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Database: PDB
Entry: 5LZG
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HEADER    TOXIN                                   29-SEP-16   5LZG              
TITLE     CHOLERA TOXIN EL TOR B-PENTAMER IN COMPLEX WITH INHIBITOR PC262       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA ENTEROTOXIN SUBUNIT B;                             
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: CHOLERA ENTEROTOXIN B CHAIN,CHOLERA ENTEROTOXIN GAMMA CHAIN,
COMPND   5 CHOLERAGENOID;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 STRAIN: ATCC 39315 / EL TOR INABA N16961;                            
SOURCE   6 GENE: CTXB, TOXB, VC_1456;                                           
SOURCE   7 EXPRESSION_SYSTEM: VIBRIO SP.;                                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 678                                         
KEYWDS    CHOLERA TOXIN B-PENTAMER, INHIBITOR, TOXIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.HEGGELUND,T.MARTINSEN,U.KRENGEL                                   
REVDAT   2   07-JUN-17 5LZG    1       JRNL                                     
REVDAT   1   31-MAY-17 5LZG    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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 132437                         
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6982                            
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) : 783                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 5.93                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 33                           
REMARK   3   BIN FREE R VALUE                    : 0.4130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4085                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 248                                     
REMARK   3   SOLVENT ATOMS            : 575                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.79000                                             
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : 1.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.24000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.047         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.049         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.431         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4569 ; 0.019 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  4393 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6218 ; 1.899 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10173 ; 1.258 ; 3.017       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 7.102 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   199 ;42.016 ;25.126       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   816 ;11.485 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.864 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   728 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4988 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   996 ; 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):  2103 ; 0.686 ; 0.837       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2101 ; 0.662 ; 0.834       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2632 ; 1.088 ; 1.247       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2633 ; 1.089 ; 1.248       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2466 ; 1.025 ; 1.092       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2467 ; 1.025 ; 1.093       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3571 ; 1.590 ; 1.589       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5237 ; 4.213 ;12.249       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5238 ; 4.213 ;12.256       
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): -18.9508   4.7725  11.7798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0362 T22:   0.0304                                     
REMARK   3      T33:   0.1647 T12:  -0.0037                                     
REMARK   3      T13:  -0.0746 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8625 L22:   0.7113                                     
REMARK   3      L33:   0.4998 L12:   0.0502                                     
REMARK   3      L13:   0.2136 L23:  -0.0595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0818 S12:   0.0658 S13:   0.1727                       
REMARK   3      S21:  -0.0473 S22:   0.0353 S23:   0.1716                       
REMARK   3      S31:  -0.0123 S32:   0.0057 S33:   0.0465                       
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):  -3.5539  18.6030  19.2077              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0446 T22:   0.0044                                     
REMARK   3      T33:   0.2340 T12:   0.0054                                     
REMARK   3      T13:  -0.0925 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6580 L22:   0.8164                                     
REMARK   3      L33:   0.3917 L12:   0.5015                                     
REMARK   3      L13:   0.2146 L23:  -0.0981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1135 S12:  -0.0088 S13:   0.4036                       
REMARK   3      S21:  -0.0157 S22:   0.0297 S23:   0.1568                       
REMARK   3      S31:  -0.0601 S32:  -0.0315 S33:   0.0838                       
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):  12.9918   6.5841  27.2379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0382 T22:   0.0406                                     
REMARK   3      T33:   0.1031 T12:  -0.0091                                     
REMARK   3      T13:  -0.0568 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1146 L22:   0.6812                                     
REMARK   3      L33:   0.3225 L12:   0.2720                                     
REMARK   3      L13:   0.0664 L23:   0.1845                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0048 S12:  -0.1136 S13:   0.0992                       
REMARK   3      S21:  -0.0086 S22:  -0.0247 S23:  -0.0079                       
REMARK   3      S31:  -0.0220 S32:   0.0022 S33:   0.0199                       
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):   7.8041 -14.5912  24.7914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0307 T22:   0.0178                                     
REMARK   3      T33:   0.1119 T12:  -0.0023                                     
REMARK   3      T13:  -0.0497 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9109 L22:   0.7681                                     
REMARK   3      L33:   0.3625 L12:   0.1990                                     
REMARK   3      L13:   0.2365 L23:   0.2557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:  -0.1259 S13:  -0.2696                       
REMARK   3      S21:   0.0452 S22:  -0.0009 S23:  -0.0536                       
REMARK   3      S31:   0.0177 S32:   0.0089 S33:  -0.0267                       
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): -11.8495 -15.7968  15.1420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.0194                                     
REMARK   3      T33:   0.1088 T12:  -0.0042                                     
REMARK   3      T13:  -0.0497 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6394 L22:   0.6481                                     
REMARK   3      L33:   0.3117 L12:   0.3489                                     
REMARK   3      L13:   0.2340 L23:   0.1323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:   0.0748 S13:  -0.1637                       
REMARK   3      S21:  -0.0213 S22:   0.0065 S23:   0.0194                       
REMARK   3      S31:   0.0069 S32:   0.0092 S33:  -0.0101                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5LZG 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_1200001378.                                   
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   : 139423                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 13.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.700                              
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   (%): 42.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOLE BUFFER, PH 6.5,      
REMARK 280  10% PEG 1000, 10 % PEG 3350, 10 % MPD, 0.03 M DIVALENT CATIONS,     
REMARK 280  VAPOR 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       50.94000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.14550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.94000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.14550            
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: 14030 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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   OD1  ASP A    70     NH1  ARG E    67              2.12            
REMARK 500   NH1  ARG C    67     OD1  ASP D    70              2.14            
REMARK 500   NH1  ARG D    67     OD1  ASP E    70              2.17            
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    TYR B  27   CE1   TYR B  27   CZ     -0.079                       
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    ARG A  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG C  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG D  67   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG E  35   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG E  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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       -4.72     78.21                                   
REMARK 500    PRO A  93      154.97    -49.75                                   
REMARK 500    LYS B  34       -1.11     76.52                                   
REMARK 500    ASN C  21       52.05     39.76                                   
REMARK 500    LYS C  34       -0.23     75.93                                   
REMARK 500    GLU C  83      -70.94    -82.71                                   
REMARK 500    GLU D  83      -70.73    -82.18                                   
REMARK 500    LYS E  34       -2.73     77.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BN A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BN C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BN D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7BN E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD E 202                 
DBREF  5LZG A    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZG B    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZG C    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZG D    1   103  UNP    P01556   CHTB_VIBCH      22    124             
DBREF  5LZG E    1   103  UNP    P01556   CHTB_VIBCH      22    124             
SEQRES   1 A  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 A  103  ASN THR GLN ILE TYR 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 ILE 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 CYS 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 CYS ALA GLU TYR HIS          
SEQRES   2 B  103  ASN THR GLN ILE TYR 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 ILE 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 CYS 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 TYR 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 ILE 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 CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE TYR 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 ILE 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 TYR 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 ILE 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              
HET    7BN  A 201      43                                                       
HET    TRS  A 202       8                                                       
HET    IMD  A 203       5                                                       
HET    7BN  B 201      43                                                       
HET    7BN  C 201      43                                                       
HET    PEG  C 202       7                                                       
HET    7BN  D 201      43                                                       
HET    IMD  D 202       5                                                       
HET    7BN  E 201      43                                                       
HET    MRD  E 202       8                                                       
HETNAM     7BN (2~{R},4~{S},5~{R},6~{R})-5-ACETAMIDO-2-[4-[3-[2-                
HETNAM   2 7BN  [(2~{S},3~{R},4~{R},5~{R},6~{R})-6-(HYDROXYMETHYL)-3,           
HETNAM   3 7BN  4,5-TRIS(OXIDANYL)OXAN-2-YL]ETHYLAMINO]-3-                      
HETNAM   4 7BN  OXIDANYLIDENE-PROPYL]-1,2,3-TRIAZOL-1-YL]-4-OXIDANYL-           
HETNAM   5 7BN  6-[(1~{R},2~{R})-1,2,3-TRIS(OXIDANYL)PROPYL]OXANE-2-            
HETNAM   6 7BN  CARBOXYLIC ACID                                                 
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   6  7BN    5(C24 H39 N5 O14)                                            
FORMUL   7  TRS    C4 H12 N O3 1+                                               
FORMUL   8  IMD    2(C3 H5 N2 1+)                                               
FORMUL  11  PEG    C4 H10 O3                                                    
FORMUL  15  MRD    C6 H14 O2                                                    
FORMUL  16  HOH   *575(H2 O)                                                    
HELIX    1   1 ILE A    5  GLU A   11  1                                   7    
HELIX    2   2 ASP A   59  THR A   78  5                                  20    
HELIX    3   3 ILE B    5  GLU B   11  1                                   7    
HELIX    4   4 ASP B   59  LEU B   77  5                                  19    
HELIX    5   5 ILE C    5  GLU C   11  1                                   7    
HELIX    6   6 ASP C   59  THR C   78  5                                  20    
HELIX    7   7 ILE D    5  GLU D   11  1                                   7    
HELIX    8   8 ASP D   59  THR D   78  5                                  20    
HELIX    9   9 ILE E    5  GLU E   11  1                                   7    
HELIX   10  10 ASP E   59  THR E   78  5                                  20    
SHEET    1   A 3 THR A  15  THR A  19  0                                        
SHEET    2   A 3 VAL A  82  TRP A  88 -1  N  VAL A  87   O  GLN A  16           
SHEET    3   A 3 ALA A  98  MET A 101 -1  N  SER A 100   O  GLU A  83           
SHEET    1   B 3 SER A  26  SER A  30  0                                        
SHEET    2   B 3 MET A  37  THR A  41 -1  N  THR A  41   O  SER A  26           
SHEET    3   B 3 ILE A  47  VAL A  50 -1  N  VAL A  50   O  ALA A  38           
SHEET    1   C 3 THR B  15  THR B  19  0                                        
SHEET    2   C 3 VAL B  82  TRP B  88 -1  N  VAL B  87   O  GLN B  16           
SHEET    3   C 3 ALA B  98  MET B 101 -1  N  SER B 100   O  GLU B  83           
SHEET    1   D 3 SER B  26  SER B  30  0                                        
SHEET    2   D 3 MET B  37  THR B  41 -1  N  THR B  41   O  SER B  26           
SHEET    3   D 3 ILE B  47  VAL B  50 -1  N  VAL B  50   O  ALA B  38           
SHEET    1   E 3 THR C  15  THR C  19  0                                        
SHEET    2   E 3 VAL C  82  TRP C  88 -1  N  VAL C  87   O  GLN C  16           
SHEET    3   E 3 ALA C  98  MET C 101 -1  N  SER C 100   O  GLU C  83           
SHEET    1   F 3 SER C  26  SER C  30  0                                        
SHEET    2   F 3 MET C  37  THR C  41 -1  N  THR C  41   O  SER C  26           
SHEET    3   F 3 ILE C  47  VAL C  50 -1  N  VAL C  50   O  ALA C  38           
SHEET    1   G 3 THR D  15  THR D  19  0                                        
SHEET    2   G 3 VAL D  82  TRP D  88 -1  N  VAL D  87   O  GLN D  16           
SHEET    3   G 3 ALA D  98  MET D 101 -1  N  SER D 100   O  GLU D  83           
SHEET    1   H 3 SER D  26  SER D  30  0                                        
SHEET    2   H 3 MET D  37  THR D  41 -1  N  THR D  41   O  SER D  26           
SHEET    3   H 3 ILE D  47  VAL D  50 -1  N  VAL D  50   O  ALA D  38           
SHEET    1   I 3 THR E  15  THR E  19  0                                        
SHEET    2   I 3 VAL E  82  TRP E  88 -1  N  VAL E  87   O  GLN E  16           
SHEET    3   I 3 ALA E  98  MET E 101 -1  N  SER E 100   O  GLU E  83           
SHEET    1   J 3 SER E  26  SER E  30  0                                        
SHEET    2   J 3 MET E  37  THR E  41 -1  N  THR E  41   O  SER E  26           
SHEET    3   J 3 ILE E  47  VAL E  50 -1  N  VAL E  50   O  ALA E  38           
SSBOND   1 CYS A    9    CYS A   86                          1555   1555  2.05  
SSBOND   2 CYS B    9    CYS B   86                          1555   1555  2.06  
SSBOND   3 CYS C    9    CYS C   86                          1555   1555  2.08  
SSBOND   4 CYS D    9    CYS D   86                          1555   1555  2.05  
SSBOND   5 CYS E    9    CYS E   86                          1555   1555  2.05  
CISPEP   1 THR A   92    PRO A   93          0       -15.35                     
CISPEP   2 THR B   92    PRO B   93          0       -13.83                     
CISPEP   3 THR C   92    PRO C   93          0        -1.54                     
CISPEP   4 THR D   92    PRO D   93          0        -2.68                     
CISPEP   5 THR D   92    PRO D   93          0       -13.34                     
CISPEP   6 THR E   92    PRO E   93          0       -14.79                     
SITE     1 AC1 24 GLU A  11  TYR A  12  HIS A  13  GLU A  51                    
SITE     2 AC1 24 GLN A  56  HIS A  57  ILE A  58  GLN A  61                    
SITE     3 AC1 24 TRP A  88  ASN A  90  LYS A  91  IMD A 203                    
SITE     4 AC1 24 HOH A 323  HOH A 339  HOH A 346  HOH A 348                    
SITE     5 AC1 24 HOH A 350  HOH A 356  HOH A 357  HOH A 366                    
SITE     6 AC1 24 HOH A 375  GLY B  33  LYS B  34  HOH C 314                    
SITE     1 AC2  8 TYR A  76  LEU A  77  GLU A  79  HOH A 304                    
SITE     2 AC2  8 HOH A 314  THR E  78  GLU E  79  ALA E  80                    
SITE     1 AC3  3 ALA A  10  GLU A  11  7BN A 201                               
SITE     1 AC4 20 GLU B  11  TYR B  12  HIS B  13  GLU B  51                    
SITE     2 AC4 20 GLN B  56  HIS B  57  ILE B  58  GLN B  61                    
SITE     3 AC4 20 TRP B  88  ASN B  90  LYS B  91  HOH B 308                    
SITE     4 AC4 20 HOH B 309  HOH B 316  HOH B 331  HOH B 339                    
SITE     5 AC4 20 HOH B 345  HOH B 373  GLY C  33  HOH C 362                    
SITE     1 AC5 26 GLU C  11  TYR C  12  HIS C  13  GLU C  51                    
SITE     2 AC5 26 GLN C  56  HIS C  57  ILE C  58  GLN C  61                    
SITE     3 AC5 26 TRP C  88  ASN C  90  LYS C  91  PEG C 202                    
SITE     4 AC5 26 HOH C 312  HOH C 316  HOH C 319  HOH C 330                    
SITE     5 AC5 26 HOH C 335  HOH C 337  HOH C 346  HOH C 353                    
SITE     6 AC5 26 HOH C 364  HOH C 368  HOH C 386  GLY D  33                    
SITE     7 AC5 26 HOH D 373  TYR E  18                                          
SITE     1 AC6  5 ALA C  10  GLU C  11  TYR C  12  HIS C  13                    
SITE     2 AC6  5 7BN C 201                                                     
SITE     1 AC7 23 TYR A  18  GLU D  11  TYR D  12  HIS D  13                    
SITE     2 AC7 23 GLU D  51  GLN D  56  ILE D  58  GLN D  61                    
SITE     3 AC7 23 TRP D  88  ASN D  90  LYS D  91  HOH D 305                    
SITE     4 AC7 23 HOH D 308  HOH D 322  HOH D 324  HOH D 325                    
SITE     5 AC7 23 HOH D 329  HOH D 335  HOH D 350  HOH D 351                    
SITE     6 AC7 23 HOH D 372  GLY E  33  HOH E 373                               
SITE     1 AC8  4 HIS B  13  ALA D  10  HIS D  13  HOH D 354                    
SITE     1 AC9 23 GLY A  33  LYS A  34  GLU E  11  TYR E  12                    
SITE     2 AC9 23 HIS E  13  GLU E  51  GLN E  56  HIS E  57                    
SITE     3 AC9 23 ILE E  58  GLN E  61  TRP E  88  ASN E  90                    
SITE     4 AC9 23 LYS E  91  HOH E 301  HOH E 303  HOH E 306                    
SITE     5 AC9 23 HOH E 309  HOH E 312  HOH E 321  HOH E 326                    
SITE     6 AC9 23 HOH E 360  HOH E 372  HOH E 393                               
SITE     1 AD1  3 LEU E  77  HOH E 305  HOH E 331                               
CRYST1  101.880   66.291   77.407  90.00 105.74  90.00 C 1 2 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      0.009815  0.000000  0.002767        0.00000                         
SCALE2      0.000000  0.015085  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013422        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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