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Database: PDB
Entry: 1CHQ
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HEADER    TOXIN                                   15-FEB-95   1CHQ              
TITLE     SURPRISING LEADS FOR A CHOLERA TOXIN RECEPTOR BINDING ANTAGONIST;     
TITLE    2 CRYSTALLOGRAPHIC STUDIES OF CTB MUTANTS                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B PENTAMER;                                  
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 SYNONYM: CHOLERAGEN;                                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 STRAIN: OGAWA 41 (CLASSICAL);                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOXIN                                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   5   21-JUN-17 1CHQ    1       REMARK                                   
REVDAT   4   12-FEB-14 1CHQ    1       REMARK                                   
REVDAT   3   24-FEB-09 1CHQ    1       VERSN                                    
REVDAT   2   01-APR-03 1CHQ    1       JRNL                                     
REVDAT   1   08-MAR-96 1CHQ    0                                                
JRNL        AUTH   E.A.MERRITT,S.SARFATY,T.T.CHANG,L.M.PALMER,M.G.JOBLING,      
JRNL        AUTH 2 R.K.HOLMES,W.G.HOL                                           
JRNL        TITL   SURPRISING LEADS FOR A CHOLERA TOXIN RECEPTOR-BINDING        
JRNL        TITL 2 ANTAGONIST: CRYSTALLOGRAPHIC STUDIES OF CTB MUTANTS.         
JRNL        REF    STRUCTURE                     V.   3   561 1995              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   8590017                                                      
JRNL        DOI    10.1016/S0969-2126(01)00190-3                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.A.MERRITT,S.SARFATY,F.VAN DEN AKKER,C.L'HOIR,J.A.MARTIAL,  
REMARK   1  AUTH 2 W.G.J.HOL                                                    
REMARK   1  TITL   2.2 ANGSTROMS CRYSTAL STRUCTURE OF CHOLERA TOXIN B5 PENTAMER 
REMARK   1  TITL 2 BOUND TO RECEPTOR GM1 PENTASACCHARIDE                        
REMARK   1  REF    PROTEIN SCI.                  V.   3   166 1994              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.G.JOBLING,R.K.HOLMES                                       
REMARK   1  TITL   ANALYSIS OF STRUCTURE AND FUNCTION OF THE B SUBUNIT OF       
REMARK   1  TITL 2 CHOLERA TOXIN BY THE USE OF SITE-DIRECTED MUTAGENESIS        
REMARK   1  REF    MOL.MICROBIOL.                V.   5  1755 1991              
REMARK   1  REFN                   ISSN 0950-382X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22154                          
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 SET) : 0.208                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4010                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.70                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.810                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDB.                                
REMARK 100 THE DEPOSITION ID IS D_1000172335.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS X1000                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28288                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 2.020                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.4                                   
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       51.30000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.30000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.69500            
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: CHOLERA TOXIN IS AN AB5 HEXAMER.  THE B-PENTAMER OF          
REMARK 300 CHOLERA TOXIN IS RESPONSIBLE FOR RECEPTOR RECOGNITION AND            
REMARK 300 BINDING.                                                             
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: 11890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE FIVE IDENTICAL B SUBUNITS ARE LABELLED AS CHAINS D, E,           
REMARK 400 F, G, AND H CORRESPONDING TO CHAIN IDENTIFIERS USED FOR              
REMARK 400 THE RELATED HEAT-LABILE ENTEROTOXIN (LT) FROM ESCHERICHIA            
REMARK 400 COLI AND FOR THE WILD TYPE CHOLERA TOXIN/RECEPTOR COMPLEX.           
REMARK 400                                                                      
REMARK 400 SUBUNIT    CHAIN           RESIDUES                                  
REMARK 400                                                                      
REMARK 400   B#1        D              1 - 103                                  
REMARK 400   B#2        E              1 - 103                                  
REMARK 400   B#3        F              1 - 103                                  
REMARK 400   B#4        G              1 - 103                                  
REMARK 400   B#5        H              1 - 103                                  
REMARK 400   WATER                     1 - 105                                  
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS D  34    CB   CG   CD   CE   NZ                              
REMARK 470     ASP D  35    CB   CG   OD1  OD2                                  
REMARK 470     LYS E  34    CB   CG   CD   CE   NZ                              
REMARK 470     ASP E  35    CB   CG   OD1  OD2                                  
REMARK 470     LYS F  34    CB   CG   CD   CE   NZ                              
REMARK 470     ASP F  35    CB   CG   OD1  OD2                                  
REMARK 470     LYS G  34    CB   CG   CD   CE   NZ                              
REMARK 470     ASP G  35    CB   CG   OD1  OD2                                  
REMARK 470     LYS H  34    CB   CG   CD   CE   NZ                              
REMARK 470     ASP H  35    CB   CG   OD1  OD2                                  
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      -38.65     71.80                                   
REMARK 500    ASP D  35       41.23   -101.38                                   
REMARK 500    GLU D  36      104.25    -54.37                                   
REMARK 500    PRO D  53       85.02    -55.24                                   
REMARK 500    ILE D  58      161.53    -46.90                                   
REMARK 500    ASN D  90       23.78    -72.80                                   
REMARK 500    ALA E  10       -7.75    -58.78                                   
REMARK 500    LEU E  20      -56.52   -125.39                                   
REMARK 500    LYS E  34        3.67     42.22                                   
REMARK 500    GLU E  36       92.62    -57.11                                   
REMARK 500    SER E  55      -72.97      1.29                                   
REMARK 500    ILE E  58     -117.62    -90.21                                   
REMARK 500    ASP E  59      -61.40   -108.50                                   
REMARK 500    LYS F  34       -8.85     75.62                                   
REMARK 500    GLU F  36       83.42    -69.81                                   
REMARK 500    PRO F  53       71.65    -67.03                                   
REMARK 500    GLN F  56       42.80    -81.01                                   
REMARK 500    ILE F  58     -173.90    -64.04                                   
REMARK 500    GLU F  83      -76.43    -79.34                                   
REMARK 500    LYS G  34       -1.64     69.63                                   
REMARK 500    PRO G  53     -166.21    -58.23                                   
REMARK 500    GLU G  83      -72.64    -83.61                                   
REMARK 500    ASN H  14       37.61     71.22                                   
REMARK 500    GLN H  16      127.37   -170.48                                   
REMARK 500    ALA H  32       80.77    -59.94                                   
REMARK 500    LYS H  34      -12.86     71.50                                   
REMARK 500    GLU H  36       89.76    -67.96                                   
REMARK 500    SER H  55       35.22    -80.27                                   
REMARK 500    GLU H  83      -72.81    -80.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR E  76         0.07    SIDE CHAIN                              
REMARK 500    TYR G  12         0.08    SIDE CHAIN                              
REMARK 500    TYR G  76         0.07    SIDE CHAIN                              
REMARK 500    TYR H  12         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 SOLVENT SITE 60 IS ALMOST CERTAINLY A CHLORIDE ION, AS               
REMARK 600 ESTABLISHED FOR THE ISOMORPHOUS G33D MUTANT (PDB ENTRY               
REMARK 600 1CHP).                                                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 IN THE PENTAMER THE BETA SHEETS FROM ADJACENT MONOMERS               
REMARK 700 COMBINE TO FORM A CONTINUOUS SIX-STRANDED ANTI-PARALLEL              
REMARK 700 SHEET ACROSS EACH MONOMER-MONOMER INTERFACE.                         
DBREF  1CHQ D    1   103  UNP    P01556   CHTB_VIBCH      29    131             
DBREF  1CHQ E    1   103  UNP    P01556   CHTB_VIBCH      29    131             
DBREF  1CHQ F    1   103  UNP    P01556   CHTB_VIBCH      29    131             
DBREF  1CHQ G    1   103  UNP    P01556   CHTB_VIBCH      29    131             
DBREF  1CHQ H    1   103  UNP    P01556   CHTB_VIBCH      29    131             
SEQADV 1CHQ ASP D   35  UNP  P01556    ARG    63 ENGINEERED                     
SEQADV 1CHQ ASP E   35  UNP  P01556    ARG    63 ENGINEERED                     
SEQADV 1CHQ ASP F   35  UNP  P01556    ARG    63 ENGINEERED                     
SEQADV 1CHQ ASP G   35  UNP  P01556    ARG    63 ENGINEERED                     
SEQADV 1CHQ ASP H   35  UNP  P01556    ARG    63 ENGINEERED                     
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 ASP 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 ASP 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 ASP 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 ASP 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 ASP 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              
FORMUL   6  HOH   *105(H2 O)                                                    
HELIX    1 DA1 ILE D    5  CYS D    9  1                                   5    
HELIX    2 DA2 ASP D   59  THR D   78  1                                  20    
HELIX    3 EA1 ILE E    5  CYS E    9  1                                   5    
HELIX    4 EA2 LYS E   62  THR E   78  1                                  17    
HELIX    5 FA1 ILE F    5  CYS F    9  1                                   5    
HELIX    6 FA2 ASP F   59  THR F   78  1                                  20    
HELIX    7 GA1 ILE G    5  CYS G    9  1                                   5    
HELIX    8 HA2 GLN G   61  THR G   78  1                                  18    
HELIX    9 GA1 ILE H    5  CYS H    9  1                                   5    
HELIX   10 HA2 SER H   60  THR H   78  1                                  19    
SHEET    1 BB1 6 THR D  15  ASP D  22  0                                        
SHEET    2 BB1 6 VAL D  82  TRP D  88 -1                                        
SHEET    3 BB1 6 HIS D  94  ALA D 102 -1                                        
SHEET    4 BB1 6 SER E  26  SER E  30 -1                                        
SHEET    5 BB1 6 MET E  37  THR E  41 -1                                        
SHEET    6 BB1 6 THR E  47  VAL E  50 -1                                        
SHEET    1 BB2 6 THR E  15  ASP E  22  0                                        
SHEET    2 BB2 6 VAL E  82  TRP E  88 -1                                        
SHEET    3 BB2 6 HIS E  94  ALA E 102 -1                                        
SHEET    4 BB2 6 SER F  26  SER F  30 -1                                        
SHEET    5 BB2 6 MET F  37  THR F  41 -1                                        
SHEET    6 BB2 6 THR F  47  VAL F  50 -1                                        
SHEET    1 BB3 6 THR F  15  ASP F  22  0                                        
SHEET    2 BB3 6 VAL F  82  TRP F  88 -1                                        
SHEET    3 BB3 6 HIS F  94  ALA F 102 -1                                        
SHEET    4 BB3 6 SER G  26  SER G  30 -1                                        
SHEET    5 BB3 6 MET G  37  THR G  41 -1                                        
SHEET    6 BB3 6 THR G  47  VAL G  50 -1                                        
SHEET    1 BB4 6 THR G  15  ASP G  22  0                                        
SHEET    2 BB4 6 VAL G  82  TRP G  88 -1                                        
SHEET    3 BB4 6 HIS G  94  ALA G 102 -1                                        
SHEET    4 BB4 6 SER H  26  SER H  30 -1                                        
SHEET    5 BB4 6 MET H  37  THR H  41 -1                                        
SHEET    6 BB4 6 THR H  47  VAL H  50 -1                                        
SHEET    1 BB5 6 THR H  15  ASP H  22  0                                        
SHEET    2 BB5 6 VAL H  82  TRP H  88 -1                                        
SHEET    3 BB5 6 HIS H  94  ALA H 102 -1                                        
SHEET    4 BB5 6 SER D  26  SER D  30 -1                                        
SHEET    5 BB5 6 MET D  37  THR D  41 -1                                        
SHEET    6 BB5 6 THR D  47  VAL D  50 -1                                        
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.02  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.03  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.02  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.03  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.03  
CISPEP   1 THR D   92    PRO D   93          0        -0.21                     
CISPEP   2 THR E   92    PRO E   93          0        -0.34                     
CISPEP   3 THR F   92    PRO F   93          0         0.03                     
CISPEP   4 THR G   92    PRO G   93          0        -0.34                     
CISPEP   5 THR H   92    PRO H   93          0        -0.97                     
CRYST1  102.600   67.390   98.810  90.00 131.63  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      0.009747  0.000000  0.008663        0.00000                         
SCALE2      0.000000  0.014839  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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