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Database: PDB
Entry: 2ZKY
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Original site: 2ZKY 
HEADER    OXIDOREDUCTASE                          31-MAR-08   2ZKY              
TITLE     CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G93A     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P                                    
KEYWDS    OXIDOREDUCTASE, HUMAN CU-ZN SUPEROXIDE DISMUTASE, ALS, FALS, METAL-   
KEYWDS   2 BINDING, DISEASE MUTATION, E.C.1.15.1.1, AMYOTROPHIC LATERAL         
KEYWDS   3 SCLEROSIS, ANTIOXIDANT, STRUCTURAL GENOMICS, NPPSFA, NATIONAL        
KEYWDS   4 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN         
KEYWDS   5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,M.SHIROUZU,M.URUSHITANI,           
AUTHOR   2 R.TAKAHASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS          
AUTHOR   3 INITIATIVE (RSGI)                                                    
REVDAT   2   04-APR-12 2ZKY    1       SPRSDE VERSN                             
REVDAT   1   24-MAR-09 2ZKY    0                                                
SPRSDE     04-APR-12 2ZKY      2YQX                                             
JRNL        AUTH   S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,M.SHIROUZU,M.URUSHITANI,  
JRNL        AUTH 2 R.TAKAHASHI,S.YOKOYAMA                                       
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT 
JRNL        TITL 2 G93A                                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 44635.650                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 88403                          
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 SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8837                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11584                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1288                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11100                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 479                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.95000                                              
REMARK   3    B22 (A**2) : -3.76000                                             
REMARK   3    B33 (A**2) : 1.80000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.000 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.690 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.790 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 36.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028102.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94985                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.157                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1380                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.89800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.459                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PU0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CACODYLATE(PH 6.5), 0.2M NACL,      
REMARK 280  2.0M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       72.40950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.40950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       82.61900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.25450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       82.61900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.25450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.40950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       82.61900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      102.25450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.40950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       82.61900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      102.25450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.4 KCAL/MOL                        
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.4 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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     GLY A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     LEU C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     LEU D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     GLY E    -5                                                      
REMARK 465     PRO E    -4                                                      
REMARK 465     LEU E    -3                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     GLY F    -5                                                      
REMARK 465     PRO F    -4                                                      
REMARK 465     LEU F    -3                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     GLY G    -5                                                      
REMARK 465     PRO G    -4                                                      
REMARK 465     LEU G    -3                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     MET G     0                                                      
REMARK 465     GLY H    -5                                                      
REMARK 465     PRO H    -4                                                      
REMARK 465     LEU H    -3                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     SER H    -1                                                      
REMARK 465     MET H     0                                                      
REMARK 465     GLY I    -5                                                      
REMARK 465     PRO I    -4                                                      
REMARK 465     LEU I    -3                                                      
REMARK 465     GLY I    -2                                                      
REMARK 465     SER I    -1                                                      
REMARK 465     MET I     0                                                      
REMARK 465     GLY J    -5                                                      
REMARK 465     PRO J    -4                                                      
REMARK 465     LEU J    -3                                                      
REMARK 465     GLY J    -2                                                      
REMARK 465     SER J    -1                                                      
REMARK 465     MET J     0                                                      
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    LEU A 126       28.78     36.27                                   
REMARK 500    ASP C 109      -54.75      8.06                                   
REMARK 500    LEU C 126       18.93     59.83                                   
REMARK 500    SER G  25      -40.98    -25.61                                   
REMARK 500    ASN G  26       27.61   -147.08                                   
REMARK 500    SER G  68       17.51     40.92                                   
REMARK 500    ASP G  90     -167.82    -61.67                                   
REMARK 500    LEU G 126       19.94     43.24                                   
REMARK 500    LYS G 128       -9.29   -145.05                                   
REMARK 500    LYS G 136      -65.35   -109.29                                   
REMARK 500    ASN H  26       49.52    -97.91                                   
REMARK 500    ALA H  55       41.52   -104.07                                   
REMARK 500    ASN I  26       42.80   -108.71                                   
REMARK 500    ALA I  55       59.14   -114.64                                   
REMARK 500    PRO I  66       12.07    -67.50                                   
REMARK 500    LYS I 128       27.52   -148.90                                   
REMARK 500    ASN I 131     -179.02    -55.32                                   
REMARK 500    SER J 107      163.66    178.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU B  49        25.0      L          L   OUTSIDE RANGE           
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 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1  99.0                                              
REMARK 620 3 HIS A  80   ND1 115.8 118.2                                        
REMARK 620 4 ASP A  83   OD1 103.5 100.5 117.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 102.7                                              
REMARK 620 3 HIS B  80   ND1 108.0 121.4                                        
REMARK 620 4 ASP B  83   OD1 108.0 101.9 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 603  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1  99.3                                              
REMARK 620 3 HIS C  80   ND1 108.6 126.9                                        
REMARK 620 4 ASP C  83   OD1 102.6  87.1 127.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 604  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 106.3                                              
REMARK 620 3 HIS D  80   ND1 110.9 117.8                                        
REMARK 620 4 ASP D  83   OD1 104.5 102.9 113.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 605  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1 106.3                                              
REMARK 620 3 HIS E  80   ND1 113.1 122.7                                        
REMARK 620 4 ASP E  83   OD1 102.2  90.9 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 606  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 105.0                                              
REMARK 620 3 HIS F  80   ND1 115.7 121.7                                        
REMARK 620 4 ASP F  83   OD1 101.2  94.4 115.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 607  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 108.5                                              
REMARK 620 3 HIS G  80   ND1 109.6 122.1                                        
REMARK 620 4 ASP G  83   OD1 104.3  89.5 120.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 608  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1  96.9                                              
REMARK 620 3 HIS H  80   ND1 107.7 126.8                                        
REMARK 620 4 ASP H  83   OD1 110.3 105.2 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 609  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1 110.7                                              
REMARK 620 3 HIS I  80   ND1 106.7 121.9                                        
REMARK 620 4 ASP I  83   OD1 101.9 113.2 100.3                                  
REMARK 620 5 ASP I  83   OD2 154.1  78.5  86.6  53.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 610  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 105.6                                              
REMARK 620 3 HIS J  80   ND1 115.8 117.7                                        
REMARK 620 4 ASP J  83   OD1 102.1 103.3 110.6                                  
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 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 609                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 610                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZKW   RELATED DB: PDB                                   
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN SPACE GROUP          
REMARK 900 P21                                                                  
REMARK 900 RELATED ID: 2ZKX   RELATED DB: PDB                                   
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN SPACE GROUP          
REMARK 900 I212121                                                              
REMARK 900 RELATED ID: AR_001000133.1   RELATED DB: TARGETDB                    
DBREF  2ZKY A    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY B    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY C    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY D    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY E    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY F    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY G    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY H    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY I    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKY J    0   153  UNP    P00441   SODC_HUMAN       1    154             
SEQADV 2ZKY GLY A   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO A   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU A   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY A   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER A   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA A   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY B   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO B   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU B   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY B   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER B   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA B   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY C   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO C   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU C   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY C   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER C   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA C   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY D   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO D   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU D   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY D   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER D   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA D   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY E   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO E   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU E   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY E   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER E   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA E   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY F   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO F   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU F   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY F   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER F   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA F   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY G   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO G   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU G   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY G   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER G   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA G   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY H   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO H   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU H   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY H   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER H   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA H   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY I   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO I   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU I   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY I   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER I   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA I   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 2ZKY GLY J   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY PRO J   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY LEU J   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY GLY J   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY SER J   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKY ALA J   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQRES   1 A  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 A  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 A  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 A  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 A  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 A  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 A  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 A  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 A  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 A  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 A  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 A  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 A  159  ILE ALA GLN                                                  
SEQRES   1 B  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 B  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 B  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 B  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 B  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 B  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 B  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 B  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 B  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 B  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 B  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 B  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 B  159  ILE ALA GLN                                                  
SEQRES   1 C  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 C  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 C  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 C  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 C  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 C  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 C  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 C  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 C  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 C  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 C  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 C  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 C  159  ILE ALA GLN                                                  
SEQRES   1 D  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 D  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 D  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 D  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 D  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 D  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 D  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 D  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 D  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 D  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 D  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 D  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 D  159  ILE ALA GLN                                                  
SEQRES   1 E  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 E  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 E  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 E  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 E  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 E  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 E  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 E  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 E  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 E  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 E  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 E  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 E  159  ILE ALA GLN                                                  
SEQRES   1 F  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 F  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 F  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 F  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 F  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 F  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 F  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 F  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 F  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 F  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 F  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 F  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 F  159  ILE ALA GLN                                                  
SEQRES   1 G  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 G  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 G  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 G  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 G  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 G  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 G  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 G  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 G  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 G  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 G  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 G  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 G  159  ILE ALA GLN                                                  
SEQRES   1 H  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 H  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 H  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 H  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 H  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 H  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 H  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 H  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 H  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 H  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 H  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 H  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 H  159  ILE ALA GLN                                                  
SEQRES   1 I  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 I  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 I  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 I  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 I  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 I  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 I  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 I  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 I  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 I  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 I  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 I  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 I  159  ILE ALA GLN                                                  
SEQRES   1 J  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 J  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 J  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 J  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 J  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 J  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 J  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU GLY          
SEQRES   8 J  159  ASN VAL THR ALA ASP LYS ASP ALA VAL ALA ASP VAL SER          
SEQRES   9 J  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 J  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 J  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 J  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 J  159  ILE ALA GLN                                                  
HET     ZN  A 601       1                                                       
HET     ZN  B 602       1                                                       
HET     ZN  C 603       1                                                       
HET     ZN  D 604       1                                                       
HET     ZN  E 605       1                                                       
HET     ZN  F 606       1                                                       
HET     ZN  G 607       1                                                       
HET     ZN  H 608       1                                                       
HET     ZN  I 609       1                                                       
HET     ZN  J 610       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  11   ZN    10(ZN 2+)                                                    
FORMUL  21  HOH   *479(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  CYS A  111  5                                   5    
HELIX    3   3 GLU A  133  GLY A  138  1                                   6    
HELIX    4   4 ALA B   55  GLY B   61  5                                   7    
HELIX    5   5 SER B  107  CYS B  111  5                                   5    
HELIX    6   6 GLU B  133  GLY B  138  1                                   6    
HELIX    7   7 ALA C   55  GLY C   61  5                                   7    
HELIX    8   8 GLU C  133  GLY C  138  1                                   6    
HELIX    9   9 ALA D   55  GLY D   61  5                                   7    
HELIX   10  10 SER D  107  CYS D  111  5                                   5    
HELIX   11  11 GLU D  133  GLY D  138  1                                   6    
HELIX   12  12 ALA E   55  GLY E   61  5                                   7    
HELIX   13  13 SER E  107  CYS E  111  5                                   5    
HELIX   14  14 ASN E  131  THR E  137  1                                   7    
HELIX   15  15 ALA F   55  GLY F   61  5                                   7    
HELIX   16  16 ASN F  131  GLY F  138  1                                   8    
HELIX   17  17 ALA G   55  GLY G   61  5                                   7    
HELIX   18  18 CYS H   57  GLY H   61  5                                   5    
HELIX   19  19 SER H  107  CYS H  111  5                                   5    
HELIX   20  20 ALA I   55  GLY I   61  5                                   7    
HELIX   21  21 ALA J   55  GLY J   61  5                                   7    
HELIX   22  22 SER J  107  CYS J  111  5                                   5    
HELIX   23  23 ASN J  131  THR J  135  5                                   5    
SHEET    1   A 5 VAL A  94  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LYS A   9 -1  N  LEU A   8   O  GLY A  16           
SHEET    5   A 5 GLY A 150  ALA A 152 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1   C 5 VAL B  94  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  VAL B  31   O  ILE B  99           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ALA B 152 -1  O  ALA B 152   N  LYS B   3           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  PHE B  45   O  GLY B  85           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  ALA B 145   N  VAL B 119           
SHEET    1   E 5 VAL C  94  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  29   O  ASP C 101           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 THR C   2  LEU C   8 -1  N  LEU C   8   O  GLY C  16           
SHEET    5   E 5 GLY C 150  ALA C 152 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 VAL D  94  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LYS D   9 -1  N  LEU D   8   O  GLY D  16           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  ALA D 145   N  VAL D 119           
SHEET    1   I 5 VAL E  94  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    3   I 5 GLN E  15  GLU E  21 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 LYS E   3  LEU E   8 -1  N  LEU E   8   O  GLY E  16           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  ALA E 145   N  VAL E 119           
SHEET    1   K 5 VAL F  94  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  LYS F  36 -1  N  VAL F  31   O  ILE F  99           
SHEET    3   K 5 GLN F  15  GLU F  21 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 LYS F   3  LYS F   9 -1  N  CYS F   6   O  ILE F  18           
SHEET    5   K 5 GLY F 150  ALA F 152 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  PHE F  45   O  GLY F  85           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SHEET    1   M 5 VAL G  94  ASP G 101  0                                        
SHEET    2   M 5 VAL G  29  LYS G  36 -1  N  VAL G  31   O  ILE G  99           
SHEET    3   M 5 GLN G  15  GLU G  21 -1  N  ASN G  19   O  TRP G  32           
SHEET    4   M 5 LYS G   3  LYS G   9 -1  N  LEU G   8   O  GLY G  16           
SHEET    5   M 5 GLY G 150  ALA G 152 -1  O  GLY G 150   N  VAL G   5           
SHEET    1   N 4 ASP G  83  ALA G  89  0                                        
SHEET    2   N 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   N 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4   N 4 ARG G 143  VAL G 148 -1  O  GLY G 147   N  LEU G 117           
SHEET    1   O 9 LYS H   3  LYS H   9  0                                        
SHEET    2   O 9 GLN H  15  GLN H  22 -1  O  GLY H  16   N  LEU H   8           
SHEET    3   O 9 VAL H  29  LYS H  36 -1  O  TRP H  32   N  ASN H  19           
SHEET    4   O 9 ALA H  95  ASP H 101 -1  O  ALA H  95   N  ILE H  35           
SHEET    5   O 9 ASP H  83  ALA H  89 -1  N  THR H  88   O  ASP H  96           
SHEET    6   O 9 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    7   O 9 THR H 116  HIS H 120 -1  O  HIS H 120   N  GLY H  44           
SHEET    8   O 9 ARG H 143  ILE H 151 -1  O  GLY H 147   N  LEU H 117           
SHEET    9   O 9 LYS H   3  LYS H   9 -1  N  VAL H   5   O  GLY H 150           
SHEET    1   P 5 ALA I  95  ASP I 101  0                                        
SHEET    2   P 5 VAL I  29  LYS I  36 -1  N  VAL I  29   O  ASP I 101           
SHEET    3   P 5 GLN I  15  GLN I  22 -1  N  ASN I  19   O  TRP I  32           
SHEET    4   P 5 THR I   2  LEU I   8 -1  N  LEU I   8   O  GLY I  16           
SHEET    5   P 5 GLY I 150  ALA I 152 -1  O  ALA I 152   N  LYS I   3           
SHEET    1   Q 4 ASP I  83  ALA I  89  0                                        
SHEET    2   Q 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   Q 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4   Q 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   R 5 VAL J  94  ASP J 101  0                                        
SHEET    2   R 5 VAL J  29  LYS J  36 -1  N  VAL J  29   O  ASP J 101           
SHEET    3   R 5 GLN J  15  GLN J  22 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   R 5 THR J   2  LYS J   9 -1  N  LEU J   8   O  GLY J  16           
SHEET    5   R 5 GLY J 150  ALA J 152 -1  O  ALA J 152   N  LYS J   3           
SHEET    1   S 4 ASP J  83  ALA J  89  0                                        
SHEET    2   S 4 GLY J  41  HIS J  48 -1  N  PHE J  45   O  GLY J  85           
SHEET    3   S 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   S 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.06  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.08  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.06  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.07  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.07  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.07  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.07  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.06  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.05  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.05  
LINK         ND1 HIS A  63                ZN    ZN A 601     1555   1555  2.13  
LINK         ND1 HIS A  71                ZN    ZN A 601     1555   1555  2.17  
LINK         ND1 HIS A  80                ZN    ZN A 601     1555   1555  2.21  
LINK         OD1 ASP A  83                ZN    ZN A 601     1555   1555  1.97  
LINK         ND1 HIS B  63                ZN    ZN B 602     1555   1555  1.95  
LINK         ND1 HIS B  71                ZN    ZN B 602     1555   1555  2.01  
LINK         ND1 HIS B  80                ZN    ZN B 602     1555   1555  1.98  
LINK         OD1 ASP B  83                ZN    ZN B 602     1555   1555  1.93  
LINK         ND1 HIS C  63                ZN    ZN C 603     1555   1555  2.22  
LINK         ND1 HIS C  71                ZN    ZN C 603     1555   1555  2.15  
LINK         ND1 HIS C  80                ZN    ZN C 603     1555   1555  1.87  
LINK         OD1 ASP C  83                ZN    ZN C 603     1555   1555  1.88  
LINK         ND1 HIS D  63                ZN    ZN D 604     1555   1555  1.95  
LINK         ND1 HIS D  71                ZN    ZN D 604     1555   1555  2.01  
LINK         ND1 HIS D  80                ZN    ZN D 604     1555   1555  2.05  
LINK         OD1 ASP D  83                ZN    ZN D 604     1555   1555  1.94  
LINK         ND1 HIS E  63                ZN    ZN E 605     1555   1555  2.01  
LINK         ND1 HIS E  71                ZN    ZN E 605     1555   1555  2.15  
LINK         ND1 HIS E  80                ZN    ZN E 605     1555   1555  2.04  
LINK         OD1 ASP E  83                ZN    ZN E 605     1555   1555  1.92  
LINK         ND1 HIS F  63                ZN    ZN F 606     1555   1555  1.93  
LINK         ND1 HIS F  71                ZN    ZN F 606     1555   1555  2.13  
LINK         ND1 HIS F  80                ZN    ZN F 606     1555   1555  2.06  
LINK         OD1 ASP F  83                ZN    ZN F 606     1555   1555  1.86  
LINK         ND1 HIS G  63                ZN    ZN G 607     1555   1555  2.28  
LINK         ND1 HIS G  71                ZN    ZN G 607     1555   1555  2.17  
LINK         ND1 HIS G  80                ZN    ZN G 607     1555   1555  2.19  
LINK         OD1 ASP G  83                ZN    ZN G 607     1555   1555  1.94  
LINK         ND1 HIS H  63                ZN    ZN H 608     1555   1555  2.12  
LINK         ND1 HIS H  71                ZN    ZN H 608     1555   1555  1.98  
LINK         ND1 HIS H  80                ZN    ZN H 608     1555   1555  1.92  
LINK         OD1 ASP H  83                ZN    ZN H 608     1555   1555  1.87  
LINK         ND1 HIS I  63                ZN    ZN I 609     1555   1555  2.09  
LINK         ND1 HIS I  71                ZN    ZN I 609     1555   1555  2.24  
LINK         ND1 HIS I  80                ZN    ZN I 609     1555   1555  2.12  
LINK         OD1 ASP I  83                ZN    ZN I 609     1555   1555  2.00  
LINK         ND1 HIS J  63                ZN    ZN J 610     1555   1555  2.18  
LINK         ND1 HIS J  71                ZN    ZN J 610     1555   1555  2.06  
LINK         ND1 HIS J  80                ZN    ZN J 610     1555   1555  2.02  
LINK         OD1 ASP J  83                ZN    ZN J 610     1555   1555  1.91  
LINK         OD2 ASP I  83                ZN    ZN I 609     1555   1555  2.69  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC3  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC4  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC5  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 AC5  5 LYS E 136                                                     
SITE     1 AC6  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC7  5 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     2 AC7  5 LYS G 136                                                     
SITE     1 AC8  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 AC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 BC1  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
CRYST1  165.238  204.509  144.819  90.00  90.00  90.00 C 2 2 21     80          
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      0.006052  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004890  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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