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Database: PDB
Entry: 1S5D
LinkDB: 1S5D
Original site: 1S5D 
HEADER    TRANSFERASE,TOXIN                       20-JAN-04   1S5D              
TITLE     CHOLERA HOLOTOXIN WITH AN A-SUBUNIT Y30S MUTATION, CRYSTAL FORM 2     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN, A CHAIN;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NAD(+)--DIPHTHAMIDE ADP- RIBOSYLTRANSFERASE, CHOLERA        
COMPND   5 ENTEROTOXIN A SUBUNIT;                                               
COMPND   6 EC: 2.4.2.36;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CHOLERA TOXIN B PROTEIN (CTB);                             
COMPND  11 CHAIN: D, E, F, G, H;                                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CTXA, TOXA, VC1457;                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PEIA154;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE  12 ORGANISM_TAXID: 666;                                                 
SOURCE  13 GENE: CTXB, TOXB, VC1456;                                            
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PEIA154                                   
KEYWDS    CHOLERA TOXIN, HEAT-LABILE ENTEROTOXIN, ADP RIBOSE TRANSFERASES, AB5  
KEYWDS   2 TOXINS, TRANSFERASE,TOXIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.O'NEAL,E.I.AMAYA,M.G.JOBLING,R.K.HOLMES,W.G.HOL                   
REVDAT   3   13-JUL-11 1S5D    1       VERSN                                    
REVDAT   2   24-FEB-09 1S5D    1       VERSN                                    
REVDAT   1   06-APR-04 1S5D    0                                                
JRNL        AUTH   C.J.O'NEAL,E.I.AMAYA,M.G.JOBLING,R.K.HOLMES,W.G.HOL          
JRNL        TITL   CRYSTAL STRUCTURES OF AN INTRINSICALLY ACTIVE CHOLERA TOXIN  
JRNL        TITL 2 MUTANT YIELD INSIGHT INTO THE TOXIN ACTIVATION MECHANISM     
JRNL        REF    BIOCHEMISTRY                  V.  43  3772 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15049684                                                     
JRNL        DOI    10.1021/BI0360152                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 77516                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4074                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4259                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 219                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5693                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 91                                      
REMARK   3   SOLVENT ATOMS            : 603                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.102         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.063         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.973         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5902 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5169 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8000 ; 1.227 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12040 ; 0.708 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   726 ; 6.391 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   914 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6500 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1120 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1104 ; 0.221 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5933 ; 0.263 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3249 ; 0.086 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   915 ; 0.161 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.069 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.083 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.338 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.178 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3653 ; 1.063 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5887 ; 1.755 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2249 ; 1.293 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2112 ; 2.156 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1S5D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021387.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 1.0000                             
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81705                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: CTY30S FORM 3 STRUCTURE (PDB ID 1S5B)                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CITRATE, GALACTOSE,     
REMARK 280  VAPOR 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       30.02750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.32800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.95200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.32800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.02750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.95200            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     ASP A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     THR A    35                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     ASN A   189                                                      
REMARK 465     ALA A   190                                                      
REMARK 465     PRO A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     SER A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     MET A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     ASN A   197                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     LEU A   240                                                      
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     GLN A  18    CD   OE1  NE2                                       
REMARK 470     ARG A  25    NE   CZ   NH1  NH2                                  
REMARK 470     SER A  28    OG                                                  
REMARK 470     GLN A  36    CG   CD   OE1  NE2                                  
REMARK 470     THR A  48    OG1  CG2                                            
REMARK 470     ARG A  67    NE   CZ   NH1  NH2                                  
REMARK 470     LEU A  71    CD1  CD2                                            
REMARK 470     ILE A  76    CD1                                                 
REMARK 470     GLU A 110    CD   OE1  OE2                                       
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 131    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 137    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN A 138    CD   OE1  NE2                                       
REMARK 470     ARG A 141    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 172    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 175    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 202    CD   CE   NZ                                        
REMARK 470     LYS A 209    CD   CE   NZ                                        
REMARK 470     LYS A 217    NZ                                                  
REMARK 470     ASN A 234    CG   OD1                                            
REMARK 470     LYS D  34    CD   CE   NZ                                        
REMARK 470     LYS D  63    CG   CD   CE   NZ                                   
REMARK 470     LYS D  81    CE   NZ                                             
REMARK 470     LYS E  62    CD   CE   NZ                                        
REMARK 470     LYS E  63    CG   CD   CE   NZ                                   
REMARK 470     LYS E  81    NZ                                                  
REMARK 470     ASN E 103    CB   CG   OD1                                       
REMARK 470     HIS F  13    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS F  34    CE   NZ                                             
REMARK 470     LYS F  62    CE   NZ                                             
REMARK 470     LYS F  81    CE   NZ                                             
REMARK 470     LYS G  34    CD   CE   NZ                                        
REMARK 470     LYS G  62    CD   CE   NZ                                        
REMARK 470     ASN G 103    CB   CG   OD1                                       
REMARK 470     LYS H  34    CD   CE   NZ                                        
REMARK 470     LYS H  43    NZ                                                  
REMARK 470     LYS H  63    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA E   102     O    HOH E   792              1.91            
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    ARG A  54      124.25    -38.93                                   
REMARK 500    HIS A  55       23.52   -151.65                                   
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 A 329        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH E 749        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH E 761        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH G 759        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH G 764        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH H 774        DISTANCE =  5.04 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 241  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 289   O                                                      
REMARK 620 2 THR A  90   O   102.0                                              
REMARK 620 3 TYR A 150   O    98.2  92.1                                        
REMARK 620 4 ASN A   1   O    79.9 172.0  95.3                                  
REMARK 620 5 THR A  90   OG1  83.5  76.7 168.8  95.9                            
REMARK 620 6 LEU A 153   O   161.6  94.2  89.8  82.9  91.9                      
REMARK 620 N                    1     2     3     4     5                       
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 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL F 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL G 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL H 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 241                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 242                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XTC   RELATED DB: PDB                                   
REMARK 900 CHOLERA HOLOTOXIN                                                    
REMARK 900 RELATED ID: 1LTS   RELATED DB: PDB                                   
REMARK 900 HEAT-LABILE ENTEROTOXIN                                              
REMARK 900 RELATED ID: 1LTG   RELATED DB: PDB                                   
REMARK 900 HEAT-LABILE ENTEROTOXIN WITH AN A-SUBUNIT R7K MUTATION               
REMARK 900 RELATED ID: 1LTA   RELATED DB: PDB                                   
REMARK 900 HEAT-LABILE ENTEROTOXIN COMPLEXED WITH GALACTOSE                     
DBREF  1S5D A    1   240  UNP    P01555   CHTA_VIBCH      19    258             
DBREF  1S5D D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5D E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5D F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5D G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5D H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1S5D SER A   30  UNP  P01555    TYR    30 ENGINEERED                     
SEQRES   1 A  240  ASN ASP ASP LYS LEU TYR ARG ALA ASP SER ARG PRO PRO          
SEQRES   2 A  240  ASP GLU ILE LYS GLN SER GLY GLY LEU MET PRO ARG GLY          
SEQRES   3 A  240  GLN SER GLU SER PHE ASP ARG GLY THR GLN MET ASN ILE          
SEQRES   4 A  240  ASN LEU TYR ASP HIS ALA ARG GLY THR GLN THR GLY PHE          
SEQRES   5 A  240  VAL ARG HIS ASP ASP GLY TYR VAL SER THR SER ILE SER          
SEQRES   6 A  240  LEU ARG SER ALA HIS LEU VAL GLY GLN THR ILE LEU SER          
SEQRES   7 A  240  GLY HIS SER THR TYR TYR ILE TYR VAL ILE ALA THR ALA          
SEQRES   8 A  240  PRO ASN MET PHE ASN VAL ASN ASP VAL LEU GLY ALA TYR          
SEQRES   9 A  240  SER PRO HIS PRO ASP GLU GLN GLU VAL SER ALA LEU GLY          
SEQRES  10 A  240  GLY ILE PRO TYR SER GLN ILE TYR GLY TRP TYR ARG VAL          
SEQRES  11 A  240  HIS PHE GLY VAL LEU ASP GLU GLN LEU HIS ARG ASN ARG          
SEQRES  12 A  240  GLY TYR ARG ASP ARG TYR TYR SER ASN LEU ASP ILE ALA          
SEQRES  13 A  240  PRO ALA ALA ASP GLY TYR GLY LEU ALA GLY PHE PRO PRO          
SEQRES  14 A  240  GLU HIS ARG ALA TRP ARG GLU GLU PRO TRP ILE HIS HIS          
SEQRES  15 A  240  ALA PRO PRO GLY CYS GLY ASN ALA PRO ARG SER SER MET          
SEQRES  16 A  240  SER ASN THR CYS ASP GLU LYS THR GLN SER LEU GLY VAL          
SEQRES  17 A  240  LYS PHE LEU ASP GLU TYR GLN SER LYS VAL LYS ARG GLN          
SEQRES  18 A  240  ILE PHE SER GLY TYR GLN SER ASP ILE ASP THR HIS ASN          
SEQRES  19 A  240  ARG ILE LYS ASP GLU LEU                                      
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    GAL  D 704      12                                                       
HET    GAL  E 705      12                                                       
HET    GAL  F 706      12                                                       
HET    GAL  G 707      12                                                       
HET    GAL  H 708      12                                                       
HET     NA  A 241       1                                                       
HET    GOL  E 706       6                                                       
HET    GOL  D 705       6                                                       
HET    GOL  F 707       6                                                       
HET    GOL  G 708       6                                                       
HET    GOL  A 242       6                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GAL    5(C6 H12 O6)                                                 
FORMUL  12   NA    NA 1+                                                        
FORMUL  13  GOL    5(C3 H8 O3)                                                  
FORMUL  18  HOH   *603(H2 O)                                                    
HELIX    1   1 PRO A   12  GLY A   20  1                                   9    
HELIX    2   2 PRO A   24  SER A   28  5                                   5    
HELIX    3   3 ASN A   40  GLY A   47  1                                   8    
HELIX    4   4 SER A   65  LEU A   77  1                                  13    
HELIX    5   5 VAL A   97  GLY A  102  1                                   6    
HELIX    6   6 ALA A  103  SER A  105  5                                   3    
HELIX    7   7 HIS A  107  GLN A  111  5                                   5    
HELIX    8   8 ARG A  146  ASN A  152  1                                   7    
HELIX    9   9 PRO A  157  ALA A  165  5                                   9    
HELIX   10  10 HIS A  171  GLU A  176  5                                   6    
HELIX   11  11 PRO A  178  ALA A  183  5                                   6    
HELIX   12  12 THR A  198  GLN A  227  1                                  30    
HELIX   13  13 ASN D    4  ALA D   10  1                                   7    
HELIX   14  14 SER D   60  GLU D   79  1                                  20    
HELIX   15  15 ASN E    4  ALA E   10  1                                   7    
HELIX   16  16 ILE E   58  GLU E   79  1                                  22    
HELIX   17  17 ASN F    4  ALA F   10  1                                   7    
HELIX   18  18 ILE F   58  SER F   60  5                                   3    
HELIX   19  19 GLN F   61  THR F   78  1                                  18    
HELIX   20  20 ASN G    4  ALA G   10  1                                   7    
HELIX   21  21 SER G   60  THR G   78  1                                  19    
HELIX   22  22 ASN H    4  ALA H   10  1                                   7    
HELIX   23  23 ILE H   58  SER H   60  5                                   3    
HELIX   24  24 GLN H   61  GLU H   79  1                                  19    
SHEET    1   A 4 LYS A   4  ASP A   9  0                                        
SHEET    2   A 4 THR A  82  ALA A  89 -1  O  ILE A  88   N  LEU A   5           
SHEET    3   A 4 ILE A 124  HIS A 131 -1  O  VAL A 130   N  TYR A  83           
SHEET    4   A 4 VAL A 134  LEU A 135 -1  O  VAL A 134   N  HIS A 131           
SHEET    1   B 4 LYS A   4  ASP A   9  0                                        
SHEET    2   B 4 THR A  82  ALA A  89 -1  O  ILE A  88   N  LEU A   5           
SHEET    3   B 4 ILE A 124  HIS A 131 -1  O  VAL A 130   N  TYR A  83           
SHEET    4   B 4 HIS A 140  ARG A 141 -1  O  HIS A 140   N  TRP A 127           
SHEET    1   C 2 GLY A  21  LEU A  22  0                                        
SHEET    2   C 2 ILE A 119  PRO A 120 -1  O  ILE A 119   N  LEU A  22           
SHEET    1   D 3 TYR A  59  THR A  62  0                                        
SHEET    2   D 3 VAL A 113  LEU A 116 -1  O  ALA A 115   N  VAL A  60           
SHEET    3   D 3 MET A  94  ASN A  96 -1  N  PHE A  95   O  SER A 114           
SHEET    1   E20 THR H  15  ASP H  22  0                                        
SHEET    2   E20 VAL H  82  TRP H  88 -1  O  LEU H  85   N  HIS H  18           
SHEET    3   E20 HIS H  94  ALA H 102 -1  O  ALA H  97   N  CYS H  86           
SHEET    4   E20 SER D  26  SER D  30 -1  N  TYR D  27   O  MET H 101           
SHEET    5   E20 ALA D  38  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET    6   E20 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    7   E20 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SHEET    8   E20 VAL D  82  TRP D  88 -1  N  CYS D  86   O  ALA D  97           
SHEET    9   E20 THR D  15  ASP D  22 -1  N  ASP D  22   O  VAL D  82           
SHEET   10   E20 VAL D  82  TRP D  88 -1  O  VAL D  82   N  ASP D  22           
SHEET   11   E20 HIS D  94  ALA D 102 -1  O  ALA D  97   N  CYS D  86           
SHEET   12   E20 SER E  26  SER E  30 -1  O  TYR E  27   N  MET D 101           
SHEET   13   E20 ALA E  38  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET   14   E20 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET   15   E20 HIS E  94  ALA E 102  1  O  ILE E  96   N  GLN E  49           
SHEET   16   E20 VAL E  82  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET   17   E20 THR E  15  ASP E  22 -1  N  HIS E  18   O  LEU E  85           
SHEET   18   E20 VAL E  82  TRP E  88 -1  O  LEU E  85   N  HIS E  18           
SHEET   19   E20 HIS E  94  ALA E 102 -1  O  ALA E  97   N  CYS E  86           
SHEET   20   E20 SER F  26  SER F  30 -1  O  TYR F  27   N  MET E 101           
SHEET    1   F16 ALA F  38  THR F  41  0                                        
SHEET    2   F16 THR F  47  VAL F  50 -1  O  PHE F  48   N  ILE F  40           
SHEET    3   F16 HIS F  94  ALA F 102  1  O  ILE F  96   N  GLN F  49           
SHEET    4   F16 VAL F  82  TRP F  88 -1  N  CYS F  86   O  ALA F  97           
SHEET    5   F16 THR F  15  ASP F  22 -1  N  HIS F  18   O  LEU F  85           
SHEET    6   F16 VAL F  82  TRP F  88 -1  O  LEU F  85   N  HIS F  18           
SHEET    7   F16 HIS F  94  ALA F 102 -1  O  ALA F  97   N  CYS F  86           
SHEET    8   F16 SER G  26  SER G  30 -1  O  TYR G  27   N  MET F 101           
SHEET    9   F16 MET G  37  THR G  41 -1  O  ILE G  39   N  THR G  28           
SHEET   10   F16 THR G  47  VAL G  50 -1  O  PHE G  48   N  ILE G  40           
SHEET   11   F16 HIS G  94  ALA G 102  1  O  ILE G  96   N  GLN G  49           
SHEET   12   F16 VAL G  82  TRP G  88 -1  N  CYS G  86   O  ALA G  97           
SHEET   13   F16 THR G  15  ASP G  22 -1  N  HIS G  18   O  LEU G  85           
SHEET   14   F16 VAL G  82  TRP G  88 -1  O  LEU G  85   N  HIS G  18           
SHEET   15   F16 HIS G  94  ALA G 102 -1  O  ALA G  97   N  CYS G  86           
SHEET   16   F16 SER H  26  SER H  30 -1  O  TYR H  27   N  MET G 101           
SHEET    1   G 3 ALA H  38  THR H  41  0                                        
SHEET    2   G 3 THR H  47  VAL H  50 -1  O  PHE H  48   N  ILE H  40           
SHEET    3   G 3 HIS H  94  ALA H 102  1  O  ILE H  96   N  GLN H  49           
SSBOND   1 CYS A  187    CYS A  199                          1555   1555  2.03  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.38  
SSBOND   3 CYS G    9    CYS G   86                          1555   1555  2.86  
SSBOND   4 CYS H    9    CYS H   86                          1555   1555  2.05  
LINK        NA    NA A 241                 O   HOH A 289     1555   1555  2.39  
LINK        NA    NA A 241                 O   THR A  90     1555   1555  2.53  
LINK        NA    NA A 241                 O   TYR A 150     1555   1555  2.38  
LINK        NA    NA A 241                 O   ASN A   1     1555   1555  2.52  
LINK        NA    NA A 241                 OG1 THR A  90     1555   1555  2.47  
LINK        NA    NA A 241                 O   LEU A 153     1555   1555  2.30  
CISPEP   1 GLU A  177    PRO A  178          0         2.83                     
CISPEP   2 THR D   92    PRO D   93          0        -4.41                     
CISPEP   3 THR E   92    PRO E   93          0        -2.24                     
CISPEP   4 ALA E  102    ASN E  103          0        -2.16                     
CISPEP   5 THR F   92    PRO F   93          0        -2.47                     
CISPEP   6 THR G   92    PRO G   93          0        -6.09                     
CISPEP   7 THR H   92    PRO H   93          0        -2.05                     
SITE     1 AC1  9 ASN D  14  GLU D  51  GLN D  56  GLN D  61                    
SITE     2 AC1  9 TRP D  88  ASN D  90  LYS D  91  HOH D 779                    
SITE     3 AC1  9 HOH E 734                                                     
SITE     1 AC2 10 GLU E  51  GLN E  56  HIS E  57  GLN E  61                    
SITE     2 AC2 10 TRP E  88  ASN E  90  LYS E  91  HOH E 787                    
SITE     3 AC2 10 HOH E 798  HOH F 798                                          
SITE     1 AC3  8 GLU F  51  GLN F  56  GLN F  61  TRP F  88                    
SITE     2 AC3  8 ASN F  90  LYS F  91  HOH F 724  HOH F 753                    
SITE     1 AC4  8 GLU G  51  GLN G  56  HIS G  57  GLN G  61                    
SITE     2 AC4  8 TRP G  88  ASN G  90  LYS G  91  HOH G 721                    
SITE     1 AC5  9 GLU H  51  GLN H  56  GLN H  61  TRP H  88                    
SITE     2 AC5  9 ASN H  90  LYS H  91  HOH H 712  HOH H 716                    
SITE     3 AC5  9 HOH H 797                                                     
SITE     1 AC6  5 ASN A   1  THR A  90  TYR A 150  LEU A 153                    
SITE     2 AC6  5 HOH A 289                                                     
SITE     1 AC7  7 LYS A 219  ASN D 103  TYR E  76  LEU E  77                    
SITE     2 AC7  7 GLU E  79  HOH E 723  HOH E 759                               
SITE     1 AC8  6 ALA D  46  THR D  47  PRO D  93  HIS D  94                    
SITE     2 AC8  6 HOH D 746  HOH H 764                                          
SITE     1 AC9  4 ALA F  46  THR F  47  PRO F  93  HIS F  94                    
SITE     1 BC1  5 HIS G  18  ALA G  46  THR G  47  PRO G  93                    
SITE     2 BC1  5 HIS G  94                                                     
SITE     1 BC2 10 ARG A 146  ARG A 148  TYR A 149  GLN A 221                    
SITE     2 BC2 10 HOH A 283  HOH A 346  THR F  78  ALA F  80                    
SITE     3 BC2 10 LEU G  77  GLU G  79                                          
CRYST1   60.055  111.904  124.656  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      0.016651  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008936  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008022        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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