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Database: PDB
Entry: 1EEI
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HEADER    TOXIN                                   31-JAN-00   1EEI              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH METANITROPHENYL-              
TITLE    2 ALPHA-D-GALACTOSE                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CHOLERA TOXIN B);                                 
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: RECEPTOR BINDING SITE ON EACH MONOMER                 
COMPND   6 OCCUPIED BY METANITROPHENYL-ALPHA-D-GALACTOSIDE                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 STRAIN: OGAWA 41 (CLASSICAL BIOTYPE);                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOXIN,ENTEROTOXIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.MERRITT,W.G.J.HOL                                                 
REVDAT   4   24-FEB-09 1EEI    1       VERSN                                    
REVDAT   3   01-APR-03 1EEI    1       JRNL                                     
REVDAT   2   07-FEB-01 1EEI    1       JRNL                                     
REVDAT   1   16-FEB-00 1EEI    0                                                
JRNL        AUTH   E.FAN,E.A.MERRITT,Z.ZHANG,J.C.PICKENS,C.ROACH,               
JRNL        AUTH 2 M.AHN,W.G.HOL                                                
JRNL        TITL   EXPLORATION OF THE GM1 RECEPTOR-BINDING SITE OF              
JRNL        TITL 2 HEAT-LABILE ENTEROTOXIN AND CHOLERA TOXIN BY                 
JRNL        TITL 3 PHENYL-RING-CONTAINING GALACTOSE DERIVATIVES.                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   201 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11173465                                                     
JRNL        DOI    10.1107/S0907444900016814                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.A.MERRITT,P.KUHN,S.SARFATY,J.L.ERBE,R.K.HOLMES,            
REMARK   1  AUTH 2 W.G.HOL                                                      
REMARK   1  TITL   THE 1.25 A RESOLUTION REFINEMENT OF THE CHOLERA              
REMARK   1  TITL 2 TOXIN B-PENTAMER: EVIDENCE OF PEPTIDE BACKBONE               
REMARK   1  TITL 3 STRAIN AT THE RECEPTOR-BINDING SITE.                         
REMARK   1  REF    J.MOL.BIOL.                   V. 282  1043 1998              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1998.2076                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.A.MERRITT,S.SARFATY,I.K.FEIL,W.G.J.HOL                     
REMARK   1  TITL   STRUCTURAL FOUNDATION FOR THE DESIGN OF RECEPTOR             
REMARK   1  TITL 2 ANTAGONISTS TARGETING ESCHERICHIA HEAT-LABILE                
REMARK   1  TITL 3 ENTEROTOXIN                                                  
REMARK   1  REF    STRUCTURE                     V.   5  1485 1997              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  DOI    10.1016/S0969-2126(97)00298-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40342                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1982                            
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            : 4070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 105                                     
REMARK   3   SOLVENT ATOMS            : 455                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED 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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.58                            
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 1EEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010495.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : DOUBLE-FOCUS MIRRORS MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40887                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMEN         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3CHB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP, PH 4.0, VAPOR              
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       34.45000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.33000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.77500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.33000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.45000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.77500            
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: 15040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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: 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    ASN D  14       66.44     33.28                                   
REMARK 500    ASN D  21       56.81     39.88                                   
REMARK 500    GLU D  51      156.37    -48.31                                   
REMARK 500    ASN D  90       30.11    -90.85                                   
REMARK 500    LYS E  34       -0.50     68.11                                   
REMARK 500    GLU E  83      -71.14    -74.52                                   
REMARK 500    ARG F  35       34.31   -141.81                                   
REMARK 500    GLN G  16      149.36   -173.03                                   
REMARK 500    GLU G  83      -70.07    -77.17                                   
REMARK 500    PRO H  53      102.68    -56.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 568        DISTANCE =  5.13 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAA D 504                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAA E 505                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAA F 506                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAA G 507                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAA H 508                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CHB   RELATED DB: PDB                                   
REMARK 900 CHOLERA TOXIN B-PENTAMER COMPLEXED WITH RECEPTOR GM1                 
REMARK 900 PENTASACCHARIDE                                                      
REMARK 900 RELATED ID: 1LT6   RELATED DB: PDB                                   
REMARK 900 HEAT-LABILE ENTEROTOXIN B-PENTAMER COMPLEXED WITH                    
REMARK 900 METANITROPHENYL-ALPHA-D-GALACTOSE                                    
REMARK 900 RELATED ID: 1EEF   RELATED DB: PDB                                   
REMARK 900 HEAT-LABILE ENTEROTOXIN B-PENTAMER COMPLEXED WITH BINDING            
REMARK 900 SITE INHIBITOR ZTOI061                                               
DBREF  1EEI D    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1EEI E    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1EEI F    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1EEI G    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1EEI H    1   103  UNP    Q57193   Q57193_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    GAA  D 504      21                                                       
HET    GAA  E 505      21                                                       
HET    GAA  F 506      21                                                       
HET    GAA  G 507      21                                                       
HET    GAA  H 508      21                                                       
HETNAM     GAA METANITROPHENYL-ALPHA-D-GALACTOSIDE                              
FORMUL   6  GAA    5(C12 H15 N O8)                                              
FORMUL  11  HOH   *455(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 ILE E   58  GLU E   79  1                                  22    
HELIX    5   5 ASN F    4  ALA F   10  1                                   7    
HELIX    6   6 ILE F   58  GLU F   79  1                                  22    
HELIX    7   7 ASN G    4  ALA G   10  1                                   7    
HELIX    8   8 ILE G   58  SER G   60  5                                   3    
HELIX    9   9 GLN G   61  GLU G   79  1                                  19    
HELIX   10  10 ASN H    4  ALA H   10  1                                   7    
HELIX   11  11 SER H   60  GLU H   79  1                                  20    
SHEET    1   A39 THR D  15  ASP D  22  0                                        
SHEET    2   A39 VAL D  82  TRP D  88 -1  N  VAL D  82   O  ASP D  22           
SHEET    3   A39 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET    4   A39 SER E  26  SER E  30  1  O  TYR E  27   N  MET D 101           
SHEET    5   A39 MET E  37  THR E  41 -1  O  MET E  37   N  SER E  30           
SHEET    6   A39 THR E  47  VAL E  50 -1  N  PHE E  48   O  ILE E  40           
SHEET    7   A39 HIS E  94  ALA E 102  1  O  HIS E  94   N  GLN E  49           
SHEET    8   A39 VAL E  82  TRP E  88 -1  N  GLU E  83   O  SER E 100           
SHEET    9   A39 THR E  15  ASP E  22 -1  O  GLN E  16   N  VAL E  87           
SHEET   10   A39 VAL E  82  TRP E  88 -1  N  VAL E  82   O  ASP E  22           
SHEET   11   A39 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET   12   A39 SER F  26  SER F  30 -1  N  TYR F  27   O  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  HIS F  94   N  GLN F  49           
SHEET   16   A39 VAL F  82  TRP F  88 -1  N  GLU F  83   O  SER F 100           
SHEET   17   A39 THR F  15  ASP F  22 -1  O  GLN F  16   N  VAL F  87           
SHEET   18   A39 VAL F  82  TRP F  88 -1  N  VAL F  82   O  ASP F  22           
SHEET   19   A39 HIS F  94  ALA F 102 -1  O  ALA F  95   N  TRP F  88           
SHEET   20   A39 SER G  26  SER G  30 -1  O  TYR G  27   N  MET F 101           
SHEET   21   A39 ALA G  38  THR G  41 -1  O  ILE G  39   N  THR G  28           
SHEET   22   A39 THR G  47  VAL G  50 -1  N  PHE G  48   O  ILE G  40           
SHEET   23   A39 HIS G  94  ALA G 102  1  O  HIS G  94   N  GLN G  49           
SHEET   24   A39 VAL G  82  TRP G  88 -1  N  GLU G  83   O  SER G 100           
SHEET   25   A39 THR G  15  ASP G  22 -1  O  GLN G  16   N  VAL G  87           
SHEET   26   A39 VAL G  82  TRP G  88 -1  N  VAL G  82   O  ASP G  22           
SHEET   27   A39 HIS G  94  ALA G 102 -1  O  ALA G  95   N  TRP G  88           
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  MET H  37   N  SER H  30           
SHEET   30   A39 THR H  47  VAL H  50 -1  N  PHE H  48   O  ILE H  40           
SHEET   31   A39 HIS H  94  ALA H 102  1  O  HIS H  94   N  GLN H  49           
SHEET   32   A39 VAL H  82  TRP H  88 -1  N  GLU H  83   O  SER H 100           
SHEET   33   A39 THR H  15  ASP H  22 -1  O  GLN H  16   N  VAL H  87           
SHEET   34   A39 VAL H  82  TRP H  88 -1  N  VAL H  82   O  ASP H  22           
SHEET   35   A39 HIS H  94  ALA H 102 -1  O  ALA H  95   N  TRP H  88           
SHEET   36   A39 SER D  26  SER D  30 -1  N  TYR D  27   O  MET H 101           
SHEET   37   A39 MET D  37  THR D  41 -1  O  MET D  37   N  SER D  30           
SHEET   38   A39 THR D  47  VAL D  50 -1  N  PHE D  48   O  ILE D  40           
SHEET   39   A39 HIS D  94  ALA D 102  1  O  HIS D  94   N  GLN D  49           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.03  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.04  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.01  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.03  
CISPEP   1 THR D   92    PRO D   93          0         0.08                     
CISPEP   2 THR E   92    PRO E   93          0        -0.12                     
CISPEP   3 THR F   92    PRO F   93          0        -0.22                     
CISPEP   4 THR G   92    PRO G   93          0        -0.31                     
CISPEP   5 THR H   92    PRO H   93          0         0.64                     
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 D 520  HOH D 533  GLN E  16  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 E 511  GLY F  33                                          
SITE     1 AC3 13 TYR F  12  GLU F  51  GLN F  56  HIS F  57                    
SITE     2 AC3 13 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC3 13 HOH F 523  HOH F 540  HOH F 552  GLN G  16                    
SITE     4 AC3 13 GLY G  33                                                     
SITE     1 AC4 10 TYR G  12  GLU G  51  GLN G  56  HIS G  57                    
SITE     2 AC4 10 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 AC4 10 HOH G 527  GLY H  33                                          
SITE     1 AC5 11 GLY D  33  TYR H  12  HIS H  13  GLU H  51                    
SITE     2 AC5 11 GLN H  56  GLN H  61  GLU H  79  TRP H  88                    
SITE     3 AC5 11 ASN H  90  LYS H  91  HOH H 552                               
CRYST1   68.900   69.550  130.660  90.00  90.00  90.00 P 21 21 21   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      0.014510  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014380  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007650        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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