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Database: PDB
Entry: 1RDP
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HEADER    TOXIN                                   05-NOV-03   1RDP              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                      
TITLE    2 NITROPHENOL-GALACTOSIDE LIGAND BV3                                   
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 1RDP    1       VERSN                                    
REVDAT   1   26-OCT-04 1RDP    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.    1.35 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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 100384                         
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) : 0.132                           
REMARK   3   R VALUE            (WORKING SET) : 0.130                           
REMARK   3   FREE R VALUE                     : 0.171                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5029                            
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) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4743                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 242                          
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4093                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 494                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.055         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.942         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.979                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4312 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3745 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5840 ; 1.501 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8773 ; 0.867 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   511 ; 6.952 ; 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):   684 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4634 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   762 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   842 ; 0.227 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4684 ; 0.297 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2296 ; 0.085 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   669 ; 0.176 ; 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):    15 ; 0.258 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    29 ; 0.355 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.146 ; 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):  2581 ; 2.658 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4194 ; 3.476 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1731 ; 4.376 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1646 ; 6.083 ; 6.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4312 ; 2.112 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   494 ;21.699 ;15.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4233 ; 6.002 ;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, MAXIMUM LIKELIHOOD                                
REMARK   4                                                                      
REMARK   4 1RDP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020668.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-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) : 0.9791                             
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   : 100384                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
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     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY                : 3.660                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.22                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XTALVIEW                                              
REMARK 200 STARTING MODEL: PDB ENTRY 3CHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 8000, 50 MM NACL, 100 MM         
REMARK 280  TRIS-HCL, 20MM MGCL2, AND 2.3MM BV3, PH 7.5, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 298.0K                                    
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       51.04500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.04500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.03950            
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: 15650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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   O    HOH F  1290     O    HOH F  1389              2.02            
REMARK 500   OG1  THR G     1     O    HOH G  1458              2.05            
REMARK 500   OD1  ASP D    59     O    HOH D  1376              2.05            
REMARK 500   OD2  ASP H    59     O    HOH H  1385              2.08            
REMARK 500   O    HOH D  1174     O    HOH D  1332              2.09            
REMARK 500   O    HOH H  1320     O    HOH H  1414              2.18            
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    ASP D  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP F  59   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG H  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS D  34       -0.26     70.97                                   
REMARK 500    GLU F  83      -70.86    -77.85                                   
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     BV3 D  104                                                       
REMARK 610     BV3 E  105                                                       
REMARK 610     BV3 F  106                                                       
REMARK 610     BV3 G  107                                                       
REMARK 610     BV3 H  108                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV3 D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV3 E 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV3 F 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV3 G 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BV3 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 PGE 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: 1RD9   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                     
REMARK 900 NITROPHENOL-GALACTOSIDE LIGAND BV2                                   
REMARK 900 RELATED ID: 1RF2   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH BIVALENT                     
REMARK 900 NITROPHENOL-GALACTOSIDE LIGAND BV4                                   
DBREF  1RDP D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RDP E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RDP F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RDP G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1RDP 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    BV3  D 104      24                                                       
HET    BV3  E 105      24                                                       
HET    BV3  F 106      24                                                       
HET    BV3  G 107      24                                                       
HET    BV3  H 108      24                                                       
HET    TRS  H 109       8                                                       
HET    PGE  H 110      12                                                       
HETNAM     BV3 1,3-BIS-([[3-(4-{3-[3-NITRO-5-(GALACTOPYRANOSYLOXY)-             
HETNAM   2 BV3  BENZOYLAMINO]-PROPYL}-PIPERAZIN-1-YL)-PROPYLAMINO-3,4-          
HETNAM   3 BV3  DIOXO-CYCLOBUTENYL]-AMINO-ETHYL]-AMINO-CARBONYLOXY)-2-          
HETNAM   4 BV3  AMINO-PROPANE                                                   
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     BV3 BV3                                                              
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   6  BV3    5(C63 H91 N15 O26)                                           
FORMUL  11  TRS    C4 H12 N O3 1+                                               
FORMUL  12  PGE    C6 H14 O4                                                    
FORMUL  13  HOH   *494(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  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    
SHEET    1   A39 THR D  15  ASP D  22  0                                        
SHEET    2   A39 VAL D  82  TRP D  88 -1  O  LEU D  85   N  HIS D  18           
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  HIS E  18   O  LEU E  85           
SHEET   10   A39 VAL E  82  TRP E  88 -1  O  LEU E  85   N  HIS E  18           
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  GLU F  29   N  ILE E  99           
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 LYS F  81  TRP F  88 -1  N  CYS F  86   O  ALA F  97           
SHEET   17   A39 THR F  15  LYS F  23 -1  N  GLN F  16   O  VAL F  87           
SHEET   18   A39 LYS F  81  TRP F  88 -1  O  VAL F  87   N  GLN F  16           
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  GLU H  29   N  ILE G  99           
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  HIS H  18   O  LEU H  85           
SHEET   34   A39 VAL H  82  TRP H  88 -1  O  LEU H  85   N  HIS H  18           
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  2.05  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.04  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.06  
CISPEP   1 THR D   92    PRO D   93          0        -8.18                     
CISPEP   2 THR E   92    PRO E   93          0        -7.90                     
CISPEP   3 THR F   92    PRO F   93          0        -9.84                     
CISPEP   4 THR G   92    PRO G   93          0       -10.75                     
CISPEP   5 THR H   92    PRO H   93          0       -10.86                     
SITE     1 AC1 10 TYR D  12  GLU D  51  GLN D  56  HIS D  57                    
SITE     2 AC1 10 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     3 AC1 10 HOH D1423  GLY E  33                                          
SITE     1 AC2 10 TYR E  12  GLU E  51  GLN E  56  HIS E  57                    
SITE     2 AC2 10 GLN E  61  TRP E  88  ASN E  90  LYS E  91                    
SITE     3 AC2 10 HOH E1419  GLY F  33                                          
SITE     1 AC3 11 TYR F  12  GLU F  51  GLN F  56  HIS F  57                    
SITE     2 AC3 11 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC3 11 HOH F1400  HOH F1404  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 G1395  HOH G1396  HOH G1397  GLY H  33                    
SITE     1 AC5 11 GLY D  33  HOH E1415  TYR H  12  GLU H  51                    
SITE     2 AC5 11 GLN H  56  GLN H  61  TRP H  88  ASN H  90                    
SITE     3 AC5 11 LYS H  91  HOH H1406  HOH H1407                               
SITE     1 AC6 10 ARG D  35  ASN F  14  ASN F  89  ASN F  90                    
SITE     2 AC6 10 THR H   1  PRO H   2  ASP H   7  GLU H  11                    
SITE     3 AC6 10 HOH H1444  HOH H1447                                          
SITE     1 AC7  8 LYS D  91  THR D  92  ASN F  89  ASN F  90                    
SITE     2 AC7  8 LYS F  91  THR F  92  THR H   1  HOH H1284                    
CRYST1  102.090   66.079   78.715  90.00 105.83  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  0.002778        0.00000                         
SCALE2      0.000000  0.015133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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