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Database: PDB
Entry: 1PZJ
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Original site: 1PZJ 
HEADER    TOXIN                                   11-JUL-03   1PZJ              
TITLE     CHOLERA TOXIN B-PENTAMER COMPLEXED WITH NITROPHENYL                   
TITLE    2 GALACTOSIDE 5                                                        
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 1PZJ    1       VERSN                                    
REVDAT   1   09-MAR-04 1PZJ    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.    1.46 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) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 80755                          
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) : 0.117                           
REMARK   3   R VALUE            (WORKING SET) : 0.115                           
REMARK   3   FREE R VALUE                     : 0.159                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4274                            
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) : 1.46                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5733                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 317                          
REMARK   3   BIN FREE R VALUE                    : 0.1730                       
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          : 185                                     
REMARK   3   SOLVENT ATOMS            : 650                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.063         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.059         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.793         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4380 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3870 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5930 ; 1.485 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9116 ; 1.111 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 6.914 ; 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 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4616 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   768 ; 0.018 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   846 ; 0.228 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4630 ; 0.280 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2331 ; 0.099 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   816 ; 0.174 ; 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 ; 0.190 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    46 ; 0.262 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    37 ; 0.190 ; 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 ; 2.299 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4190 ; 3.207 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1793 ; 4.971 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1715 ; 6.726 ; 8.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4370 ; 2.462 ; 4.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   650 ;21.284 ;20.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4280 ; 6.274 ;20.000       
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 1PZJ 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 RCSB019727.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85036                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.180                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.46                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.601                              
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   (%): 31.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 42% PEG 350, 50 MM NACL, 100 MM          
REMARK 280  TRIS-HCL PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE         
REMARK 280  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       50.87700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.99900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.87700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.99900            
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: 14420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 22300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH F1586  LIES ON A SPECIAL POSITION.                          
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 H  1265     O    HOH H  1462              2.02            
REMARK 500   O    HOH G  1158     O    HOH G  1482              2.04            
REMARK 500   CD1  ILE F    17     O    HOH F  1107              2.07            
REMARK 500   O    HOH H  1437     O    HOH H  1496              2.07            
REMARK 500   OG1  THR H     1     O    HOH H  1428              2.10            
REMARK 500   O    HOH G  1158     O    HOH G  1464              2.14            
REMARK 500   O    HOH F  1060     O    HOH F  1262              2.15            
REMARK 500   O    HOH E  1178     O    HOH E  1455              2.17            
REMARK 500   O    HOH F  1271     O    HOH F  1413              2.18            
REMARK 500   NE2  GLN G     3     O    HOH G  1625              2.19            
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 F  59   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 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    GLU D  83      -70.61    -77.94                                   
REMARK 500    ASN F  21       53.22     39.22                                   
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 F1145        DISTANCE =  5.18 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15B D 104                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J15 E 105                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J15 F 106                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15B G 107                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15B H 108                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PZI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1PZK   RELATED DB: PDB                                   
DBREF  1PZJ D    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZJ E    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZJ F    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZJ G    1   103  UNP    Q57193   Q57193_VIBCH    22    124             
DBREF  1PZJ 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    15B  D 104      37                                                       
HET    J15  E 105      37                                                       
HET    J15  F 106      37                                                       
HET    15B  G 107      37                                                       
HET    15B  H 108      37                                                       
HETNAM     15B N-{3-[4-(3-AMINO-PROPYL)-PIPERAZIN-1-YL]-PROPYL}-3-              
HETNAM   2 15B  NITRO-5-(GALACTOPYRANOSYL)-BETA-BENZAMIDE                       
HETNAM     J15 N-{3-[4-(3-AMINO-PROPYL)-PIPERAZIN-1-YL]-PROPYL}-3-              
HETNAM   2 J15  NITRO-5-(GALACTOPYRANOSYL)-ALPHA-BENZAMIDE                      
FORMUL   6  15B    3(C23 H37 N5 O9)                                             
FORMUL   7  J15    2(C23 H37 N5 O9)                                             
FORMUL  11  HOH   *650(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  ALA H   10  1                                   7    
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  2.05  
SSBOND   2 CYS E    9    CYS E   86                          1555   1555  2.03  
SSBOND   3 CYS F    9    CYS F   86                          1555   1555  2.04  
SSBOND   4 CYS G    9    CYS G   86                          1555   1555  2.04  
SSBOND   5 CYS H    9    CYS H   86                          1555   1555  2.04  
CISPEP   1 THR D   92    PRO D   93          0       -11.45                     
CISPEP   2 THR E   92    PRO E   93          0       -11.57                     
CISPEP   3 THR F   92    PRO F   93          0       -10.29                     
CISPEP   4 THR G   92    PRO G   93          0        -8.92                     
CISPEP   5 THR H   92    PRO H   93          0       -13.55                     
SITE     1 AC1 17 GLU D  11  LYS D  34  GLU D  51  GLN D  56                    
SITE     2 AC1 17 HIS D  57  GLN D  61  TRP D  88  ASN D  90                    
SITE     3 AC1 17 LYS D  91  HOH D1513  HOH D1515  HOH D1516                    
SITE     4 AC1 17 HOH D1520  HOH D1521  HOH D1608  ILE H  58                    
SITE     5 AC1 17 HOH H1611                                                     
SITE     1 AC2 13 GLU E  11  TYR E  12  GLU E  51  GLN E  56                    
SITE     2 AC2 13 HIS E  57  GLN E  61  TRP E  88  ASN E  90                    
SITE     3 AC2 13 LYS E  91  HOH E1488  HOH E1517  HOH E1596                    
SITE     4 AC2 13 GLY F  33                                                     
SITE     1 AC3 13 GLU F  11  TYR F  12  GLU F  51  GLN F  56                    
SITE     2 AC3 13 HIS F  57  GLN F  61  TRP F  88  ASN F  90                    
SITE     3 AC3 13 LYS F  91  HOH F1491  HOH F1636  GLY G  33                    
SITE     4 AC3 13 ARG G  35                                                     
SITE     1 AC4 17 GLN D  16  GLU G  11  TYR G  12  GLU G  51                    
SITE     2 AC4 17 GLN G  56  HIS G  57  GLN G  61  TRP G  88                    
SITE     3 AC4 17 ASN G  90  LYS G  91  HOH G1492  HOH G1494                    
SITE     4 AC4 17 HOH G1509  HOH G1527  GLY H  33  ARG H  35                    
SITE     5 AC4 17 HOH H1338                                                     
SITE     1 AC5 18 GLY D  33  LYS D  34  ARG D  35  GLN E  16                    
SITE     2 AC5 18 HOH E1093  GLU H  11  TYR H  12  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 H1382  HOH H1483                    
SITE     5 AC5 18 HOH H1512  HOH H1650                                          
CRYST1  101.754   65.998   77.362  90.00 105.44  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      0.009828  0.000000  0.002714        0.00000                         
SCALE2      0.000000  0.015152  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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