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Database: PDB
Entry: 4OH2
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Original site: 4OH2 
HEADER    OXIDOREDUCTASE                          16-JAN-14   4OH2              
TITLE     CRYSTAL STRUCTURE OF CU/ZN SUPEROXIDE DISMUTASE I149T                 
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 SYNONYM: SUPEROXIDE DISMUTASE 1, HSOD1;                              
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: HOMO SAPIENS SOD1, SOD1;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.CRANE,G.E.MERZ                                                    
REVDAT   3   22-NOV-17 4OH2    1       REMARK                                   
REVDAT   2   22-OCT-14 4OH2    1       JRNL                                     
REVDAT   1   15-OCT-14 4OH2    0                                                
JRNL        AUTH   G.E.MERZ,P.P.BORBAT,A.J.PRATT,E.D.GETZOFF,J.H.FREED,         
JRNL        AUTH 2 B.R.CRANE                                                    
JRNL        TITL   COPPER-BASED PULSED DIPOLAR ESR SPECTROSCOPY AS A PROBE OF   
JRNL        TITL 2 PROTEIN CONFORMATION LINKED TO DISEASE STATES.               
JRNL        REF    BIOPHYS.J.                    V. 107  1669 2014              
JRNL        REFN                   ISSN 0006-3495                               
JRNL        PMID   25296320                                                     
JRNL        DOI    10.1016/J.BPJ.2014.07.068                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 95240                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.1059 -  5.7386    0.99     6997   150  0.1658 0.2013        
REMARK   3     2  5.7386 -  4.5578    1.00     6883   148  0.1360 0.1472        
REMARK   3     3  4.5578 -  3.9825    1.00     6784   146  0.1210 0.1864        
REMARK   3     4  3.9825 -  3.6188    1.00     6783   145  0.1416 0.1882        
REMARK   3     5  3.6188 -  3.3596    1.00     6755   145  0.1575 0.2020        
REMARK   3     6  3.3596 -  3.1616    1.00     6769   145  0.1650 0.2089        
REMARK   3     7  3.1616 -  3.0034    1.00     6729   145  0.1738 0.2716        
REMARK   3     8  3.0034 -  2.8727    1.00     6757   144  0.1882 0.2849        
REMARK   3     9  2.8727 -  2.7621    1.00     6740   145  0.1987 0.2616        
REMARK   3    10  2.7621 -  2.6669    1.00     6695   143  0.1934 0.2977        
REMARK   3    11  2.6669 -  2.5835    1.00     6720   143  0.1913 0.2365        
REMARK   3    12  2.5835 -  2.5097    1.00     6728   145  0.1921 0.2696        
REMARK   3    13  2.5097 -  2.4436    0.98     6603   141  0.2069 0.2798        
REMARK   3    14  2.4436 -  2.3840    0.79     5299   113  0.2193 0.2836        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.350           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.77                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.015          11355                                  
REMARK   3   ANGLE     :  1.452          15325                                  
REMARK   3   CHIRALITY :  0.060           1700                                  
REMARK   3   PLANARITY :  0.007           2075                                  
REMARK   3   DIHEDRAL  : 13.981           4075                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084483.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : BENT, TRIANGULAR SI(111) CRYSTAL   
REMARK 200                                   FOR HORIZONTAL FOCUSING; RHODIUM-  
REMARK 200                                   COATED SILION MIRROR FOR           
REMARK 200                                   VERTICAL FOCUSSING                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95372                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.20900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
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) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NACL, 100MM TRIS-HCL PH 7.6,       
REMARK 280  2.8M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K     
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       72.20350            
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       72.20350            
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       82.54950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.90550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       82.54950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.90550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.20350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       82.54950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.90550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.20350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       82.54950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.90550            
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: 13830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 1340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     THR A   54   CB   OG1                                            
REMARK 480     LYS D   30   CD   CE   NZ                                        
REMARK 480     SER I   98   N    CA   C    O    CB   OG                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU D    21     OG   SER I    98              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B  55       52.62   -117.25                                   
REMARK 500    ASP B  90     -175.01    -68.85                                   
REMARK 500    SER C  98       76.94   -163.48                                   
REMARK 500    LYS C 128       55.60    -93.85                                   
REMARK 500    GLU E  40      132.99    -38.69                                   
REMARK 500    ALA E  55       47.50   -141.69                                   
REMARK 500    ARG E  69     -145.28    -99.21                                   
REMARK 500    ASP E  90     -159.13    -74.58                                   
REMARK 500    SER E  98       89.87   -165.22                                   
REMARK 500    ALA E 123      142.87    -33.74                                   
REMARK 500    LYS E 128       60.01   -116.58                                   
REMARK 500    ASN E 139       45.37     38.23                                   
REMARK 500    ASN F  26      -14.00     68.42                                   
REMARK 500    ASP G  90     -167.43    -76.20                                   
REMARK 500    SER G  98      100.60   -164.38                                   
REMARK 500    SER G  98       84.30   -168.41                                   
REMARK 500    LEU G 126       36.59     71.02                                   
REMARK 500    LYS G 128       70.46   -110.11                                   
REMARK 500    ASN H  26       14.37     48.33                                   
REMARK 500    GLU I  40      129.76    -32.55                                   
REMARK 500    ALA I  55       68.01   -112.66                                   
REMARK 500    ASN I  65       56.67   -149.29                                   
REMARK 500    SER I  68       31.86     37.90                                   
REMARK 500    ARG I  69     -166.76    -69.01                                   
REMARK 500    HIS I 110      119.78   -169.66                                   
REMARK 500    SER I 111      107.37     91.64                                   
REMARK 500    LYS I 128       34.98   -152.24                                   
REMARK 500    ASN I 131     -168.85   -163.41                                   
REMARK 500    ASN J  26       -2.99     67.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS I  110     SER I  111                  -32.30                    
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 E 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  80   ND1                                                    
REMARK 620 2 ASP E  83   OD1 127.8                                              
REMARK 620 3 HIS E  71   ND1 130.9  79.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 120   NE2                                                    
REMARK 620 2 HIS I  48   NE2 113.6                                              
REMARK 620 3 HIS I  46   ND1 101.4 145.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  80   ND1 114.7                                              
REMARK 620 3 HIS J  71   ND1 100.3 118.8                                        
REMARK 620 4 HIS J  63   ND1 109.2 107.8 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  83   OD1                                                    
REMARK 620 2 HIS B  80   ND1 119.0                                              
REMARK 620 3 HIS B  71   ND1  95.5 119.2                                        
REMARK 620 4 HIS B  63   ND1 109.1 108.6 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  63   ND1 102.6                                              
REMARK 620 3 HIS F  71   ND1  98.7 106.7                                        
REMARK 620 4 HIS F  80   ND1 115.2 109.9 121.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  83   OD1                                                    
REMARK 620 2 HIS H  63   ND1 104.9                                              
REMARK 620 3 HIS H  80   ND1 116.8 103.6                                        
REMARK 620 4 HIS H  71   ND1  97.8 104.4 127.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  83   OD1                                                    
REMARK 620 2 HIS I  63   ND1 107.0                                              
REMARK 620 3 HIS I  80   ND1 122.4 110.1                                        
REMARK 620 4 HIS I  71   ND1  97.1 105.6 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J 120   NE2                                                    
REMARK 620 2 HIS J  48   NE2 117.5                                              
REMARK 620 3 HIS J  46   ND1  99.1 143.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  63   ND1 110.8                                              
REMARK 620 3 HIS A  80   ND1 117.1 106.0                                        
REMARK 620 4 HIS A  71   ND1  92.9 104.2 124.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 120   NE2                                                    
REMARK 620 2 HIS D  46   ND1  98.6                                              
REMARK 620 3 HIS D  48   NE2 117.6 143.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  48   NE2 119.1                                              
REMARK 620 3 HIS F  46   ND1  96.4 144.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A  46   ND1 104.7                                              
REMARK 620 3 HIS A  48   NE2 115.6 139.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 120   NE2                                                    
REMARK 620 2 HIS B  48   NE2 118.7                                              
REMARK 620 3 HIS B  46   ND1 102.2 139.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  80   ND1                                                    
REMARK 620 2 ASP D  83   OD1 114.8                                              
REMARK 620 3 HIS D  63   ND1 104.7 108.1                                        
REMARK 620 4 HIS D  71   ND1 121.0 103.7 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 120   NE2                                                    
REMARK 620 2 HIS H  48   NE2 113.8                                              
REMARK 620 3 HIS H  46   ND1  98.9 146.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 120   NE2                                                    
REMARK 620 2 HIS C  48   NE2 118.8                                              
REMARK 620 3 HIS C  46   ND1 101.0 140.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  83   OD1                                                    
REMARK 620 2 HIS G  80   ND1 124.8                                              
REMARK 620 3 HIS G  71   ND1  81.3 123.2                                        
REMARK 620 4 HIS G  63   ND1  88.8 118.7 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  48   NE2                                                    
REMARK 620 2 HIS G  46   ND1 144.9                                              
REMARK 620 3 HIS G 120   NE2 107.8 106.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  83   OD1                                                    
REMARK 620 2 HIS C  80   ND1 123.6                                              
REMARK 620 3 HIS C  63   ND1 105.4 110.6                                        
REMARK 620 4 HIS C  71   ND1  93.9 122.4  96.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  48   NE2                                                    
REMARK 620 2 HIS E 120   NE2 110.2                                              
REMARK 620 3 HIS E  46   ND1 151.0  97.6                                        
REMARK 620 N                    1     2                                         
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 202                  
DBREF  4OH2 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 G    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 H    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 I    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4OH2 J    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 4OH2 ALA A    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER A  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR A  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA B    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER B  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR B  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA C    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER C  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR C  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA D    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER D  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR D  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA E    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER E  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR E  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA F    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER F  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR F  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA G    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER G  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR G  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA H    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER H  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR H  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA I    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER I  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR I  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQADV 4OH2 ALA J    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 4OH2 SER J  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 4OH2 THR J  149  UNP  P00441    ILE   150 ENGINEERED MUTATION            
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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL THR 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 LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL THR GLY ILE ALA GLN                      
HET     CU  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     CU  B 201       1                                                       
HET     ZN  B 202       1                                                       
HET     CU  C 201       1                                                       
HET     ZN  C 202       1                                                       
HET     CU  D 201       1                                                       
HET     ZN  D 202       1                                                       
HET     CU  E 201       1                                                       
HET     ZN  E 202       1                                                       
HET     CU  F 201       1                                                       
HET     ZN  F 202       1                                                       
HET     CU  G 201       1                                                       
HET     ZN  G 202       1                                                       
HET     CU  H 201       1                                                       
HET     ZN  H 202       1                                                       
HET     CU  I 201       1                                                       
HET     ZN  I 202       1                                                       
HET     CU  J 201       1                                                       
HET     ZN  J 202       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL  11   CU    10(CU 2+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  HOH   *639(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 ASN A  131  GLY A  138  1                                   8    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 SER B  107  SER B  111  5                                   5    
HELIX    5   5 GLU B  133  GLY B  138  1                                   6    
HELIX    6   6 ALA C   55  GLY C   61  5                                   7    
HELIX    7   7 GLU C  133  GLY C  138  1                                   6    
HELIX    8   8 ALA D   55  GLY D   61  5                                   7    
HELIX    9   9 GLU D  133  GLY D  138  1                                   6    
HELIX   10  10 ALA E   55  GLY E   61  5                                   7    
HELIX   11  11 ASN E  131  THR E  135  5                                   5    
HELIX   12  12 ALA F   55  GLY F   61  5                                   7    
HELIX   13  13 SER F  107  SER F  111  5                                   5    
HELIX   14  14 ASN F  131  THR F  137  1                                   7    
HELIX   15  15 ALA G   55  GLY G   61  5                                   7    
HELIX   16  16 ALA H   55  GLY H   61  5                                   7    
HELIX   17  17 GLU H  133  GLY H  138  1                                   6    
HELIX   18  18 ALA I   55  GLY I   61  5                                   7    
HELIX   19  19 GLU I  132  LYS I  136  5                                   5    
HELIX   20  20 ALA J   55  GLY J   61  5                                   7    
HELIX   21  21 GLU J  133  GLY J  138  1                                   6    
SHEET    1   A 5 ALA A  95  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  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -1  N  LEU A   8   O  GLY A  16           
SHEET    5   A 5 GLY A 150  ILE A 151 -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  HIS A 120   N  GLY A  44           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  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  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LYS B   9 -1  N  THR B   2   O  GLN B  22           
SHEET    5   C 5 GLY B 150  ALA B 152 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  VAL B  47 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  HIS B 120   N  GLY B  44           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 9 THR C   2  LEU C   8  0                                        
SHEET    2   E 9 GLN C  15  GLN C  22 -1  O  GLY C  16   N  LEU C   8           
SHEET    3   E 9 VAL C  29  LYS C  36 -1  O  TRP C  32   N  ASN C  19           
SHEET    4   E 9 ALA C  95  ASP C 101 -1  O  ASP C 101   N  VAL C  29           
SHEET    5   E 9 ASP C  83  ALA C  89 -1  N  THR C  88   O  ASP C  96           
SHEET    6   E 9 GLY C  41  VAL C  47 -1  N  GLY C  41   O  ALA C  89           
SHEET    7   E 9 THR C 116  HIS C 120 -1  O  HIS C 120   N  GLY C  44           
SHEET    8   E 9 ARG C 143  ALA C 152 -1  O  GLY C 147   N  LEU C 117           
SHEET    9   E 9 THR C   2  LEU C   8 -1  N  VAL C   5   O  GLY C 150           
SHEET    1   F 5 ALA D  95  ASP D 101  0                                        
SHEET    2   F 5 VAL D  29  LYS D  36 -1  N  VAL D  29   O  ASP D 101           
SHEET    3   F 5 GLN D  15  GLN D  22 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   F 5 THR D   2  LYS D   9 -1  N  LEU D   8   O  GLY D  16           
SHEET    5   F 5 GLY D 150  ALA D 152 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   G 4 ASP D  83  ALA D  89  0                                        
SHEET    2   G 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   G 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   G 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1   H 9 THR E   2  LEU E   8  0                                        
SHEET    2   H 9 GLN E  15  GLN E  22 -1  O  GLY E  16   N  LEU E   8           
SHEET    3   H 9 VAL E  29  LYS E  36 -1  O  TRP E  32   N  ASN E  19           
SHEET    4   H 9 ALA E  95  ASP E 101 -1  O  ASP E 101   N  VAL E  29           
SHEET    5   H 9 ASP E  83  ALA E  89 -1  N  THR E  88   O  ASP E  96           
SHEET    6   H 9 GLY E  41  VAL E  47 -1  N  GLY E  41   O  ALA E  89           
SHEET    7   H 9 THR E 116  HIS E 120 -1  O  VAL E 118   N  HIS E  46           
SHEET    8   H 9 ARG E 143  ILE E 151 -1  O  GLY E 147   N  LEU E 117           
SHEET    9   H 9 THR E   2  LEU E   8 -1  N  VAL E   5   O  GLY E 150           
SHEET    1   I 5 ALA F  95  ASP F 101  0                                        
SHEET    2   I 5 VAL F  29  LYS F  36 -1  N  VAL F  29   O  ASP F 101           
SHEET    3   I 5 GLN F  15  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   I 5 THR F   2  LEU F   8 -1  N  ALA F   4   O  PHE F  20           
SHEET    5   I 5 GLY F 150  ALA F 152 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   J 4 ASP F  83  ALA F  89  0                                        
SHEET    2   J 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   J 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   J 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SHEET    1   K 9 THR G   2  LEU G   8  0                                        
SHEET    2   K 9 GLN G  15  GLN G  22 -1  O  GLY G  16   N  LEU G   8           
SHEET    3   K 9 VAL G  29  LYS G  36 -1  O  TRP G  32   N  ASN G  19           
SHEET    4   K 9 ALA G  95  ASP G 101 -1  O  ALA G  95   N  ILE G  35           
SHEET    5   K 9 ASP G  83  ALA G  89 -1  N  THR G  88   O  ASP G  96           
SHEET    6   K 9 GLY G  41  VAL G  47 -1  N  GLY G  41   O  ALA G  89           
SHEET    7   K 9 THR G 116  HIS G 120 -1  O  HIS G 120   N  GLY G  44           
SHEET    8   K 9 ARG G 143  ALA G 152 -1  O  GLY G 147   N  LEU G 117           
SHEET    9   K 9 THR G   2  LEU G   8 -1  N  VAL G   5   O  GLY G 150           
SHEET    1   L 8 ASP H  83  ALA H  89  0                                        
SHEET    2   L 8 GLY H  41  VAL H  47 -1  N  HIS H  43   O  VAL H  87           
SHEET    3   L 8 THR H 116  HIS H 120 -1  O  VAL H 118   N  HIS H  46           
SHEET    4   L 8 ARG H 143  ALA H 152 -1  O  GLY H 147   N  LEU H 117           
SHEET    5   L 8 THR H   2  LYS H   9 -1  N  VAL H   5   O  GLY H 150           
SHEET    6   L 8 GLN H  15  GLN H  22 -1  O  GLY H  16   N  LEU H   8           
SHEET    7   L 8 VAL H  29  LYS H  36 -1  O  TRP H  32   N  ASN H  19           
SHEET    8   L 8 ALA H  95  ASP H 101 -1  O  ALA H  95   N  ILE H  35           
SHEET    1   M 5 ALA I  95  ASP I 101  0                                        
SHEET    2   M 5 VAL I  29  LYS I  36 -1  N  VAL I  29   O  ASP I 101           
SHEET    3   M 5 GLN I  15  GLN I  22 -1  N  ASN I  19   O  TRP I  32           
SHEET    4   M 5 THR I   2  LEU I   8 -1  N  LEU I   8   O  GLY I  16           
SHEET    5   M 5 GLY I 150  ALA I 152 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   N 4 ASP I  83  ALA I  89  0                                        
SHEET    2   N 4 GLY I  41  VAL I  47 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   N 4 THR I 116  HIS I 120 -1  O  VAL I 118   N  HIS I  46           
SHEET    4   N 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   O 5 ALA J  95  ASP J 101  0                                        
SHEET    2   O 5 VAL J  29  LYS J  36 -1  N  ILE J  35   O  ALA J  95           
SHEET    3   O 5 GLN J  15  GLN J  22 -1  N  GLN J  15   O  LYS J  36           
SHEET    4   O 5 THR J   2  LYS J   9 -1  N  LEU J   8   O  GLY J  16           
SHEET    5   O 5 GLY J 150  ALA J 152 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   P 4 ASP J  83  ALA J  89  0                                        
SHEET    2   P 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   P 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   P 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  2.13  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.17  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.12  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.16  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.11  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.14  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.11  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.10  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.08  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.11  
LINK         ND1 HIS E  80                ZN    ZN E 202     1555   1555  1.82  
LINK         NE2 HIS I 120                CU    CU I 201     1555   1555  1.85  
LINK         OD1 ASP J  83                ZN    ZN J 202     1555   1555  1.89  
LINK         OD1 ASP B  83                ZN    ZN B 202     1555   1555  1.91  
LINK         OD1 ASP F  83                ZN    ZN F 202     1555   1555  1.93  
LINK         OD1 ASP H  83                ZN    ZN H 202     1555   1555  1.94  
LINK         OD1 ASP I  83                ZN    ZN I 202     1555   1555  1.95  
LINK         NE2 HIS J 120                CU    CU J 201     1555   1555  1.95  
LINK         OD1 ASP E  83                ZN    ZN E 202     1555   1555  1.95  
LINK         OD1 ASP A  83                ZN    ZN A 202     1555   1555  1.96  
LINK         NE2 HIS D 120                CU    CU D 201     1555   1555  1.96  
LINK         NE2 HIS F 120                CU    CU F 201     1555   1555  1.97  
LINK         NE2 HIS A 120                CU    CU A 201     1555   1555  1.98  
LINK         ND1 HIS H  63                ZN    ZN H 202     1555   1555  1.99  
LINK         NE2 HIS B 120                CU    CU B 201     1555   1555  1.99  
LINK         ND1 HIS H  80                ZN    ZN H 202     1555   1555  2.01  
LINK         ND1 HIS D  80                ZN    ZN D 202     1555   1555  2.01  
LINK         NE2 HIS H 120                CU    CU H 201     1555   1555  2.02  
LINK         ND1 HIS A  63                ZN    ZN A 202     1555   1555  2.02  
LINK         ND1 HIS H  71                ZN    ZN H 202     1555   1555  2.03  
LINK         ND1 HIS F  63                ZN    ZN F 202     1555   1555  2.03  
LINK         OD1 ASP D  83                ZN    ZN D 202     1555   1555  2.03  
LINK         ND1 HIS A  46                CU    CU A 201     1555   1555  2.05  
LINK         ND1 HIS A  80                ZN    ZN A 202     1555   1555  2.06  
LINK         NE2 HIS J  48                CU    CU J 201     1555   1555  2.07  
LINK         ND1 HIS D  63                ZN    ZN D 202     1555   1555  2.07  
LINK         ND1 HIS B  80                ZN    ZN B 202     1555   1555  2.08  
LINK         ND1 HIS F  71                ZN    ZN F 202     1555   1555  2.08  
LINK         ND1 HIS F  80                ZN    ZN F 202     1555   1555  2.08  
LINK         NE2 HIS C 120                CU    CU C 201     1555   1555  2.09  
LINK         NE2 HIS H  48                CU    CU H 201     1555   1555  2.09  
LINK         NE2 HIS F  48                CU    CU F 201     1555   1555  2.10  
LINK         NE2 HIS B  48                CU    CU B 201     1555   1555  2.10  
LINK         OD1 ASP G  83                ZN    ZN G 202     1555   1555  2.10  
LINK         ND1 HIS J  80                ZN    ZN J 202     1555   1555  2.11  
LINK         ND1 HIS D  71                ZN    ZN D 202     1555   1555  2.11  
LINK         ND1 HIS B  71                ZN    ZN B 202     1555   1555  2.12  
LINK         NE2 HIS C  48                CU    CU C 201     1555   1555  2.12  
LINK         ND1 HIS B  63                ZN    ZN B 202     1555   1555  2.12  
LINK         NE2 HIS G  48                CU    CU G 201     1555   1555  2.13  
LINK         ND1 HIS D  46                CU    CU D 201     1555   1555  2.14  
LINK         OD1 ASP C  83                ZN    ZN C 202     1555   1555  2.14  
LINK         NE2 HIS D  48                CU    CU D 201     1555   1555  2.16  
LINK         ND1 HIS J  46                CU    CU J 201     1555   1555  2.17  
LINK         ND1 HIS C  46                CU    CU C 201     1555   1555  2.18  
LINK         ND1 HIS J  71                ZN    ZN J 202     1555   1555  2.18  
LINK         ND1 HIS C  80                ZN    ZN C 202     1555   1555  2.18  
LINK         ND1 HIS J  63                ZN    ZN J 202     1555   1555  2.18  
LINK         NE2 HIS I  48                CU    CU I 201     1555   1555  2.18  
LINK         ND1 HIS H  46                CU    CU H 201     1555   1555  2.18  
LINK         ND1 HIS I  63                ZN    ZN I 202     1555   1555  2.19  
LINK         ND1 HIS I  80                ZN    ZN I 202     1555   1555  2.19  
LINK         ND1 HIS F  46                CU    CU F 201     1555   1555  2.20  
LINK         ND1 HIS B  46                CU    CU B 201     1555   1555  2.20  
LINK         ND1 HIS C  63                ZN    ZN C 202     1555   1555  2.20  
LINK         NE2 HIS A  48                CU    CU A 201     1555   1555  2.22  
LINK         ND1 HIS A  71                ZN    ZN A 202     1555   1555  2.24  
LINK         ND1 HIS G  46                CU    CU G 201     1555   1555  2.26  
LINK         NE2 HIS E  48                CU    CU E 201     1555   1555  2.26  
LINK         NE2 HIS E 120                CU    CU E 201     1555   1555  2.27  
LINK         NE2 HIS G 120                CU    CU G 201     1555   1555  2.29  
LINK         ND1 HIS G  80                ZN    ZN G 202     1555   1555  2.32  
LINK         ND1 HIS G  71                ZN    ZN G 202     1555   1555  2.37  
LINK         ND1 HIS E  71                ZN    ZN E 202     1555   1555  2.40  
LINK         ND1 HIS E  46                CU    CU E 201     1555   1555  2.42  
LINK         ND1 HIS C  71                ZN    ZN C 202     1555   1555  2.42  
LINK         ND1 HIS I  46                CU    CU I 201     1555   1555  2.45  
LINK         ND1 HIS I  71                ZN    ZN I 202     1555   1555  2.49  
LINK         ND1 HIS G  63                ZN    ZN G 202     1555   1555  2.66  
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 B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC5  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 BC6  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC8  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  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                    
CRYST1  165.099  203.811  144.407  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      0.006057  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004907  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006925        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system