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Database: PDB
Entry: 1RD9
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Original site: 1RD9 
HEADER    TOXIN                                   05-NOV-03   1RD9              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                      
TITLE    2 NITROPHENOL-GALACTOSIDE LIGAND BV2                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B PROTEIN (CTB);                             
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;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD                                      
KEYWDS    BIVALENT, CHOLERA, TOXIN, PENTAMER, COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.PICKENS,D.D.MITCHELL,J.LIU,X.TAN,Z.ZHANG,C.L.VERLINDE,            
AUTHOR   2 W.G.HOL,E.FAN                                                        
REVDAT   2   24-FEB-09 1RD9    1       VERSN                                    
REVDAT   1   26-OCT-04 1RD9    0                                                
JRNL        AUTH   J.C.PICKENS,D.D.MITCHELL,J.LIU,X.TAN,Z.ZHANG,                
JRNL        AUTH 2 C.L.VERLINDE,W.G.HOL,E.FAN                                   
JRNL        TITL   NONSPANNING BIVALENT LIGANDS AS IMPROVED SURFACE             
JRNL        TITL 2 RECEPTOR BINDING INHIBITORS OF THE CHOLERA TOXIN B           
JRNL        TITL 3 PENTAMER.                                                    
JRNL        REF    CHEM.BIOL.                    V.  11  1205 2004              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   15380181                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2004.06.008                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 77876                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.134                           
REMARK   3   R VALUE            (WORKING SET) : 0.131                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4090                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.44                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.48                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4271                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 230                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4079                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 163                                     
REMARK   3   SOLVENT ATOMS            : 491                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.073         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.217         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.979                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4322 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3722 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5849 ; 1.464 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8723 ; 0.880 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   511 ; 6.976 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   683 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4630 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   760 ; 0.010 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   817 ; 0.225 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4861 ; 0.335 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2270 ; 0.085 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   638 ; 0.164 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.309 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    34 ; 0.290 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.107 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2580 ; 3.455 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4186 ; 4.444 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1742 ; 5.667 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1663 ; 7.499 ; 8.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4322 ; 2.480 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   491 ;19.220 ;15.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4242 ; 7.200 ;15.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1RD9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020665.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-03                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81971                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440                              
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     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: XTALVIEW                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 38% PEG 300, 50 MM NACL, 100 MM          
REMARK 280  TRIS-HCL, AND 2.3MM BV2, PH 7.5, VAPOR DIFFUSION, SITTING           
REMARK 280  DROP, TEMPERATURE 298K                                              
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       50.99150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.99150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.03600            
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: 16110 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 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 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   OG1  THR D     1     O    HOH D  1441              2.07            
REMARK 500   O    HOH G  1282     O    HOH G  1413              2.12            
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    GLU D  83      -70.70    -75.47                                   
REMARK 500    ASN G  21       55.67     38.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BV2 D  104                                                       
REMARK 610     BV2 E  105                                                       
REMARK 610     BV2 F  106                                                       
REMARK 610     BV2 G  107                                                       
REMARK 610     BV2 H  108                                                       
REMARK 610     P6G H  110                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV2 D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV2 E 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV2 F 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV2 G 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV2 H 108                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS H 109                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G H 110                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RCV   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                     
REMARK 900 NITROPHENOL-GALACTOSIDE LIGAND BV1                                   
REMARK 900 RELATED ID: 1RDP   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                     
REMARK 900 NITROPHENOL-GALACTOSIDE LIGAND BV3                                   
REMARK 900 RELATED ID: 1RF2   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                     
REMARK 900 NITROPHENOL-GALACTOSIDE LIGAND BV4                                   
DBREF  1RD9 D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RD9 E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RD9 F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RD9 G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RD9 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    BV2  D 104      24                                                       
HET    BV2  E 105      37                                                       
HET    BV2  F 106      24                                                       
HET    BV2  G 107      24                                                       
HET    BV2  H 108      37                                                       
HET    TRS  H 109       8                                                       
HET    P6G  H 110       9                                                       
HETNAM     BV2 1,3-BIS-([3-(4-{3-[3-NITRO-5-(GALACTOPYRANOSYLOXY)-              
HETNAM   2 BV2  BENZOYLAMINO]-PROPYL}-PIPERAZIN-1-YL)-PROPYL-AMINO]-            
HETNAM   3 BV2  CARBONYLOXY)-2-AMINO-PROPANE                                    
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     BV2 BV2                                                              
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   6  BV2    5(C51 H79 N11 O22)                                           
FORMUL  11  TRS    C4 H12 N O3 1+                                               
FORMUL  12  P6G    C12 H26 O7                                                   
FORMUL  13  HOH   *491(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  ALA H   10  1                                   7    
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  O  VAL D  87   N  GLN D  16           
SHEET    3   A39 HIS D  94  ALA D 102 -1  O  ALA D  97   N  CYS D  86           
SHEET    4   A39 SER E  26  SER E  30 -1  O  GLU E  29   N  ILE D  99           
SHEET    5   A39 ALA E  38  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET    6   A39 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET    7   A39 HIS E  94  ALA E 102  1  O  ILE E  96   N  GLN E  49           
SHEET    8   A39 VAL E  82  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET    9   A39 THR E  15  ASP E  22 -1  N  GLN E  16   O  VAL E  87           
SHEET   10   A39 VAL E  82  TRP E  88 -1  O  VAL E  87   N  GLN E  16           
SHEET   11   A39 HIS E  94  ALA E 102 -1  O  ALA E  97   N  CYS E  86           
SHEET   12   A39 SER F  26  SER F  30 -1  O  TYR F  27   N  MET E 101           
SHEET   13   A39 ALA F  38  THR F  41 -1  O  ILE F  39   N  THR F  28           
SHEET   14   A39 THR F  47  VAL F  50 -1  O  PHE F  48   N  ILE F  40           
SHEET   15   A39 HIS F  94  ALA F 102  1  O  ILE F  96   N  GLN F  49           
SHEET   16   A39 VAL F  82  TRP F  88 -1  N  CYS F  86   O  ALA F  97           
SHEET   17   A39 THR F  15  ASP F  22 -1  N  ASP F  22   O  VAL F  82           
SHEET   18   A39 VAL F  82  TRP F  88 -1  O  VAL F  82   N  ASP F  22           
SHEET   19   A39 HIS F  94  ALA F 102 -1  O  ALA F  97   N  CYS F  86           
SHEET   20   A39 SER G  26  SER G  30 -1  O  TYR G  27   N  MET F 101           
SHEET   21   A39 MET G  37  THR G  41 -1  O  ILE G  39   N  THR G  28           
SHEET   22   A39 THR G  47  VAL G  50 -1  O  PHE G  48   N  ILE G  40           
SHEET   23   A39 HIS G  94  ALA G 102  1  O  ILE G  96   N  GLN G  49           
SHEET   24   A39 VAL G  82  TRP G  88 -1  N  CYS G  86   O  ALA G  97           
SHEET   25   A39 THR G  15  ASP G  22 -1  N  HIS G  18   O  LEU G  85           
SHEET   26   A39 VAL G  82  TRP G  88 -1  O  LEU G  85   N  HIS G  18           
SHEET   27   A39 HIS G  94  ALA G 102 -1  O  ALA G  97   N  CYS G  86           
SHEET   28   A39 SER H  26  SER H  30 -1  O  TYR H  27   N  MET G 101           
SHEET   29   A39 MET H  37  THR H  41 -1  O  ILE H  39   N  THR H  28           
SHEET   30   A39 THR H  47  VAL H  50 -1  O  PHE H  48   N  ILE H  40           
SHEET   31   A39 HIS H  94  ALA H 102  1  O  ILE H  96   N  GLN H  49           
SHEET   32   A39 VAL H  82  TRP H  88 -1  N  CYS H  86   O  ALA H  97           
SHEET   33   A39 THR H  15  ASP H  22 -1  N  GLN H  16   O  VAL H  87           
SHEET   34   A39 VAL H  82  TRP H  88 -1  O  VAL H  87   N  GLN H  16           
SHEET   35   A39 HIS H  94  ALA H 102 -1  O  ALA H  97   N  CYS H  86           
SHEET   36   A39 SER D  26  SER D  30 -1  N  TYR D  27   O  MET H 101           
SHEET   37   A39 ALA D  38  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET   38   A39 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET   39   A39 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.06  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.04  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.04  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.08  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.07  
CISPEP   1 THR D   92    PRO D   93          0       -10.96                     
CISPEP   2 THR E   92    PRO E   93          0        -9.06                     
CISPEP   3 THR F   92    PRO F   93          0        -8.80                     
CISPEP   4 THR G   92    PRO G   93          0        -9.55                     
CISPEP   5 THR H   92    PRO H   93          0        -9.82                     
SITE     1 AC1 12 TYR D  12  GLU D  51  GLN D  56  HIS D  57                    
SITE     2 AC1 12 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     3 AC1 12 HOH D1198  HOH D1386  GLY E  33  HOH H1334                    
SITE     1 AC2 13 GLU E  11  TYR E  12  GLU E  51  GLN E  56                    
SITE     2 AC2 13 HIS E  57  GLN E  61  TRP E  88  ASN E  90                    
SITE     3 AC2 13 LYS E  91  HOH E1151  HOH E1488  GLY F  33                    
SITE     4 AC2 13 ARG F  35                                                     
SITE     1 AC3 10 TYR F  12  GLU F  51  GLN F  56  HIS F  57                    
SITE     2 AC3 10 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC3 10 HOH F1479  GLY G  33                                          
SITE     1 AC4 12 TYR G  12  GLU G  51  GLN G  56  HIS G  57                    
SITE     2 AC4 12 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 AC4 12 HOH G1004  HOH G1333  HOH G1476  GLY H  33                    
SITE     1 AC5 15 GLY D  33  LYS D  34  GLU H  11  TYR H  12                    
SITE     2 AC5 15 GLU H  51  GLN H  56  HIS H  57  GLN H  61                    
SITE     3 AC5 15 TRP H  88  ASN H  90  LYS H  91  HOH H1029                    
SITE     4 AC5 15 HOH H1269  HOH H1285  HOH H1490                               
SITE     1 AC6  8 ARG D  35  ASN F  14  ASN F  89  ASN F  90                    
SITE     2 AC6  8 THR H   1  PRO H   2  GLU H  11  HOH H1483                    
SITE     1 AC7  5 LYS D  91  THR D  92  THR H   1  HOH H1471                    
SITE     2 AC7  5 HOH H1491                                                     
CRYST1  101.983   66.072   77.818  90.00 105.84  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      0.009806  0.000000  0.002782        0.00000                         
SCALE2      0.000000  0.015135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013358        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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