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Database: PDB
Entry: 1S5B
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Original site: 1S5B 
HEADER    TRANSFERASE,TOXIN                       20-JAN-04   1S5B              
TITLE     CHOLERA HOLOTOXIN WITH AN A-SUBUNIT Y30S MUTATION FORM 3              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN, A CHAIN PRECURSOR;                    
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 1S5B    1       VERSN                                    
REVDAT   2   24-FEB-09 1S5B    1       VERSN                                    
REVDAT   1   06-APR-04 1S5B    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.    2.13 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 43956                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2340                            
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) : 2.13                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.19                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3043                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 160                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5647                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 404                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.06000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.214         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.175         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5771 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5064 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7824 ; 1.282 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11807 ; 0.704 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   713 ; 6.546 ; 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):   877 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6428 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1115 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1211 ; 0.213 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5988 ; 0.263 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3320 ; 0.090 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   649 ; 0.205 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.133 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.194 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    30 ; 0.303 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.273 ; 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):  3598 ; 0.887 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5796 ; 1.436 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2173 ; 0.910 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2028 ; 1.432 ; 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  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    25                          
REMARK   3    RESIDUE RANGE :   A    37        A    46                          
REMARK   3    RESIDUE RANGE :   A    53        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2030 -54.6980  55.3960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1762 T22:   0.0959                                     
REMARK   3      T33:   0.3296 T12:   0.0353                                     
REMARK   3      T13:   0.0809 T23:   0.1181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2715 L22:   1.6371                                     
REMARK   3      L33:   2.9628 L12:  -0.1587                                     
REMARK   3      L13:   0.0665 L23:   0.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0203 S12:  -0.3180 S13:  -0.6007                       
REMARK   3      S21:   0.0774 S22:  -0.0507 S23:   0.0531                       
REMARK   3      S31:   0.3147 S32:   0.1723 S33:   0.0709                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   198        A   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6840 -40.9270  56.9300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2209 T22:   0.1891                                     
REMARK   3      T33:   0.1743 T12:  -0.0056                                     
REMARK   3      T13:   0.0527 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7466 L22:   2.7617                                     
REMARK   3      L33:   4.3377 L12:  -2.9898                                     
REMARK   3      L13:   3.6784 L23:  -3.1681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2577 S12:  -0.7048 S13:   0.2173                       
REMARK   3      S21:   0.1441 S22:   0.0933 S23:  -0.2369                       
REMARK   3      S31:  -0.0900 S32:  -0.4415 S33:   0.1644                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8580 -18.8430  40.8220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1875 T22:   0.0795                                     
REMARK   3      T33:   0.1424 T12:   0.0406                                     
REMARK   3      T13:  -0.0345 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2880 L22:   0.8909                                     
REMARK   3      L33:   0.2904 L12:   0.5901                                     
REMARK   3      L13:  -0.2251 L23:  -0.3065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:  -0.0253 S13:   0.1033                       
REMARK   3      S21:   0.1136 S22:  -0.0286 S23:  -0.0283                       
REMARK   3      S31:   0.0446 S32:   0.0417 S33:   0.0581                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5720 -33.4460  25.1790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1580 T22:   0.1027                                     
REMARK   3      T33:   0.1514 T12:  -0.0195                                     
REMARK   3      T13:  -0.0299 T23:   0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0457 L22:   0.1334                                     
REMARK   3      L33:   1.2097 L12:   0.0623                                     
REMARK   3      L13:  -0.4861 L23:   0.2617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0500 S12:   0.2642 S13:   0.0166                       
REMARK   3      S21:   0.1194 S22:   0.0118 S23:   0.1212                       
REMARK   3      S31:  -0.1102 S32:  -0.0533 S33:   0.0382                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6670 -46.9000  32.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1565 T22:   0.1029                                     
REMARK   3      T33:   0.1246 T12:   0.0773                                     
REMARK   3      T13:   0.0321 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3012 L22:   1.1408                                     
REMARK   3      L33:   0.3677 L12:   0.2252                                     
REMARK   3      L13:  -0.1475 L23:  -0.0355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0302 S12:   0.1085 S13:   0.1220                       
REMARK   3      S21:  -0.0879 S22:   0.0109 S23:   0.2121                       
REMARK   3      S31:  -0.0891 S32:  -0.0275 S33:   0.0193                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3370 -40.6400  52.5280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1623 T22:   0.0553                                     
REMARK   3      T33:   0.1378 T12:   0.0112                                     
REMARK   3      T13:  -0.0519 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6927 L22:   0.1523                                     
REMARK   3      L33:   1.0178 L12:   0.4287                                     
REMARK   3      L13:  -0.3148 L23:  -0.4056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0799 S12:   0.0144 S13:   0.0828                       
REMARK   3      S21:  -0.1739 S22:  -0.0087 S23:  -0.0614                       
REMARK   3      S31:  -0.0616 S32:  -0.1433 S33:  -0.0712                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4520 -23.1800  57.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1732 T22:   0.0881                                     
REMARK   3      T33:   0.1451 T12:   0.0043                                     
REMARK   3      T13:   0.0322 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8262 L22:   0.7970                                     
REMARK   3      L33:   0.9251 L12:   0.2770                                     
REMARK   3      L13:  -0.1461 L23:   0.4269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0481 S12:  -0.1473 S13:   0.0504                       
REMARK   3      S21:  -0.0235 S22:  -0.0342 S23:   0.0117                       
REMARK   3      S31:  -0.0728 S32:   0.1109 S33:  -0.0139                       
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 1S5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021385.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
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: PDB ENTRIES 1LTG, 3CHB                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000MME, MES, KEMPTIDE, PH 6.5,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       53.71550            
REMARK 290   SMTRY3   2  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 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     GLY A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     SER A    28                                                      
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    36                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     THR A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     PHE A    52                                                      
REMARK 465     GLU A   137                                                      
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    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  78    CB   OG                                             
REMARK 470     SER A  81    CB   OG                                             
REMARK 470     ASP A 109    CB   CG   OD1  OD2                                  
REMARK 470     GLN A 111    CB   CG   CD   OE1  NE2                             
REMARK 470     HIS A 131    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 138    CB   CG   CD   OE1  NE2                             
REMARK 470     HIS A 140    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 172    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ILE A 180    CG1  CG2  CD1                                       
REMARK 470     GLU A 201    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 202    CD   CE   NZ                                        
REMARK 470     LYS A 217    NZ                                                  
REMARK 470     ARG A 235    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS D  62    CG   CD   CE   NZ                                   
REMARK 470     LYS D  63    CE   NZ                                             
REMARK 470     LYS E  43    CG   CD   CE   NZ                                   
REMARK 470     LYS E  81    CG   CD   CE   NZ                                   
REMARK 470     LYS G  62    CD   CE   NZ                                        
REMARK 470     LYS G  63    CE   NZ                                             
REMARK 470     LYS G  81    CE   NZ                                             
REMARK 470     LYS H  34    CD   CE   NZ                                        
REMARK 470     LYS H  62    CE   NZ                                             
REMARK 470     LYS H  63    CG   CD   CE   NZ                                   
REMARK 470     LYS H  81    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   OE2  GLU A   112     OG   SER A   114              1.93            
REMARK 500   O    HOH F   157     O    HOH F   168              2.08            
REMARK 500   O    HOH D   108     O    HOH D   144              2.11            
REMARK 500   OE1  GLU E    51     O    HOH E   144              2.12            
REMARK 500   O    HOH H   114     O    HOH H   145              2.17            
REMARK 500   O    HOH F   124     O    HOH F   131              2.17            
REMARK 500   OH   TYR D    27     OE1  GLU D    29              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   343     O    HOH D   119     1655     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   2   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 200   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 229   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG G  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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    ARG A  54      107.53    -31.44                                   
REMARK 500    HIS A  55       22.15   -142.97                                   
REMARK 500    SER A  78       98.84    -67.55                                   
REMARK 500    GLU D  83      -72.84    -76.47                                   
REMARK 500    LYS E  34       -1.24     70.23                                   
REMARK 500    GLU E  83      -71.85    -73.04                                   
REMARK 500    ASN F  21       55.82     37.68                                   
REMARK 500    LYS H  34       -8.43     83.42                                   
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 308        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A 312        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 323        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 352        DISTANCE =  5.56 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 281  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  90   O                                                      
REMARK 620 2 THR A  90   OG1  81.6                                              
REMARK 620 3 HOH A 287   O   104.3  83.6                                        
REMARK 620 4 TYR A 150   O    91.3 169.7  90.9                                  
REMARK 620 5 LEU A 153   O    98.0  96.7 157.5  91.7                            
REMARK 620 6 ASN A   1   O   176.6  95.3  76.5  91.9  81.0                      
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 NA A 281                  
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  1S5B A    1   240  UNP    P01555   CHTA_VIBCH      19    258             
DBREF  1S5B D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5B E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5B F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5B G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5B H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1S5B 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     NA  A 281       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   7   NA    NA 1+                                                        
FORMUL   8  HOH   *404(H2 O)                                                    
HELIX    1   1 PRO A   12  GLY A   20  1                                   9    
HELIX    2   2 ASN A   40  ARG A   46  1                                   7    
HELIX    3   3 SER A   65  LEU A   77  1                                  13    
HELIX    4   4 VAL A   97  GLY A  102  1                                   6    
HELIX    5   5 ALA A  103  SER A  105  5                                   3    
HELIX    6   6 HIS A  107  GLN A  111  5                                   5    
HELIX    7   7 ARG A  146  ASN A  152  1                                   7    
HELIX    8   8 PRO A  157  ALA A  165  5                                   9    
HELIX    9   9 HIS A  171  GLU A  176  5                                   6    
HELIX   10  10 PRO A  178  HIS A  182  5                                   5    
HELIX   11  11 THR A  198  TYR A  226  1                                  29    
HELIX   12  12 ASN D    4  GLU D   11  1                                   8    
HELIX   13  13 ILE D   58  GLU D   79  1                                  22    
HELIX   14  14 ASN E    4  ALA E   10  1                                   7    
HELIX   15  15 SER E   60  THR E   78  1                                  19    
HELIX   16  16 ASN F    4  GLU F   11  1                                   8    
HELIX   17  17 ILE F   58  GLU F   79  1                                  22    
HELIX   18  18 ASN G    4  ALA G   10  1                                   7    
HELIX   19  19 ASP G   59  THR G   78  1                                  20    
HELIX   20  20 ASN H    4  ALA H   10  1                                   7    
HELIX   21  21 SER H   60  GLU H   79  1                                  20    
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  GLY A 126   N  VAL A  87           
SHEET    4   A 4 VAL A 134  ARG A 141 -1  O  HIS A 140   N  TRP A 127           
SHEET    1   B 2 GLY A  21  LEU A  22  0                                        
SHEET    2   B 2 ILE A 119  PRO A 120 -1  O  ILE A 119   N  LEU A  22           
SHEET    1   C 3 TYR A  59  THR A  62  0                                        
SHEET    2   C 3 VAL A 113  LEU A 116 -1  O  ALA A 115   N  VAL A  60           
SHEET    3   C 3 MET A  94  ASN A  96 -1  N  PHE A  95   O  SER A 114           
SHEET    1   D17 THR H  15  ASP H  22  0                                        
SHEET    2   D17 VAL H  82  TRP H  88 -1  O  LEU H  85   N  HIS H  18           
SHEET    3   D17 HIS H  94  ALA H 102 -1  O  ALA H  97   N  CYS H  86           
SHEET    4   D17 SER D  26  SER D  30 -1  N  GLU D  29   O  ILE H  99           
SHEET    5   D17 ALA D  38  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET    6   D17 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    7   D17 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SHEET    8   D17 VAL D  82  TRP D  88 -1  N  CYS D  86   O  ALA D  97           
SHEET    9   D17 THR D  15  ASP D  22 -1  N  LEU D  20   O  GLU D  83           
SHEET   10   D17 VAL D  82  TRP D  88 -1  O  GLU D  83   N  LEU D  20           
SHEET   11   D17 HIS D  94  ALA D 102 -1  O  ALA D  97   N  CYS D  86           
SHEET   12   D17 SER E  26  SER E  30 -1  O  TYR E  27   N  MET D 101           
SHEET   13   D17 ALA E  38  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET   14   D17 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET   15   D17 HIS E  94  ALA E 102  1  O  ILE E  96   N  GLN E  49           
SHEET   16   D17 VAL E  82  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET   17   D17 THR E  15  ASP E  22 -1  N  HIS E  18   O  LEU E  85           
SHEET    1   E13 VAL E  82  TRP E  88  0                                        
SHEET    2   E13 HIS E  94  ALA E 102 -1  O  ALA E  97   N  CYS E  86           
SHEET    3   E13 SER F  26  SER F  30 -1  O  TYR F  27   N  MET E 101           
SHEET    4   E13 ALA F  38  THR F  41 -1  O  ILE F  39   N  THR F  28           
SHEET    5   E13 THR F  47  VAL F  50 -1  O  PHE F  48   N  ILE F  40           
SHEET    6   E13 HIS F  94  ALA F 102  1  O  ILE F  96   N  GLN F  49           
SHEET    7   E13 VAL F  82  TRP F  88 -1  N  CYS F  86   O  ALA F  97           
SHEET    8   E13 THR F  15  ASP F  22 -1  N  HIS F  18   O  LEU F  85           
SHEET    9   E13 VAL F  82  TRP F  88 -1  O  LEU F  85   N  HIS F  18           
SHEET   10   E13 HIS F  94  ALA F 102 -1  O  ALA F  97   N  CYS F  86           
SHEET   11   E13 SER G  26  SER G  30 -1  O  TYR G  27   N  MET F 101           
SHEET   12   E13 ALA G  38  THR G  41 -1  O  ILE G  39   N  THR G  28           
SHEET   13   E13 THR G  47  VAL G  50 -1  O  PHE G  48   N  ILE G  40           
SHEET    1   F 9 HIS G  94  ALA G 102  0                                        
SHEET    2   F 9 LYS G  81  TRP G  88 -1  N  CYS G  86   O  ALA G  97           
SHEET    3   F 9 THR G  15  LYS G  23 -1  N  HIS G  18   O  LEU G  85           
SHEET    4   F 9 LYS G  81  TRP G  88 -1  O  LEU G  85   N  HIS G  18           
SHEET    5   F 9 HIS G  94  ALA G 102 -1  O  ALA G  97   N  CYS G  86           
SHEET    6   F 9 SER H  26  SER H  30 -1  O  GLU H  29   N  ILE G  99           
SHEET    7   F 9 ALA H  38  THR H  41 -1  O  ILE H  39   N  THR H  28           
SHEET    8   F 9 THR H  47  VAL H  50 -1  O  PHE H  48   N  ILE H  40           
SHEET    9   F 9 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  2.04  
SSBOND   2 CYS D    9    CYS D   86                          1555   1555  2.12  
SSBOND   3 CYS E    9    CYS E   86                          1555   1555  2.06  
SSBOND   4 CYS F    9    CYS F   86                          1555   1555  2.09  
SSBOND   5 CYS G    9    CYS G   86                          1555   1555  2.09  
SSBOND   6 CYS H    9    CYS H   86                          1555   1555  2.09  
LINK        NA    NA A 281                 O   THR A  90     1555   1555  2.47  
LINK        NA    NA A 281                 OG1 THR A  90     1555   1555  2.36  
LINK        NA    NA A 281                 O   HOH A 287     1555   1555  2.55  
LINK        NA    NA A 281                 O   TYR A 150     1555   1555  2.34  
LINK        NA    NA A 281                 O   LEU A 153     1555   1555  2.20  
LINK         O   ASN A   1                NA    NA A 281     1555   1555  2.63  
CISPEP   1 GLU A  177    PRO A  178          0         0.44                     
CISPEP   2 THR D   92    PRO D   93          0        -6.19                     
CISPEP   3 THR E   92    PRO E   93          0       -10.09                     
CISPEP   4 THR F   92    PRO F   93          0        -6.87                     
CISPEP   5 THR G   92    PRO G   93          0        -8.78                     
CISPEP   6 THR H   92    PRO H   93          0        -9.21                     
SITE     1 AC1  5 ASN A   1  THR A  90  TYR A 150  LEU A 153                    
SITE     2 AC1  5 HOH A 287                                                     
CRYST1   60.104  107.431   65.950  90.00  91.29  90.00 P 1 21 1     10          
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      0.016638  0.000000  0.000375        0.00000                         
SCALE2      0.000000  0.009308  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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