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Database: PDB
Entry: 5LZH
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Original site: 5LZH 
HEADER    TOXIN                                   29-SEP-16   5LZH              
TITLE     CHOLERA TOXIN CLASSICAL B-PENTAMER IN COMPLEX WITH INHIBITOR PC262    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN B SUBUNIT;                             
COMPND   3 CHAIN: A, B, D;                                                      
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN B-SUBUNIT,CHOLERA ENTEROTOXIN SUBUNIT B,
COMPND   5 CHOLERA TOXIN B PROTEIN (CTB),CHOLERA TOXIN B SUBUNIT,CHOLERA TOXIN  
COMPND   6 BETA SUBUNIT,CHOLERA TOXIN SUBUNIT B,CHOLERAE TOXIN B SUBUNIT,CTXB;  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CHOLERA ENTEROTOXIN B SUBUNIT;                             
COMPND  10 CHAIN: C, E;                                                         
COMPND  11 SYNONYM: CHOLERA ENTEROTOXIN B-SUBUNIT,CHOLERA ENTEROTOXIN SUBUNIT B,
COMPND  12 CHOLERA TOXIN B PROTEIN (CTB),CHOLERA TOXIN B SUBUNIT,CHOLERA TOXIN  
COMPND  13 BETA SUBUNIT,CHOLERA TOXIN SUBUNIT B,CHOLERAE TOXIN B SUBUNIT,CTXB;  
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CTXB, EN12_07055, ERS013165_03981, ERS013197_06217,            
SOURCE   5 ERS013202_03762, ERS013206_03003, ERS013207_03244;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE  10 ORGANISM_TAXID: 666;                                                 
SOURCE  11 GENE: CTXB, EN12_07055, ERS013165_03981, ERS013197_06217,            
SOURCE  12 ERS013202_03762, ERS013206_03003, ERS013207_03244;                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CHOLERA TOXIN B-PENTAMER, INHIBITOR, TOXIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,T.MARTINSEN,U.KRENGEL                                   
REVDAT   2   07-JUN-17 5LZH    1       JRNL                                     
REVDAT   1   31-MAY-17 5LZH    0                                                
JRNL        AUTH   J.E.HEGGELUND,A.MACKENZIE,T.MARTINSEN,J.BENJAMIN HEIM,       
JRNL        AUTH 2 P.CHESHEV,A.BERNARDI,U.KRENGEL                               
JRNL        TITL   TOWARDS NEW CHOLERA PROPHYLACTICS AND TREATMENT: CRYSTAL     
JRNL        TITL 2 STRUCTURES OF BACTERIAL ENTEROTOXINS IN COMPLEX WITH GM1     
JRNL        TITL 3 MIMICS.                                                      
JRNL        REF    SCI REP                       V.   7  2326 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28539625                                                     
JRNL        DOI    10.1038/S41598-017-02179-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
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) : 1.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 73.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 128966                         
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6823                            
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) : 1.13                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 825                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 6.44                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.5810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4076                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 241                                     
REMARK   3   SOLVENT ATOMS            : 608                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.27000                                             
REMARK   3    B22 (A**2) : -0.90000                                             
REMARK   3    B33 (A**2) : 1.88000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.054         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.058         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.685         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4591 ; 0.027 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  4408 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6256 ; 2.501 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10221 ; 1.373 ; 3.017       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   558 ; 7.702 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   194 ;43.342 ;25.103       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   819 ;12.476 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;21.882 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   738 ; 0.155 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5023 ; 0.015 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   992 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2133 ; 0.791 ; 0.973       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2131 ; 0.780 ; 0.970       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2679 ; 1.143 ; 1.453       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2680 ; 1.144 ; 1.454       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2458 ; 1.223 ; 1.201       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2458 ; 1.223 ; 1.201       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3562 ; 1.841 ; 1.757       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5396 ; 4.634 ;14.184       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5396 ; 4.633 ;14.180       
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  : 5                                          
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   103                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8634   4.8089  11.7992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0095 T22:   0.0420                                     
REMARK   3      T33:   0.1369 T12:  -0.0070                                     
REMARK   3      T13:  -0.0137 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6541 L22:   0.6395                                     
REMARK   3      L33:   0.4269 L12:  -0.0680                                     
REMARK   3      L13:  -0.0576 L23:  -0.1133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0440 S12:   0.0604 S13:   0.0691                       
REMARK   3      S21:  -0.0379 S22:   0.0238 S23:   0.1708                       
REMARK   3      S31:  -0.0210 S32:  -0.0163 S33:   0.0202                       
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 :   B     1        B   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5319  18.5284  19.2258              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0038 T22:   0.0064                                     
REMARK   3      T33:   0.1452 T12:  -0.0005                                     
REMARK   3      T13:   0.0118 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1544 L22:   0.6539                                     
REMARK   3      L33:   0.4639 L12:   0.2851                                     
REMARK   3      L13:  -0.0403 L23:  -0.1902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0049 S12:   0.0014 S13:   0.2555                       
REMARK   3      S21:  -0.0037 S22:   0.0248 S23:   0.1745                       
REMARK   3      S31:  -0.0153 S32:  -0.0359 S33:  -0.0199                       
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 :   C     1        C   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9495   6.5360  27.0954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0103 T22:   0.0689                                     
REMARK   3      T33:   0.0368 T12:  -0.0115                                     
REMARK   3      T13:   0.0148 T23:  -0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3068 L22:   0.9407                                     
REMARK   3      L33:   0.1175 L12:   0.0975                                     
REMARK   3      L13:   0.0922 L23:   0.0467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0236 S12:  -0.1724 S13:   0.0612                       
REMARK   3      S21:   0.0223 S22:  -0.0156 S23:  -0.0260                       
REMARK   3      S31:  -0.0185 S32:  -0.0036 S33:  -0.0080                       
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 :   D     1        D   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7589 -14.5302  24.6783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0192 T22:   0.0479                                     
REMARK   3      T33:   0.1336 T12:  -0.0055                                     
REMARK   3      T13:  -0.0039 T23:   0.0389                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5280 L22:   0.8979                                     
REMARK   3      L33:   0.3297 L12:   0.3473                                     
REMARK   3      L13:   0.2763 L23:   0.2994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0723 S12:  -0.1236 S13:  -0.3679                       
REMARK   3      S21:   0.0734 S22:  -0.0278 S23:  -0.0772                       
REMARK   3      S31:  -0.0049 S32:  -0.0009 S33:  -0.0446                       
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 :   E     1        E   103                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8147 -15.7068  14.9395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0032 T22:   0.0336                                     
REMARK   3      T33:   0.0877 T12:  -0.0022                                     
REMARK   3      T13:   0.0159 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4888 L22:   0.8769                                     
REMARK   3      L33:   0.2474 L12:   0.7309                                     
REMARK   3      L13:   0.2832 L23:   0.1464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0077 S12:   0.0797 S13:  -0.0822                       
REMARK   3      S21:   0.0071 S22:   0.0064 S23:   0.0337                       
REMARK   3      S31:   0.0063 S32:  -0.0029 S33:   0.0014                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5LZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001379.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-15                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.991872                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135800                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 73.7                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 13.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.730                              
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: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOLE PH 6.5, 8%           
REMARK 280  PEG1000, 8% PEG 3350, 8% MPD, 0.03 M DIVALENT CATIONS, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.86800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.86800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.03150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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   OD   CSX B     9     SG   CSX B    86              1.84            
REMARK 500   OD   CSX D     9     SG   CSX D    86              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   384     O    HOH D   384     2556     1.05            
REMARK 500  CA     CA E   203    CA     CA E   203     2556     1.63            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  83   CD    GLU A  83   OE1     0.073                       
REMARK 500    TYR B  27   CE1   TYR B  27   CZ     -0.096                       
REMARK 500    SER C  30   CA    SER C  30   CB      0.092                       
REMARK 500    GLU D  29   CB    GLU D  29   CG     -0.136                       
REMARK 500    SER D  55   CB    SER D  55   OG     -0.103                       
REMARK 500    GLU E  83   CD    GLU E  83   OE2     0.089                       
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  22   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A  67   CG  -  CD  -  NE  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    MET A 101   CG  -  SD  -  CE  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ARG B  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    GLU C  29   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG C  67   CG  -  CD  -  NE  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    ARG C  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP D  22   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP D  22   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LYS D  62   CD  -  CE  -  NZ  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    ASP D  70   CB  -  CG  -  OD2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP E  22   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  34       -3.22     77.52                                   
REMARK 500    GLU A  83      -74.02    -79.09                                   
REMARK 500    ASN B  14       34.66     70.11                                   
REMARK 500    ASN C  21       52.89     37.80                                   
REMARK 500    ASN C  44        3.85    -68.65                                   
REMARK 500    LYS E  34       -1.17     76.13                                   
REMARK 500    GLU E  83      -71.60    -80.19                                   
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 GLN B   49     VAL B   50                  149.48                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLU D  29         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE1                                                    
REMARK 620 2 GLU C  79   OE1  27.1                                              
REMARK 620 3 GLU C  79   OE2  45.9  30.5                                        
REMARK 620 4 GLU B  79   OE1  87.9 102.3  81.7                                  
REMARK 620 5 HOH B 303   O    57.2  83.4  86.7  49.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  79   OE2                                                    
REMARK 620 2 HOH C 347   O    64.0                                              
REMARK 620 3 GLU B  79   OE1 128.1  77.6                                        
REMARK 620 4 GLU B  79   OE1 128.0  76.0   2.3                                  
REMARK 620 5 GLU B  79   OE2 137.4  81.8  10.4   9.7                            
REMARK 620 6 GLU B  79   OE2 137.4  83.9   9.4   9.5   3.3                      
REMARK 620 7 HOH B 303   O    66.0 129.4 144.6 146.9 145.5 142.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 321   O                                                      
REMARK 620 2 HOH D 321   O   137.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BO A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BO B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BO C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BO D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BO E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203                  
DBREF  5LZH A    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5LZH B    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5LZH C    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5LZH D    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
DBREF  5LZH E    1   103  UNP    Q57193   Q57193_VIBCL    22    124             
SEQRES   1 A  103  THR PRO GLN ASN ILE THR ASP LEU CSX ALA GLU TYR HIS          
SEQRES   2 A  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 A  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 A  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 A  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 A  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 A  103  GLU ALA LYS VAL GLU LYS LEU CSX VAL TRP ASN ASN LYS          
SEQRES   8 A  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 B  103  THR PRO GLN ASN ILE THR ASP LEU CSX ALA GLU TYR HIS          
SEQRES   2 B  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 B  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 B  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 B  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 B  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 B  103  GLU ALA LYS VAL GLU LYS LEU CSX VAL TRP ASN ASN LYS          
SEQRES   8 B  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 C  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 C  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 C  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 C  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 C  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 C  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 C  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 C  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CSX 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 CSX 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              
MODRES 5LZH CSX A    9  CYS  MODIFIED RESIDUE                                   
MODRES 5LZH CSX A   86  CYS  MODIFIED RESIDUE                                   
MODRES 5LZH CSX B    9  CYS  MODIFIED RESIDUE                                   
MODRES 5LZH CSX B   86  CYS  MODIFIED RESIDUE                                   
MODRES 5LZH CSX D    9  CYS  MODIFIED RESIDUE                                   
MODRES 5LZH CSX D   86  CYS  MODIFIED RESIDUE                                   
HET    CSX  A   9       7                                                       
HET    CSX  A  86       7                                                       
HET    CSX  B   9       7                                                       
HET    CSX  B  86       7                                                       
HET    CSX  D   9       7                                                       
HET    CSX  D  86       7                                                       
HET    7BO  A 201      43                                                       
HET    7BO  B 201      43                                                       
HET    MRD  B 202       8                                                       
HET    7BO  C 201      43                                                       
HET     CA  C 202       1                                                       
HET     CA  C 203       1                                                       
HET    7BO  D 201      43                                                       
HET    TRS  D 202       8                                                       
HET    7BO  E 201      43                                                       
HET    PEG  E 202       7                                                       
HET     CA  E 203       1                                                       
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM     7BO (2~{R},4~{S},5~{R},6~{R})-5-ACETAMIDO-2-[4-[3-[2-                
HETNAM   2 7BO  [(2~{S},3~{R},4~{R},5~{R},6~{R})-6-(HYDROXYMETHYL)-3,           
HETNAM   3 7BO  4,5-TRIS(OXIDANYL)OXAN-2-YL]ETHYLAMINO]-3-                      
HETNAM   4 7BO  OXIDANYLIDENE-PROPYL]-1,2,3-TRIAZOL-1-YL]-4-OXIDANYL-           
HETNAM   5 7BO  6-[(1~{R},2~{R})-1,2,3-TRIS(OXIDANYL)PROPYL]OXANE-2-            
HETNAM   6 7BO  CARBOXYLIC ACID                                                 
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   1  CSX    6(C3 H7 N O3 S)                                              
FORMUL   6  7BO    5(C24 H39 N5 O14)                                            
FORMUL   8  MRD    C6 H14 O2                                                    
FORMUL  10   CA    3(CA 2+)                                                     
FORMUL  13  TRS    C4 H12 N O3 1+                                               
FORMUL  15  PEG    C4 H10 O3                                                    
FORMUL  17  HOH   *608(H2 O)                                                    
HELIX    1   1 ASP A   59  THR A   78  1                                  20    
HELIX    2   2 ASP B   59  THR B   78  1                                  20    
HELIX    3   3 ILE C    5  GLU C   11  1                                   7    
HELIX    4   4 ASP C   59  LEU C   77  5                                  19    
HELIX    5   5 ASP D   59  THR D   78  5                                  20    
HELIX    6   6 ILE E    5  GLU E   11  1                                   7    
HELIX    7   7 ASP E   59  THR E   78  1                                  20    
SHEET    1   A 3 SER A  26  SER A  30  0                                        
SHEET    2   A 3 MET A  37  THR A  41 -1  N  THR A  41   O  SER A  26           
SHEET    3   A 3 THR A  47  VAL A  50 -1  N  VAL A  50   O  ALA A  38           
SHEET    1   B 3 SER B  26  SER B  30  0                                        
SHEET    2   B 3 MET B  37  THR B  41 -1  N  THR B  41   O  SER B  26           
SHEET    3   B 3 THR B  47  VAL B  50 -1  N  VAL B  50   O  ALA B  38           
SHEET    1   C 3 THR C  15  THR C  19  0                                        
SHEET    2   C 3 VAL C  82  TRP C  88 -1  N  VAL C  87   O  GLN C  16           
SHEET    3   C 3 ALA C  98  MET C 101 -1  N  SER C 100   O  GLU C  83           
SHEET    1   D 3 SER C  26  SER C  30  0                                        
SHEET    2   D 3 MET C  37  THR C  41 -1  N  THR C  41   O  SER C  26           
SHEET    3   D 3 THR C  47  VAL C  50 -1  N  VAL C  50   O  ALA C  38           
SHEET    1   E 3 SER D  26  SER D  30  0                                        
SHEET    2   E 3 MET D  37  THR D  41 -1  N  THR D  41   O  SER D  26           
SHEET    3   E 3 THR D  47  VAL D  50 -1  N  VAL D  50   O  ALA D  38           
SHEET    1   F 3 THR E  15  THR E  19  0                                        
SHEET    2   F 3 VAL E  82  TRP E  88 -1  N  VAL E  87   O  GLN E  16           
SHEET    3   F 3 ALA E  98  MET E 101 -1  N  SER E 100   O  GLU E  83           
SHEET    1   G 3 SER E  26  SER E  30  0                                        
SHEET    2   G 3 MET E  37  THR E  41 -1  N  THR E  41   O  SER E  26           
SHEET    3   G 3 THR E  47  VAL E  50 -1  N  VAL E  50   O  ALA E  38           
SSBOND   1 CSX A    9    CSX A   86                          1555   1555  2.04  
SSBOND   2 CSX B    9    CSX B   86                          1555   1555  2.08  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.06  
SSBOND   4 CSX D    9    CSX D   86                          1555   1555  2.06  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.05  
LINK         C   LEU A   8                 N   CSX A   9     1555   1555  1.35  
LINK         C   CSX A   9                 N   ALA A  10     1555   1555  1.34  
LINK         C   LEU A  85                 N   CSX A  86     1555   1555  1.32  
LINK         C   CSX A  86                 N   VAL A  87     1555   1555  1.33  
LINK         C   LEU B   8                 N   CSX B   9     1555   1555  1.31  
LINK         C   CSX B   9                 N   ALA B  10     1555   1555  1.32  
LINK         C   LEU B  85                 N   CSX B  86     1555   1555  1.34  
LINK         C   CSX B  86                 N   VAL B  87     1555   1555  1.32  
LINK         OE1AGLU C  79                CA    CA C 202     1555   1555  2.94  
LINK         OE1BGLU C  79                CA    CA C 202     1555   1555  2.59  
LINK         OE2AGLU C  79                CA    CA C 202     1555   1555  2.57  
LINK         OE2BGLU C  79                CA    CA C 203     1555   1555  2.54  
LINK         C  ALEU D   8                 N   CSX D   9     1555   1555  1.34  
LINK         C  BLEU D   8                 N   CSX D   9     1555   1555  1.34  
LINK         C   CSX D   9                 N   ALA D  10     1555   1555  1.34  
LINK         C   LEU D  85                 N   CSX D  86     1555   1555  1.35  
LINK         C   CSX D  86                 N   VAL D  87     1555   1555  1.33  
LINK        CA    CA C 203                 O   HOH C 347     1555   1555  2.67  
LINK        CA    CA E 203                 O   HOH D 321     1555   1555  2.40  
LINK         OE1AGLU B  79                CA    CA C 203     1555   2556  2.85  
LINK         OE1BGLU B  79                CA    CA C 202     1555   2556  2.60  
LINK         OE1BGLU B  79                CA    CA C 203     1555   2556  3.19  
LINK         OE2AGLU B  79                CA    CA C 203     1555   2556  3.13  
LINK         OE2BGLU B  79                CA    CA C 203     1555   2556  2.62  
LINK        CA    CA C 202                 O   HOH B 303     1555   2556  2.06  
LINK        CA    CA C 203                 O   HOH B 303     1555   2556  2.07  
LINK        CA    CA E 203                 O   HOH D 321     1555   2556  2.26  
CISPEP   1 THR A   92    PRO A   93          0       -12.28                     
CISPEP   2 THR B   92    PRO B   93          0       -13.07                     
CISPEP   3 THR C   92    PRO C   93          0       -10.62                     
CISPEP   4 THR D   92    PRO D   93          0       -10.31                     
CISPEP   5 THR D   92    PRO D   93          0        -4.98                     
CISPEP   6 THR E   92    PRO E   93          0        -8.40                     
CISPEP   7 THR E   92    PRO E   93          0       -13.81                     
SITE     1 AC1 22 GLU A  11  TYR A  12  HIS A  13  GLU A  51                    
SITE     2 AC1 22 GLN A  56  HIS A  57  ILE A  58  GLN A  61                    
SITE     3 AC1 22 TRP A  88  ASN A  90  LYS A  91  HOH A 311                    
SITE     4 AC1 22 HOH A 316  HOH A 323  HOH A 331  HOH A 350                    
SITE     5 AC1 22 HOH A 358  HOH A 367  HOH A 369  HOH A 372                    
SITE     6 AC1 22 GLY B  33  HOH C 321                                          
SITE     1 AC2 22 GLU B  11  TYR B  12  HIS B  13  GLU B  51                    
SITE     2 AC2 22 GLN B  56  HIS B  57  ILE B  58  GLN B  61                    
SITE     3 AC2 22 TRP B  88  ASN B  90  LYS B  91  HOH B 314                    
SITE     4 AC2 22 HOH B 318  HOH B 323  HOH B 325  HOH B 337                    
SITE     5 AC2 22 HOH B 338  HOH B 345  HOH B 356  HOH B 368                    
SITE     6 AC2 22 HOH B 371  GLY C  33                                          
SITE     1 AC3  6 HIS B  13  ALA D  10  GLU D  11  TYR D  12                    
SITE     2 AC3  6 HIS D  13  7BO D 201                                          
SITE     1 AC4 23 GLU C  11  TYR C  12  HIS C  13  GLU C  51                    
SITE     2 AC4 23 GLN C  56  GLN C  61  TRP C  88  ASN C  90                    
SITE     3 AC4 23 LYS C  91  HOH C 310  HOH C 311  HOH C 324                    
SITE     4 AC4 23 HOH C 331  HOH C 332  HOH C 333  HOH C 334                    
SITE     5 AC4 23 HOH C 344  HOH C 349  HOH C 354  HOH C 361                    
SITE     6 AC4 23 HOH C 367  GLY D  33  LYS D  34                               
SITE     1 AC5  3 GLU B  79  HOH B 303  GLU C  79                               
SITE     1 AC6  4 GLU B  79  HOH B 303  GLU C  79  HOH C 347                    
SITE     1 AC7 22 HOH A 356  MRD B 202  HOH B 350  GLU D  11                    
SITE     2 AC7 22 TYR D  12  HIS D  13  GLU D  51  GLN D  56                    
SITE     3 AC7 22 GLN D  61  TRP D  88  ASN D  90  LYS D  91                    
SITE     4 AC7 22 HOH D 303  HOH D 324  HOH D 329  HOH D 338                    
SITE     5 AC7 22 HOH D 340  HOH D 347  HOH D 348  HOH D 360                    
SITE     6 AC7 22 HOH D 370  GLY E  33                                          
SITE     1 AC8  6 THR D  78  ASN D 103  HOH D 321  HOH D 341                    
SITE     2 AC8  6 TYR E  76  LEU E  77                                          
SITE     1 AC9 24 GLY A  33  LYS A  34  ILE D  58  GLU E  11                    
SITE     2 AC9 24 TYR E  12  HIS E  13  GLU E  51  GLN E  56                    
SITE     3 AC9 24 HIS E  57  ILE E  58  GLN E  61  TRP E  88                    
SITE     4 AC9 24 ASN E  90  LYS E  91  HOH E 304  HOH E 307                    
SITE     5 AC9 24 HOH E 313  HOH E 318  HOH E 325  HOH E 330                    
SITE     6 AC9 24 HOH E 339  HOH E 362  HOH E 371  HOH E 374                    
SITE     1 AD1  4 THR E  41  PHE E  42  GLY E  45  HOH E 397                    
SITE     1 AD2  2 HOH D 321  GLU E  79                                          
CRYST1  101.736   66.063   76.389  90.00 105.67  90.00 C 1 2 1      12          
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      0.009829  0.000000  0.002756        0.00000                         
SCALE2      0.000000  0.015137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013596        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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