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Database: PDB
Entry: 1PZK
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HEADER    TOXIN                                   11-JUL-03   1PZK              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH N-ACYL PHENYL                 
TITLE    2 GALACTOSIDE 9H                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLERA TOXIN B SUBUNIT;                                   
COMPND   3 CHAIN: D, E, F, G, H;                                                
COMPND   4 SYNONYM: CTB; CHOLERA TOXIN B PROTEIN; CHOLERA TOXIN                 
COMPND   5 SUBUNIT B;                                                           
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 GENE: CAA41591;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD                                      
KEYWDS    PENTAMER, MONOVALENT, TOXIN, INHIBITOR, CHOLERA                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.MITCHELL,J.C.PICKENS,K.KOROTKOV,E.FAN,W.G.J.HOL                   
REVDAT   2   24-FEB-09 1PZK    1       VERSN                                    
REVDAT   1   09-MAR-04 1PZK    0                                                
JRNL        AUTH   D.D.MITCHELL,J.C.PICKENS,K.KOROTKOV,E.FAN,W.G.J.HOL          
JRNL        TITL   3,5-SUBSTITUTED PHENYL GALACTOSIDES AS LEADS IN              
JRNL        TITL 2 DESIGNING EFFECTIVE CHOLERA TOXIN ANTAGONISTS;               
JRNL        TITL 3 SYNTHESIS AND CRYSTALLOGRAPHIC STUDIES                       
JRNL        REF    BIOORG.MED.CHEM.              V.  12   907 2004              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   14980603                                                     
JRNL        DOI    10.1016/J.BMC.2003.12.019                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 99104                          
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) : 0.134                           
REMARK   3   R VALUE            (WORKING SET) : 0.132                           
REMARK   3   FREE R VALUE                     : 0.173                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5202                            
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) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4703                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 237                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4095                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 121                                     
REMARK   3   SOLVENT ATOMS            : 630                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.13                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05000                                             
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): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.035         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.888         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.967                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4312 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3809 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5841 ; 1.626 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8964 ; 1.381 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 6.924 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   680 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4596 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   773 ; 0.014 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   845 ; 0.227 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4505 ; 0.276 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2217 ; 0.104 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   807 ; 0.165 ; 0.500       
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):    13 ; 0.276 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.353 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.229 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2577 ; 2.338 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4190 ; 3.117 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1725 ; 4.209 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1626 ; 5.694 ; 6.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4302 ; 1.618 ; 2.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   630 ;16.123 ;10.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4216 ; 5.081 ;10.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1PZK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019728.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : SI 220                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104310                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 3.140                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.860                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XTALVIEW                                              
REMARK 200 STARTING MODEL: 3CHB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG 550 MME, 50 MM NACL, 100 MM      
REMARK 280  TRIS PH 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K        
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       51.02400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.06850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.02400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.06850            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   O    HOH D  1171     O    HOH D  1360              1.97            
REMARK 500   O    HOH G  1038     O    HOH G  1436              2.10            
REMARK 500   NZ   LYS F    63     O    HOH F  1372              2.13            
REMARK 500   O    HOH G  1391     O    HOH G  1561              2.18            
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    GLU E  83      -71.72    -75.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D1393        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH D1502        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH E1510        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH G1529        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH G1536        DISTANCE =  6.30 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     J12 G  104                                                       
REMARK 610     J12 D  105                                                       
REMARK 610     J12 E  106                                                       
REMARK 610     J12 F  107                                                       
REMARK 610     J12 H  108                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J12 G 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J12 D 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J12 E 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J12 F 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J12 H 108                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PZI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1PZJ   RELATED DB: PDB                                   
DBREF  1PZK D    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZK E    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZK F    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZK G    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZK H    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
SEQRES   1 D  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 D  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 D  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 D  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 D  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 D  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 D  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 D  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 E  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 E  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 E  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 E  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 E  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 E  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 E  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 E  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 F  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 F  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 F  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 F  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 F  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 F  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 F  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 F  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 G  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 G  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 G  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 G  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 G  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 G  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 G  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 G  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
SEQRES   1 H  103  THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS          
SEQRES   2 H  103  ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER          
SEQRES   3 H  103  TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE          
SEQRES   4 H  103  ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL          
SEQRES   5 H  103  PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE          
SEQRES   6 H  103  GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR          
SEQRES   7 H  103  GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS          
SEQRES   8 H  103  THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN              
HET    J12  G 104      21                                                       
HET    J12  D 105      21                                                       
HET    J12  E 106      21                                                       
HET    J12  F 107      21                                                       
HET    J12  H 108      37                                                       
HETNAM     J12 N-{3-[4-(3-AMINO-PROPYL)-PIPERAZIN-1-YL]-PROPYL}-3-(2-           
HETNAM   2 J12  THIOPHEN-2-YL-ACETYLAMINO)-5-(3,4,5-TRIHYDROXY-6-               
HETNAM   3 J12  HYDROXYMETHYL-TETRAHYDRO-PYRAN-2-YLOXY)-BENZAMIDE               
FORMUL   6  J12    5(C29 H43 N5 O8 S)                                           
FORMUL  11  HOH   *630(H2 O)                                                    
HELIX    1   1 ASN D    4  ALA D   10  1                                   7    
HELIX    2   2 SER D   60  GLU D   79  1                                  20    
HELIX    3   3 ASN E    4  ALA E   10  1                                   7    
HELIX    4   4 SER E   60  GLU E   79  1                                  20    
HELIX    5   5 ASN F    4  GLU F   11  1                                   8    
HELIX    6   6 SER F   60  GLU F   79  1                                  20    
HELIX    7   7 ASN G    4  ALA G   10  1                                   7    
HELIX    8   8 SER G   60  GLU G   79  1                                  20    
HELIX    9   9 ASN H    4  GLU H   11  1                                   8    
HELIX   10  10 SER H   60  GLU H   79  1                                  20    
SHEET    1  3040 SER D  26  SER D  30  0                                        
SHEET    2  3040 MET D  37  THR D  41 -1  O  MET D  37   N  SER D  30           
SHEET    3  3040 THR D  47  VAL D  50 -1  N  PHE D  48   O  ILE D  40           
SHEET    4  3040 HIS D  94  ALA D 102  1  O  HIS D  94   N  GLN D  49           
SHEET    5  3040 VAL D  82  TRP D  88 -1  N  GLU D  83   O  SER D 100           
SHEET    6  3040 THR D  15  ASP D  22 -1  O  GLN D  16   N  VAL D  87           
SHEET    7  3040 VAL D  82  TRP D  88 -1  N  VAL D  82   O  ASP D  22           
SHEET    8  3040 HIS D  94  ALA D 102 -1  O  ALA D  95   N  TRP D  88           
SHEET    9  3040 SER E  26  SER E  30  1  O  TYR E  27   N  MET D 101           
SHEET   10  3040 ALA E  38  THR E  41 -1  N  ILE E  39   O  THR E  28           
SHEET   11  3040 THR E  47  VAL E  50 -1  N  PHE E  48   O  ILE E  40           
SHEET   12  3040 HIS E  94  ALA E 102  1  O  HIS E  94   N  GLN E  49           
SHEET   13  3040 VAL E  82  TRP E  88 -1  N  GLU E  83   O  SER E 100           
SHEET   14  3040 THR E  15  ASP E  22 -1  O  GLN E  16   N  VAL E  87           
SHEET   15  3040 VAL E  82  TRP E  88 -1  N  VAL E  82   O  ASP E  22           
SHEET   16  3040 HIS E  94  ALA E 102 -1  O  ALA E  95   N  TRP E  88           
SHEET   17  3040 SER F  26  SER F  30 -1  O  TYR F  27   N  MET E 101           
SHEET   18  3040 ALA F  38  THR F  41 -1  O  ILE F  39   N  THR F  28           
SHEET   19  3040 THR F  47  VAL F  50 -1  N  PHE F  48   O  ILE F  40           
SHEET   20  3040 HIS F  94  ALA F 102  1  O  HIS F  94   N  GLN F  49           
SHEET   21  3040 VAL F  82  TRP F  88 -1  N  GLU F  83   O  SER F 100           
SHEET   22  3040 THR F  15  ASP F  22 -1  O  GLN F  16   N  VAL F  87           
SHEET   23  3040 VAL F  82  TRP F  88 -1  N  VAL F  82   O  ASP F  22           
SHEET   24  3040 HIS F  94  ALA F 102 -1  O  ALA F  95   N  TRP F  88           
SHEET   25  3040 SER G  26  SER G  30 -1  O  TYR G  27   N  MET F 101           
SHEET   26  3040 MET G  37  THR G  41 -1  O  MET G  37   N  SER G  30           
SHEET   27  3040 THR G  47  VAL G  50 -1  N  PHE G  48   O  ILE G  40           
SHEET   28  3040 HIS G  94  ALA G 102  1  O  HIS G  94   N  GLN G  49           
SHEET   29  3040 VAL G  82  TRP G  88 -1  N  GLU G  83   O  SER G 100           
SHEET   30  3040 THR G  15  ASP G  22 -1  O  GLN G  16   N  VAL G  87           
SHEET   31  3040 VAL G  82  TRP G  88 -1  N  VAL G  82   O  ASP G  22           
SHEET   32  3040 HIS G  94  ALA G 102 -1  O  ALA G  95   N  TRP G  88           
SHEET   33  3040 SER H  26  SER H  30 -1  O  TYR H  27   N  MET G 101           
SHEET   34  3040 MET H  37  THR H  41 -1  O  MET H  37   N  SER H  30           
SHEET   35  3040 THR H  47  VAL H  50 -1  O  PHE H  48   N  ILE H  40           
SHEET   36  3040 HIS H  94  ALA H 102  1  O  HIS H  94   N  GLN H  49           
SHEET   37  3040 VAL H  82  TRP H  88 -1  N  GLU H  83   O  SER H 100           
SHEET   38  3040 THR H  15  ASP H  22 -1  O  GLN H  16   N  VAL H  87           
SHEET   39  3040 VAL H  82  TRP H  88 -1  N  VAL H  82   O  ASP H  22           
SHEET   40  3040 HIS H  94  ALA H 102 -1  O  ALA H  95   N  TRP H  88           
SSBOND   1 CYS D    9    CYS D   86                          1555   1555  2.04  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.04  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.04  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.05  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.04  
CISPEP   1 THR D   92    PRO D   93          0       -10.91                     
CISPEP   2 THR E   92    PRO E   93          0        -8.95                     
CISPEP   3 THR F   92    PRO F   93          0       -11.06                     
CISPEP   4 THR G   92    PRO G   93          0       -10.55                     
CISPEP   5 THR H   92    PRO H   93          0       -10.54                     
SITE     1 AC1 12 HOH D1431  HIS G  13  GLU G  51  GLN G  56                    
SITE     2 AC1 12 GLN G  61  TRP G  88  ASN G  90  LYS G  91                    
SITE     3 AC1 12 HOH G1466  HOH G1467  HOH G1477  HOH G1627                    
SITE     1 AC2 14 TYR D  12  HIS D  13  GLU D  51  GLN D  56                    
SITE     2 AC2 14 HIS D  57  GLN D  61  TRP D  88  ASN D  90                    
SITE     3 AC2 14 LYS D  91  HOH D1576  HOH D1577  HOH D1578                    
SITE     4 AC2 14 HOH D1586  HOH E1480                                          
SITE     1 AC3 12 TYR E  12  HIS E  13  GLU E  51  GLN E  56                    
SITE     2 AC3 12 GLN E  61  TRP E  88  ASN E  90  LYS E  91                    
SITE     3 AC3 12 HOH E1591  HOH E1592  HOH E1624  HOH F1479                    
SITE     1 AC4 12 HIS F  13  GLU F  51  GLN F  56  HIS F  57                    
SITE     2 AC4 12 GLN F  61  TRP F  88  ASN F  90  LYS F  91                    
SITE     3 AC4 12 HOH F1605  HOH F1606  HOH F1625  HOH G1478                    
SITE     1 AC5 18 LYS D  34  ARG D  35  HOH D1572  HOH E1456                    
SITE     2 AC5 18 GLU H  11  TYR H  12  HIS H  13  GLU H  51                    
SITE     3 AC5 18 GLN H  56  HIS H  57  GLN H  61  TRP H  88                    
SITE     4 AC5 18 ASN H  90  LYS H  91  HOH H1481  HOH H1485                    
SITE     5 AC5 18 HOH H1570  HOH H1571                                          
CRYST1  102.048   66.137   78.185  90.00 105.78  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      0.009799  0.000000  0.002769        0.00000                         
SCALE2      0.000000  0.015120  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013291        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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