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Database: PDB
Entry: 4MTD
LinkDB: 4MTD
Original site: 4MTD 
HEADER    DNA BINDING PROTEIN/DNA                 19-SEP-13   4MTD              
TITLE     ZINC UPTAKE REGULATOR COMPLEXED WITH ZINC AND DNA                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZINC UPTAKE REGULATION PROTEIN;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ZINC UPTAKE REGULATOR;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ZNUABC OPERATOR DNA;                                       
COMPND   8 CHAIN: Y;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: ZNUABC OPERATOR DNA;                                       
COMPND  12 CHAIN: Z;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B4046, JW5714, YJBK, ZUR;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24D;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN-DNA COMPLEX, WINGED-HELIX, DNA-BINDING REGULATORY PROTEIN,    
KEYWDS   2 HELIX-TURN-HELIX, WINGED HELIX, ZINC REGULATED REPRESSOR, DNA        
KEYWDS   3 BINDING, DNA BINDING PROTEIN-DNA COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.A.GILSTON,A.MONDRAGON,T.V.O'HALLORAN                                
REVDAT   3   28-FEB-24 4MTD    1       REMARK LINK                              
REVDAT   2   12-NOV-14 4MTD    1       JRNL                                     
REVDAT   1   05-NOV-14 4MTD    0                                                
JRNL        AUTH   B.A.GILSTON,S.WANG,M.D.MARCUS,M.A.CANALIZO-HERNANDEZ,        
JRNL        AUTH 2 E.P.SWINDELL,Y.XUE,A.MONDRAGON,T.V.O'HALLORAN                
JRNL        TITL   STRUCTURAL AND MECHANISTIC BASIS OF ZINC REGULATION ACROSS   
JRNL        TITL 2 THE E. COLI ZUR REGULON.                                     
JRNL        REF    PLOS BIOL.                    V.  12 01987 2014              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   25369000                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1001987                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 43139                          
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) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2290                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3120                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 141                          
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4632                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1355                                    
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.20000                                              
REMARK   3    B22 (A**2) : -2.84000                                             
REMARK   3    B33 (A**2) : -1.45000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.334         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.258         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.890         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6263 ; 0.006 ; 0.017       
REMARK   3   BOND LENGTHS OTHERS               (A):  5328 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8742 ; 1.117 ; 1.763       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12290 ; 0.896 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   596 ; 6.342 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   218 ;32.824 ;24.404       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   832 ;14.167 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;12.306 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   948 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6175 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1339 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2390 ; 2.748 ; 6.306       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2389 ; 2.748 ; 6.304       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2981 ; 4.637 ; 9.446       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3873 ; 3.181 ; 6.693       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4MTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082340.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 78                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : BERYLLIUM LENSES                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45429                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 0.1 M CITRATE,   
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
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       96.66200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.23500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       96.66200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.23500            
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 300 REMARK: A DIMER OF DIMERS IS COMPLEXED WITH THE DUPLEX DNA MOLECULE. 
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, Y, Z                      
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 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ARG A   153                                                      
REMARK 465     HIS A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     CYS A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     VAL A   164                                                      
REMARK 465     GLN A   165                                                      
REMARK 465     VAL A   166                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     LYS A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     ARG A   171                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ARG B   153                                                      
REMARK 465     HIS B   154                                                      
REMARK 465     PRO B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     GLN B   157                                                      
REMARK 465     CYS B   158                                                      
REMARK 465     GLN B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     VAL B   164                                                      
REMARK 465     GLN B   165                                                      
REMARK 465     VAL B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     LYS B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     ARG B   171                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     ARG C   153                                                      
REMARK 465     HIS C   154                                                      
REMARK 465     PRO C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     GLN C   157                                                      
REMARK 465     CYS C   158                                                      
REMARK 465     GLN C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     ASP C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     SER C   163                                                      
REMARK 465     VAL C   164                                                      
REMARK 465     GLN C   165                                                      
REMARK 465     VAL C   166                                                      
REMARK 465     LYS C   167                                                      
REMARK 465     LYS C   168                                                      
REMARK 465     LYS C   169                                                      
REMARK 465     PRO C   170                                                      
REMARK 465     ARG C   171                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D   153                                                      
REMARK 465     HIS D   154                                                      
REMARK 465     PRO D   155                                                      
REMARK 465     GLU D   156                                                      
REMARK 465     GLN D   157                                                      
REMARK 465     CYS D   158                                                      
REMARK 465     GLN D   159                                                      
REMARK 465     HIS D   160                                                      
REMARK 465     ASP D   161                                                      
REMARK 465     HIS D   162                                                      
REMARK 465     SER D   163                                                      
REMARK 465     VAL D   164                                                      
REMARK 465     GLN D   165                                                      
REMARK 465     VAL D   166                                                      
REMARK 465     LYS D   167                                                      
REMARK 465     LYS D   168                                                      
REMARK 465     LYS D   169                                                      
REMARK 465     PRO D   170                                                      
REMARK 465     ARG D   171                                                      
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     DA Y   1   P      DA Y   1   OP3    -0.122                       
REMARK 500     DT Z   1   P      DT Z   1   OP3    -0.121                       
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    ASN A  83       83.24    -68.24                                   
REMARK 500    PHE A  91      -80.36    -67.32                                   
REMARK 500    PRO B  94     -142.97    -75.98                                   
REMARK 500    ALA B 114       77.89   -168.60                                   
REMARK 500    ASP C  39       54.28    -98.71                                   
REMARK 500    GLN C  73     -159.88    -72.94                                   
REMARK 500    THR C  95      111.98    -38.87                                   
REMARK 500    ASN D  21       67.28   -108.40                                   
REMARK 500    ASP D  39       37.73    -92.32                                   
REMARK 500    LEU D  90       25.41   -145.19                                   
REMARK 500    THR D  95      150.87    -49.75                                   
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 A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  77   NE2                                                    
REMARK 620 2 CYS A  88   SG  104.4                                              
REMARK 620 3 HIS A  96   NE2 107.4 114.4                                        
REMARK 620 4 GLU A 111   OE1  99.7 136.2  91.8                                  
REMARK 620 5 GLU A 111   OE2  90.4  89.2 144.6  54.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 103   SG                                                     
REMARK 620 2 CYS A 106   SG  101.3                                              
REMARK 620 3 CYS A 143   SG  122.0 114.3                                        
REMARK 620 4 CYS A 146   SG  102.4 106.6 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  77   NE2                                                    
REMARK 620 2 CYS B  88   SG  107.0                                              
REMARK 620 3 HIS B  96   NE2 107.7 111.3                                        
REMARK 620 4 GLU B 111   OE1  88.3 145.5  92.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 103   SG                                                     
REMARK 620 2 CYS B 106   SG   98.6                                              
REMARK 620 3 CYS B 143   SG  119.6 105.4                                        
REMARK 620 4 CYS B 146   SG   85.8 111.8 130.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  77   NE2                                                    
REMARK 620 2 CYS C  88   SG  110.8                                              
REMARK 620 3 HIS C  96   NE2 104.3 101.9                                        
REMARK 620 4 GLU C 111   OE1 102.2 140.9  89.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 103   SG                                                     
REMARK 620 2 CYS C 106   SG  108.2                                              
REMARK 620 3 CYS C 143   SG  110.1 109.7                                        
REMARK 620 4 CYS C 146   SG   97.6 121.8 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  77   NE2                                                    
REMARK 620 2 CYS D  88   SG  105.8                                              
REMARK 620 3 HIS D  96   NE2 109.3 107.4                                        
REMARK 620 4 GLU D 111   OE1  95.6 144.8  90.8                                  
REMARK 620 5 GLU D 111   OE2 106.2  92.7 131.9  54.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 103   SG                                                     
REMARK 620 2 CYS D 106   SG  102.4                                              
REMARK 620 3 CYS D 143   SG  120.2 105.8                                        
REMARK 620 4 CYS D 146   SG   86.1 105.6 132.6                                  
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 A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MTE   RELATED DB: PDB                                   
DBREF  4MTD A    1   171  UNP    P0AC51   ZUR_ECOLI        1    171             
DBREF  4MTD B    1   171  UNP    P0AC51   ZUR_ECOLI        1    171             
DBREF  4MTD C    1   171  UNP    P0AC51   ZUR_ECOLI        1    171             
DBREF  4MTD D    1   171  UNP    P0AC51   ZUR_ECOLI        1    171             
DBREF  4MTD Y    1    33  PDB    4MTD     4MTD             1     33             
DBREF  4MTD Z    1    33  PDB    4MTD     4MTD             1     33             
SEQRES   1 A  171  MET GLU LYS THR THR THR GLN GLU LEU LEU ALA GLN ALA          
SEQRES   2 A  171  GLU LYS ILE CYS ALA GLN ARG ASN VAL ARG LEU THR PRO          
SEQRES   3 A  171  GLN ARG LEU GLU VAL LEU ARG LEU MET SER LEU GLN ASP          
SEQRES   4 A  171  GLY ALA ILE SER ALA TYR ASP LEU LEU ASP LEU LEU ARG          
SEQRES   5 A  171  GLU ALA GLU PRO GLN ALA LYS PRO PRO THR VAL TYR ARG          
SEQRES   6 A  171  ALA LEU ASP PHE LEU LEU GLU GLN GLY PHE VAL HIS LYS          
SEQRES   7 A  171  VAL GLU SER THR ASN SER TYR VAL LEU CYS HIS LEU PHE          
SEQRES   8 A  171  ASP GLN PRO THR HIS THR SER ALA MET PHE ILE CYS ASP          
SEQRES   9 A  171  ARG CYS GLY ALA VAL LYS GLU GLU CYS ALA GLU GLY VAL          
SEQRES  10 A  171  GLU ASP ILE MET HIS THR LEU ALA ALA LYS MET GLY PHE          
SEQRES  11 A  171  ALA LEU ARG HIS ASN VAL ILE GLU ALA HIS GLY LEU CYS          
SEQRES  12 A  171  ALA ALA CYS VAL GLU VAL GLU ALA CYS ARG HIS PRO GLU          
SEQRES  13 A  171  GLN CYS GLN HIS ASP HIS SER VAL GLN VAL LYS LYS LYS          
SEQRES  14 A  171  PRO ARG                                                      
SEQRES   1 B  171  MET GLU LYS THR THR THR GLN GLU LEU LEU ALA GLN ALA          
SEQRES   2 B  171  GLU LYS ILE CYS ALA GLN ARG ASN VAL ARG LEU THR PRO          
SEQRES   3 B  171  GLN ARG LEU GLU VAL LEU ARG LEU MET SER LEU GLN ASP          
SEQRES   4 B  171  GLY ALA ILE SER ALA TYR ASP LEU LEU ASP LEU LEU ARG          
SEQRES   5 B  171  GLU ALA GLU PRO GLN ALA LYS PRO PRO THR VAL TYR ARG          
SEQRES   6 B  171  ALA LEU ASP PHE LEU LEU GLU GLN GLY PHE VAL HIS LYS          
SEQRES   7 B  171  VAL GLU SER THR ASN SER TYR VAL LEU CYS HIS LEU PHE          
SEQRES   8 B  171  ASP GLN PRO THR HIS THR SER ALA MET PHE ILE CYS ASP          
SEQRES   9 B  171  ARG CYS GLY ALA VAL LYS GLU GLU CYS ALA GLU GLY VAL          
SEQRES  10 B  171  GLU ASP ILE MET HIS THR LEU ALA ALA LYS MET GLY PHE          
SEQRES  11 B  171  ALA LEU ARG HIS ASN VAL ILE GLU ALA HIS GLY LEU CYS          
SEQRES  12 B  171  ALA ALA CYS VAL GLU VAL GLU ALA CYS ARG HIS PRO GLU          
SEQRES  13 B  171  GLN CYS GLN HIS ASP HIS SER VAL GLN VAL LYS LYS LYS          
SEQRES  14 B  171  PRO ARG                                                      
SEQRES   1 C  171  MET GLU LYS THR THR THR GLN GLU LEU LEU ALA GLN ALA          
SEQRES   2 C  171  GLU LYS ILE CYS ALA GLN ARG ASN VAL ARG LEU THR PRO          
SEQRES   3 C  171  GLN ARG LEU GLU VAL LEU ARG LEU MET SER LEU GLN ASP          
SEQRES   4 C  171  GLY ALA ILE SER ALA TYR ASP LEU LEU ASP LEU LEU ARG          
SEQRES   5 C  171  GLU ALA GLU PRO GLN ALA LYS PRO PRO THR VAL TYR ARG          
SEQRES   6 C  171  ALA LEU ASP PHE LEU LEU GLU GLN GLY PHE VAL HIS LYS          
SEQRES   7 C  171  VAL GLU SER THR ASN SER TYR VAL LEU CYS HIS LEU PHE          
SEQRES   8 C  171  ASP GLN PRO THR HIS THR SER ALA MET PHE ILE CYS ASP          
SEQRES   9 C  171  ARG CYS GLY ALA VAL LYS GLU GLU CYS ALA GLU GLY VAL          
SEQRES  10 C  171  GLU ASP ILE MET HIS THR LEU ALA ALA LYS MET GLY PHE          
SEQRES  11 C  171  ALA LEU ARG HIS ASN VAL ILE GLU ALA HIS GLY LEU CYS          
SEQRES  12 C  171  ALA ALA CYS VAL GLU VAL GLU ALA CYS ARG HIS PRO GLU          
SEQRES  13 C  171  GLN CYS GLN HIS ASP HIS SER VAL GLN VAL LYS LYS LYS          
SEQRES  14 C  171  PRO ARG                                                      
SEQRES   1 D  171  MET GLU LYS THR THR THR GLN GLU LEU LEU ALA GLN ALA          
SEQRES   2 D  171  GLU LYS ILE CYS ALA GLN ARG ASN VAL ARG LEU THR PRO          
SEQRES   3 D  171  GLN ARG LEU GLU VAL LEU ARG LEU MET SER LEU GLN ASP          
SEQRES   4 D  171  GLY ALA ILE SER ALA TYR ASP LEU LEU ASP LEU LEU ARG          
SEQRES   5 D  171  GLU ALA GLU PRO GLN ALA LYS PRO PRO THR VAL TYR ARG          
SEQRES   6 D  171  ALA LEU ASP PHE LEU LEU GLU GLN GLY PHE VAL HIS LYS          
SEQRES   7 D  171  VAL GLU SER THR ASN SER TYR VAL LEU CYS HIS LEU PHE          
SEQRES   8 D  171  ASP GLN PRO THR HIS THR SER ALA MET PHE ILE CYS ASP          
SEQRES   9 D  171  ARG CYS GLY ALA VAL LYS GLU GLU CYS ALA GLU GLY VAL          
SEQRES  10 D  171  GLU ASP ILE MET HIS THR LEU ALA ALA LYS MET GLY PHE          
SEQRES  11 D  171  ALA LEU ARG HIS ASN VAL ILE GLU ALA HIS GLY LEU CYS          
SEQRES  12 D  171  ALA ALA CYS VAL GLU VAL GLU ALA CYS ARG HIS PRO GLU          
SEQRES  13 D  171  GLN CYS GLN HIS ASP HIS SER VAL GLN VAL LYS LYS LYS          
SEQRES  14 D  171  PRO ARG                                                      
SEQRES   1 Y   33   DA  DG  DA  DA  DG  DT  DG  DT  DG  DA  DT  DA  DT          
SEQRES   2 Y   33   DT  DA  DT  DA  DA  DC  DA  DT  DT  DT  DC  DA  DT          
SEQRES   3 Y   33   DG  DA  DC  DT  DA  DT  DG                                  
SEQRES   1 Z   33   DT  DA  DG  DT  DC  DA  DT  DG  DA  DA  DA  DT  DG          
SEQRES   2 Z   33   DT  DT  DA  DT  DA  DA  DT  DA  DT  DC  DA  DC  DA          
SEQRES   3 Z   33   DC  DT  DT  DC  DT  DC  DA                                  
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  B 201       1                                                       
HET     ZN  B 202       1                                                       
HET     ZN  C 201       1                                                       
HET     ZN  C 202       1                                                       
HET     ZN  D 201       1                                                       
HET     ZN  D 202       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    8(ZN 2+)                                                     
HELIX    1   1 THR A    4  ARG A   20  1                                  17    
HELIX    2   2 THR A   25  GLN A   38  1                                  14    
HELIX    3   3 SER A   43  GLU A   55  1                                  13    
HELIX    4   4 LYS A   59  GLN A   73  1                                  15    
HELIX    5   5 ALA A  114  MET A  128  1                                  15    
HELIX    6   6 CYS A  143  CYS A  152  1                                  10    
HELIX    7   7 THR B    4  ARG B   20  1                                  17    
HELIX    8   8 THR B   25  GLN B   38  1                                  14    
HELIX    9   9 SER B   43  GLU B   55  1                                  13    
HELIX   10  10 LYS B   59  GLN B   73  1                                  15    
HELIX   11  11 ALA B  114  MET B  128  1                                  15    
HELIX   12  12 CYS B  143  CYS B  152  1                                  10    
HELIX   13  13 THR C    6  ARG C   20  1                                  15    
HELIX   14  14 THR C   25  GLN C   38  1                                  14    
HELIX   15  15 SER C   43  GLU C   55  1                                  13    
HELIX   16  16 LYS C   59  GLN C   73  1                                  15    
HELIX   17  17 GLU C   80  ASN C   83  5                                   4    
HELIX   18  18 ALA C  114  MET C  128  1                                  15    
HELIX   19  19 CYS C  143  CYS C  152  1                                  10    
HELIX   20  20 THR D    5  ARG D   20  1                                  16    
HELIX   21  21 THR D   25  LEU D   37  1                                  13    
HELIX   22  22 SER D   43  GLU D   55  1                                  13    
HELIX   23  23 LYS D   59  GLN D   73  1                                  15    
HELIX   24  24 ALA D  114  MET D  128  1                                  15    
HELIX   25  25 CYS D  143  ALA D  151  1                                   9    
SHEET    1   A 2 VAL A  76  VAL A  79  0                                        
SHEET    2   A 2 SER A  84  LEU A  87 -1  O  SER A  84   N  VAL A  79           
SHEET    1   B 6 VAL A 109  GLU A 112  0                                        
SHEET    2   B 6 ALA A  99  CYS A 103 -1  N  ALA A  99   O  GLU A 112           
SHEET    3   B 6 ALA A 131  LEU A 142  1  O  ALA A 139   N  MET A 100           
SHEET    4   B 6 ALA D 131  LEU D 142 -1  O  HIS D 134   N  HIS A 140           
SHEET    5   B 6 ALA D  99  CYS D 103  1  N  MET D 100   O  ALA D 139           
SHEET    6   B 6 VAL D 109  GLU D 112 -1  O  GLU D 112   N  ALA D  99           
SHEET    1   C 2 VAL B  76  VAL B  79  0                                        
SHEET    2   C 2 SER B  84  LEU B  87 -1  O  SER B  84   N  VAL B  79           
SHEET    1   D 6 VAL B 109  CYS B 113  0                                        
SHEET    2   D 6 SER B  98  CYS B 103 -1  N  ALA B  99   O  GLU B 112           
SHEET    3   D 6 ALA B 131  LEU B 142  1  O  ALA B 139   N  MET B 100           
SHEET    4   D 6 ALA C 131  LEU C 142 -1  O  GLU C 138   N  VAL B 136           
SHEET    5   D 6 SER C  98  CYS C 103  1  N  MET C 100   O  ALA C 139           
SHEET    6   D 6 VAL C 109  CYS C 113 -1  O  LYS C 110   N  PHE C 101           
SHEET    1   E 2 VAL C  76  VAL C  79  0                                        
SHEET    2   E 2 SER C  84  LEU C  87 -1  O  SER C  84   N  VAL C  79           
SHEET    1   F 2 VAL D  76  VAL D  79  0                                        
SHEET    2   F 2 SER D  84  LEU D  87 -1  O  VAL D  86   N  HIS D  77           
LINK         NE2 HIS A  77                ZN    ZN A 202     1555   1555  2.07  
LINK         SG  CYS A  88                ZN    ZN A 202     1555   1555  2.32  
LINK         NE2 HIS A  96                ZN    ZN A 202     1555   1555  2.09  
LINK         SG  CYS A 103                ZN    ZN A 201     1555   1555  2.31  
LINK         SG  CYS A 106                ZN    ZN A 201     1555   1555  2.35  
LINK         OE1 GLU A 111                ZN    ZN A 202     1555   1555  1.99  
LINK         OE2 GLU A 111                ZN    ZN A 202     1555   1555  2.63  
LINK         SG  CYS A 143                ZN    ZN A 201     1555   1555  2.33  
LINK         SG  CYS A 146                ZN    ZN A 201     1555   1555  2.31  
LINK         NE2 HIS B  77                ZN    ZN B 201     1555   1555  2.08  
LINK         SG  CYS B  88                ZN    ZN B 201     1555   1555  2.31  
LINK         NE2 HIS B  96                ZN    ZN B 201     1555   1555  2.08  
LINK         SG  CYS B 103                ZN    ZN B 202     1555   1555  2.35  
LINK         SG  CYS B 106                ZN    ZN B 202     1555   1555  2.34  
LINK         OE1 GLU B 111                ZN    ZN B 201     1555   1555  1.99  
LINK         SG  CYS B 143                ZN    ZN B 202     1555   1555  2.33  
LINK         SG  CYS B 146                ZN    ZN B 202     1555   1555  2.31  
LINK         NE2 HIS C  77                ZN    ZN C 202     1555   1555  2.08  
LINK         SG  CYS C  88                ZN    ZN C 202     1555   1555  2.33  
LINK         NE2 HIS C  96                ZN    ZN C 202     1555   1555  2.08  
LINK         SG  CYS C 103                ZN    ZN C 201     1555   1555  2.34  
LINK         SG  CYS C 106                ZN    ZN C 201     1555   1555  2.30  
LINK         OE1 GLU C 111                ZN    ZN C 202     1555   1555  1.99  
LINK         SG  CYS C 143                ZN    ZN C 201     1555   1555  2.33  
LINK         SG  CYS C 146                ZN    ZN C 201     1555   1555  2.31  
LINK         NE2 HIS D  77                ZN    ZN D 202     1555   1555  2.08  
LINK         SG  CYS D  88                ZN    ZN D 202     1555   1555  2.31  
LINK         NE2 HIS D  96                ZN    ZN D 202     1555   1555  2.08  
LINK         SG  CYS D 103                ZN    ZN D 201     1555   1555  2.34  
LINK         SG  CYS D 106                ZN    ZN D 201     1555   1555  2.34  
LINK         OE1 GLU D 111                ZN    ZN D 202     1555   1555  1.98  
LINK         OE2 GLU D 111                ZN    ZN D 202     1555   1555  2.64  
LINK         SG  CYS D 143                ZN    ZN D 201     1555   1555  2.34  
LINK         SG  CYS D 146                ZN    ZN D 201     1555   1555  2.34  
SITE     1 AC1  4 CYS A 103  CYS A 106  CYS A 143  CYS A 146                    
SITE     1 AC2  4 HIS A  77  CYS A  88  HIS A  96  GLU A 111                    
SITE     1 AC3  4 HIS B  77  CYS B  88  HIS B  96  GLU B 111                    
SITE     1 AC4  4 CYS B 103  CYS B 106  CYS B 143  CYS B 146                    
SITE     1 AC5  4 CYS C 103  CYS C 106  CYS C 143  CYS C 146                    
SITE     1 AC6  4 HIS C  77  CYS C  88  HIS C  96  GLU C 111                    
SITE     1 AC7  4 CYS D 103  CYS D 106  CYS D 143  CYS D 146                    
SITE     1 AC8  4 HIS D  77  CYS D  88  HIS D  96  GLU D 111                    
CRYST1  193.324   80.470   98.770  90.00 120.15  90.00 C 1 2 1      16          
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      0.005173  0.000000  0.003005        0.00000                         
SCALE2      0.000000  0.012427  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011709        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system