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Database: PDB
Entry: 1S5E
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Original site: 1S5E 
HEADER    TRANSFERASE,TOXIN                       20-JAN-04   1S5E              
TITLE     CHOLERA HOLOTOXIN, CRYSTAL FORM 1                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN, A CHAIN PRECURSOR;                    
COMPND   3 CHAIN: A, B;                                                         
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 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CHOLERA TOXIN B PROTEIN (CTB);                             
COMPND  10 CHAIN: D, E, F, G, H, J, K, L, M, N;                                 
COMPND  11 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: PARCT5;                                   
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: PARCT5                                    
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 1S5E    1       VERSN                                    
REVDAT   2   24-FEB-09 1S5E    1       VERSN                                    
REVDAT   1   06-APR-04 1S5E    0                                                
JRNL        AUTH   C.J.O'NEAL,E.I.AMAYA,M.G.JOBLING,R.K.HOLMES,W.G.HOL          
JRNL        TITL   CRYSTAL STRUCTURES OF AN INTRINSICALLY ACTIVE CHOLERA TOXIN  
JRNL        TITL 2 MUTANT YIELD INSIGHT INTO THE TOXIN ACTIVATION MECHANISM     
JRNL        REF    BIOCHEMISTRY                  V.  43  3772 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15049684                                                     
JRNL        DOI    10.1021/BI0360152                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 116190                         
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6126                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8128                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 440                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11664                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 748                                     
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) : 13.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : 0.14000                                              
REMARK   3    B33 (A**2) : -0.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.950         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11939 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 10434 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16183 ; 1.410 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24337 ; 0.787 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1473 ; 6.531 ; 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):  1804 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13319 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2323 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2252 ; 0.217 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 11932 ; 0.267 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  6786 ; 0.090 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1297 ; 0.170 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     5 ; 0.120 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    16 ; 0.267 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    75 ; 0.371 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.158 ; 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):  7409 ; 1.157 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11945 ; 1.874 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4530 ; 1.447 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4238 ; 2.300 ; 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  : 14                                         
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    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2190 -18.3640  39.7010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1885 T22:   0.1281                                     
REMARK   3      T33:   0.2006 T12:   0.0234                                     
REMARK   3      T13:   0.0407 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8067 L22:   1.4120                                     
REMARK   3      L33:   2.3027 L12:   0.1312                                     
REMARK   3      L13:   0.6359 L23:   0.6478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0943 S12:   0.0835 S13:  -0.2063                       
REMARK   3      S21:  -0.0745 S22:   0.0252 S23:  -0.1162                       
REMARK   3      S31:   0.2671 S32:   0.2322 S33:  -0.1195                       
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   197        A   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9800  -2.7630  38.0360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2045 T22:   0.1811                                     
REMARK   3      T33:   0.2013 T12:  -0.0284                                     
REMARK   3      T13:   0.0486 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1663 L22:   2.3858                                     
REMARK   3      L33:   5.7476 L12:   1.8503                                     
REMARK   3      L13:   3.4465 L23:   3.7350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0786 S12:   0.1979 S13:   0.0215                       
REMARK   3      S21:  -0.0455 S22:   0.0885 S23:  -0.1166                       
REMARK   3      S31:  -0.0174 S32:   0.2106 S33:  -0.0099                       
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):  33.4510  -2.5260  42.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1927 T22:   0.1218                                     
REMARK   3      T33:   0.2322 T12:  -0.0024                                     
REMARK   3      T13:   0.0352 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2182 L22:   0.7473                                     
REMARK   3      L33:   0.8522 L12:  -0.2617                                     
REMARK   3      L13:  -0.0621 L23:  -0.2269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0282 S12:   0.0724 S13:  -0.1167                       
REMARK   3      S21:  -0.0400 S22:  -0.0303 S23:  -0.0840                       
REMARK   3      S31:   0.0477 S32:   0.0560 S33:   0.0585                       
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):  21.0710  14.6510  36.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2072 T22:   0.1502                                     
REMARK   3      T33:   0.1738 T12:   0.0100                                     
REMARK   3      T13:   0.0315 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3906 L22:   1.7607                                     
REMARK   3      L33:   0.7739 L12:  -0.4164                                     
REMARK   3      L13:  -0.3995 L23:   0.1169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0610 S12:   0.1672 S13:   0.0754                       
REMARK   3      S21:  -0.1287 S22:  -0.0263 S23:  -0.0664                       
REMARK   3      S31:  -0.0614 S32:  -0.0932 S33:  -0.0347                       
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):   8.1110  19.6630  53.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2041 T22:   0.1258                                     
REMARK   3      T33:   0.2290 T12:   0.0164                                     
REMARK   3      T13:   0.0288 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1349 L22:   0.7880                                     
REMARK   3      L33:   1.1598 L12:  -0.1830                                     
REMARK   3      L13:  -0.5558 L23:   0.0129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0773 S12:   0.0423 S13:   0.1176                       
REMARK   3      S21:  -0.0284 S22:  -0.0191 S23:   0.1119                       
REMARK   3      S31:  -0.1480 S32:  -0.0834 S33:  -0.0582                       
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   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7180   5.5090  69.7110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2086 T22:   0.1823                                     
REMARK   3      T33:   0.1746 T12:   0.0123                                     
REMARK   3      T13:   0.0353 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4019 L22:   1.3685                                     
REMARK   3      L33:   1.0624 L12:  -0.1792                                     
REMARK   3      L13:  -0.2112 L23:  -0.0618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0686 S12:  -0.3068 S13:  -0.0278                       
REMARK   3      S21:   0.1504 S22:   0.0260 S23:   0.0559                       
REMARK   3      S31:   0.0177 S32:   0.0150 S33:   0.0426                       
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):  28.2480  -8.2960  62.6740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0888 T22:   0.0420                                     
REMARK   3      T33:   0.1264 T12:   0.0302                                     
REMARK   3      T13:   0.0277 T23:   0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9463 L22:   0.7386                                     
REMARK   3      L33:   0.9734 L12:  -0.0990                                     
REMARK   3      L13:  -0.4496 L23:   0.2693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1182 S12:  -0.2842 S13:  -0.2664                       
REMARK   3      S21:   0.0508 S22:   0.0384 S23:  -0.0204                       
REMARK   3      S31:   0.0609 S32:   0.0784 S33:   0.0798                       
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 :   B     1        B   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1270  30.1970   8.2880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1596 T22:   0.1177                                     
REMARK   3      T33:   0.2342 T12:  -0.0010                                     
REMARK   3      T13:   0.0416 T23:  -0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5044 L22:   1.1017                                     
REMARK   3      L33:   1.1141 L12:  -0.0579                                     
REMARK   3      L13:  -0.0197 L23:   0.0673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0246 S12:   0.0624 S13:  -0.1368                       
REMARK   3      S21:   0.0179 S22:  -0.0288 S23:   0.0615                       
REMARK   3      S31:   0.0996 S32:   0.0433 S33:   0.0042                       
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 :   B   198        B   235                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.1030  43.1270   3.2020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1582 T22:   0.1679                                     
REMARK   3      T33:   0.2079 T12:   0.0003                                     
REMARK   3      T13:   0.0576 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7803 L22:   4.8300                                     
REMARK   3      L33:   3.9229 L12:   3.4357                                     
REMARK   3      L13:   3.3046 L23:   4.0547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0267 S12:   0.2553 S13:  -0.0186                       
REMARK   3      S21:  -0.0730 S22:   0.0983 S23:  -0.1264                       
REMARK   3      S31:  -0.0082 S32:   0.0873 S33:  -0.0716                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.1880  44.5160   7.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1821 T22:   0.1491                                     
REMARK   3      T33:   0.2131 T12:  -0.0023                                     
REMARK   3      T13:   0.0225 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5445 L22:   0.8330                                     
REMARK   3      L33:   1.2712 L12:  -0.4720                                     
REMARK   3      L13:  -0.1186 L23:  -0.3253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0243 S12:   0.1444 S13:  -0.0725                       
REMARK   3      S21:  -0.0191 S22:  -0.0472 S23:  -0.0404                       
REMARK   3      S31:   0.0069 S32:   0.0287 S33:   0.0229                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1110  59.9600  -2.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1905 T22:   0.1983                                     
REMARK   3      T33:   0.1871 T12:   0.0508                                     
REMARK   3      T13:   0.0351 T23:   0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3992 L22:   1.5771                                     
REMARK   3      L33:   0.8486 L12:  -0.3519                                     
REMARK   3      L13:  -0.2249 L23:   0.3024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1567 S12:   0.3890 S13:   0.2155                       
REMARK   3      S21:  -0.1710 S22:  -0.1707 S23:  -0.0317                       
REMARK   3      S31:  -0.0916 S32:  -0.0910 S33:   0.0140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9030  68.8880  13.0180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1700 T22:   0.1076                                     
REMARK   3      T33:   0.2856 T12:   0.0145                                     
REMARK   3      T13:   0.0332 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6917 L22:   1.8390                                     
REMARK   3      L33:   0.8976 L12:  -0.7528                                     
REMARK   3      L13:  -0.2565 L23:   0.1329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0728 S12:   0.0989 S13:   0.2536                       
REMARK   3      S21:  -0.0806 S22:  -0.0743 S23:   0.1409                       
REMARK   3      S31:  -0.1348 S32:  -0.0636 S33:   0.0015                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     1        M   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0240  58.7250  32.0790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2083 T22:   0.1653                                     
REMARK   3      T33:   0.2255 T12:   0.0034                                     
REMARK   3      T13:   0.0658 T23:  -0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4422 L22:   1.5424                                     
REMARK   3      L33:   1.2603 L12:  -0.4701                                     
REMARK   3      L13:   0.0627 L23:  -0.0875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0548 S12:  -0.2720 S13:   0.1420                       
REMARK   3      S21:   0.2414 S22:   0.0856 S23:   0.1190                       
REMARK   3      S31:  -0.0322 S32:  -0.0499 S33:  -0.0309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     1        N   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6930  43.7800  28.7570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2135 T22:   0.1493                                     
REMARK   3      T33:   0.1890 T12:   0.0015                                     
REMARK   3      T13:   0.0173 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0037 L22:   1.0670                                     
REMARK   3      L33:   0.8634 L12:  -0.3370                                     
REMARK   3      L13:  -0.3311 L23:   0.2329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0578 S12:  -0.2646 S13:  -0.0429                       
REMARK   3      S21:   0.1521 S22:   0.0410 S23:   0.0227                       
REMARK   3      S31:   0.0437 S32:   0.0437 S33:   0.0169                       
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 1S5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021388.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0781                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122327                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.850                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: CTY30S FORM 3 STRUCTURE (PDB ID 1S5B)                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM ACETATE,             
REMARK 280  GALACTOSE, 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       54.11500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 16680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 28020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 16830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J, K, L, M, N                      
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     THR A    50                                                      
REMARK 465     SER A   194                                                      
REMARK 465     MET A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     LEU A   240                                                      
REMARK 465     ASN G   103                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     PRO B   191                                                      
REMARK 465     ARG B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     MET B   195                                                      
REMARK 465     SER B   196                                                      
REMARK 465     ASN B   197                                                      
REMARK 465     ILE B   236                                                      
REMARK 465     LYS B   237                                                      
REMARK 465     ASP B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     LEU B   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     ASP A  14    OD1  OD2                                            
REMARK 470     LYS A  17    CD   CE   NZ                                        
REMARK 470     GLN A  18    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  32    CB   CG   OD1  OD2                                  
REMARK 470     THR A  35    CB   OG1  CG2                                       
REMARK 470     ARG A  67    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER A  78    CB   OG                                             
REMARK 470     GLU A 137    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN A 138    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG A 141    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 172    CZ   NH1  NH2                                       
REMARK 470     LYS A 209    CD   CE   NZ                                        
REMARK 470     ILE A 236    CB   CG1  CG2  CD1                                  
REMARK 470     GLN D   3    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  43    CD   CE   NZ                                        
REMARK 470     LYS D  62    CE   NZ                                             
REMARK 470     LYS D  63    CG   CD   CE   NZ                                   
REMARK 470     LYS E  81    CG   CD   CE   NZ                                   
REMARK 470     THR F  92    CG2                                                 
REMARK 470     LYS G  63    CE   NZ                                             
REMARK 470     LYS H  62    CD   CE   NZ                                        
REMARK 470     LYS H  81    CE   NZ                                             
REMARK 470     ARG B  46    NE   CZ   NH1  NH2                                  
REMARK 470     PHE B  52    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 135    CD1  CD2                                            
REMARK 470     GLU B 137    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 138    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 189    CB   CG   OD1                                       
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     ASN B 234    CG   OD1                                            
REMARK 470     ARG B 235    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS J  63    NZ                                                  
REMARK 470     LYS J  81    CE   NZ                                             
REMARK 470     LEU K   8    CD2                                                 
REMARK 470     LYS K  81    CG   CD   CE   NZ                                   
REMARK 470     LYS K  91    NZ                                                  
REMARK 470     LEU L   8    CD1                                                 
REMARK 470     LYS L  34    CD   CE   NZ                                        
REMARK 470     LYS L  43    CE   NZ                                             
REMARK 470     LYS L  62    CD   CE   NZ                                        
REMARK 470     LYS L  91    CG   CD   CE   NZ                                   
REMARK 470     LYS M  34    CD   CE   NZ                                        
REMARK 470     SER M  55    CB   OG                                             
REMARK 470     LYS M  63    CG   CD   CE   NZ                                   
REMARK 470     LYS N  43    CG   CD   CE   NZ                                   
REMARK 470     LYS N  62    CE   NZ                                             
REMARK 470     LYS N  63    CG   CD   CE   NZ                                   
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 J   7   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP L  59   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU N  31   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  33       38.14    -94.23                                   
REMARK 500    HIS A  55       19.80   -149.91                                   
REMARK 500    ASN D  14       32.09    -95.02                                   
REMARK 500    LYS D  34       -4.02     75.83                                   
REMARK 500    LYS H  34       -5.30     79.25                                   
REMARK 500    GLU H  83      -74.66    -79.65                                   
REMARK 500    ARG B  54      120.70    -38.76                                   
REMARK 500    HIS B  55       27.28   -149.42                                   
REMARK 500    PRO B  92       10.48    -68.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR M    1     PRO M    2                  143.88                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL H  82        24.8      L          L   OUTSIDE RANGE           
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 B 303        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH G 133        DISTANCE =  5.30 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 THR A  90   OG1                                                    
REMARK 620 2 ASN A   1   O    94.9                                              
REMARK 620 3 THR A  90   O    76.7 171.1                                        
REMARK 620 4 HOH A 262   O    79.8  80.4 100.8                                  
REMARK 620 5 LEU A 153   O    93.0  83.3  94.0 161.5                            
REMARK 620 6 TYR A 150   O   168.4  96.4  92.1  99.4  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 241  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 153   O                                                      
REMARK 620 2 ASN B   1   O    81.1                                              
REMARK 620 3 THR B  90   O    89.2 168.1                                        
REMARK 620 4 HOH B 267   O   159.2  80.3 107.8                                  
REMARK 620 5 TYR B 150   O    87.9  91.5  95.1 102.0                            
REMARK 620 6 THR B  90   OG1  91.2  97.1  76.1  81.7 171.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL D 751                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL J 752                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 241                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 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  1S5E A    1   240  UNP    P01555   CHTA_VIBCH      19    258             
DBREF  1S5E D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E F    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E G    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E H    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E B    1   240  UNP    P01555   CHTA_VIBCH      19    258             
DBREF  1S5E J    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E K    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E L    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E M    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  1S5E N    1   103  UNP    P01556   CHTB_VIBCH      22    124             
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 TYR 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              
SEQRES   1 B  240  ASN ASP ASP LYS LEU TYR ARG ALA ASP SER ARG PRO PRO          
SEQRES   2 B  240  ASP GLU ILE LYS GLN SER GLY GLY LEU MET PRO ARG GLY          
SEQRES   3 B  240  GLN SER GLU TYR PHE ASP ARG GLY THR GLN MET ASN ILE          
SEQRES   4 B  240  ASN LEU TYR ASP HIS ALA ARG GLY THR GLN THR GLY PHE          
SEQRES   5 B  240  VAL ARG HIS ASP ASP GLY TYR VAL SER THR SER ILE SER          
SEQRES   6 B  240  LEU ARG SER ALA HIS LEU VAL GLY GLN THR ILE LEU SER          
SEQRES   7 B  240  GLY HIS SER THR TYR TYR ILE TYR VAL ILE ALA THR ALA          
SEQRES   8 B  240  PRO ASN MET PHE ASN VAL ASN ASP VAL LEU GLY ALA TYR          
SEQRES   9 B  240  SER PRO HIS PRO ASP GLU GLN GLU VAL SER ALA LEU GLY          
SEQRES  10 B  240  GLY ILE PRO TYR SER GLN ILE TYR GLY TRP TYR ARG VAL          
SEQRES  11 B  240  HIS PHE GLY VAL LEU ASP GLU GLN LEU HIS ARG ASN ARG          
SEQRES  12 B  240  GLY TYR ARG ASP ARG TYR TYR SER ASN LEU ASP ILE ALA          
SEQRES  13 B  240  PRO ALA ALA ASP GLY TYR GLY LEU ALA GLY PHE PRO PRO          
SEQRES  14 B  240  GLU HIS ARG ALA TRP ARG GLU GLU PRO TRP ILE HIS HIS          
SEQRES  15 B  240  ALA PRO PRO GLY CYS GLY ASN ALA PRO ARG SER SER MET          
SEQRES  16 B  240  SER ASN THR CYS ASP GLU LYS THR GLN SER LEU GLY VAL          
SEQRES  17 B  240  LYS PHE LEU ASP GLU TYR GLN SER LYS VAL LYS ARG GLN          
SEQRES  18 B  240  ILE PHE SER GLY TYR GLN SER ASP ILE ASP THR HIS ASN          
SEQRES  19 B  240  ARG ILE LYS ASP GLU LEU                                      
SEQRES   1 J  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 J  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 J  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 J  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 J  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 J  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 J  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 J  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 K  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 K  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 K  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 K  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 K  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 K  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 K  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 K  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 L  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 L  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 L  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 L  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 L  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 L  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 L  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 L  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 M  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 M  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 M  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 M  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 M  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 M  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 M  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 M  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 N  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 N  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 N  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 N  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 N  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 N  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 N  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 N  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET    GAL  D 751      12                                                       
HET    GAL  J 752      12                                                       
HET     NA  A 241       1                                                       
HET     NA  B 241       1                                                       
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM      NA SODIUM ION                                                       
FORMUL  13  GAL    2(C6 H12 O6)                                                 
FORMUL  15   NA    2(NA 1+)                                                     
FORMUL  17  HOH   *748(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  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 ASN A  197  TYR A  226  1                                  30    
HELIX   12  12 ASP A  231  ILE A  236  1                                   6    
HELIX   13  13 ASN D    4  ALA D   10  1                                   7    
HELIX   14  14 SER D   60  THR D   78  1                                  19    
HELIX   15  15 ASN E    4  ALA E   10  1                                   7    
HELIX   16  16 SER E   60  GLU E   79  1                                  20    
HELIX   17  17 ASN F    4  ALA F   10  1                                   7    
HELIX   18  18 ILE F   58  GLU F   79  1                                  22    
HELIX   19  19 ASN G    4  GLU G   11  1                                   8    
HELIX   20  20 SER G   60  THR G   78  1                                  19    
HELIX   21  21 ASN H    4  ALA H   10  1                                   7    
HELIX   22  22 SER H   60  GLU H   79  1                                  20    
HELIX   23  23 PRO B   12  GLY B   20  1                                   9    
HELIX   24  24 ARG B   33  MET B   37  5                                   5    
HELIX   25  25 ASN B   40  GLY B   47  1                                   8    
HELIX   26  26 SER B   65  LEU B   77  1                                  13    
HELIX   27  27 VAL B   97  GLY B  102  1                                   6    
HELIX   28  28 ALA B  103  SER B  105  5                                   3    
HELIX   29  29 HIS B  107  GLN B  111  5                                   5    
HELIX   30  30 ARG B  146  ASN B  152  1                                   7    
HELIX   31  31 PRO B  157  ALA B  165  5                                   9    
HELIX   32  32 HIS B  171  GLU B  176  5                                   6    
HELIX   33  33 PRO B  178  HIS B  182  5                                   5    
HELIX   34  34 THR B  198  GLN B  227  1                                  30    
HELIX   35  35 ASN J    4  ALA J   10  1                                   7    
HELIX   36  36 SER J   60  GLU J   79  1                                  20    
HELIX   37  37 ASN K    4  GLU K   11  1                                   8    
HELIX   38  38 ILE K   58  THR K   78  1                                  21    
HELIX   39  39 ASN L    4  ALA L   10  1                                   7    
HELIX   40  40 SER L   60  GLU L   79  1                                  20    
HELIX   41  41 ASN M    4  GLU M   11  1                                   8    
HELIX   42  42 SER M   60  THR M   78  1                                  19    
HELIX   43  43 ASN N    4  ALA N   10  1                                   7    
HELIX   44  44 SER N   60  GLU N   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  VAL A 130   N  TYR A  83           
SHEET    4   A 4 VAL A 134  LEU A 135 -1  O  VAL A 134   N  HIS A 131           
SHEET    1   B 4 LYS A   4  ASP A   9  0                                        
SHEET    2   B 4 THR A  82  ALA A  89 -1  O  ILE A  88   N  LEU A   5           
SHEET    3   B 4 ILE A 124  HIS A 131 -1  O  VAL A 130   N  TYR A  83           
SHEET    4   B 4 HIS A 140  ARG A 141 -1  O  HIS A 140   N  TRP A 127           
SHEET    1   C 2 GLY A  21  LEU A  22  0                                        
SHEET    2   C 2 ILE A 119  PRO A 120 -1  O  ILE A 119   N  LEU A  22           
SHEET    1   D 3 TYR A  59  THR A  62  0                                        
SHEET    2   D 3 VAL A 113  LEU A 116 -1  O  ALA A 115   N  VAL A  60           
SHEET    3   D 3 MET A  94  ASN A  96 -1  N  PHE A  95   O  SER A 114           
SHEET    1   E 9 HIS F  94  ALA F 102  0                                        
SHEET    2   E 9 SER D  26  SER D  30 -1  N  TYR D  27   O  MET F 101           
SHEET    3   E 9 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    4   E 9 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN B  49           
SHEET    5   E 9 VAL D  82  TRP D  88 -1  N  CYS D  86   O  ALA D  97           
SHEET    6   E 9 THR D  15  ASP D  22 -1  N  HIS D  18   O  LEU D  85           
SHEET    7   E 9 VAL D  82  TRP D  88 -1  O  LEU D  85   N  HIS D  18           
SHEET    8   E 9 HIS D  94  ALA D 102 -1  O  ALA D  97   N  CYS D  86           
SHEET    1   F 8 SER E  26  SER E  30  0                                        
SHEET    2   F 8 MET E  37  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET    3   F 8 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET    4   F 8 HIS E  94  ALA E 102  1  O  ILE E  96   N  GLN E  49           
SHEET    5   F 8 VAL E  82  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET    6   F 8 THR E  15  ASP E  22 -1  N  HIS E  18   O  LEU E  85           
SHEET    7   F 8 VAL E  82  TRP E  88 -1  O  LEU E  85   N  HIS E  18           
SHEET    8   F 8 HIS E  94  ALA E 102 -1  O  ALA E  97   N  CYS E  86           
SHEET    1   G 8 SER D  26  SER D  30  0                                        
SHEET    2   G 8 MET D  37  THR D  41 -1  O  ILE D  39   N  THR D  28           
SHEET    3   G 8 THR D  47  VAL D  50 -1  O  PHE D  48   N  ILE D  40           
SHEET    4   G 8 HIS D  94  ALA D 102  1  O  ILE D  96   N  GLN D  49           
SHEET    5   G 8 VAL D  82  TRP D  88 -1  N  CYS D  86   O  ALA D  97           
SHEET    6   G 8 THR D  15  ASP D  22 -1  N  GLN D  16   O  VAL D  87           
SHEET    7   G 8 VAL D  82  TRP D  88 -1  O  VAL D  87   N  GLN D  16           
SHEET    8   G 8 HIS D  94  ALA D 102 -1  O  ALA D  97   N  CYS D  86           
SHEET    1   H 8 SER E  26  SER E  30  0                                        
SHEET    2   H 8 MET E  37  THR E  41 -1  O  ILE E  39   N  THR E  28           
SHEET    3   H 8 THR E  47  VAL E  50 -1  O  PHE E  48   N  ILE E  40           
SHEET    4   H 8 HIS E  94  MET E 101  1  O  ILE E  96   N  GLN E  49           
SHEET    5   H 8 LYS E  81  TRP E  88 -1  N  CYS E  86   O  ALA E  97           
SHEET    6   H 8 THR E  15  LYS E  23 -1  N  HIS E  18   O  LEU E  85           
SHEET    7   H 8 LYS E  81  TRP E  88 -1  O  LEU E  85   N  HIS E  18           
SHEET    8   H 8 HIS E  94  MET E 101 -1  O  ALA E  97   N  CYS E  86           
SHEET    1   I 8 SER F  26  SER F  30  0                                        
SHEET    2   I 8 ALA F  38  THR F  41 -1  O  ILE F  39   N  THR F  28           
SHEET    3   I 8 THR F  47  VAL F  50 -1  O  PHE F  48   N  ILE F  40           
SHEET    4   I 8 HIS F  94  ALA F 102  1  O  ILE F  96   N  GLN F  49           
SHEET    5   I 8 VAL F  82  TRP F  88 -1  N  CYS F  86   O  ALA F  97           
SHEET    6   I 8 THR F  15  ASP F  22 -1  N  HIS F  18   O  LEU F  85           
SHEET    7   I 8 VAL F  82  TRP F  88 -1  O  LEU F  85   N  HIS F  18           
SHEET    8   I 8 HIS F  94  ALA F 102 -1  O  ALA F  97   N  CYS F  86           
SHEET    1   J 4 LYS B   4  ASP B   9  0                                        
SHEET    2   J 4 THR B  82  ALA B  89 -1  O  ILE B  88   N  LEU B   5           
SHEET    3   J 4 ILE B 124  HIS B 131 -1  O  VAL B 130   N  TYR B  83           
SHEET    4   J 4 VAL B 134  LEU B 135 -1  O  VAL B 134   N  HIS B 131           
SHEET    1   K 4 LYS B   4  ASP B   9  0                                        
SHEET    2   K 4 THR B  82  ALA B  89 -1  O  ILE B  88   N  LEU B   5           
SHEET    3   K 4 ILE B 124  HIS B 131 -1  O  VAL B 130   N  TYR B  83           
SHEET    4   K 4 HIS B 140  ARG B 141 -1  O  HIS B 140   N  TRP B 127           
SHEET    1   L 2 GLY B  21  LEU B  22  0                                        
SHEET    2   L 2 ILE B 119  PRO B 120 -1  O  ILE B 119   N  LEU B  22           
SHEET    1   M 3 TYR B  59  THR B  62  0                                        
SHEET    2   M 3 VAL B 113  LEU B 116 -1  O  ALA B 115   N  VAL B  60           
SHEET    3   M 3 MET B  94  ASN B  96 -1  N  PHE B  95   O  SER B 114           
SHEET    1   N 9 HIS L  94  ALA L 102  0                                        
SHEET    2   N 9 SER H  26  SER H  30 -1  N  TYR H  27   O  MET L 101           
SHEET    3   N 9 ALA H  38  THR H  41 -1  O  ILE H  39   N  THR H  28           
SHEET    4   N 9 THR H  47  VAL H  50 -1  O  PHE H  48   N  ILE H  40           
SHEET    5   N 9 HIS H  94  ALA H 102  1  O  ILE H  96   N  GLN H  49           
SHEET    6   N 9 VAL H  82  TRP H  88 -1  N  CYS H  86   O  ALA H  97           
SHEET    7   N 9 THR H  15  ASP H  22 -1  N  GLN H  16   O  VAL H  87           
SHEET    8   N 9 VAL H  82  TRP H  88 -1  O  VAL H  87   N  GLN H  16           
SHEET    9   N 9 HIS H  94  ALA H 102 -1  O  ALA H  97   N  CYS H  86           
SHEET    1   O 8 SER K  26  SER K  30  0                                        
SHEET    2   O 8 ALA K  38  THR K  41 -1  O  ILE K  39   N  THR K  28           
SHEET    3   O 8 THR K  47  VAL K  50 -1  O  PHE K  48   N  ILE K  40           
SHEET    4   O 8 HIS K  94  ALA K 102  1  O  ILE K  96   N  GLN K  49           
SHEET    5   O 8 VAL K  82  TRP K  88 -1  N  CYS K  86   O  ALA K  97           
SHEET    6   O 8 THR K  15  ASP K  22 -1  N  HIS K  18   O  LEU K  85           
SHEET    7   O 8 VAL K  82  TRP K  88 -1  O  LEU K  85   N  HIS K  18           
SHEET    8   O 8 HIS K  94  ALA K 102 -1  O  ALA K  97   N  CYS K  86           
SHEET    1   P 8 SER J  26  SER J  30  0                                        
SHEET    2   P 8 MET J  37  THR J  41 -1  O  ILE J  39   N  THR J  28           
SHEET    3   P 8 THR J  47  VAL J  50 -1  O  PHE J  48   N  ILE J  40           
SHEET    4   P 8 HIS J  94  ALA J 102  1  O  ILE J  96   N  GLN J  49           
SHEET    5   P 8 VAL J  82  TRP J  88 -1  N  CYS J  86   O  ALA J  97           
SHEET    6   P 8 THR J  15  ASP J  22 -1  N  HIS J  18   O  LEU J  85           
SHEET    7   P 8 VAL J  82  TRP J  88 -1  O  LEU J  85   N  HIS J  18           
SHEET    8   P 8 HIS J  94  ALA J 102 -1  O  ALA J  97   N  CYS J  86           
SHEET    1   Q 8 SER K  26  SER K  30  0                                        
SHEET    2   Q 8 MET K  37  THR K  41 -1  O  ILE K  39   N  THR K  28           
SHEET    3   Q 8 THR K  47  VAL K  50 -1  O  PHE K  48   N  ILE K  40           
SHEET    4   Q 8 HIS K  94  ALA K 102  1  O  ILE K  96   N  GLN K  49           
SHEET    5   Q 8 VAL K  82  TRP K  88 -1  N  CYS K  86   O  ALA K  97           
SHEET    6   Q 8 THR K  15  ASP K  22 -1  N  ASP K  22   O  VAL K  82           
SHEET    7   Q 8 VAL K  82  TRP K  88 -1  O  VAL K  82   N  ASP K  22           
SHEET    8   Q 8 HIS K  94  ALA K 102 -1  O  ALA K  97   N  CYS K  86           
SHEET    1   R 8 SER L  26  SER L  30  0                                        
SHEET    2   R 8 ALA L  38  THR L  41 -1  O  ILE L  39   N  THR L  28           
SHEET    3   R 8 THR L  47  VAL L  50 -1  O  PHE L  48   N  ILE L  40           
SHEET    4   R 8 HIS L  94  ALA L 102  1  O  ILE L  96   N  GLN L  49           
SHEET    5   R 8 VAL L  82  TRP L  88 -1  N  CYS L  86   O  ALA L  97           
SHEET    6   R 8 THR L  15  ASP L  22 -1  N  GLN L  16   O  VAL L  87           
SHEET    7   R 8 VAL L  82  TRP L  88 -1  O  VAL L  87   N  GLN L  16           
SHEET    8   R 8 HIS L  94  ALA L 102 -1  O  ALA L  97   N  CYS L  86           
SSBOND   1 CYS A  187    CYS A  199                          1555   1555  2.06  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.03  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.05  
SSBOND   4 CYS H    9    CYS H   86                          1555   1555  2.06  
SSBOND   5 CYS B  187    CYS B  199                          1555   1555  2.05  
SSBOND   6 CYS K    9    CYS K   86                          1555   1555  2.05  
SSBOND   7 CYS L    9    CYS L   86                          1555   1555  2.07  
SSBOND   8 CYS M    9    CYS M   86                          1555   1555  2.06  
SSBOND   9 CYS N    9    CYS N   86                          1555   1555  2.96  
LINK        NA    NA A 241                 OG1 THR A  90     1555   1555  2.50  
LINK        NA    NA A 241                 O   ASN A   1     1555   1555  2.50  
LINK        NA    NA A 241                 O   THR A  90     1555   1555  2.54  
LINK        NA    NA A 241                 O   HOH A 262     1555   1555  2.42  
LINK        NA    NA A 241                 O   LEU A 153     1555   1555  2.33  
LINK        NA    NA A 241                 O   TYR A 150     1555   1555  2.32  
LINK        NA    NA B 241                 O   LEU B 153     1555   1555  2.36  
LINK        NA    NA B 241                 O   ASN B   1     1555   1555  2.53  
LINK        NA    NA B 241                 O   THR B  90     1555   1555  2.52  
LINK        NA    NA B 241                 O   HOH B 267     1555   1555  2.18  
LINK        NA    NA B 241                 O   TYR B 150     1555   1555  2.39  
LINK        NA    NA B 241                 OG1 THR B  90     1555   1555  2.48  
CISPEP   1 GLU A  177    PRO A  178          0         1.79                     
CISPEP   2 THR D   92    PRO D   93          0        -4.32                     
CISPEP   3 THR E   92    PRO E   93          0        -4.57                     
CISPEP   4 THR F   92    PRO F   93          0        -4.96                     
CISPEP   5 THR G   92    PRO G   93          0        -7.97                     
CISPEP   6 THR H   92    PRO H   93          0        -5.96                     
CISPEP   7 GLU B  177    PRO B  178          0         4.35                     
CISPEP   8 THR J   92    PRO J   93          0        -6.58                     
CISPEP   9 THR K   92    PRO K   93          0        -1.54                     
CISPEP  10 THR L   92    PRO L   93          0        -6.23                     
CISPEP  11 THR M   92    PRO M   93          0        -4.85                     
CISPEP  12 THR N   92    PRO N   93          0        -5.56                     
SITE     1 AC1  8 ASN D  14  GLU D  51  GLN D  56  GLN D  61                    
SITE     2 AC1  8 TRP D  88  ASN D  90  LYS D  91  HOH E 155                    
SITE     1 AC2  9 ASN J  14  GLU J  51  GLN J  56  HIS J  57                    
SITE     2 AC2  9 GLN J  61  TRP J  88  ASN J  90  LYS J  91                    
SITE     3 AC2  9 HOH K 116                                                     
SITE     1 AC3  5 ASN A   1  THR A  90  TYR A 150  LEU A 153                    
SITE     2 AC3  5 HOH A 262                                                     
SITE     1 AC4  5 ASN B   1  THR B  90  TYR B 150  LEU B 153                    
SITE     2 AC4  5 HOH B 267                                                     
CRYST1   59.931  108.230  122.976  90.00  95.89  90.00 P 1 21 1     20          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016686  0.000000  0.001722        0.00000                         
SCALE2      0.000000  0.009240  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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