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Database: PDB
Entry: 1G8Z
LinkDB: 1G8Z
Original site: 1G8Z 
HEADER    TOXIN                                   21-NOV-00   1G8Z              
TITLE     HIS57ALA MUTANT OF CHOLERA TOXIN B-PENATMER                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B PROTEIN;                                   
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 SYNONYM: CTB;                                                        
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 GENE: CTXB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TOXIN                                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.T.AMAN,S.FRASER,E.A.MERRITT,C.RODIGHERIO,M.KENNY                    
REVDAT   3   24-FEB-09 1G8Z    1       VERSN                                    
REVDAT   2   01-APR-03 1G8Z    1       JRNL                                     
REVDAT   1   25-JUL-01 1G8Z    0                                                
JRNL        AUTH   A.T.AMAN,S.FRASER,E.A.MERRITT,C.RODIGHERIO,M.KENNY,          
JRNL        AUTH 2 M.AHN,W.G.HOL,N.A.WILLIAMS,W.I.LENCER,T.R.HIRST              
JRNL        TITL   A MUTANT CHOLERA TOXIN B SUBUNIT THAT BINDS GM1-             
JRNL        TITL 2 GANGLIOSIDE BUT LACKS IMMUNOMODULATORY OR TOXIC              
JRNL        TITL 3 ACTIVITY.                                                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  98  8536 2001              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   11447291                                                     
JRNL        DOI    10.1073/PNAS.161273098                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 34780                          
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 + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.991                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1827                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4045                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 446                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.103         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.551         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.030 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.032 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.003 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.111 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.176 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.246 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.136 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.960 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 14.898; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.962 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.891 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.833 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.288 ; 3.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G8Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012382.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36777                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.0000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, NACL, TRIS HCL,                
REMARK 280  GALACTOSE, PH 8.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       50.68100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.36100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.68100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.36100            
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 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: 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    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    GLN E  16   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    LYS E  34   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    TYR F  27   CB  -  CG  -  CD2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    TYR G  27   CB  -  CG  -  CD2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    TYR G  27   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG G  73   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       -8.26     79.39                                   
REMARK 500    GLU D  83      -73.93    -79.39                                   
REMARK 500    LEU E  20      -59.18   -120.79                                   
REMARK 500    SER F  55      107.44    -56.67                                   
REMARK 500    GLN F  56       72.58     39.30                                   
REMARK 500    LYS H  34       -0.28     72.28                                   
REMARK 500    GLU H  83      -70.84    -78.13                                   
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 F 184        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH D 185        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH D 186        DISTANCE =  5.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 104                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 104                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 104                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CHB   RELATED DB: PDB                                   
REMARK 900 1.25A RESOLUTION STRUCTURE OF HIS94ARG MUTANT OF CHOLERA             
REMARK 900 TOXIN B-PENTAMER                                                     
REMARK 900 RELATED ID: 2CHB   RELATED DB: PDB                                   
REMARK 900 2.0A STRUCTURE OF WILD-TYPE CHOLERA TOXIN B-PENTAMER                 
DBREF  1G8Z D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1G8Z E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1G8Z F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1G8Z G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1G8Z H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1G8Z ALA D   57  UNP  P01556    HIS    78 ENGINEERED                     
SEQADV 1G8Z ALA E   57  UNP  P01556    HIS    78 ENGINEERED                     
SEQADV 1G8Z ALA F   57  UNP  P01556    HIS    78 ENGINEERED                     
SEQADV 1G8Z ALA G   57  UNP  P01556    HIS    78 ENGINEERED                     
SEQADV 1G8Z ALA H   57  UNP  P01556    HIS    78 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 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 ALA 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 ALA 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 ALA 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 ALA 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 ALA 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    GAL  D 104      12                                                       
HET    GAL  F 104      12                                                       
HET    GAL  G 104      12                                                       
HET    GAL  H 104      12                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
FORMUL   6  GAL    4(C6 H12 O6)                                                 
FORMUL  10  HOH   *446(H2 O)                                                    
HELIX    1   1 ASN D    4  GLU D   11  1                                   8    
HELIX    2   2 ILE D   58  GLU D   79  1                                  22    
HELIX    3   3 ASN E    4  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  GLU G   79  1                                  22    
HELIX    9   9 ASN H    4  ALA H   10  1                                   7    
HELIX   10  10 ILE H   58  GLU H   79  1                                  22    
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 THR D  47  VAL D  50  1  O  THR D  47   N  HIS D  94           
SHEET    5   A39 ALA D  38  THR D  41 -1  O  ALA D  38   N  VAL D  50           
SHEET    6   A39 SER D  26  SER D  30 -1  O  SER D  26   N  THR D  41           
SHEET    7   A39 HIS H  94  ALA H 102 -1  O  ILE H  99   N  GLU D  29           
SHEET    8   A39 VAL H  82  TRP H  88 -1  N  GLU H  83   O  SER H 100           
SHEET    9   A39 THR H  15  ASP H  22 -1  O  GLN H  16   N  VAL H  87           
SHEET   10   A39 VAL H  82  TRP H  88 -1  N  VAL H  82   O  ASP H  22           
SHEET   11   A39 HIS H  94  ALA H 102 -1  O  ALA H  95   N  TRP H  88           
SHEET   12   A39 THR H  47  VAL H  50  1  O  THR H  47   N  HIS H  94           
SHEET   13   A39 ALA H  38  THR H  41 -1  O  ALA H  38   N  VAL H  50           
SHEET   14   A39 SER H  26  SER H  30 -1  O  SER H  26   N  THR H  41           
SHEET   15   A39 HIS G  94  ALA G 102 -1  O  ILE G  99   N  GLU H  29           
SHEET   16   A39 VAL G  82  TRP G  88 -1  N  GLU G  83   O  SER G 100           
SHEET   17   A39 THR G  15  ASP G  22 -1  O  GLN G  16   N  VAL G  87           
SHEET   18   A39 VAL G  82  TRP G  88 -1  N  VAL G  82   O  ASP G  22           
SHEET   19   A39 HIS G  94  ALA G 102 -1  O  ALA G  95   N  TRP G  88           
SHEET   20   A39 THR G  47  VAL G  50  1  O  THR G  47   N  HIS G  94           
SHEET   21   A39 MET G  37  THR G  41 -1  O  ALA G  38   N  VAL G  50           
SHEET   22   A39 SER G  26  SER G  30 -1  O  SER G  26   N  THR G  41           
SHEET   23   A39 HIS F  94  ALA F 102 -1  O  ILE F  99   N  GLU G  29           
SHEET   24   A39 VAL F  82  TRP F  88 -1  N  GLU F  83   O  SER F 100           
SHEET   25   A39 THR F  15  ASP F  22 -1  O  GLN F  16   N  VAL F  87           
SHEET   26   A39 VAL F  82  TRP F  88 -1  N  VAL F  82   O  ASP F  22           
SHEET   27   A39 HIS F  94  ALA F 102 -1  O  ALA F  95   N  TRP F  88           
SHEET   28   A39 THR F  47  VAL F  50  1  O  THR F  47   N  HIS F  94           
SHEET   29   A39 MET F  37  THR F  41 -1  O  ALA F  38   N  VAL F  50           
SHEET   30   A39 SER F  26  SER F  30 -1  O  SER F  26   N  THR F  41           
SHEET   31   A39 HIS E  94  ALA E 102  1  N  ILE E  99   O  GLU F  29           
SHEET   32   A39 LYS E  81  TRP E  88 -1  O  LYS E  81   N  ALA E 102           
SHEET   33   A39 THR E  15  LYS E  23 -1  O  GLN E  16   N  VAL E  87           
SHEET   34   A39 LYS E  81  TRP E  88 -1  N  VAL E  82   O  ASP E  22           
SHEET   35   A39 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET   36   A39 THR E  47  VAL E  50  1  O  THR E  47   N  HIS E  94           
SHEET   37   A39 ALA E  38  THR E  41 -1  O  ALA E  38   N  VAL E  50           
SHEET   38   A39 SER E  26  SER E  30 -1  O  SER E  26   N  THR E  41           
SHEET   39   A39 HIS D  94  ALA D 102 -1  N  ILE D  99   O  GLU E  29           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.09  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.10  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.09  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.08  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.12  
CISPEP   1 THR D   92    PRO D   93          0        -0.44                     
CISPEP   2 THR E   92    PRO E   93          0        -4.10                     
CISPEP   3 THR F   92    PRO F   93          0        -5.61                     
CISPEP   4 THR G   92    PRO G   93          0         0.64                     
CISPEP   5 THR H   92    PRO H   93          0        -0.98                     
SITE     1 AC1  8 GLU D  51  GLN D  61  TRP D  88  ASN D  90                    
SITE     2 AC1  8 LYS D  91  HOH D 140  HOH D 169  HOH D 178                    
SITE     1 AC2  9 GLU F  51  GLN F  61  TRP F  88  ASN F  90                    
SITE     2 AC2  9 LYS F  91  HOH F 157  HOH F 171  HOH G 155                    
SITE     3 AC2  9 ALA H  10                                                     
SITE     1 AC3 10 THR D   1  GLN E  49  GLU E  51  HOH E 150                    
SITE     2 AC3 10 GLU G  51  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 AC3 10 HOH G 176  HOH G 185                                          
SITE     1 AC4  8 GLU H  51  GLN H  61  TRP H  88  ASN H  90                    
SITE     2 AC4  8 LYS H  91  HOH H 146  HOH H 157  HOH H 173                    
CRYST1  101.362  114.722   45.591  90.00  90.00  90.00 P 21 21 2    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      0.009866  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021934        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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