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Database: PDB
Entry: 1FUN
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Original site: 1FUN 
HEADER    OXIDOREDUCTASE                          23-JUL-98   1FUN              
TITLE     SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU,             
TITLE    2 CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E,            
TITLE    3 C6A, C111S)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, F, B, G, C, H, D, I, E, J;                                 
COMPND   4 SYNONYM: SOD;                                                        
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: FIVE BIOLOGICAL DIMERS ARE PRESENT IN THE             
COMPND   9 CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THEY ARE A AND F, B AND            
COMPND  10 G, C AND H, D AND I, E AND J.                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.LO,J.A.TAINER,E.D.GETZOFF                                         
REVDAT   2   24-FEB-09 1FUN    1       VERSN                                    
REVDAT   1   23-JUL-99 1FUN    0                                                
JRNL        AUTH   C.L.FISHER,D.E.CABELLI,R.A.HALLEWELL,P.BEROZA,               
JRNL        AUTH 2 T.P.LO,E.D.GETZOFF,J.A.TAINER                                
JRNL        TITL   COMPUTATIONAL, PULSE-RADIOLYTIC, AND STRUCTURAL              
JRNL        TITL 2 INVESTIGATIONS OF LYSINE-136 AND ITS ROLE IN THE             
JRNL        TITL 3 ELECTROSTATIC TRIAD OF HUMAN CU,ZN SUPEROXIDE                
JRNL        TITL 4 DISMUTASE.                                                   
JRNL        REF    PROTEINS                      V.  29   103 1997              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   9294870                                                      
JRNL        DOI    10.1002/(SICI)1097-0134(199709)29:1<103::AID-PROT8>          
JRNL        DOI  2 3.0.CO;2-G                                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 55654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11090                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 239                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FUN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
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       72.75000            
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       72.75000            
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      102.60000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.75000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.75000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       83.50000            
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: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 1330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
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: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 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: 1450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
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: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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  65       70.14   -150.54                                   
REMARK 500    LYS A  75       40.77   -102.07                                   
REMARK 500    LYS A  91        2.79    -68.88                                   
REMARK 500    SER A  98       73.30   -151.58                                   
REMARK 500    ASP A 125       27.54    -78.01                                   
REMARK 500    LEU A 126       42.14     30.49                                   
REMARK 500    SER F  25      -60.22    -20.03                                   
REMARK 500    ASP F  90     -167.69    -72.33                                   
REMARK 500    SER F  98       90.95   -165.28                                   
REMARK 500    LYS F 128       31.85    -95.85                                   
REMARK 500    THR F 135       32.91    -95.32                                   
REMARK 500    GLU F 136      -42.09   -145.05                                   
REMARK 500    ASP B  11       36.46    -78.28                                   
REMARK 500    GLU B  40      130.78    -26.53                                   
REMARK 500    CYS B  57      -16.06    -44.81                                   
REMARK 500    SER B  68       53.55     33.55                                   
REMARK 500    SER B  98       83.13   -169.33                                   
REMARK 500    ASP B 125       21.58    -77.94                                   
REMARK 500    LEU B 126       16.72     47.16                                   
REMARK 500    GLU B 136      -71.31   -101.97                                   
REMARK 500    SER G  25        7.93    -56.17                                   
REMARK 500    ASN G  26       12.30   -166.65                                   
REMARK 500    ALA G  55       43.69    -94.43                                   
REMARK 500    PHE G  64      102.87    -52.89                                   
REMARK 500    SER G  98       98.19   -162.72                                   
REMARK 500    HIS G 110       38.44    -96.63                                   
REMARK 500    ARG C  69     -162.79   -100.15                                   
REMARK 500    HIS C 110       45.98   -106.15                                   
REMARK 500    GLU C 136      -65.96   -106.99                                   
REMARK 500    LYS H  23      -70.27    -66.13                                   
REMARK 500    LYS H 128       38.34    -96.62                                   
REMARK 500    LYS D  23      -73.37    -82.26                                   
REMARK 500    SER D  25        1.15    -49.04                                   
REMARK 500    ASN D  26        7.35   -155.15                                   
REMARK 500    ALA D  55       40.66   -102.81                                   
REMARK 500    ASN D  65       81.80   -150.99                                   
REMARK 500    SER D  68       16.92     43.89                                   
REMARK 500    GLU D  77      -78.29    -63.52                                   
REMARK 500    ARG D  79      144.53   -177.22                                   
REMARK 500    ASP D 125       47.83    -92.55                                   
REMARK 500    LEU D 126       44.40     35.80                                   
REMARK 500    LYS D 128       43.36    -80.80                                   
REMARK 500    ALA I  60        0.31    -69.57                                   
REMARK 500    SER I  68       48.41     32.61                                   
REMARK 500    SER I  98       84.69   -158.42                                   
REMARK 500    LYS E  75       33.57    -76.87                                   
REMARK 500    ASP E  90     -170.60    -69.44                                   
REMARK 500    SER E  98       92.57   -166.62                                   
REMARK 500    HIS E 110       45.16   -101.64                                   
REMARK 500    GLU E 136      -77.97   -103.89                                   
REMARK 500    ASP J  11       37.93    -78.21                                   
REMARK 500    GLU J  21      127.13   -171.50                                   
REMARK 500    LYS J  23      -72.42    -60.58                                   
REMARK 500    ALA J  55       50.01   -103.12                                   
REMARK 500    SER J  59       -7.79    -58.99                                   
REMARK 500    ASP J  92       42.97   -100.70                                   
REMARK 500    ASP J  96       73.63   -110.13                                   
REMARK 500    SER J  98      113.77   -165.42                                   
REMARK 500    SER J 102       48.38   -144.57                                   
REMARK 500    VAL J 103      -49.40   -135.68                                   
REMARK 500    LEU J 126       16.78     52.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH I 415        DISTANCE =  5.16 ANGSTROMS                       
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                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 138.7                                              
REMARK 620 3 HIS A  63   NE2  70.8  96.5                                        
REMARK 620 4 HIS A 120   NE2 106.7 108.3 137.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 ASP A  83   OD1  95.2                                              
REMARK 620 3 HIS A  63   ND1 109.9 107.2                                        
REMARK 620 4 HIS A  80   ND1 107.6 116.5 118.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HIS B  63   NE2  94.6                                              
REMARK 620 3 HIS B 120   NE2 108.3 140.7                                        
REMARK 620 4 HIS B  46   ND1 145.7  69.9 102.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  80   ND1                                                    
REMARK 620 2 ASP B  83   OD1 114.7                                              
REMARK 620 3 HIS B  63   ND1 104.4 105.6                                        
REMARK 620 4 HIS B  71   ND1 124.8  94.7 111.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   NE2                                                    
REMARK 620 2 HIS C 120   NE2 143.6                                              
REMARK 620 3 HIS C  48   NE2  93.9 109.9                                        
REMARK 620 4 HIS C  46   ND1  75.9  96.7 145.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  83   OD1                                                    
REMARK 620 2 HIS C  71   ND1  95.7                                              
REMARK 620 3 HIS C  80   ND1 113.3 121.1                                        
REMARK 620 4 HIS C  63   ND1  93.0 115.2 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   NE2                                                    
REMARK 620 2 HIS D 120   NE2 129.3                                              
REMARK 620 3 HIS D  46   ND1  72.6  93.1                                        
REMARK 620 4 HIS D  48   NE2 102.0 101.2 164.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  83   OD1                                                    
REMARK 620 2 HIS D  71   ND1  97.3                                              
REMARK 620 3 HIS D  80   ND1  96.7 107.1                                        
REMARK 620 4 HIS D  63   ND1  94.4 141.4 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 120   NE2                                                    
REMARK 620 2 HIS E  46   ND1 104.9                                              
REMARK 620 3 HIS E  48   NE2 119.6 133.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  83   OD2                                                    
REMARK 620 2 ASP E  83   OD1  54.5                                              
REMARK 620 3 HIS E  80   ND1  93.3 115.7                                        
REMARK 620 4 HIS E  71   ND1  63.0 100.8 111.0                                  
REMARK 620 5 HIS E  63   ND1 164.9 110.4  93.6 126.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F  46   ND1 140.6                                              
REMARK 620 3 HIS F 120   NE2 103.4 106.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 ASP F  83   OD2  62.3                                              
REMARK 620 3 HIS F  80   ND1  99.5  89.3                                        
REMARK 620 4 HIS F  71   ND1 115.4  71.8 123.4                                  
REMARK 620 5 HIS F  63   ND1  91.3 153.6  95.5 124.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  48   NE2                                                    
REMARK 620 2 HIS G 120   NE2 102.5                                              
REMARK 620 3 HIS G  46   ND1 143.4 104.7                                        
REMARK 620 4 HIS G  63   NE2 100.2 144.6  70.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  80   ND1                                                    
REMARK 620 2 ASP G  83   OD1 108.0                                              
REMARK 620 3 HIS G  63   ND1 106.2  98.6                                        
REMARK 620 4 ASP G  83   OD2  94.1  53.6 150.2                                  
REMARK 620 5 HIS G  71   ND1 112.7 112.8 117.3  72.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  63   NE2                                                    
REMARK 620 2 HIS H 120   NE2 146.1                                              
REMARK 620 3 HIS H  46   ND1  71.0  97.3                                        
REMARK 620 4 HIS H  48   NE2 100.8 108.2 138.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  80   ND1                                                    
REMARK 620 2 ASP H  83   OD2  84.7                                              
REMARK 620 3 HIS H  71   ND1 123.7  71.1                                        
REMARK 620 4 HIS H  63   ND1 111.4 150.0 114.7                                  
REMARK 620 5 ASP H  83   OD1 100.8  50.8 101.3 100.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  46   ND1                                                    
REMARK 620 2 HIS I 120   NE2  89.7                                              
REMARK 620 3 HIS I  48   NE2 149.6 113.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  80   ND1 105.2                                              
REMARK 620 3 ASP I  83   OD1 102.1  95.2                                        
REMARK 620 4 HIS I  71   ND1 120.5 122.6 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  46   ND1                                                    
REMARK 620 2 HIS J  63   NE2  84.7                                              
REMARK 620 3 HIS J 120   NE2 100.9 142.5                                        
REMARK 620 4 HIS J  48   NE2 126.1 107.5  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  71   ND1                                                    
REMARK 620 2 HIS J  80   ND1 114.0                                              
REMARK 620 3 ASP J  83   OD1  98.8  95.3                                        
REMARK 620 4 HIS J  63   ND1 118.5 112.4 114.6                                  
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 CU A 154                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154                  
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 200                 
DBREF  1FUN A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1FUN J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1FUN ALA A    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER A  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU A  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA F    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER F  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU F  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA B    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER B  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU B  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA G    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER G  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU G  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA C    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER C  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU C  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA H    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER H  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU H  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA D    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER D  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU D  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA I    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER I  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU I  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA E    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER E  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU E  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQADV 1FUN ALA J    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1FUN SER J  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1FUN GLU J  136  UNP  P00441    LYS   136 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET    SO4  F 200       5                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL  11   CU    10(CU 2+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  SO4    O4 S 2-                                                      
FORMUL  32  HOH   *239(H2 O)                                                    
HELIX    1   1 THR A   58  ALA A   60  5                                   3    
HELIX    2   2 SER A  134  THR A  137  1                                   4    
HELIX    3   3 THR F   58  ALA F   60  5                                   3    
HELIX    4   4 GLU F  133  THR F  135  5                                   3    
HELIX    5   5 GLY B   56  ALA B   60  5                                   5    
HELIX    6   6 GLU B  132  GLU B  136  1                                   5    
HELIX    7   7 GLY G   56  ALA G   60  5                                   5    
HELIX    8   8 GLU G  132  THR G  137  5                                   6    
HELIX    9   9 GLY C   56  ALA C   60  5                                   5    
HELIX   10  10 GLU C  132  GLU C  136  1                                   5    
HELIX   11  11 GLY H   56  ALA H   60  5                                   5    
HELIX   12  12 GLU H  132  THR H  135  5                                   4    
HELIX   13  13 THR D   58  ALA D   60  5                                   3    
HELIX   14  14 GLY D  108  HIS D  110  5                                   3    
HELIX   15  15 GLU D  132  GLU D  136  1                                   5    
HELIX   16  16 GLY I   56  ALA I   60  5                                   5    
HELIX   17  17 GLU I  132  THR I  135  5                                   4    
HELIX   18  18 THR E   58  ALA E   60  5                                   3    
HELIX   19  19 GLU E  132  THR E  135  5                                   4    
HELIX   20  20 THR J   58  ALA J   60  5                                   3    
HELIX   21  21 GLU J  132  THR J  135  5                                   4    
SHEET    1   A 4 LYS A   3  LEU A   8  0                                        
SHEET    2   A 4 GLN A  15  GLU A  21 -1  N  PHE A  20   O  ALA A   4           
SHEET    3   A 4 VAL A  29  LYS A  36 -1  N  LYS A  36   O  GLN A  15           
SHEET    4   A 4 ALA A  95  ASP A 101 -1  N  ASP A 101   O  VAL A  29           
SHEET    1   B 2 GLY A  41  GLY A  44  0                                        
SHEET    2   B 2 ASN A  86  ALA A  89 -1  N  ALA A  89   O  GLY A  41           
SHEET    1   C 3 PHE A  45  HIS A  48  0                                        
SHEET    2   C 3 THR A 116  HIS A 120 -1  N  VAL A 118   O  HIS A  46           
SHEET    3   C 3 ARG A 143  VAL A 148 -1  N  GLY A 147   O  LEU A 117           
SHEET    1   D 5 ILE F 149  ILE F 151  0                                        
SHEET    2   D 5 LYS F   3  LEU F   8 -1  N  VAL F   5   O  GLY F 150           
SHEET    3   D 5 GLN F  15  GLN F  22 -1  N  PHE F  20   O  ALA F   4           
SHEET    4   D 5 VAL F  29  LYS F  36 -1  N  LYS F  36   O  GLN F  15           
SHEET    5   D 5 VAL F  94  ASP F 101 -1  N  ASP F 101   O  VAL F  29           
SHEET    1   E 2 GLY F  41  GLY F  44  0                                        
SHEET    2   E 2 ASN F  86  ALA F  89 -1  N  ALA F  89   O  GLY F  41           
SHEET    1   F 3 PHE F  45  HIS F  48  0                                        
SHEET    2   F 3 THR F 116  HIS F 120 -1  N  VAL F 118   O  HIS F  46           
SHEET    3   F 3 ARG F 143  VAL F 148 -1  N  GLY F 147   O  LEU F 117           
SHEET    1   G 4 LYS B   3  LEU B   8  0                                        
SHEET    2   G 4 GLN B  15  GLU B  21 -1  N  PHE B  20   O  ALA B   4           
SHEET    3   G 4 TRP B  32  LYS B  36 -1  N  LYS B  36   O  GLN B  15           
SHEET    4   G 4 ALA B  95  SER B  98 -1  N  VAL B  97   O  GLY B  33           
SHEET    1   H 2 GLY B  41  GLY B  44  0                                        
SHEET    2   H 2 ASN B  86  ALA B  89 -1  N  ALA B  89   O  GLY B  41           
SHEET    1   I 3 PHE B  45  VAL B  47  0                                        
SHEET    2   I 3 THR B 116  HIS B 120 -1  N  VAL B 118   O  HIS B  46           
SHEET    3   I 3 ARG B 143  VAL B 148 -1  N  GLY B 147   O  LEU B 117           
SHEET    1   J 4 LYS G   3  LEU G   8  0                                        
SHEET    2   J 4 GLN G  15  GLU G  21 -1  N  PHE G  20   O  ALA G   4           
SHEET    3   J 4 VAL G  29  LYS G  36 -1  N  LYS G  36   O  GLN G  15           
SHEET    4   J 4 ALA G  95  ASP G 101 -1  N  ASP G 101   O  VAL G  29           
SHEET    1   K 2 GLY G  41  GLY G  44  0                                        
SHEET    2   K 2 ASN G  86  ALA G  89 -1  N  ALA G  89   O  GLY G  41           
SHEET    1   L 3 PHE G  45  HIS G  48  0                                        
SHEET    2   L 3 THR G 116  HIS G 120 -1  N  VAL G 118   O  HIS G  46           
SHEET    3   L 3 ARG G 143  VAL G 148 -1  N  GLY G 147   O  LEU G 117           
SHEET    1   M 4 LYS C   3  LYS C   9  0                                        
SHEET    2   M 4 GLN C  15  GLN C  22 -1  N  PHE C  20   O  ALA C   4           
SHEET    3   M 4 VAL C  29  LYS C  36 -1  N  LYS C  36   O  GLN C  15           
SHEET    4   M 4 SER C  98  ASP C 101 -1  N  ASP C 101   O  VAL C  29           
SHEET    1   N 2 GLY C  41  GLY C  44  0                                        
SHEET    2   N 2 ASN C  86  ALA C  89 -1  N  ALA C  89   O  GLY C  41           
SHEET    1   O 3 PHE C  45  HIS C  48  0                                        
SHEET    2   O 3 THR C 116  HIS C 120 -1  N  VAL C 118   O  HIS C  46           
SHEET    3   O 3 ARG C 143  VAL C 148 -1  N  GLY C 147   O  LEU C 117           
SHEET    1   P 5 ILE H 149  ILE H 151  0                                        
SHEET    2   P 5 LYS H   3  LYS H   9 -1  N  VAL H   5   O  GLY H 150           
SHEET    3   P 5 GLN H  15  GLU H  21 -1  N  PHE H  20   O  ALA H   4           
SHEET    4   P 5 VAL H  29  LYS H  36 -1  N  LYS H  36   O  GLN H  15           
SHEET    5   P 5 SER H  98  ASP H 101 -1  N  ASP H 101   O  VAL H  29           
SHEET    1   Q 2 GLY H  41  GLY H  44  0                                        
SHEET    2   Q 2 ASN H  86  ALA H  89 -1  N  ALA H  89   O  GLY H  41           
SHEET    1   R 3 PHE H  45  HIS H  48  0                                        
SHEET    2   R 3 THR H 116  HIS H 120 -1  N  VAL H 118   O  HIS H  46           
SHEET    3   R 3 ARG H 143  VAL H 148 -1  N  GLY H 147   O  LEU H 117           
SHEET    1   S 5 ILE D 149  ILE D 151  0                                        
SHEET    2   S 5 LYS D   3  LYS D   9 -1  N  VAL D   5   O  GLY D 150           
SHEET    3   S 5 GLN D  15  GLU D  21 -1  N  PHE D  20   O  ALA D   4           
SHEET    4   S 5 VAL D  29  LYS D  36 -1  N  LYS D  36   O  GLN D  15           
SHEET    5   S 5 ALA D  95  ASP D 101 -1  N  ASP D 101   O  VAL D  29           
SHEET    1   T 2 GLY D  41  GLY D  44  0                                        
SHEET    2   T 2 ASN D  86  ALA D  89 -1  N  ALA D  89   O  GLY D  41           
SHEET    1   U 3 PHE D  45  HIS D  48  0                                        
SHEET    2   U 3 THR D 116  HIS D 120 -1  N  VAL D 118   O  HIS D  46           
SHEET    3   U 3 ARG D 143  VAL D 148 -1  N  GLY D 147   O  LEU D 117           
SHEET    1   V 5 ILE I 149  ILE I 151  0                                        
SHEET    2   V 5 LYS I   3  LEU I   8 -1  N  VAL I   5   O  GLY I 150           
SHEET    3   V 5 GLN I  15  GLN I  22 -1  N  PHE I  20   O  ALA I   4           
SHEET    4   V 5 VAL I  29  LYS I  36 -1  N  LYS I  36   O  GLN I  15           
SHEET    5   V 5 VAL I  94  ASP I 101 -1  N  ASP I 101   O  VAL I  29           
SHEET    1   W 2 GLY I  41  GLY I  44  0                                        
SHEET    2   W 2 ASN I  86  ALA I  89 -1  N  ALA I  89   O  GLY I  41           
SHEET    1   X 3 PHE I  45  HIS I  48  0                                        
SHEET    2   X 3 THR I 116  HIS I 120 -1  N  VAL I 118   O  HIS I  46           
SHEET    3   X 3 ARG I 143  VAL I 148 -1  N  GLY I 147   O  LEU I 117           
SHEET    1   Y 4 LYS E   3  LEU E   8  0                                        
SHEET    2   Y 4 GLN E  15  GLU E  21 -1  N  PHE E  20   O  ALA E   4           
SHEET    3   Y 4 VAL E  29  LYS E  36 -1  N  LYS E  36   O  GLN E  15           
SHEET    4   Y 4 ALA E  95  ASP E 101 -1  N  ASP E 101   O  VAL E  29           
SHEET    1   Z 2 GLY E  41  GLY E  44  0                                        
SHEET    2   Z 2 ASN E  86  ALA E  89 -1  N  ALA E  89   O  GLY E  41           
SHEET    1  AA 3 PHE E  45  VAL E  47  0                                        
SHEET    2  AA 3 THR E 116  HIS E 120 -1  N  VAL E 118   O  HIS E  46           
SHEET    3  AA 3 ARG E 143  VAL E 148 -1  N  GLY E 147   O  LEU E 117           
SHEET    1  AB 4 SER J  98  ASP J 101  0                                        
SHEET    2  AB 4 VAL J  29  LYS J  36 -1  N  VAL J  31   O  ILE J  99           
SHEET    3  AB 4 GLY J  12  GLU J  21 -1  N  ASN J  19   O  TRP J  32           
SHEET    4  AB 4 LYS J   3  GLY J  10 -1  N  GLY J  10   O  GLY J  12           
SHEET    1  AC 2 GLY J  41  GLY J  44  0                                        
SHEET    2  AC 2 ASN J  86  ALA J  89 -1  N  ALA J  89   O  GLY J  41           
SHEET    1  AD 3 PHE J  45  HIS J  48  0                                        
SHEET    2  AD 3 THR J 116  HIS J 120 -1  N  VAL J 118   O  HIS J  46           
SHEET    3  AD 3 ARG J 143  VAL J 148 -1  N  GLY J 147   O  LEU J 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.02  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.02  
SSBOND   3 CYS B   57    CYS B  146                          1555   1555  2.00  
SSBOND   4 CYS G   57    CYS G  146                          1555   1555  2.02  
SSBOND   5 CYS C   57    CYS C  146                          1555   1555  2.01  
SSBOND   6 CYS H   57    CYS H  146                          1555   1555  2.02  
SSBOND   7 CYS D   57    CYS D  146                          1555   1555  2.03  
SSBOND   8 CYS I   57    CYS I  146                          1555   1555  2.01  
SSBOND   9 CYS E   57    CYS E  146                          1555   1555  2.04  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.03  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.15  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.09  
LINK        CU    CU A 154                 NE2 HIS A  63     1555   1555  2.63  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.07  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.01  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.89  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  1.96  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.08  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.14  
LINK        CU    CU B 154                 NE2 HIS B  63     1555   1555  2.45  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  1.94  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.10  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  1.84  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.91  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.23  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  1.99  
LINK        CU    CU C 154                 NE2 HIS C  63     1555   1555  2.42  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  1.95  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  2.11  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  1.93  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.91  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.03  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  1.90  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  1.99  
LINK        CU    CU D 154                 NE2 HIS D  63     1555   1555  2.56  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  2.00  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.32  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  2.20  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  2.23  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.09  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.23  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.05  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  1.90  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.33  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.38  
LINK        ZN    ZN E 155                 OD2 ASP E  83     1555   1555  2.59  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  2.13  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  2.17  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.50  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.24  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.10  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.06  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  2.15  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.89  
LINK        ZN    ZN F 155                 OD2 ASP F  83     1555   1555  2.29  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  1.86  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  1.94  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  1.62  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  2.19  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  2.05  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.20  
LINK        CU    CU G 154                 NE2 HIS G  63     1555   1555  2.43  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  1.91  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.96  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.10  
LINK        ZN    ZN G 155                 OD2 ASP G  83     1555   1555  2.67  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  1.98  
LINK        CU    CU H 154                 NE2 HIS H  63     1555   1555  2.50  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  2.00  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  1.96  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  2.12  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  1.94  
LINK        ZN    ZN H 155                 OD2 ASP H  83     1555   1555  2.77  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  1.95  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  1.97  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.93  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  1.86  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  2.04  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  1.92  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  1.85  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  1.70  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  1.81  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  1.82  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.07  
LINK        CU    CU J 154                 NE2 HIS J  63     1555   1555  2.34  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.05  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  2.35  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.08  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  1.97  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  2.04  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  2.27  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 AC4  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC5  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC6  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC7  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 AC8  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 AC9  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 BC1  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 BC2  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC3  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC4  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 BC5  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 BC6  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC7  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 BC8  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC9  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 CC1  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC3  4 LYS F  75  LYS F 128  LYS G 128  LYS H 128                    
CRYST1  205.200  167.000  145.500  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      0.004873  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005988  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006873        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system