYS H    86              2.07            
REMARK 500   SG   CSS E     9     SG   CYS E    86              2.08            
REMARK 500   N    THR G     1     O    HOH G   219              2.19            
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   OG   SER F    55     OG   SER F    55     2555     1.89            
REMARK 500   O    HOH D  2310     O    HOH G   215     3445     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU H  83   CD    GLU H  83   OE1    -0.080                       
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    THR D   1   N   -  CA  -  CB  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASP D   7   CB  -  CG  -  OD1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    HIS D  18   CE1 -  NE2 -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D  22   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    PHE D  48   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG D  73   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG D  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    HIS D  94   CE1 -  NE2 -  CD2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASN D 103   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PHE E  48   CB  -  CG  -  CD1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    THR F   1   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    GLU F  11   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    HIS F  18   CE1 -  NE2 -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP G   7   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    HIS G  18   CE1 -  NE2 -  CD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    PHE G  42   CB  -  CG  -  CD1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG G  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TYR G  76   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR G  76   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    TYR H  27   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG H  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 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 E  34       -1.54     76.58                                   
REMARK 500    GLU E  83      -72.00    -78.87                                   
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 G 128        DISTANCE =  9.37 ANGSTROMS                       
REMARK 525    HOH G 164        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH E1308        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH F1317        DISTANCE =  8.25 ANGSTROMS                       
REMARK 525    HOH H 224        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E1323        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH D2326        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH H 246        DISTANCE =  5.43 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 LIGAND 233 (BMSC-0013) IS A DECAVALENT LIGAND                        
REMARK 600 CONSISTING OF A PENTACYCLEN CORE TO WHICH ARE                        
REMARK 600 ATTACHED FIVE LONG ARMS, EACH CONTAINING FOUR                        
REMARK 600 'LINKER' MOIETIES FOLLOWED BY A SQUARIC ACID                         
REMARK 600 MOIETY AND THEN BRANCHING TO PRESENT TWO MONOVALENT                  
REMARK 600 LIGANDS DERIVED FROM BETA-D-GALACTOSE. A SINGLE COPY                 
REMARK 600 OF THE DECAVALENT LIGAND LIES ON A 2-FOLD AND                        
REMARK 600 STRADDLES TWO CRYSTALLOGRAPHIC ASYMMETRIC UNITS.                     
REMARK 600 THE CENTRAL CORE AND LINKER GROUPS DO NOT SATISFY                    
REMARK 600 CRYSTALLOGRAPHIC SYMMETRY AND ARE NOT VISIBLE IN                     
REMARK 600 THE STRUCTURE AND HENCE NOT PRESENT IN THIS MODEL.                   
REMARK 600 THE SULFUR ATOM BELONGS TO AN UNKNOWN SPECIES                        
REMARK 600 (RESIDUE 109, CHAINS D-H) CONSTITUTING A PARTIAL-                    
REMARK 600 OCCUPANCY IMPROPERLY FORMED CYSTEINE DISULFIDE BETWEEN               
REMARK 600 RESIDUES 9 AND 86.  THAT IS, ~80% OF THE TIME THERE IS A             
REMARK 600 9-86 DISULFIDE AND ~20% OF THE TIME THERE IS A 9-???                 
REMARK 600 DISULFIDE.                                                           
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED                                
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED                                
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN F 1208                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 233 D 2201                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 233 D 2203                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQ D 2202                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 233 E 1204                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 233 E 1206                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQ E 1205                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 233 F 1207                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CHB   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN PENTAMER WITH RECEPTOR GM1 OLIGOSACCHARIDE             
REMARK 900 RELATED ID: 1LLR   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN PENTAMER WITH PENTAVALENT LIGAND BMSC-0012             
DBREF  1MD2 D    1   103  GB     48890    X58785          22    124             
DBREF  1MD2 E    1   103  GB     48890    X58785          22    124             
DBREF  1MD2 F    1   103  GB     48890    X58785          22    124             
DBREF  1MD2 G    1   103  GB     48890    X58785          22    124             
DBREF  1MD2 H    1   103  GB     48890    X58785          22    124             
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CSS 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 CSS 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 CSS 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 CSS 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 CSS 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              
MODRES 1MD2 CSS D    9  CYS  S-MERCAPTOCYSTEINE                                 
MODRES 1MD2 CSS E    9  CYS  S-MERCAPTOCYSTEINE                                 
MODRES 1MD2 CSS F    9  CYS  S-MERCAPTOCYSTEINE                                 
MODRES 1MD2 CSS G    9  CYS  S-MERCAPTOCYSTEINE                                 
MODRES 1MD2 CSS H    9  CYS  S-MERCAPTOCYSTEINE                                 
HET    CSS  D   9       8                                                       
HET    CSS  E   9       8                                                       
HET    CSS  F   9       8                                                       
HET    CSS  G   9       8                                                       
HET    CSS  H   9       8                                                       
HET    CYN  F1208       2                                                       
HET    233  D2201      48                                                       
HET    233  D2203      48                                                       
HET     SQ  D2202      12                                                       
HET    233  E1204      24                                                       
HET    233  E1206      24                                                       
HET     SQ  E1205      11                                                       
HET    233  F1207      24                                                       
HETNAM     CSS S-MERCAPTOCYSTEINE                                               
HETNAM     CYN CYANIDE ION                                                      
HETNAM     233 [5-(3,4,5-TRIHYDROXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-           
HETNAM   2 233  2-YLCARBAMOYL)-PENTYL]-CARBAMIC ACID METHYL ESTER               
HETNAM      SQ 3-ETHYLAMINO-4-METHYLAMINO-CYCLOBUTANE-1,2-DIONE                 
HETSYN     233 BMSC-0013                                                        
HETSYN      SQ SQUARIC ACID                                                     
FORMUL   1  CSS    5(C3 H7 N O2 S2)                                             
FORMUL   6  CYN    C N 1-                                                       
FORMUL   7  233    5(C14 H26 N2 O8)                                             
FORMUL   9   SQ    2(C7 H12 N2 O2)                                              
FORMUL  14  HOH   *674(H2 O)                                                    
HELIX    1   1 ASN D    4  GLU D   11  1                                   8    
HELIX    2   2 ILE D   58  GLU D   79  1                                  22    
HELIX    3   3 ASN E    4  GLU E   11  1                                   8    
HELIX    4   4 SER E   60  GLU E   79  1                                  20    
HELIX    5   5 ASN F    4  ALA F   10  1                                   7    
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    
LINK         C5 A SQ D2202                 C17A233 D2203     1555   1555  1.52  
LINK         C17A233 D2201                 C5 A SQ D2202     1555   1555  1.52  
LINK         C17B233 D2201                 C5 B SQ D2202     1555   1555  1.53  
LINK         C5 B SQ D2202                 C17B233 D2203     1555   1555  1.53  
LINK         C5   SQ E1205                 C17 233 E1206     1555   1555  1.63  
LINK         C17 233 E1204                 C5   SQ E1205     1555   1555  1.64  
LINK         C   LEU D   8                 N   CSS D   9     1555   1555  1.32  
LINK         C   CSS D   9                 N   ALA D  10     1555   1555  1.33  
LINK         C   LEU E   8                 N   CSS E   9     1555   1555  1.34  
LINK         C   CSS E   9                 N   ALA E  10     1555   1555  1.35  
LINK         C   LEU F   8                 N   CSS F   9     1555   1555  1.34  
LINK         C   CSS F   9                 N   ALA F  10     1555   1555  1.33  
LINK         C   LEU G   8                 N   CSS G   9     1555   1555  1.33  
LINK         C   CSS G   9                 N   ALA G  10     1555   1555  1.31  
LINK         C   LEU H   8                 N   CSS H   9     1555   1555  1.33  
LINK         C   CSS H   9                 N   ALA H  10     1555   1555  1.34  
CISPEP   1 THR D   92    PRO D   93          0       -12.15                     
CISPEP   2 THR E   92    PRO E   93          0        -5.95                     
CISPEP   3 THR F   92    PRO F   93          0        -9.49                     
CISPEP   4 THR G   92    PRO G   93          0        -8.86                     
CISPEP   5 THR H   92    PRO H   93          0        -8.64                     
SITE     1 AC1  1 233 F1207                                                     
SITE     1 AC2 19 HIS D  13  GLU D  51  GLN D  56  HIS D  57                    
SITE     2 AC2 19 ILE D  58  GLN D  61  TRP D  88  ASN D  90                    
SITE     3 AC2 19 LYS D  91   SQ D2202  233 D2203  HOH D2244                    
SITE     4 AC2 19 HOH D2260  HOH D2319  HOH D2345  HOH D2349                    
SITE     5 AC2 19 HOH E1227  ILE H  58  ASP H  59                               
SITE     1 AC3 19 233 D2201   SQ D2202  HOH D2224  HOH D2321                    
SITE     2 AC3 19 GLN E  16  GLU H  51  SER H  55  GLN H  56                    
SITE     3 AC3 19 HIS H  57  ILE H  58  GLN H  61  TRP H  88                    
SITE     4 AC3 19 ASN H  90  LYS H  91  HOH H 127  HOH H 133                    
SITE     5 AC3 19 HOH H 134  HOH H 173  HOH H 250                               
SITE     1 AC4  4 233 D2201  233 D2203  GLN E  16  HIS E  18                    
SITE     1 AC5 15 GLU E  51  GLN E  56  HIS E  57  GLN E  61                    
SITE     2 AC5 15 TRP E  88  ASN E  90  LYS E  91   SQ E1205                    
SITE     3 AC5 15 233 E1206  HOH E1245  HOH E1280  HOH E1287                    
SITE     4 AC5 15 HOH E1311  HOH F1225  SER G  55                               
SITE     1 AC6 19 233 E1204   SQ E1205  GLU G  51  SER G  55                    
SITE     2 AC6 19 GLN G  56  HIS G  57  ILE G  58  GLN G  61                    
SITE     3 AC6 19 TRP G  88  ASN G  90  LYS G  91  HOH G 115                    
SITE     4 AC6 19 HOH G 129  HOH G 132  HOH G 139  HOH G 182                    
SITE     5 AC6 19 HOH G 220  HOH G 239  HOH H 128                               
SITE     1 AC7  8 233 E1204  233 E1206  HOH E1253  HOH E1311                    
SITE     2 AC7  8 GLY G  54  SER G  55  HIS G  57  LYS G  62                    
SITE     1 AC8 13 GLU F  51  SER F  55  GLN F  56  HIS F  57                    
SITE     2 AC8 13 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC8 13 CYN F1208  HOH F1228  HOH F1237  HOH F1321                    
SITE     4 AC8 13 HOH F1332                                                     
CRYST1  102.124   66.176   78.221  90.00 106.33  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      0.009792  0.000000  0.002869        0.00000                         
SCALE2      0.000000  0.015111  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013322        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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