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Database: PDB
Entry: 1S5C
LinkDB: 1S5C
Original site: 1S5C 
HEADER    TRANSFERASE,TOXIN                       20-JAN-04   1S5C              
TITLE     CHOLERA HOLOTOXIN WITH AN A-SUBUNIT Y30S MUTATION, CRYSTAL FORM 1     
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 ENTEROTOXIN B-SUBUNIT;                             
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 1S5C    1       VERSN                                    
REVDAT   2   24-FEB-09 1S5C    1       VERSN                                    
REVDAT   1   06-APR-04 1S5C    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22291                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1208                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1568                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5612                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 94                                      
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) : 16.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.338         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.248         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.120        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5734 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4973 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7784 ; 1.215 ; 1.928       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11565 ; 0.873 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   722 ; 6.877 ; 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):   868 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6470 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1114 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1194 ; 0.176 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5920 ; 0.195 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3308 ; 0.084 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   196 ; 0.209 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.080 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    37 ; 0.102 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):   105 ; 0.194 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.245 ; 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):  3623 ; 0.869 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5812 ; 1.425 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2111 ; 1.365 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1972 ; 2.178 ; 6.000       
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  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    25                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5091  50.1618  37.2870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0677 T22:   0.0969                                     
REMARK   3      T33:   0.1608 T12:  -0.0300                                     
REMARK   3      T13:   0.0729 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8572 L22:   0.9164                                     
REMARK   3      L33:   2.4556 L12:   0.6103                                     
REMARK   3      L13:   1.8334 L23:   0.3966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.2543 S13:   0.3721                       
REMARK   3      S21:   0.1112 S22:   0.1517 S23:   0.2376                       
REMARK   3      S31:  -0.1977 S32:   0.3746 S33:  -0.1310                       
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    37        A    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8786  39.6345  50.2792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1237 T22:   0.1825                                     
REMARK   3      T33:   0.0863 T12:   0.0255                                     
REMARK   3      T13:   0.0232 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -1.2436 L22:   5.8612                                     
REMARK   3      L33:   1.5758 L12:  -2.5024                                     
REMARK   3      L13:  -2.8294 L23:   2.1392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1862 S12:  -0.2391 S13:  -0.0347                       
REMARK   3      S21:   0.2560 S22:  -0.1310 S23:  -0.0720                       
REMARK   3      S31:  -0.6554 S32:   0.1717 S33:  -0.0552                       
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 :   A    51        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8698  43.4263  39.6357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0604 T22:   0.1180                                     
REMARK   3      T33:   0.1219 T12:   0.0306                                     
REMARK   3      T13:   0.0328 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1362 L22:   1.0263                                     
REMARK   3      L33:   1.4230 L12:   0.8612                                     
REMARK   3      L13:  -0.2638 L23:  -0.3808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0461 S12:   0.0566 S13:   0.1597                       
REMARK   3      S21:   0.1264 S22:   0.0893 S23:   0.0832                       
REMARK   3      S31:  -0.0657 S32:   0.0127 S33:  -0.1355                       
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 :   A   196        A   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5273  32.5465  32.9032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1212 T22:   0.1840                                     
REMARK   3      T33:   0.0977 T12:   0.0775                                     
REMARK   3      T13:   0.0427 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9968 L22:   0.1139                                     
REMARK   3      L33:   6.3171 L12:   0.6897                                     
REMARK   3      L13:  -2.9042 L23:  -0.8784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0264 S12:  -0.1093 S13:  -0.0958                       
REMARK   3      S21:  -0.0738 S22:   0.0144 S23:   0.0433                       
REMARK   3      S31:   0.0984 S32:   0.1408 S33:   0.0119                       
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 :   D     1        D   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.4254  35.6661  28.1031              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0663 T22:   0.1164                                     
REMARK   3      T33:   0.1035 T12:   0.0118                                     
REMARK   3      T13:  -0.0071 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1830 L22:   2.0059                                     
REMARK   3      L33:   1.4382 L12:   0.2152                                     
REMARK   3      L13:   0.9981 L23:  -0.7148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0679 S12:  -0.0933 S13:   0.0209                       
REMARK   3      S21:  -0.0057 S22:  -0.0245 S23:  -0.0609                       
REMARK   3      S31:  -0.0015 S32:   0.0700 S33:   0.0924                       
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 :   E     1        E   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1596  18.8236  20.8257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1197 T22:   0.0652                                     
REMARK   3      T33:   0.0800 T12:   0.0087                                     
REMARK   3      T13:  -0.0260 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3064 L22:   1.3011                                     
REMARK   3      L33:   1.7413 L12:   0.5905                                     
REMARK   3      L13:   0.4072 L23:   0.3503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0972 S12:  -0.1098 S13:  -0.1221                       
REMARK   3      S21:   0.0019 S22:   0.0245 S23:  -0.0479                       
REMARK   3      S31:   0.1569 S32:   0.0359 S33:  -0.1217                       
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 :   F     1        F   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6407  26.6190   5.5000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1029 T22:   0.1221                                     
REMARK   3      T33:   0.0608 T12:  -0.0295                                     
REMARK   3      T13:   0.0230 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9827 L22:   2.4017                                     
REMARK   3      L33:   0.5315 L12:  -0.4141                                     
REMARK   3      L13:   0.3851 L23:  -0.1412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:  -0.0239 S13:   0.0718                       
REMARK   3      S21:  -0.1097 S22:  -0.0126 S23:   0.0797                       
REMARK   3      S31:   0.1098 S32:  -0.0163 S33:   0.0084                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
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):  38.0236  47.9032   2.7548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0649 T22:   0.1024                                     
REMARK   3      T33:   0.0643 T12:   0.0002                                     
REMARK   3      T13:   0.0612 T23:   0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5219 L22:   3.4372                                     
REMARK   3      L33:   1.3745 L12:  -0.0378                                     
REMARK   3      L13:   0.5392 L23:   0.2297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0516 S12:   0.0198 S13:  -0.0276                       
REMARK   3      S21:  -0.1078 S22:   0.0344 S23:  -0.1904                       
REMARK   3      S31:  -0.0884 S32:  -0.0559 S33:   0.0172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
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):  54.2276  53.2305  16.3289              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0908 T22:   0.0121                                     
REMARK   3      T33:   0.1620 T12:  -0.0309                                     
REMARK   3      T13:  -0.0834 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2106 L22:   2.0199                                     
REMARK   3      L33:   2.6727 L12:  -0.6682                                     
REMARK   3      L13:   0.9446 L23:  -0.2388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2392 S12:   0.1098 S13:   0.2217                       
REMARK   3      S21:   0.1905 S22:   0.0063 S23:  -0.3428                       
REMARK   3      S31:  -0.2903 S32:   0.0278 S33:   0.2329                       
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 1S5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021386.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-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               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0414                             
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   : 23503                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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   (%): 43.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000MME, MES, PH 6.5, VAPOR          
REMARK 280  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       42.59950            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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     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     THR A    50                                                      
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     ARG A   235                                                      
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     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     PHE A  52    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ARG A  67    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLN A  74    CD   OE1  NE2                                       
REMARK 470     ILE A  76    CD1                                                 
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 134    CB   CG1  CG2                                       
REMARK 470     ASP A 136    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 137    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG A 141    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG A 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 175    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASN A 189    CB   CG   OD1                                       
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 202    CD   CE   NZ                                        
REMARK 470     LYS A 217    CD   CE   NZ                                        
REMARK 470     LYS A 219    CE   NZ                                             
REMARK 470     ASN A 234    CB   CG   OD1                                       
REMARK 470     LYS D  34    CD   CE   NZ                                        
REMARK 470     SER D  55    CB   OG                                             
REMARK 470     GLN D  56    CB   CG   CD   OE1  NE2                             
REMARK 470     ILE D  58    CB   CG1  CG2  CD1                                  
REMARK 470     ASP D  59    CB   CG   OD1  OD2                                  
REMARK 470     LYS D  62    CD   CE   NZ                                        
REMARK 470     LYS D  63    CG   CD   CE   NZ                                   
REMARK 470     LYS D  81    CE   NZ                                             
REMARK 470     ASN D 103    CB   CG   OD1                                       
REMARK 470     LYS E  34    CE   NZ                                             
REMARK 470     LYS E  43    CD   CE   NZ                                        
REMARK 470     LYS E  62    CB   CG   CD   CE   NZ                              
REMARK 470     LYS E  63    CG   CD   CE   NZ                                   
REMARK 470     LYS E  81    CD   CE   NZ                                        
REMARK 470     ASN F 103    CB   CG   OD1                                       
REMARK 470     LYS G  43    CG   CD   CE   NZ                                   
REMARK 470     LYS G  62    CG   CD   CE   NZ                                   
REMARK 470     LYS G  63    CG   CD   CE   NZ                                   
REMARK 470     LYS G  81    CD   CE   NZ                                        
REMARK 470     ASN G 103    CB   CG   OD1                                       
REMARK 470     HIS H  13    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     GLN H  16    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS H  34    CD   CE   NZ                                        
REMARK 470     LYS H  43    CG   CD   CE   NZ                                   
REMARK 470     ALA H  46    CB                                                  
REMARK 470     LYS H  63    CG   CD   CE   NZ                                   
REMARK 470     LYS H  81    CD   CE   NZ                                        
REMARK 470     LYS H  84    CG   CD   CE   NZ                                   
REMARK 470     LYS H  91    CB   CG   CD   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   OG   SER A   216     OE1  GLU E    79              2.18            
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  43   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    ASN A  40      116.74   -160.60                                   
REMARK 500    ARG A  54      106.62    -20.64                                   
REMARK 500    HIS A  55       25.00   -144.47                                   
REMARK 500    LEU A  77       31.01    -86.79                                   
REMARK 500    PRO A 120      156.52    -49.16                                   
REMARK 500    ASN D  44        5.13    -67.87                                   
REMARK 500    PRO D  53      104.22    -50.94                                   
REMARK 500    ILE D  58     -130.30    -80.49                                   
REMARK 500    ASN F  21       56.53     33.42                                   
REMARK 500    ASN G  21       49.58     37.38                                   
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 252        DISTANCE =  5.23 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 ASN A   1   O                                                      
REMARK 620 2 THR A  90   OG1 103.5                                              
REMARK 620 3 TYR A 150   O   100.6 152.0                                        
REMARK 620 4 THR A  90   O   159.7  66.6  86.0                                  
REMARK 620 5 LEU A 153   O    76.8  88.9  82.9  85.1                            
REMARK 620 N                    1     2     3     4                             
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 241                  
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  1S5C A    1   240  UNP    P01555   CHTA_VIBCH      19    258             
DBREF  1S5C D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5C E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5C F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5C G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5C H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQADV 1S5C 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 241       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   7   NA    NA 1+                                                        
FORMUL   8  HOH   *94(H2 O)                                                     
HELIX    1   1 PRO A   12  GLY A   20  1                                   9    
HELIX    2   2 ASN A   40  GLY A   47  1                                   8    
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  GLU A  110  5                                   4    
HELIX    7   7 ARG A  146  ASN A  152  1                                   7    
HELIX    8   8 PRO A  157  GLY A  163  1                                   7    
HELIX    9   9 HIS A  171  GLU A  176  5                                   6    
HELIX   10  10 PRO A  178  ALA A  183  5                                   6    
HELIX   11  11 ASN A  197  GLN A  227  1                                  31    
HELIX   12  12 ASN D    4  GLU D   11  1                                   8    
HELIX   13  13 ASP D   59  GLU D   79  1                                  21    
HELIX   14  14 ASN E    4  ALA E   10  1                                   7    
HELIX   15  15 SER E   60  GLU E   79  1                                  20    
HELIX   16  16 ASN F    4  ALA F   10  1                                   7    
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 ILE G   58  THR G   78  1                                  21    
HELIX   20  20 ASN H    4  ALA H   10  1                                   7    
HELIX   21  21 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  GLY A 126   N  VAL A  87           
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  GLY A 126   N  VAL A  87           
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  SER A  63  0                                        
SHEET    2   D 3 GLU A 112  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   E14 THR F  15  ASP F  22  0                                        
SHEET    2   E14 VAL F  82  TRP F  88 -1  O  LEU F  85   N  HIS F  18           
SHEET    3   E14 HIS F  94  ALA F 102 -1  O  ALA F  97   N  CYS F  86           
SHEET    4   E14 SER D  26  SER D  30 -1  N  TYR D  27   O  MET F 101           
SHEET    5   E14 MET D  37  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET    6   E14 PHE D  48  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    7   E14 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SHEET    8   E14 VAL D  82  TRP D  88 -1  N  TRP D  88   O  ALA D  95           
SHEET    9   E14 THR D  15  ASP D  22 -1  N  GLN D  16   O  VAL D  87           
SHEET   10   E14 VAL D  82  TRP D  88 -1  O  VAL D  87   N  GLN D  16           
SHEET   11   E14 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET   12   E14 SER E  26  SER E  30 -1  O  GLU E  29   N  ILE D  99           
SHEET   13   E14 MET E  37  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET   14   E14 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET    1   F11 HIS E  94  ALA E 102  0                                        
SHEET    2   F11 VAL E  82  TRP E  88 -1  N  TRP E  88   O  ALA E  95           
SHEET    3   F11 THR E  15  ASP E  22 -1  N  HIS E  18   O  LEU E  85           
SHEET    4   F11 VAL E  82  TRP E  88 -1  O  LEU E  85   N  HIS E  18           
SHEET    5   F11 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET    6   F11 SER D  26  SER D  30 -1  O  GLU D  29   N  ILE E  99           
SHEET    7   F11 ALA D  38  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET    8   F11 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    9   F11 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SHEET   10   F11 VAL D  82  TRP D  88 -1  N  TRP D  88   O  ALA D  95           
SHEET   11   F11 THR D  15  ASP D  22 -1  N  HIS D  18   O  LEU D  85           
SHEET    1   G11 VAL D  82  TRP D  88  0                                        
SHEET    2   G11 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET    3   G11 SER E  26  SER E  30 -1  O  TYR E  27   N  MET D 101           
SHEET    4   G11 MET E  37  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET    5   G11 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET    6   G11 HIS E  94  ALA E 102  1  O  ILE E  96   N  GLN E  49           
SHEET    7   G11 LYS E  81  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET    8   G11 THR E  15  LYS E  23 -1  N  LEU E  20   O  GLU E  83           
SHEET    9   G11 LYS E  81  TRP E  88 -1  O  GLU E  83   N  LEU E  20           
SHEET   10   G11 HIS E  94  ALA E 102 -1  O  ALA E  97   N  CYS E  86           
SHEET   11   G11 SER F  26  SER F  30 -1  O  TYR F  27   N  MET E 101           
SHEET    1   H 3 ALA F  38  THR F  41  0                                        
SHEET    2   H 3 THR F  47  VAL F  50 -1  O  PHE F  48   N  ILE F  40           
SHEET    3   H 3 HIS F  94  ALA F 102  1  O  ILE F  96   N  GLN F  49           
SSBOND   1 CYS A  187    CYS A  199                          1555   1555  2.03  
SSBOND   2 CYS D    9    CYS D   86                          1555   1555  2.02  
SSBOND   3 CYS E    9    CYS E   86                          1555   1555  2.03  
SSBOND   4 CYS F    9    CYS F   86                          1555   1555  2.04  
SSBOND   5 CYS G    9    CYS G   86                          1555   1555  2.03  
SSBOND   6 CYS H    9    CYS H   86                          1555   1555  2.05  
LINK        NA    NA A 241                 O   ASN A   1     1555   1555  2.32  
LINK        NA    NA A 241                 OG1 THR A  90     1555   1555  2.57  
LINK        NA    NA A 241                 O   TYR A 150     1555   1555  2.35  
LINK         O   THR A  90                NA    NA A 241     1555   1555  2.66  
LINK         O   LEU A 153                NA    NA A 241     1555   1555  2.62  
CISPEP   1 GLU A  177    PRO A  178          0         4.79                     
CISPEP   2 THR D   92    PRO D   93          0         3.81                     
CISPEP   3 THR E   92    PRO E   93          0        -5.24                     
CISPEP   4 THR F   92    PRO F   93          0        -0.79                     
CISPEP   5 THR G   92    PRO G   93          0        -2.02                     
CISPEP   6 THR H   92    PRO H   93          0        -1.34                     
SITE     1 AC1  4 ASN A   1  THR A  90  TYR A 150  LEU A 153                    
CRYST1   58.818   85.199   71.255  90.00 104.48  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      0.017002  0.000000  0.004391        0.00000                         
SCALE2      0.000000  0.011737  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014495        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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