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Database: PDB
Entry: 1VZY
LinkDB: 1VZY
Original site: 1VZY 
HEADER    CHAPERONE                               29-MAY-04   1VZY              
TITLE     CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS HSP33                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 33 KDA CHAPERONIN;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HEAT SHOCK PROTEIN 33 HOMOLOG, HSP33;                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: ZN ATOMS, MUTATION E100A AND Q101A                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS 168;                          
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    CHAPERONE, HEAT SHOCK PROTEIN, CRYSTAL ENGINEERING, MOLECULAR         
KEYWDS   2 CHAPERONE, REDOX-ACTIVE CENTER, PSI, PROTEIN STRUCTURE INITIATIVE,   
KEYWDS   3 MCSG, MIDWEST CENTER FOR STRUCTURAL GENOMICS                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.K.JANDA,Y.DEVEDJIEV,U.DEREWENDA,Z.DAUTER,J.BIELNICKI,D.R.COOPER,    
AUTHOR   2 A.JOACHIMIAK,Z.S.DEREWENDA,MIDWEST CENTER FOR STRUCTURAL GENOMICS    
AUTHOR   3 (MCSG)                                                               
REVDAT   6   21-AUG-19 1VZY    1       REMARK                                   
REVDAT   5   28-MAR-18 1VZY    1       SOURCE JRNL                              
REVDAT   4   24-FEB-09 1VZY    1       VERSN                                    
REVDAT   3   31-JAN-05 1VZY    1       KEYWDS                                   
REVDAT   2   19-JAN-05 1VZY    1       KEYWDS AUTHOR REMARK                     
REVDAT   1   06-OCT-04 1VZY    0                                                
JRNL        AUTH   I.JANDA,Y.DEVEDJIEV,U.DEREWENDA,Z.DAUTER,J.BIELNICKI,        
JRNL        AUTH 2 D.R.COOPER,P.C.GRAF,A.JOACHIMIAK,U.JAKOB,Z.S.DEREWENDA       
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE REDUCED, ZN2+-BOUND FORM OF THE 
JRNL        TITL 2 B. SUBTILIS HSP33 CHAPERONE AND ITS IMPLICATIONS FOR THE     
JRNL        TITL 3 ACTIVATION MECHANISM.                                        
JRNL        REF    STRUCTURE                     V.  12  1901 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15458638                                                     
JRNL        DOI    10.1016/J.STR.2004.08.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 56615                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1186                            
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) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4121                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4382                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.69000                                              
REMARK   3    B22 (A**2) : 0.69000                                              
REMARK   3    B33 (A**2) : -1.03000                                             
REMARK   3    B12 (A**2) : 0.34000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.138         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.766         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4464 ; 0.025 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4141 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6026 ; 1.848 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9653 ; 0.913 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   574 ; 6.625 ; 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):   693 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4991 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   824 ; 0.010 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   869 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4701 ; 0.255 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2706 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   198 ; 0.156 ; 0.200       
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):    19 ; 0.619 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    72 ; 0.301 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.651 ; 0.200       
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):  2860 ; 1.335 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4578 ; 2.260 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1604 ; 3.210 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1448 ; 5.019 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL PLUS MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. DISORDERED REGION IN MOLECULE B (FROM GLY 252 - GLY      
REMARK   3  264) WAS MODELED BASED ON CORRSEPONDING FRAGMENT IN MOLECULE A,     
REMARK   3  AND OCCUPANCIES WERE SET TO 0.01.                                   
REMARK   4                                                                      
REMARK   4 1VZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAY-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290015132.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28310,1.2837                     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124827                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.5700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.640                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M K/NA TARTRATE, 0.1 M HEPES PH      
REMARK 280  7.5, PH 7.50                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.48033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.96067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.96067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.48033            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED MUTATION GLU 100 ALA AND GLN 101 ALA IN CHAINS            
REMARK 400  A AND B.                                                            
REMARK 400                                                                      
REMARK 400  REDOX REGULATED MOLECULAR CHAPERONE. PROTECTS BOTH                  
REMARK 400  THERMALLY UNFOLDING AND OXIDATIVELY DAMAGED PROTEINS FROM           
REMARK 400  IRREVERSIBLE AGGREGATION. PLAYS AN IMPORTANT ROLE IN THE            
REMARK 400  BACTERIAL DEFENSE SYSTEM.                                           
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   291                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     GLN B   288                                                      
REMARK 465     THR B   289                                                      
REMARK 465     THR B   290                                                      
REMARK 465     ARG B   291                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A 290    CG2                                                 
REMARK 470     ARG B 194    CG   CD   NE   CZ   NH1  NH2                        
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   C    ACT A  1292     O    HOH A  2146              0.97            
REMARK 500   O    ACT A  1292     O    HOH A  2146              1.41            
REMARK 500   OXT  ACT A  1292     O    HOH A  2146              1.56            
REMARK 500   CH3  ACT A  1292     O    HOH A  2146              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2084     O    HOH A  2084     4555     0.99            
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    MET A   1   CG    MET A   1   SD      0.158                       
REMARK 500    MET B  24   CG    MET B  24   SD      0.207                       
REMARK 500    VAL B 218   CB    VAL B 218   CG1    -0.136                       
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    MET A  24   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 261   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG B 107   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP B 142   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    SER A 136      -58.91   -125.72                                   
REMARK 500    LEU A 139      -51.86     83.15                                   
REMARK 500    ASN A 167       -6.52     82.61                                   
REMARK 500    GLN A 197      -12.20    171.43                                   
REMARK 500    GLN A 263      176.30    175.47                                   
REMARK 500    LEU B 139      -51.88     85.36                                   
REMARK 500    ASN B 167       -2.24     77.99                                   
REMARK 500    GLU B 186      -39.50    172.36                                   
REMARK 500    ARG B 241      -60.73    135.98                                   
REMARK 500    LYS B 252      -73.60    -76.39                                   
REMARK 500    ASP B 256     -102.84    -75.18                                   
REMARK 500    MET B 257      -35.79     11.85                                   
REMARK 500    ILE B 258      -98.29    -98.54                                   
REMARK 500    GLU B 259       -7.95    -10.28                                   
REMARK 500    LEU B 285      -61.43   -131.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1291  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 235   SG                                                     
REMARK 620 2 CYS A 268   SG  108.2                                              
REMARK 620 3 CYS A 237   SG  111.9 107.1                                        
REMARK 620 4 CYS A 271   SG  119.3 106.8 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1287  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 271   SG                                                     
REMARK 620 2 CYS B 235   SG  122.4                                              
REMARK 620 3 CYS B 268   SG  111.5 108.2                                        
REMARK 620 4 CYS B 237   SG  100.2 107.4 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1291                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1292                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1287                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1289                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC1014   RELATED DB: TARGETDB                           
DBREF  1VZY A    1   291  UNP    P37565   HSLO_BACSU       1    291             
DBREF  1VZY B    1   291  UNP    P37565   HSLO_BACSU       1    291             
SEQADV 1VZY ALA A  100  UNP  P37565    GLU   100 ENGINEERED MUTATION            
SEQADV 1VZY ALA A  101  UNP  P37565    GLN   101 ENGINEERED MUTATION            
SEQADV 1VZY ALA B  100  UNP  P37565    GLU   100 ENGINEERED MUTATION            
SEQADV 1VZY ALA B  101  UNP  P37565    GLN   101 ENGINEERED MUTATION            
SEQRES   1 A  291  MET ASP TYR LEU VAL LYS ALA LEU ALA TYR ASP GLY LYS          
SEQRES   2 A  291  VAL ARG ALA TYR ALA ALA ARG THR THR ASP MET VAL ASN          
SEQRES   3 A  291  GLU GLY GLN ARG ARG HIS GLY THR TRP PRO THR ALA SER          
SEQRES   4 A  291  ALA ALA LEU GLY ARG THR MET THR ALA SER LEU MET LEU          
SEQRES   5 A  291  GLY ALA MET LEU LYS GLY ASP ASP LYS LEU THR VAL LYS          
SEQRES   6 A  291  ILE GLU GLY GLY GLY PRO ILE GLY ALA ILE VAL ALA ASP          
SEQRES   7 A  291  ALA ASN ALA LYS GLY GLU VAL ARG ALA TYR VAL SER ASN          
SEQRES   8 A  291  PRO GLN VAL HIS PHE ASP LEU ASN ALA ALA GLY LYS LEU          
SEQRES   9 A  291  ASP VAL ARG ARG ALA VAL GLY THR ASN GLY THR LEU SER          
SEQRES  10 A  291  VAL VAL LYS ASP LEU GLY LEU ARG GLU PHE PHE THR GLY          
SEQRES  11 A  291  GLN VAL GLU ILE VAL SER GLY GLU LEU GLY ASP ASP PHE          
SEQRES  12 A  291  THR TYR TYR LEU VAL SER SER GLU GLN VAL PRO SER SER          
SEQRES  13 A  291  VAL GLY VAL GLY VAL LEU VAL ASN PRO ASP ASN THR ILE          
SEQRES  14 A  291  LEU ALA ALA GLY GLY PHE ILE ILE GLN LEU MET PRO GLY          
SEQRES  15 A  291  THR ASP ASP GLU THR ILE THR LYS ILE GLU GLN ARG LEU          
SEQRES  16 A  291  SER GLN VAL GLU PRO ILE SER LYS LEU ILE GLN LYS GLY          
SEQRES  17 A  291  LEU THR PRO GLU GLU ILE LEU GLU GLU VAL LEU GLY GLU          
SEQRES  18 A  291  LYS PRO GLU ILE LEU GLU THR MET PRO VAL ARG PHE HIS          
SEQRES  19 A  291  CYS PRO CYS SER LYS GLU ARG PHE GLU THR ALA ILE LEU          
SEQRES  20 A  291  GLY LEU GLY LYS LYS GLU ILE GLN ASP MET ILE GLU GLU          
SEQRES  21 A  291  ASP GLY GLN ALA GLU ALA VAL CYS HIS PHE CYS ASN GLU          
SEQRES  22 A  291  LYS TYR LEU PHE THR LYS GLU GLU LEU GLU GLY LEU ARG          
SEQRES  23 A  291  ASP GLN THR THR ARG                                          
SEQRES   1 B  291  MET ASP TYR LEU VAL LYS ALA LEU ALA TYR ASP GLY LYS          
SEQRES   2 B  291  VAL ARG ALA TYR ALA ALA ARG THR THR ASP MET VAL ASN          
SEQRES   3 B  291  GLU GLY GLN ARG ARG HIS GLY THR TRP PRO THR ALA SER          
SEQRES   4 B  291  ALA ALA LEU GLY ARG THR MET THR ALA SER LEU MET LEU          
SEQRES   5 B  291  GLY ALA MET LEU LYS GLY ASP ASP LYS LEU THR VAL LYS          
SEQRES   6 B  291  ILE GLU GLY GLY GLY PRO ILE GLY ALA ILE VAL ALA ASP          
SEQRES   7 B  291  ALA ASN ALA LYS GLY GLU VAL ARG ALA TYR VAL SER ASN          
SEQRES   8 B  291  PRO GLN VAL HIS PHE ASP LEU ASN ALA ALA GLY LYS LEU          
SEQRES   9 B  291  ASP VAL ARG ARG ALA VAL GLY THR ASN GLY THR LEU SER          
SEQRES  10 B  291  VAL VAL LYS ASP LEU GLY LEU ARG GLU PHE PHE THR GLY          
SEQRES  11 B  291  GLN VAL GLU ILE VAL SER GLY GLU LEU GLY ASP ASP PHE          
SEQRES  12 B  291  THR TYR TYR LEU VAL SER SER GLU GLN VAL PRO SER SER          
SEQRES  13 B  291  VAL GLY VAL GLY VAL LEU VAL ASN PRO ASP ASN THR ILE          
SEQRES  14 B  291  LEU ALA ALA GLY GLY PHE ILE ILE GLN LEU MET PRO GLY          
SEQRES  15 B  291  THR ASP ASP GLU THR ILE THR LYS ILE GLU GLN ARG LEU          
SEQRES  16 B  291  SER GLN VAL GLU PRO ILE SER LYS LEU ILE GLN LYS GLY          
SEQRES  17 B  291  LEU THR PRO GLU GLU ILE LEU GLU GLU VAL LEU GLY GLU          
SEQRES  18 B  291  LYS PRO GLU ILE LEU GLU THR MET PRO VAL ARG PHE HIS          
SEQRES  19 B  291  CYS PRO CYS SER LYS GLU ARG PHE GLU THR ALA ILE LEU          
SEQRES  20 B  291  GLY LEU GLY LYS LYS GLU ILE GLN ASP MET ILE GLU GLU          
SEQRES  21 B  291  ASP GLY GLN ALA GLU ALA VAL CYS HIS PHE CYS ASN GLU          
SEQRES  22 B  291  LYS TYR LEU PHE THR LYS GLU GLU LEU GLU GLY LEU ARG          
SEQRES  23 B  291  ASP GLN THR THR ARG                                          
HET     ZN  A1291       1                                                       
HET    ACT  A1292       4                                                       
HET    ACT  A1293       4                                                       
HET    ACT  A1294       4                                                       
HET    ACT  A1295       4                                                       
HET     ZN  B1287       1                                                       
HET    ACT  B1288       4                                                       
HET    ACT  B1289       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  ACT    6(C2 H3 O2 1-)                                               
FORMUL  11  HOH   *277(H2 O)                                                    
HELIX    1   1 THR A   21  GLY A   33  1                                  13    
HELIX    2   2 TRP A   35  ALA A   54  1                                  20    
HELIX    3   3 ASP A  105  GLY A  111  1                                   7    
HELIX    4   4 LEU A  139  GLN A  152  1                                  14    
HELIX    5   5 ASP A  184  SER A  196  1                                  13    
HELIX    6   6 PRO A  200  GLY A  208  1                                   9    
HELIX    7   7 THR A  210  GLY A  220  1                                  11    
HELIX    8   8 SER A  238  GLY A  248  1                                  11    
HELIX    9   9 GLY A  250  GLY A  262  1                                  13    
HELIX   10  10 LYS A  279  THR A  289  1                                  11    
HELIX   11  11 THR B   21  GLY B   33  1                                  13    
HELIX   12  12 TRP B   35  ALA B   54  1                                  20    
HELIX   13  13 ASP B  105  GLY B  111  1                                   7    
HELIX   14  14 LEU B  139  SER B  150  1                                  12    
HELIX   15  15 GLU B  186  VAL B  198  1                                  13    
HELIX   16  16 PRO B  200  LYS B  207  1                                   8    
HELIX   17  17 THR B  210  GLY B  220  1                                  11    
HELIX   18  18 SER B  238  GLY B  248  1                                  11    
HELIX   19  19 LYS B  251  GLU B  260  1                                  10    
HELIX   20  20 LYS B  279  GLY B  284  1                                   6    
SHEET    1  AA 5 SER A 155  VAL A 163  0                                        
SHEET    2  AA 5 ILE A 169  LEU A 179 -1  N  LEU A 170   O  LEU A 162           
SHEET    3  AA 5 VAL A  14  ARG A  20 -1  O  ARG A  15   N  GLN A 178           
SHEET    4  AA 5 TYR A   3  ALA A   9 -1  O  TYR A   3   N  ARG A  20           
SHEET    5  AA 5 GLU A 224  PRO A 230 -1  O  GLU A 224   N  LEU A   8           
SHEET    1  AB12 ARG A 232  PHE A 233  0                                        
SHEET    2  AB12 GLU A  84  VAL A  89  1  N  VAL A  85   O  ARG A 232           
SHEET    3  AB12 ALA A  74  ASN A  80 -1  O  VAL A  76   N  TYR A  88           
SHEET    4  AB12 LYS A  61  GLU A  67 -1  O  LEU A  62   N  ALA A  79           
SHEET    5  AB12 THR A 115  ASP A 121 -1  O  THR A 115   N  GLU A  67           
SHEET    6  AB12 GLU A 126  GLU A 133 -1  O  PHE A 128   N  LYS A 120           
SHEET    7  AB12 GLU B 126  GLU B 133 -1  O  PHE B 127   N  GLN A 131           
SHEET    8  AB12 THR B 115  GLY B 123 -1  O  LEU B 116   N  VAL B 132           
SHEET    9  AB12 LYS B  61  GLU B  67 -1  O  LYS B  61   N  ASP B 121           
SHEET   10  AB12 ILE B  75  ASN B  80 -1  O  ILE B  75   N  ILE B  66           
SHEET   11  AB12 GLU B  84  VAL B  89 -1  O  GLU B  84   N  ASN B  80           
SHEET   12  AB12 ARG B 232  PHE B 233  1  O  ARG B 232   N  VAL B  85           
SHEET    1  AC 2 GLN A 263  VAL A 267  0                                        
SHEET    2  AC 2 LYS A 274  THR A 278 -1  O  TYR A 275   N  ALA A 266           
SHEET    1  BA 5 SER B 155  VAL B 163  0                                        
SHEET    2  BA 5 ILE B 169  LEU B 179 -1  N  LEU B 170   O  LEU B 162           
SHEET    3  BA 5 VAL B  14  ARG B  20 -1  O  ARG B  15   N  GLN B 178           
SHEET    4  BA 5 TYR B   3  ALA B   9 -1  O  TYR B   3   N  ARG B  20           
SHEET    5  BA 5 GLU B 224  PRO B 230 -1  O  GLU B 224   N  LEU B   8           
SHEET    1  BB 2 GLN B 263  VAL B 267  0                                        
SHEET    2  BB 2 LYS B 274  THR B 278 -1  O  TYR B 275   N  ALA B 266           
LINK        ZN    ZN A1291                 SG  CYS A 235     1555   1555  2.22  
LINK        ZN    ZN A1291                 SG  CYS A 268     1555   1555  2.44  
LINK        ZN    ZN A1291                 SG  CYS A 237     1555   1555  2.26  
LINK        ZN    ZN A1291                 SG  CYS A 271     1555   1555  2.26  
LINK        ZN    ZN B1287                 SG  CYS B 271     1555   1555  2.23  
LINK        ZN    ZN B1287                 SG  CYS B 235     1555   1555  2.22  
LINK        ZN    ZN B1287                 SG  CYS B 268     1555   1555  2.28  
LINK        ZN    ZN B1287                 SG  CYS B 237     1555   1555  2.44  
SITE     1 AC1  4 CYS A 235  CYS A 237  CYS A 268  CYS A 271                    
SITE     1 AC2  8 SER A 238  LYS A 239  TYR A 275  HOH A2145                    
SITE     2 AC2  8 HOH A2146  ASN B 164  PRO B 165  ASP B 166                    
SITE     1 AC3  3 TRP A  35  PRO A  36  ASN A 167                               
SITE     1 AC4  3 ARG A 125  ALA A 266  VAL A 267                               
SITE     1 AC5  3 LYS A 239  TYR A 275  LEU A 276                               
SITE     1 AC6  4 CYS B 235  CYS B 237  CYS B 268  CYS B 271                    
SITE     1 AC7  3 ARG B  86  ARG B 241  HIS B 269                               
SITE     1 AC8  2 ALA B 100  ARG B 107                                          
CRYST1  115.292  115.292  106.441  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008674  0.005008  0.000000        0.00000                         
SCALE2      0.000000  0.010015  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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