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Database: PDB
Entry: 5K02
LinkDB: 5K02
Original site: 5K02 
HEADER    OXIDOREDUCTASE                          17-MAY-16   5K02              
TITLE     STRUCTURE OF HUMAN SOD1 WITH T2D MUTATION                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND   4 V, W, X;                                                             
COMPND   5 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   6 EC: 1.15.1.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    SOD1, PHOSPHOMIMETIC MUTATION, OXIDOREDUCTASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.FAY,C.ZHU,W.CUI,H.KE,N.V.DOKHOLYAN                                
REVDAT   3   22-NOV-17 5K02    1       REMARK                                   
REVDAT   2   13-SEP-17 5K02    1       JRNL                                     
REVDAT   1   23-NOV-16 5K02    0                                                
JRNL        AUTH   J.M.FAY,C.ZHU,E.A.PROCTOR,Y.TAO,W.CUI,H.KE,N.V.DOKHOLYAN     
JRNL        TITL   A PHOSPHOMIMETIC MUTATION STABILIZES SOD1 AND RESCUES CELL   
JRNL        TITL 2 VIABILITY IN THE CONTEXT OF AN ALS-ASSOCIATED MUTATION.      
JRNL        REF    STRUCTURE                     V.  24  1898 2016              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   27667694                                                     
JRNL        DOI    10.1016/J.STR.2016.08.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 149.92                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 329360                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 17889                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 19832                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 984                          
REMARK   3   BIN FREE R VALUE                    : 0.2360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 26664                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 684                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.69000                                             
REMARK   3    B22 (A**2) : -3.19000                                             
REMARK   3    B33 (A**2) : 6.88000                                              
REMARK   3    B12 (A**2) : -8.40000                                             
REMARK   3    B13 (A**2) : 6.77000                                              
REMARK   3    B23 (A**2) : -1.89000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.024         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.022         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.053         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.863         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.967                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 27288 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 36600 ; 1.084 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3648 ; 5.992 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1176 ;41.908 ;25.714       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4440 ;16.108 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;14.025 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4008 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20784 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5K02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221471.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 431865                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 149.920                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
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: CU,ZN SUPEROXIDE DISMUTASE (PDB ID: 1SPD)            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: T2D WAS CRYSTALLIZED IN A BUFFER OF 2    
REMARK 280  M (NH4)2SO4, 0.1 M SODIUM CACODYLATE, 20% MPD AND 10 MM ZNCL2       
REMARK 280  (PH 6.5) AFTER A PERIOD OF APPROXIMATELY 5 MONTHS., VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
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: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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: 1690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       55.76036            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -56.21964            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  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: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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: 1630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: I                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       55.76036            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
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: 1630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -56.21964            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
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: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
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: 8                                                       
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: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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 APPLY THE FOLLOWING TO CHAINS: O                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       55.76036            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
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: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W                                     
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 APPLY THE FOLLOWING TO CHAINS: P                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -56.21964            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
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: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, V                                  
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: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R                                     
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 APPLY THE FOLLOWING TO CHAINS: U                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -55.76036            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
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: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S                                     
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 APPLY THE FOLLOWING TO CHAINS: T                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       56.21964            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -97.08784            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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   O    HOH H   305     O    HOH H   317              1.82            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO N  28   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  55       55.70   -116.27                                   
REMARK 500    ARG A  69     -166.70   -126.40                                   
REMARK 500    LEU B  67        5.80    -67.27                                   
REMARK 500    HIS B 110       37.68    -91.26                                   
REMARK 500    ALA C  55       42.06    -90.45                                   
REMARK 500    SER C  98       93.97   -163.14                                   
REMARK 500    ASP D  90     -168.69    -79.67                                   
REMARK 500    LYS D 136      -55.54   -120.17                                   
REMARK 500    CYS E   6      118.56   -163.80                                   
REMARK 500    LYS E 136      -58.97   -122.56                                   
REMARK 500    ALA E 140        5.44    -67.85                                   
REMARK 500    ASP F  90     -169.59    -72.10                                   
REMARK 500    LYS F 136      -72.79   -113.19                                   
REMARK 500    ASN F 139       26.82     48.18                                   
REMARK 500    ASN G  26       67.73   -104.54                                   
REMARK 500    ALA G  55       63.25   -117.58                                   
REMARK 500    ASP G  90     -168.79    -74.70                                   
REMARK 500    SER H  68       25.58     48.52                                   
REMARK 500    HIS H 110       12.42    -69.02                                   
REMARK 500    LYS H 136      -65.83   -109.42                                   
REMARK 500    ALA I  55       47.85   -106.83                                   
REMARK 500    PHE I  64      104.10    -59.47                                   
REMARK 500    ARG I 115     -169.39   -101.51                                   
REMARK 500    LYS I 136      -72.07   -130.96                                   
REMARK 500    ASN I 139       23.21     46.84                                   
REMARK 500    LYS J 136      -57.13   -130.66                                   
REMARK 500    ALA K  55       48.56   -107.82                                   
REMARK 500    ASN K  65       75.44   -151.03                                   
REMARK 500    LYS K 136      -52.77   -122.24                                   
REMARK 500    ALA K 140       13.46    -64.34                                   
REMARK 500    SER L  68       32.74     39.22                                   
REMARK 500    ASP L  90     -169.16    -77.69                                   
REMARK 500    LYS L 128       24.79    -77.57                                   
REMARK 500    SER M  68       57.69     38.88                                   
REMARK 500    ALA N  55       45.28    -98.89                                   
REMARK 500    ASN N  65       57.98   -140.48                                   
REMARK 500    ASP N  96       78.29   -100.42                                   
REMARK 500    HIS N 110       32.38    -80.31                                   
REMARK 500    SER O  68        9.75     59.58                                   
REMARK 500    ARG O  69     -165.07    -73.47                                   
REMARK 500    LYS O 136      -60.45   -109.91                                   
REMARK 500    LYS P 136      -70.34   -110.57                                   
REMARK 500    CYS Q   6      115.61   -161.92                                   
REMARK 500    ALA Q  55       51.61   -107.80                                   
REMARK 500    LYS Q 136      -58.64   -129.00                                   
REMARK 500    ALA Q 140        0.80    -68.33                                   
REMARK 500    GLU R  40      129.62    -37.93                                   
REMARK 500    ALA R  55       40.53   -107.84                                   
REMARK 500    ASN R 139       10.09     59.31                                   
REMARK 500    ALA R 140        8.06    -64.76                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
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 A 336        DISTANCE =  5.92 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 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 125.7                                              
REMARK 620 3 HIS A  63   NE2  83.8  99.9                                        
REMARK 620 4 HIS A 120   NE2  90.3 114.1 141.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 104.3                                              
REMARK 620 3 HIS A  80   ND1 119.8 124.0                                        
REMARK 620 4 ASP A  83   OD1 100.0  99.2 104.8                                  
REMARK 620 N                    1     2     3                                   
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  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 139.4                                              
REMARK 620 3 HIS B 120   NE2  90.4 107.6                                        
REMARK 620 N                    1     2                                         
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 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 105.1                                              
REMARK 620 3 HIS B  80   ND1 126.3 128.1                                        
REMARK 620 4 ASP B  83   OD1  94.6  81.5  99.2                                  
REMARK 620 N                    1     2     3                                   
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  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 127.8                                              
REMARK 620 3 HIS C  63   NE2  90.6 101.9                                        
REMARK 620 4 HIS C 120   NE2  89.8 105.4 144.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 105.3                                              
REMARK 620 3 HIS C  80   ND1 142.0 112.6                                        
REMARK 620 4 ASP C  83   OD1 104.4  76.1  86.8                                  
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  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 116.6                                              
REMARK 620 3 HIS D 120   NE2  80.9 117.7                                        
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  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 107.6                                              
REMARK 620 3 HIS D  80   ND1 124.8 127.4                                        
REMARK 620 4 ASP D  83   OD1  98.5  84.5  91.9                                  
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  46   ND1                                                    
REMARK 620 2 HIS E  48   NE2 109.7                                              
REMARK 620 3 HIS E 120   NE2 119.1 122.0                                        
REMARK 620 N                    1     2                                         
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  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1  94.5                                              
REMARK 620 3 HIS E  80   ND1  93.5 126.8                                        
REMARK 620 4 ASP E  83   OD1  99.9 100.9 129.2                                  
REMARK 620 5 ASP E  83   OD2 158.2  88.6 101.9  58.4                            
REMARK 620 N                    1     2     3     4                             
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  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 115.5                                              
REMARK 620 3 HIS F 120   NE2  82.3 121.5                                        
REMARK 620 N                    1     2                                         
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 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 107.9                                              
REMARK 620 3 HIS F  80   ND1 116.2 124.0                                        
REMARK 620 4 ASP F  83   OD1  97.0  95.7 110.7                                  
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  46   ND1                                                    
REMARK 620 2 HIS G  48   NE2 138.1                                              
REMARK 620 3 HIS G 120   NE2 106.3 105.6                                        
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 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 101.7                                              
REMARK 620 3 HIS G  80   ND1  93.9 120.8                                        
REMARK 620 4 ASP G  83   OD1  90.8 111.5 125.1                                  
REMARK 620 5 ASP G  83   OD2 148.9  82.5 110.5  59.6                            
REMARK 620 N                    1     2     3     4                             
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  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 121.2                                              
REMARK 620 3 HIS H 120   NE2  95.2 129.8                                        
REMARK 620 N                    1     2                                         
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 HIS H  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1 103.7                                              
REMARK 620 3 HIS H  80   ND1 103.3 120.6                                        
REMARK 620 4 ASP H  83   OD1 103.6 106.3 117.1                                  
REMARK 620 N                    1     2     3                                   
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  46   ND1                                                    
REMARK 620 2 HIS I  48   NE2 142.4                                              
REMARK 620 3 HIS I 120   NE2 102.7 108.3                                        
REMARK 620 N                    1     2                                         
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 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1 109.0                                              
REMARK 620 3 HIS I  80   ND1 101.6 125.6                                        
REMARK 620 4 ASP I  83   OD1 102.0  95.4 121.1                                  
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  46   ND1                                                    
REMARK 620 2 HIS J  48   NE2 115.3                                              
REMARK 620 3 HIS J 120   NE2  85.5 114.9                                        
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 HIS J  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 109.6                                              
REMARK 620 3 HIS J  80   ND1 102.8 126.4                                        
REMARK 620 4 ASP J  83   OD1  84.7  90.1 135.1                                  
REMARK 620 5 ASP J  83   OD2 140.0  73.5 106.3  55.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  46   ND1                                                    
REMARK 620 2 HIS K  48   NE2 129.4                                              
REMARK 620 3 HIS K 120   NE2 103.0 110.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  63   ND1                                                    
REMARK 620 2 HIS K  71   ND1 109.2                                              
REMARK 620 3 HIS K  80   ND1 122.7 115.4                                        
REMARK 620 4 ASP K  83   OD1  97.2  97.9 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  46   ND1                                                    
REMARK 620 2 HIS L  48   NE2 122.6                                              
REMARK 620 3 HIS L 120   NE2  99.9 110.6                                        
REMARK 620 4 HOH L 301   O    63.7  71.6  85.2                                  
REMARK 620 5 HOH L 303   O   130.4 100.0  85.8 164.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  63   ND1                                                    
REMARK 620 2 HIS L  71   ND1 119.6                                              
REMARK 620 3 HIS L  80   ND1 128.2 112.2                                        
REMARK 620 4 ASP L  83   OD1 103.2  88.4  76.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU M 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  46   ND1                                                    
REMARK 620 2 HIS M  48   NE2 131.1                                              
REMARK 620 3 HIS M 120   NE2 108.3 103.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN M 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  63   ND1                                                    
REMARK 620 2 HIS M  71   ND1  98.9                                              
REMARK 620 3 HIS M  80   ND1  85.4 105.3                                        
REMARK 620 4 ASP M  83   OD1 138.2  81.0 135.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU N 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  46   ND1                                                    
REMARK 620 2 HIS N  48   NE2 137.8                                              
REMARK 620 3 HIS N  63   NE2  93.2  96.3                                        
REMARK 620 4 HIS N 120   NE2  89.1 108.3 140.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  63   ND1                                                    
REMARK 620 2 HIS N  71   ND1  97.7                                              
REMARK 620 3 HIS N  80   ND1 127.5 111.3                                        
REMARK 620 4 ASP N  83   OD1 110.1  73.5 119.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU O 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O  46   ND1                                                    
REMARK 620 2 HIS O  48   NE2 138.5                                              
REMARK 620 3 HIS O 120   NE2  98.6 113.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN O 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O  63   ND1                                                    
REMARK 620 2 HIS O  71   ND1 101.9                                              
REMARK 620 3 HIS O  80   ND1 122.1  99.0                                        
REMARK 620 4 ASP O  83   OD1 113.0 103.1 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU P 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  46   ND1                                                    
REMARK 620 2 HIS P  48   NE2 141.2                                              
REMARK 620 3 HIS P 120   NE2 100.8 106.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  63   ND1                                                    
REMARK 620 2 HIS P  71   ND1  96.0                                              
REMARK 620 3 HIS P  80   ND1 103.6 112.1                                        
REMARK 620 4 ASP P  83   OD1 117.3  90.8 130.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU Q 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  46   ND1                                                    
REMARK 620 2 HIS Q  48   NE2 124.9                                              
REMARK 620 3 HIS Q 120   NE2  97.5 113.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  63   ND1                                                    
REMARK 620 2 HIS Q  71   ND1 107.0                                              
REMARK 620 3 HIS Q  80   ND1 132.7 110.8                                        
REMARK 620 4 ASP Q  83   OD1  98.5  80.4 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU R 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS R  46   ND1                                                    
REMARK 620 2 HIS R  48   NE2 137.5                                              
REMARK 620 3 HIS R 120   NE2 109.8 112.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN R 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS R  63   ND1                                                    
REMARK 620 2 HIS R  71   ND1  99.6                                              
REMARK 620 3 HIS R  80   ND1 126.8 126.1                                        
REMARK 620 4 ASP R  83   OD1 104.9  87.3 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU S 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS S  46   ND1                                                    
REMARK 620 2 HIS S  48   NE2 112.5                                              
REMARK 620 3 HIS S 120   NE2 115.5 124.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN S 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS S  63   ND1                                                    
REMARK 620 2 HIS S  71   ND1 108.4                                              
REMARK 620 3 HIS S  80   ND1 133.5 116.3                                        
REMARK 620 4 ASP S  83   OD1 105.2  90.7  87.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU T 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS T  46   ND1                                                    
REMARK 620 2 HIS T  48   NE2 136.1                                              
REMARK 620 3 HIS T 120   NE2 108.0 113.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN T 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS T  63   ND1                                                    
REMARK 620 2 HIS T  71   ND1 100.9                                              
REMARK 620 3 HIS T  80   ND1 129.0 124.8                                        
REMARK 620 4 ASP T  83   OD1  96.3  88.2 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU U 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS U  46   ND1                                                    
REMARK 620 2 HIS U  48   NE2 124.2                                              
REMARK 620 3 HIS U 120   NE2 106.2 129.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN U 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS U  63   ND1                                                    
REMARK 620 2 HIS U  71   ND1 106.4                                              
REMARK 620 3 HIS U  80   ND1 130.7 122.9                                        
REMARK 620 4 ASP U  83   OD1  98.4  84.1  85.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU V 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  46   ND1                                                    
REMARK 620 2 HIS V  48   NE2 125.2                                              
REMARK 620 3 HIS V 120   NE2 117.7 116.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN V 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  63   ND1                                                    
REMARK 620 2 HIS V  71   ND1 114.6                                              
REMARK 620 3 HIS V  80   ND1 107.1 122.6                                        
REMARK 620 4 ASP V  83   OD1 115.7  91.5 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU W 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS W  46   ND1                                                    
REMARK 620 2 HIS W  48   NE2 133.5                                              
REMARK 620 3 HIS W 120   NE2  95.3 118.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN W 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS W  63   ND1                                                    
REMARK 620 2 HIS W  71   ND1 101.6                                              
REMARK 620 3 HIS W  80   ND1 108.9 114.6                                        
REMARK 620 4 ASP W  83   OD1 114.8  83.3 127.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU X 201  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X  46   ND1                                                    
REMARK 620 2 HIS X  48   NE2 130.8                                              
REMARK 620 3 HIS X  63   NE2  86.9  97.8                                        
REMARK 620 4 HIS X 120   NE2  91.8 107.0 147.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN X 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X  63   ND1                                                    
REMARK 620 2 HIS X  71   ND1 102.9                                              
REMARK 620 3 HIS X  80   ND1 105.2 110.5                                        
REMARK 620 4 ASP X  83   OD1 108.4  94.8 131.6                                  
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 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: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU J 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU K 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU L 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU M 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN M 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU N 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN N 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU O 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN O 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU P 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN P 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU Q 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU R 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU S 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN S 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU T 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN T 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU U 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN U 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU V 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN V 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU W 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN W 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU X 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN X 202                  
DBREF  5K02 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 G    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 H    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 I    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 J    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 K    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 L    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 M    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 N    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 O    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 P    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 Q    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 R    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 S    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 T    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 U    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 V    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 W    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  5K02 X    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 5K02 ASP A    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP B    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP C    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP D    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP E    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP F    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP G    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP H    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP I    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP J    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP K    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP L    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP M    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP N    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP O    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP P    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP Q    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP R    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP S    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP T    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP U    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP V    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP W    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQADV 5K02 ASP X    2  UNP  P00441    THR     3 ENGINEERED MUTATION            
SEQRES   1 A  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA ASP LYS ALA VAL CYS 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 CYS 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 ILE GLY ILE ALA GLN                      
SEQRES   1 K  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 K  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 K  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 K  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 K  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 K  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 K  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 K  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 K  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 K  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 K  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 K  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 L  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 L  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 L  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 L  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 L  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 L  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 L  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 L  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 L  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 L  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 L  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 L  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 M  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 M  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 M  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 M  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 M  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 M  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 M  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 M  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 M  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 M  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 M  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 M  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 N  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 N  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 N  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 N  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 N  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 N  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 N  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 N  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 N  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 N  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 N  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 N  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 O  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 O  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 O  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 O  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 O  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 O  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 O  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 O  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 O  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 O  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 O  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 O  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 P  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 P  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 P  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 P  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 P  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 P  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 P  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 P  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 P  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 P  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 P  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 P  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 Q  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 Q  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 Q  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 Q  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 Q  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 Q  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 Q  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 Q  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 Q  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 Q  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 Q  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 Q  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 R  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 R  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 R  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 R  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 R  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 R  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 R  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 R  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 R  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 R  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 R  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 R  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 S  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 S  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 S  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 S  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 S  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 S  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 S  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 S  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 S  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 S  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 S  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 S  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 T  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 T  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 T  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 T  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 T  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 T  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 T  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 T  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 T  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 T  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 T  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 T  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 U  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 U  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 U  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 U  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 U  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 U  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 U  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 U  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 U  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 U  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 U  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 U  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 V  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 V  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 V  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 V  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 V  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 V  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 V  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 V  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 V  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 V  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 V  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 V  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 W  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 W  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 W  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 W  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 W  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 W  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 W  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 W  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 W  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 W  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 W  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 W  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 X  153  ALA ASP LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 X  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 X  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 X  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 X  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 X  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 X  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 X  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 X  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 X  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 X  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 X  153  LEU ALA CYS GLY VAL ILE 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                                                       
HET     CU  K 201       1                                                       
HET     ZN  K 202       1                                                       
HET     CU  L 201       1                                                       
HET     ZN  L 202       1                                                       
HET     CU  M 201       1                                                       
HET     ZN  M 202       1                                                       
HET     CU  N 201       1                                                       
HET     ZN  N 202       1                                                       
HET     CU  O 201       1                                                       
HET     ZN  O 202       1                                                       
HET     CU  P 201       1                                                       
HET     ZN  P 202       1                                                       
HET     CU  Q 201       1                                                       
HET     ZN  Q 202       1                                                       
HET     CU  R 201       1                                                       
HET     ZN  R 202       1                                                       
HET     CU  S 201       1                                                       
HET     ZN  S 202       1                                                       
HET     CU  T 201       1                                                       
HET     ZN  T 202       1                                                       
HET     CU  U 201       1                                                       
HET     ZN  U 202       1                                                       
HET     CU  V 201       1                                                       
HET     ZN  V 202       1                                                       
HET     CU  W 201       1                                                       
HET     ZN  W 202       1                                                       
HET     CU  X 201       1                                                       
HET     ZN  X 202       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL  25   CU    24(CU 2+)                                                    
FORMUL  26   ZN    24(ZN 2+)                                                    
FORMUL  73  HOH   *684(H2 O)                                                    
HELIX    1 AA1 ALA A   55  GLY A   61  5                                   7    
HELIX    2 AA2 GLU A  133  GLY A  138  1                                   6    
HELIX    3 AA3 CYS B   57  GLY B   61  5                                   5    
HELIX    4 AA4 ALA C   55  GLY C   61  5                                   7    
HELIX    5 AA5 ASN C  131  THR C  135  5                                   5    
HELIX    6 AA6 ALA D   55  GLY D   61  5                                   7    
HELIX    7 AA7 SER D  107  CYS D  111  5                                   5    
HELIX    8 AA8 CYS E   57  GLY E   61  5                                   5    
HELIX    9 AA9 ALA F   55  GLY F   61  5                                   7    
HELIX   10 AB1 ALA G   55  GLY G   61  5                                   7    
HELIX   11 AB2 GLU G  133  GLY G  138  1                                   6    
HELIX   12 AB3 ALA H   55  GLY H   61  5                                   7    
HELIX   13 AB4 CYS I   57  GLY I   61  5                                   5    
HELIX   14 AB5 CYS J   57  GLY J   61  5                                   5    
HELIX   15 AB6 ALA K   55  GLY K   61  5                                   7    
HELIX   16 AB7 ALA L   55  GLY L   61  5                                   7    
HELIX   17 AB8 ALA M   55  GLY M   61  5                                   7    
HELIX   18 AB9 ASN M  131  THR M  137  1                                   7    
HELIX   19 AC1 ALA N   55  GLY N   61  5                                   7    
HELIX   20 AC2 ALA O   55  GLY O   61  5                                   7    
HELIX   21 AC3 CYS P   57  GLY P   61  5                                   5    
HELIX   22 AC4 ALA Q   55  GLY Q   61  5                                   7    
HELIX   23 AC5 ASN Q  131  THR Q  135  5                                   5    
HELIX   24 AC6 ALA R   55  GLY R   61  5                                   7    
HELIX   25 AC7 CYS S   57  GLY S   61  5                                   5    
HELIX   26 AC8 CYS T   57  GLY T   61  5                                   5    
HELIX   27 AC9 ALA U   55  GLY U   61  5                                   7    
HELIX   28 AD1 ASN U  131  THR U  135  5                                   5    
HELIX   29 AD2 CYS V   57  GLY V   61  5                                   5    
HELIX   30 AD3 CYS W   57  GLY W   61  5                                   5    
HELIX   31 AD4 SER W  107  CYS W  111  5                                   5    
HELIX   32 AD5 CYS X   57  GLY X   61  5                                   5    
SHEET    1 AA1 4 VAL A   7  LEU A   8  0                                        
SHEET    2 AA1 4 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    3 AA1 4 VAL A  29  LYS A  36 -1  O  LYS A  36   N  GLN A  15           
SHEET    4 AA1 4 ALA A  95  ASP A 101 -1  O  ILE A  99   N  VAL A  31           
SHEET    1 AA2 4 VAL A   7  LEU A   8  0                                        
SHEET    2 AA2 4 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    3 AA2 4 ASP A   2  VAL A   5 -1  N  ALA A   4   O  PHE A  20           
SHEET    4 AA2 4 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1 AA3 4 ASP A  83  ALA A  89  0                                        
SHEET    2 AA3 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3 AA3 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4 AA3 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1 AA4 8 ASP B  83  ALA B  89  0                                        
SHEET    2 AA4 8 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3 AA4 8 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4 AA4 8 ARG B 143  ILE B 151 -1  O  ALA B 145   N  VAL B 119           
SHEET    5 AA4 8 ASP B   2  GLY B  10 -1  N  VAL B   5   O  GLY B 150           
SHEET    6 AA4 8 GLN B  15  GLN B  22 -1  O  PHE B  20   N  ALA B   4           
SHEET    7 AA4 8 VAL B  29  LYS B  36 -1  O  TRP B  32   N  ASN B  19           
SHEET    8 AA4 8 SER B  98  ASP B 101 -1  O  ASP B 101   N  VAL B  29           
SHEET    1 AA5 9 ASP C   2  LEU C   8  0                                        
SHEET    2 AA5 9 GLN C  15  GLN C  22 -1  O  ILE C  18   N  CYS C   6           
SHEET    3 AA5 9 VAL C  29  LYS C  36 -1  O  TRP C  32   N  ASN C  19           
SHEET    4 AA5 9 ALA C  95  ASP C 101 -1  O  ILE C  99   N  VAL C  31           
SHEET    5 AA5 9 ASP C  83  ALA C  89 -1  O  THR C  88   N  ASP C  96           
SHEET    6 AA5 9 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    7 AA5 9 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    8 AA5 9 ARG C 143  ALA C 152 -1  O  GLY C 147   N  LEU C 117           
SHEET    9 AA5 9 ASP C   2  LEU C   8 -1  N  VAL C   5   O  GLY C 150           
SHEET    1 AA6 5 ALA D  95  ASP D 101  0                                        
SHEET    2 AA6 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3 AA6 5 GLN D  15  GLN D  22 -1  N  ASN D  19   O  TRP D  32           
SHEET    4 AA6 5 ASP D   2  LEU D   8 -1  N  LEU D   8   O  GLY D  16           
SHEET    5 AA6 5 GLY D 150  ALA D 152 -1  O  ALA D 152   N  LYS D   3           
SHEET    1 AA7 4 ASP D  83  ALA D  89  0                                        
SHEET    2 AA7 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3 AA7 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4 AA7 4 ARG D 143  VAL D 148 -1  O  LEU D 144   N  VAL D 119           
SHEET    1 AA810 GLY E 150  ILE E 151  0                                        
SHEET    2 AA810 ASP E   2  GLY E  10 -1  N  VAL E   5   O  GLY E 150           
SHEET    3 AA810 ARG E 143  VAL E 148 -1  O  CYS E 146   N  LYS E   9           
SHEET    4 AA810 THR E 116  HIS E 120 -1  N  VAL E 119   O  LEU E 144           
SHEET    5 AA810 GLY E  41  HIS E  48 -1  N  HIS E  48   O  THR E 116           
SHEET    6 AA810 ASP E  83  ALA E  89 -1  O  GLY E  85   N  PHE E  45           
SHEET    7 AA810 VAL E  94  ASP E 101 -1  O  ASP E  96   N  THR E  88           
SHEET    8 AA810 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    9 AA810 GLN E  15  GLN E  22 -1  N  ASN E  19   O  TRP E  32           
SHEET   10 AA810 ASP E   2  GLY E  10 -1  N  ALA E   4   O  PHE E  20           
SHEET    1 AA9 9 ASP F   2  LEU F   8  0                                        
SHEET    2 AA9 9 GLN F  15  GLN F  22 -1  O  GLN F  22   N  ASP F   2           
SHEET    3 AA9 9 VAL F  29  LYS F  36 -1  O  TRP F  32   N  ASN F  19           
SHEET    4 AA9 9 ALA F  95  ASP F 101 -1  O  ILE F  99   N  VAL F  31           
SHEET    5 AA9 9 ASP F  83  ALA F  89 -1  N  THR F  88   O  ASP F  96           
SHEET    6 AA9 9 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    7 AA9 9 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    8 AA9 9 ARG F 143  ILE F 151 -1  O  ALA F 145   N  VAL F 119           
SHEET    9 AA9 9 ASP F   2  LEU F   8 -1  N  VAL F   5   O  GLY F 150           
SHEET    1 AB1 5 ALA G  95  ASP G 101  0                                        
SHEET    2 AB1 5 VAL G  29  LYS G  36 -1  N  VAL G  31   O  ILE G  99           
SHEET    3 AB1 5 GLN G  15  GLN G  22 -1  N  ASN G  19   O  TRP G  32           
SHEET    4 AB1 5 ASP G   2  LEU G   8 -1  N  ALA G   4   O  PHE G  20           
SHEET    5 AB1 5 GLY G 150  ILE G 151 -1  O  GLY G 150   N  VAL G   5           
SHEET    1 AB2 4 ASP G  83  ALA G  89  0                                        
SHEET    2 AB2 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3 AB2 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4 AB2 4 ARG G 143  VAL G 148 -1  O  ALA G 145   N  VAL G 119           
SHEET    1 AB3 5 ALA H  95  ASP H 101  0                                        
SHEET    2 AB3 5 VAL H  29  LYS H  36 -1  N  VAL H  29   O  ASP H 101           
SHEET    3 AB3 5 GLN H  15  GLN H  22 -1  N  ASN H  19   O  TRP H  32           
SHEET    4 AB3 5 ASP H   2  LYS H   9 -1  N  LEU H   8   O  GLY H  16           
SHEET    5 AB3 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1 AB4 4 ASP H  83  ALA H  89  0                                        
SHEET    2 AB4 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3 AB4 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4 AB4 4 ARG H 143  VAL H 148 -1  O  ALA H 145   N  VAL H 119           
SHEET    1 AB5 9 ASP I   2  LEU I   8  0                                        
SHEET    2 AB5 9 GLN I  15  GLN I  22 -1  O  GLN I  22   N  ASP I   2           
SHEET    3 AB5 9 VAL I  29  LYS I  36 -1  O  TRP I  32   N  ASN I  19           
SHEET    4 AB5 9 VAL I  94  ASP I 101 -1  O  ILE I  99   N  VAL I  31           
SHEET    5 AB5 9 ASP I  83  ALA I  89 -1  N  THR I  88   O  ASP I  96           
SHEET    6 AB5 9 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    7 AB5 9 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    8 AB5 9 ARG I 143  ILE I 151 -1  O  ALA I 145   N  VAL I 119           
SHEET    9 AB5 9 ASP I   2  LEU I   8 -1  N  VAL I   5   O  GLY I 150           
SHEET    1 AB6 8 ASP J  83  ALA J  89  0                                        
SHEET    2 AB6 8 GLY J  41  HIS J  48 -1  N  HIS J  43   O  VAL J  87           
SHEET    3 AB6 8 THR J 116  HIS J 120 -1  O  VAL J 118   N  HIS J  46           
SHEET    4 AB6 8 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SHEET    5 AB6 8 ASP J   2  GLY J  10 -1  N  LYS J   9   O  CYS J 146           
SHEET    6 AB6 8 GLN J  15  GLN J  22 -1  O  ILE J  18   N  CYS J   6           
SHEET    7 AB6 8 VAL J  29  LYS J  36 -1  O  TRP J  32   N  ASN J  19           
SHEET    8 AB6 8 ALA J  95  ASP J 101 -1  O  ALA J  95   N  ILE J  35           
SHEET    1 AB7 6 ASP J  83  ALA J  89  0                                        
SHEET    2 AB7 6 GLY J  41  HIS J  48 -1  N  HIS J  43   O  VAL J  87           
SHEET    3 AB7 6 THR J 116  HIS J 120 -1  O  VAL J 118   N  HIS J  46           
SHEET    4 AB7 6 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SHEET    5 AB7 6 ASP J   2  GLY J  10 -1  N  LYS J   9   O  CYS J 146           
SHEET    6 AB7 6 GLY J 150  ALA J 152 -1  O  GLY J 150   N  VAL J   5           
SHEET    1 AB8 5 ALA K  95  ASP K 101  0                                        
SHEET    2 AB8 5 VAL K  29  LYS K  36 -1  N  VAL K  31   O  ILE K  99           
SHEET    3 AB8 5 GLN K  15  GLN K  22 -1  N  ASN K  19   O  TRP K  32           
SHEET    4 AB8 5 ASP K   2  LYS K   9 -1  N  LEU K   8   O  GLY K  16           
SHEET    5 AB8 5 GLY K 150  ILE K 151 -1  O  GLY K 150   N  VAL K   5           
SHEET    1 AB9 4 ASP K  83  ALA K  89  0                                        
SHEET    2 AB9 4 GLY K  41  HIS K  48 -1  N  HIS K  43   O  VAL K  87           
SHEET    3 AB9 4 THR K 116  HIS K 120 -1  O  THR K 116   N  HIS K  48           
SHEET    4 AB9 4 ARG K 143  VAL K 148 -1  O  ALA K 145   N  VAL K 119           
SHEET    1 AC1 8 ASP L  83  ALA L  89  0                                        
SHEET    2 AC1 8 GLY L  41  HIS L  48 -1  N  HIS L  43   O  VAL L  87           
SHEET    3 AC1 8 THR L 116  HIS L 120 -1  O  VAL L 118   N  HIS L  46           
SHEET    4 AC1 8 ARG L 143  GLY L 150 -1  O  ALA L 145   N  VAL L 119           
SHEET    5 AC1 8 ASP L   2  LEU L   8 -1  N  VAL L   5   O  GLY L 150           
SHEET    6 AC1 8 GLN L  15  GLN L  22 -1  O  GLY L  16   N  LEU L   8           
SHEET    7 AC1 8 VAL L  29  LYS L  36 -1  O  TRP L  32   N  ASN L  19           
SHEET    8 AC1 8 ALA L  95  ASP L 101 -1  O  ALA L  95   N  ILE L  35           
SHEET    1 AC2 8 ASP M  83  ALA M  89  0                                        
SHEET    2 AC2 8 GLY M  41  HIS M  48 -1  N  PHE M  45   O  GLY M  85           
SHEET    3 AC2 8 THR M 116  HIS M 120 -1  O  THR M 116   N  HIS M  48           
SHEET    4 AC2 8 ARG M 143  ILE M 151 -1  O  ALA M 145   N  VAL M 119           
SHEET    5 AC2 8 ASP M   2  LYS M   9 -1  N  VAL M   5   O  GLY M 150           
SHEET    6 AC2 8 GLN M  15  GLN M  22 -1  O  GLN M  22   N  ASP M   2           
SHEET    7 AC2 8 VAL M  29  LYS M  36 -1  O  TRP M  32   N  ASN M  19           
SHEET    8 AC2 8 ALA M  95  ASP M 101 -1  O  ASP M 101   N  VAL M  29           
SHEET    1 AC3 9 ASP N   2  LEU N   8  0                                        
SHEET    2 AC3 9 GLN N  15  GLN N  22 -1  O  PHE N  20   N  ALA N   4           
SHEET    3 AC3 9 VAL N  29  LYS N  36 -1  O  TRP N  32   N  ASN N  19           
SHEET    4 AC3 9 ALA N  95  ASP N 101 -1  O  ILE N  99   N  VAL N  31           
SHEET    5 AC3 9 ASP N  83  ALA N  89 -1  N  THR N  88   O  ASP N  96           
SHEET    6 AC3 9 GLY N  41  HIS N  48 -1  N  PHE N  45   O  GLY N  85           
SHEET    7 AC3 9 THR N 116  HIS N 120 -1  O  VAL N 118   N  HIS N  46           
SHEET    8 AC3 9 ARG N 143  ALA N 152 -1  O  GLY N 147   N  LEU N 117           
SHEET    9 AC3 9 ASP N   2  LEU N   8 -1  N  LYS N   3   O  ALA N 152           
SHEET    1 AC4 8 ASP O  83  ALA O  89  0                                        
SHEET    2 AC4 8 GLY O  41  HIS O  48 -1  N  GLY O  41   O  ALA O  89           
SHEET    3 AC4 8 THR O 116  HIS O 120 -1  O  VAL O 118   N  HIS O  46           
SHEET    4 AC4 8 ARG O 143  ILE O 151 -1  O  ALA O 145   N  VAL O 119           
SHEET    5 AC4 8 ASP O   2  GLY O  10 -1  N  LYS O   9   O  CYS O 146           
SHEET    6 AC4 8 GLN O  15  GLN O  22 -1  O  ILE O  18   N  CYS O   6           
SHEET    7 AC4 8 VAL O  29  LYS O  36 -1  O  TRP O  32   N  ASN O  19           
SHEET    8 AC4 8 ALA O  95  ASP O 101 -1  O  ALA O  95   N  ILE O  35           
SHEET    1 AC5 5 ALA P  95  ASP P 101  0                                        
SHEET    2 AC5 5 VAL P  29  LYS P  36 -1  N  VAL P  29   O  ASP P 101           
SHEET    3 AC5 5 GLN P  15  GLN P  22 -1  N  ASN P  19   O  TRP P  32           
SHEET    4 AC5 5 ASP P   2  LEU P   8 -1  N  CYS P   6   O  ILE P  18           
SHEET    5 AC5 5 GLY P 150  ILE P 151 -1  O  GLY P 150   N  VAL P   5           
SHEET    1 AC6 4 ASP P  83  ALA P  89  0                                        
SHEET    2 AC6 4 GLY P  41  HIS P  48 -1  N  HIS P  43   O  VAL P  87           
SHEET    3 AC6 4 THR P 116  HIS P 120 -1  O  THR P 116   N  HIS P  48           
SHEET    4 AC6 4 ARG P 143  VAL P 148 -1  O  GLY P 147   N  LEU P 117           
SHEET    1 AC710 GLY Q 150  ILE Q 151  0                                        
SHEET    2 AC710 ASP Q   2  GLY Q  10 -1  N  VAL Q   5   O  GLY Q 150           
SHEET    3 AC710 ARG Q 143  VAL Q 148 -1  O  CYS Q 146   N  LYS Q   9           
SHEET    4 AC710 THR Q 116  HIS Q 120 -1  N  VAL Q 119   O  LEU Q 144           
SHEET    5 AC710 GLY Q  41  HIS Q  48 -1  N  HIS Q  48   O  THR Q 116           
SHEET    6 AC710 ASP Q  83  ALA Q  89 -1  O  VAL Q  87   N  HIS Q  43           
SHEET    7 AC710 ALA Q  95  ASP Q 101 -1  O  ASP Q  96   N  THR Q  88           
SHEET    8 AC710 VAL Q  29  LYS Q  36 -1  N  ILE Q  35   O  ALA Q  95           
SHEET    9 AC710 GLN Q  15  GLN Q  22 -1  N  ASN Q  19   O  TRP Q  32           
SHEET   10 AC710 ASP Q   2  GLY Q  10 -1  N  CYS Q   6   O  ILE Q  18           
SHEET    1 AC8 9 ASP R   2  GLY R  10  0                                        
SHEET    2 AC8 9 GLN R  15  GLN R  22 -1  O  ILE R  18   N  CYS R   6           
SHEET    3 AC8 9 VAL R  29  LYS R  36 -1  O  TRP R  32   N  ASN R  19           
SHEET    4 AC8 9 ALA R  95  ASP R 101 -1  O  ILE R  99   N  VAL R  31           
SHEET    5 AC8 9 ASP R  83  ALA R  89 -1  N  THR R  88   O  ASP R  96           
SHEET    6 AC8 9 GLY R  41  HIS R  48 -1  N  GLY R  41   O  ALA R  89           
SHEET    7 AC8 9 THR R 116  HIS R 120 -1  O  THR R 116   N  HIS R  48           
SHEET    8 AC8 9 ARG R 143  ILE R 151 -1  O  LEU R 144   N  VAL R 119           
SHEET    9 AC8 9 ASP R   2  GLY R  10 -1  N  VAL R   5   O  GLY R 150           
SHEET    1 AC9 5 ALA S  95  ASP S 101  0                                        
SHEET    2 AC9 5 VAL S  29  LYS S  36 -1  N  ILE S  35   O  ALA S  95           
SHEET    3 AC9 5 GLN S  15  GLN S  22 -1  N  ASN S  19   O  TRP S  32           
SHEET    4 AC9 5 ASP S   2  LYS S   9 -1  N  LEU S   8   O  GLY S  16           
SHEET    5 AC9 5 GLY S 150  ILE S 151 -1  O  GLY S 150   N  VAL S   5           
SHEET    1 AD1 4 ASP S  83  ALA S  89  0                                        
SHEET    2 AD1 4 GLY S  41  HIS S  48 -1  N  GLY S  41   O  ALA S  89           
SHEET    3 AD1 4 THR S 116  HIS S 120 -1  O  THR S 116   N  HIS S  48           
SHEET    4 AD1 4 ARG S 143  VAL S 148 -1  O  LEU S 144   N  VAL S 119           
SHEET    1 AD2 5 ALA T  95  ASP T 101  0                                        
SHEET    2 AD2 5 VAL T  29  LYS T  36 -1  N  VAL T  31   O  ILE T  99           
SHEET    3 AD2 5 GLN T  15  GLN T  22 -1  N  ASN T  19   O  TRP T  32           
SHEET    4 AD2 5 ASP T   2  LEU T   8 -1  N  LEU T   8   O  GLY T  16           
SHEET    5 AD2 5 GLY T 150  ILE T 151 -1  O  GLY T 150   N  VAL T   5           
SHEET    1 AD3 4 ASP T  83  ALA T  89  0                                        
SHEET    2 AD3 4 GLY T  41  HIS T  48 -1  N  HIS T  43   O  VAL T  87           
SHEET    3 AD3 4 THR T 116  HIS T 120 -1  O  THR T 116   N  HIS T  48           
SHEET    4 AD3 4 ARG T 143  VAL T 148 -1  O  ALA T 145   N  VAL T 119           
SHEET    1 AD4 8 ASP U  83  ALA U  89  0                                        
SHEET    2 AD4 8 GLY U  41  HIS U  48 -1  N  HIS U  43   O  VAL U  87           
SHEET    3 AD4 8 THR U 116  HIS U 120 -1  O  VAL U 118   N  HIS U  46           
SHEET    4 AD4 8 ARG U 143  ILE U 151 -1  O  ALA U 145   N  VAL U 119           
SHEET    5 AD4 8 ASP U   2  GLY U  10 -1  N  VAL U   5   O  GLY U 150           
SHEET    6 AD4 8 GLN U  15  GLN U  22 -1  O  GLY U  16   N  LEU U   8           
SHEET    7 AD4 8 VAL U  29  LYS U  36 -1  O  TRP U  32   N  ASN U  19           
SHEET    8 AD4 8 SER U  98  ASP U 101 -1  O  ILE U  99   N  VAL U  31           
SHEET    1 AD5 5 ALA V  95  ASP V 101  0                                        
SHEET    2 AD5 5 VAL V  29  LYS V  36 -1  N  ILE V  35   O  ALA V  95           
SHEET    3 AD5 5 GLN V  15  GLN V  22 -1  N  ASN V  19   O  TRP V  32           
SHEET    4 AD5 5 ASP V   2  LEU V   8 -1  N  LEU V   8   O  GLY V  16           
SHEET    5 AD5 5 GLY V 150  ALA V 152 -1  O  ALA V 152   N  LYS V   3           
SHEET    1 AD6 4 ASP V  83  ALA V  89  0                                        
SHEET    2 AD6 4 GLY V  41  HIS V  48 -1  N  GLY V  41   O  ALA V  89           
SHEET    3 AD6 4 THR V 116  HIS V 120 -1  O  THR V 116   N  HIS V  48           
SHEET    4 AD6 4 ARG V 143  VAL V 148 -1  O  ALA V 145   N  VAL V 119           
SHEET    1 AD7 5 ALA W  95  ASP W 101  0                                        
SHEET    2 AD7 5 VAL W  29  LYS W  36 -1  N  VAL W  31   O  ILE W  99           
SHEET    3 AD7 5 GLN W  15  GLN W  22 -1  N  ASN W  19   O  TRP W  32           
SHEET    4 AD7 5 LYS W   3  LEU W   8 -1  N  LEU W   8   O  GLY W  16           
SHEET    5 AD7 5 GLY W 150  ILE W 151 -1  O  GLY W 150   N  VAL W   5           
SHEET    1 AD8 4 ASP W  83  ALA W  89  0                                        
SHEET    2 AD8 4 GLY W  41  HIS W  48 -1  N  PHE W  45   O  GLY W  85           
SHEET    3 AD8 4 THR W 116  HIS W 120 -1  O  THR W 116   N  HIS W  48           
SHEET    4 AD8 4 ARG W 143  VAL W 148 -1  O  ALA W 145   N  VAL W 119           
SHEET    1 AD9 8 ASP X  83  ALA X  89  0                                        
SHEET    2 AD9 8 GLY X  41  HIS X  48 -1  N  HIS X  43   O  VAL X  87           
SHEET    3 AD9 8 THR X 116  HIS X 120 -1  O  THR X 116   N  HIS X  48           
SHEET    4 AD9 8 ARG X 143  ILE X 151 -1  O  GLY X 147   N  LEU X 117           
SHEET    5 AD9 8 ASP X   2  LEU X   8 -1  N  VAL X   5   O  GLY X 150           
SHEET    6 AD9 8 GLN X  15  GLN X  22 -1  O  ILE X  18   N  CYS X   6           
SHEET    7 AD9 8 VAL X  29  LYS X  36 -1  O  TRP X  32   N  ASN X  19           
SHEET    8 AD9 8 SER X  98  ASP X 101 -1  O  ASP X 101   N  VAL X  29           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.06  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.04  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.04  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.04  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.03  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.04  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.05  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.05  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.05  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.05  
SSBOND  11 CYS K   57    CYS K  146                          1555   1555  2.04  
SSBOND  12 CYS L   57    CYS L  146                          1555   1555  2.04  
SSBOND  13 CYS M   57    CYS M  146                          1555   1555  2.04  
SSBOND  14 CYS N   57    CYS N  146                          1555   1555  2.05  
SSBOND  15 CYS O   57    CYS O  146                          1555   1555  2.04  
SSBOND  16 CYS P   57    CYS P  146                          1555   1555  2.05  
SSBOND  17 CYS Q   57    CYS Q  146                          1555   1555  2.04  
SSBOND  18 CYS R   57    CYS R  146                          1555   1555  2.04  
SSBOND  19 CYS S   57    CYS S  146                          1555   1555  2.04  
SSBOND  20 CYS T   57    CYS T  146                          1555   1555  2.05  
SSBOND  21 CYS U   57    CYS U  146                          1555   1555  2.04  
SSBOND  22 CYS V   57    CYS V  146                          1555   1555  2.04  
SSBOND  23 CYS W   57    CYS W  146                          1555   1555  2.04  
SSBOND  24 CYS X   57    CYS X  146                          1555   1555  2.04  
LINK         ND1 HIS A  46                CU    CU A 201     1555   1555  2.08  
LINK         NE2 HIS A  48                CU    CU A 201     1555   1555  2.08  
LINK         ND1 HIS A  63                ZN    ZN A 202     1555   1555  2.14  
LINK         NE2 HIS A  63                CU    CU A 201     1555   1555  2.67  
LINK         ND1 HIS A  71                ZN    ZN A 202     1555   1555  2.15  
LINK         ND1 HIS A  80                ZN    ZN A 202     1555   1555  2.13  
LINK         OD1 ASP A  83                ZN    ZN A 202     1555   1555  2.03  
LINK         NE2 HIS A 120                CU    CU A 201     1555   1555  2.07  
LINK         ND1 HIS B  46                CU    CU B 201     1555   1555  2.07  
LINK         NE2 HIS B  48                CU    CU B 201     1555   1555  2.08  
LINK         ND1 HIS B  63                ZN    ZN B 202     1555   1555  2.15  
LINK         ND1 HIS B  71                ZN    ZN B 202     1555   1555  2.15  
LINK         ND1 HIS B  80                ZN    ZN B 202     1555   1555  2.14  
LINK         OD1 ASP B  83                ZN    ZN B 202     1555   1555  2.02  
LINK         NE2 HIS B 120                CU    CU B 201     1555   1555  2.07  
LINK         ND1 HIS C  46                CU    CU C 201     1555   1555  2.08  
LINK         NE2 HIS C  48                CU    CU C 201     1555   1555  2.09  
LINK         ND1 HIS C  63                ZN    ZN C 202     1555   1555  2.13  
LINK         NE2 HIS C  63                CU    CU C 201     1555   1555  2.19  
LINK         ND1 HIS C  71                ZN    ZN C 202     1555   1555  2.16  
LINK         ND1 HIS C  80                ZN    ZN C 202     1555   1555  2.11  
LINK         OD1 ASP C  83                ZN    ZN C 202     1555   1555  2.02  
LINK         NE2 HIS C 120                CU    CU C 201     1555   1555  2.08  
LINK         ND1 HIS D  46                CU    CU D 201     1555   1555  2.09  
LINK         NE2 HIS D  48                CU    CU D 201     1555   1555  2.06  
LINK         ND1 HIS D  63                ZN    ZN D 202     1555   1555  2.14  
LINK         ND1 HIS D  71                ZN    ZN D 202     1555   1555  2.13  
LINK         ND1 HIS D  80                ZN    ZN D 202     1555   1555  2.11  
LINK         OD1 ASP D  83                ZN    ZN D 202     1555   1555  2.04  
LINK         NE2 HIS D 120                CU    CU D 201     1555   1555  2.07  
LINK         ND1 HIS E  46                CU    CU E 201     1555   1555  2.07  
LINK         NE2 HIS E  48                CU    CU E 201     1555   1555  2.06  
LINK         ND1 HIS E  63                ZN    ZN E 202     1555   1555  2.14  
LINK         ND1 HIS E  71                ZN    ZN E 202     1555   1555  2.15  
LINK         ND1 HIS E  80                ZN    ZN E 202     1555   1555  2.14  
LINK         OD1 ASP E  83                ZN    ZN E 202     1555   1555  2.01  
LINK         OD2 ASP E  83                ZN    ZN E 202     1555   1555  2.43  
LINK         NE2 HIS E 120                CU    CU E 201     1555   1555  2.06  
LINK         ND1 HIS F  46                CU    CU F 201     1555   1555  2.08  
LINK         NE2 HIS F  48                CU    CU F 201     1555   1555  2.06  
LINK         ND1 HIS F  63                ZN    ZN F 202     1555   1555  2.15  
LINK         ND1 HIS F  71                ZN    ZN F 202     1555   1555  2.15  
LINK         ND1 HIS F  80                ZN    ZN F 202     1555   1555  2.12  
LINK         OD1 ASP F  83                ZN    ZN F 202     1555   1555  2.02  
LINK         NE2 HIS F 120                CU    CU F 201     1555   1555  2.05  
LINK         ND1 HIS G  46                CU    CU G 201     1555   1555  2.06  
LINK         NE2 HIS G  48                CU    CU G 201     1555   1555  2.07  
LINK         ND1 HIS G  63                ZN    ZN G 202     1555   1555  2.14  
LINK         ND1 HIS G  71                ZN    ZN G 202     1555   1555  2.15  
LINK         ND1 HIS G  80                ZN    ZN G 202     1555   1555  2.15  
LINK         OD1 ASP G  83                ZN    ZN G 202     1555   1555  2.03  
LINK         OD2 ASP G  83                ZN    ZN G 202     1555   1555  2.35  
LINK         NE2 HIS G 120                CU    CU G 201     1555   1555  2.07  
LINK         ND1 HIS H  46                CU    CU H 201     1555   1555  2.07  
LINK         NE2 HIS H  48                CU    CU H 201     1555   1555  2.05  
LINK         ND1 HIS H  63                ZN    ZN H 202     1555   1555  2.14  
LINK         ND1 HIS H  71                ZN    ZN H 202     1555   1555  2.15  
LINK         ND1 HIS H  80                ZN    ZN H 202     1555   1555  2.14  
LINK         OD1 ASP H  83                ZN    ZN H 202     1555   1555  2.03  
LINK         NE2 HIS H 120                CU    CU H 201     1555   1555  2.05  
LINK         ND1 HIS I  46                CU    CU I 201     1555   1555  2.07  
LINK         NE2 HIS I  48                CU    CU I 201     1555   1555  2.07  
LINK         ND1 HIS I  63                ZN    ZN I 202     1555   1555  2.14  
LINK         ND1 HIS I  71                ZN    ZN I 202     1555   1555  2.16  
LINK         ND1 HIS I  80                ZN    ZN I 202     1555   1555  2.14  
LINK         OD1 ASP I  83                ZN    ZN I 202     1555   1555  2.01  
LINK         NE2 HIS I 120                CU    CU I 201     1555   1555  2.07  
LINK         ND1 HIS J  46                CU    CU J 201     1555   1555  2.07  
LINK         NE2 HIS J  48                CU    CU J 201     1555   1555  2.07  
LINK         ND1 HIS J  63                ZN    ZN J 202     1555   1555  2.14  
LINK         ND1 HIS J  71                ZN    ZN J 202     1555   1555  2.15  
LINK         ND1 HIS J  80                ZN    ZN J 202     1555   1555  2.14  
LINK         OD1 ASP J  83                ZN    ZN J 202     1555   1555  2.01  
LINK         OD2 ASP J  83                ZN    ZN J 202     1555   1555  2.60  
LINK         NE2 HIS J 120                CU    CU J 201     1555   1555  2.07  
LINK         ND1 HIS K  46                CU    CU K 201     1555   1555  2.07  
LINK         NE2 HIS K  48                CU    CU K 201     1555   1555  2.08  
LINK         ND1 HIS K  63                ZN    ZN K 202     1555   1555  2.14  
LINK         ND1 HIS K  71                ZN    ZN K 202     1555   1555  2.15  
LINK         ND1 HIS K  80                ZN    ZN K 202     1555   1555  2.14  
LINK         OD1 ASP K  83                ZN    ZN K 202     1555   1555  2.01  
LINK         NE2 HIS K 120                CU    CU K 201     1555   1555  2.07  
LINK         ND1 HIS L  46                CU    CU L 201     1555   1555  2.08  
LINK         NE2 HIS L  48                CU    CU L 201     1555   1555  2.09  
LINK         ND1 HIS L  63                ZN    ZN L 202     1555   1555  2.16  
LINK         ND1 HIS L  71                ZN    ZN L 202     1555   1555  2.15  
LINK         ND1 HIS L  80                ZN    ZN L 202     1555   1555  2.11  
LINK         OD1 ASP L  83                ZN    ZN L 202     1555   1555  2.02  
LINK         NE2 HIS L 120                CU    CU L 201     1555   1555  2.07  
LINK         ND1 HIS M  46                CU    CU M 201     1555   1555  2.07  
LINK         NE2 HIS M  48                CU    CU M 201     1555   1555  2.07  
LINK         ND1 HIS M  63                ZN    ZN M 202     1555   1555  2.12  
LINK         ND1 HIS M  71                ZN    ZN M 202     1555   1555  2.15  
LINK         ND1 HIS M  80                ZN    ZN M 202     1555   1555  2.14  
LINK         OD1 ASP M  83                ZN    ZN M 202     1555   1555  2.00  
LINK         NE2 HIS M 120                CU    CU M 201     1555   1555  2.07  
LINK         ND1 HIS N  46                CU    CU N 201     1555   1555  2.08  
LINK         NE2 HIS N  48                CU    CU N 201     1555   1555  2.08  
LINK         ND1 HIS N  63                ZN    ZN N 202     1555   1555  2.15  
LINK         NE2 HIS N  63                CU    CU N 201     1555   1555  2.63  
LINK         ND1 HIS N  71                ZN    ZN N 202     1555   1555  2.16  
LINK         ND1 HIS N  80                ZN    ZN N 202     1555   1555  2.14  
LINK         OD1 ASP N  83                ZN    ZN N 202     1555   1555  2.01  
LINK         NE2 HIS N 120                CU    CU N 201     1555   1555  2.07  
LINK         ND1 HIS O  46                CU    CU O 201     1555   1555  2.08  
LINK         NE2 HIS O  48                CU    CU O 201     1555   1555  2.07  
LINK         ND1 HIS O  63                ZN    ZN O 202     1555   1555  2.15  
LINK         ND1 HIS O  71                ZN    ZN O 202     1555   1555  2.14  
LINK         ND1 HIS O  80                ZN    ZN O 202     1555   1555  2.14  
LINK         OD1 ASP O  83                ZN    ZN O 202     1555   1555  2.01  
LINK         NE2 HIS O 120                CU    CU O 201     1555   1555  2.06  
LINK         ND1 HIS P  46                CU    CU P 201     1555   1555  2.08  
LINK         NE2 HIS P  48                CU    CU P 201     1555   1555  2.08  
LINK         ND1 HIS P  63                ZN    ZN P 202     1555   1555  2.13  
LINK         ND1 HIS P  71                ZN    ZN P 202     1555   1555  2.15  
LINK         ND1 HIS P  80                ZN    ZN P 202     1555   1555  2.15  
LINK         OD1 ASP P  83                ZN    ZN P 202     1555   1555  2.01  
LINK         NE2 HIS P 120                CU    CU P 201     1555   1555  2.07  
LINK         ND1 HIS Q  46                CU    CU Q 201     1555   1555  2.08  
LINK         NE2 HIS Q  48                CU    CU Q 201     1555   1555  2.08  
LINK         ND1 HIS Q  63                ZN    ZN Q 202     1555   1555  2.15  
LINK         ND1 HIS Q  71                ZN    ZN Q 202     1555   1555  2.15  
LINK         ND1 HIS Q  80                ZN    ZN Q 202     1555   1555  2.13  
LINK         OD1 ASP Q  83                ZN    ZN Q 202     1555   1555  2.02  
LINK         NE2 HIS Q 120                CU    CU Q 201     1555   1555  2.07  
LINK         ND1 HIS R  46                CU    CU R 201     1555   1555  2.07  
LINK         NE2 HIS R  48                CU    CU R 201     1555   1555  2.08  
LINK         ND1 HIS R  63                ZN    ZN R 202     1555   1555  2.14  
LINK         ND1 HIS R  71                ZN    ZN R 202     1555   1555  2.16  
LINK         ND1 HIS R  80                ZN    ZN R 202     1555   1555  2.15  
LINK         OD1 ASP R  83                ZN    ZN R 202     1555   1555  2.02  
LINK         NE2 HIS R 120                CU    CU R 201     1555   1555  2.07  
LINK         ND1 HIS S  46                CU    CU S 201     1555   1555  2.07  
LINK         NE2 HIS S  48                CU    CU S 201     1555   1555  2.04  
LINK         ND1 HIS S  63                ZN    ZN S 202     1555   1555  2.15  
LINK         ND1 HIS S  71                ZN    ZN S 202     1555   1555  2.14  
LINK         ND1 HIS S  80                ZN    ZN S 202     1555   1555  2.13  
LINK         OD1 ASP S  83                ZN    ZN S 202     1555   1555  2.03  
LINK         NE2 HIS S 120                CU    CU S 201     1555   1555  2.05  
LINK         ND1 HIS T  46                CU    CU T 201     1555   1555  2.08  
LINK         NE2 HIS T  48                CU    CU T 201     1555   1555  2.08  
LINK         ND1 HIS T  63                ZN    ZN T 202     1555   1555  2.14  
LINK         ND1 HIS T  71                ZN    ZN T 202     1555   1555  2.15  
LINK         ND1 HIS T  80                ZN    ZN T 202     1555   1555  2.14  
LINK         OD1 ASP T  83                ZN    ZN T 202     1555   1555  2.04  
LINK         NE2 HIS T 120                CU    CU T 201     1555   1555  2.06  
LINK         ND1 HIS U  46                CU    CU U 201     1555   1555  2.09  
LINK         NE2 HIS U  48                CU    CU U 201     1555   1555  2.08  
LINK         ND1 HIS U  63                ZN    ZN U 202     1555   1555  2.15  
LINK         ND1 HIS U  71                ZN    ZN U 202     1555   1555  2.15  
LINK         ND1 HIS U  80                ZN    ZN U 202     1555   1555  2.10  
LINK         OD1 ASP U  83                ZN    ZN U 202     1555   1555  2.03  
LINK         NE2 HIS U 120                CU    CU U 201     1555   1555  2.05  
LINK         ND1 HIS V  46                CU    CU V 201     1555   1555  2.07  
LINK         NE2 HIS V  48                CU    CU V 201     1555   1555  2.08  
LINK         ND1 HIS V  63                ZN    ZN V 202     1555   1555  2.14  
LINK         ND1 HIS V  71                ZN    ZN V 202     1555   1555  2.15  
LINK         ND1 HIS V  80                ZN    ZN V 202     1555   1555  2.15  
LINK         OD1 ASP V  83                ZN    ZN V 202     1555   1555  2.01  
LINK         NE2 HIS V 120                CU    CU V 201     1555   1555  2.06  
LINK         ND1 HIS W  46                CU    CU W 201     1555   1555  2.07  
LINK         NE2 HIS W  48                CU    CU W 201     1555   1555  2.08  
LINK         ND1 HIS W  63                ZN    ZN W 202     1555   1555  2.15  
LINK         ND1 HIS W  71                ZN    ZN W 202     1555   1555  2.14  
LINK         ND1 HIS W  80                ZN    ZN W 202     1555   1555  2.14  
LINK         OD1 ASP W  83                ZN    ZN W 202     1555   1555  2.03  
LINK         NE2 HIS W 120                CU    CU W 201     1555   1555  2.06  
LINK         ND1 HIS X  46                CU    CU X 201     1555   1555  2.08  
LINK         NE2 HIS X  48                CU    CU X 201     1555   1555  2.10  
LINK         ND1 HIS X  63                ZN    ZN X 202     1555   1555  2.15  
LINK         NE2 HIS X  63                CU    CU X 201     1555   1555  2.34  
LINK         ND1 HIS X  71                ZN    ZN X 202     1555   1555  2.15  
LINK         ND1 HIS X  80                ZN    ZN X 202     1555   1555  2.15  
LINK         OD1 ASP X  83                ZN    ZN X 202     1555   1555  2.02  
LINK         NE2 HIS X 120                CU    CU X 201     1555   1555  2.07  
LINK        CU    CU L 201                 O   HOH L 301     1555   1555  2.12  
LINK        CU    CU L 201                 O   HOH L 303     1555   1555  2.33  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 HOH A 331                                                     
SITE     1 AC2  5 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     2 AC2  5 LYS A 136                                                     
SITE     1 AC3  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC3  5 HOH B 325                                                     
SITE     1 AC4  5 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     2 AC4  5 LYS B 136                                                     
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  5 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     2 AC6  5 LYS C 136                                                     
SITE     1 AC7  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 AC7  5 HOH D 333                                                     
SITE     1 AC8  5 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     2 AC8  5 LYS D 136                                                     
SITE     1 AC9  3 HIS E  46  HIS E  48  HIS E 120                               
SITE     1 AD1  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 AD2  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AD2  5 HOH F 315                                                     
SITE     1 AD3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AD4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 AD5  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 AD6  5 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     2 AD6  5 HOH H 305                                                     
SITE     1 AD7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 AD8  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 AD9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 AE1  3 HIS J  46  HIS J  48  HIS J 120                               
SITE     1 AE2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 AE3  4 HIS K  46  HIS K  48  HIS K  63  HIS K 120                    
SITE     1 AE4  4 HIS K  63  HIS K  71  HIS K  80  ASP K  83                    
SITE     1 AE5  6 HIS L  46  HIS L  48  HIS L  63  HIS L 120                    
SITE     2 AE5  6 HOH L 301  HOH L 303                                          
SITE     1 AE6  5 HIS L  63  HIS L  71  HIS L  80  ASP L  83                    
SITE     2 AE6  5 LYS L 136                                                     
SITE     1 AE7  4 HIS M  46  HIS M  48  HIS M  63  HIS M 120                    
SITE     1 AE8  4 HIS M  63  HIS M  71  HIS M  80  ASP M  83                    
SITE     1 AE9  4 HIS N  46  HIS N  48  HIS N  63  HIS N 120                    
SITE     1 AF1  4 HIS N  63  HIS N  71  HIS N  80  ASP N  83                    
SITE     1 AF2  4 HIS O  46  HIS O  48  HIS O  63  HIS O 120                    
SITE     1 AF3  4 HIS O  63  HIS O  71  HIS O  80  ASP O  83                    
SITE     1 AF4  4 HIS P  46  HIS P  48  HIS P  63  HIS P 120                    
SITE     1 AF5  4 HIS P  63  HIS P  71  HIS P  80  ASP P  83                    
SITE     1 AF6  4 HIS Q  46  HIS Q  48  HIS Q  63  HIS Q 120                    
SITE     1 AF7  5 HIS Q  63  HIS Q  71  HIS Q  80  ASP Q  83                    
SITE     2 AF7  5 LYS Q 136                                                     
SITE     1 AF8  4 HIS R  46  HIS R  48  HIS R  63  HIS R 120                    
SITE     1 AF9  4 HIS R  63  HIS R  71  HIS R  80  ASP R  83                    
SITE     1 AG1  5 HIS S  46  HIS S  48  HIS S  63  HIS S 120                    
SITE     2 AG1  5 HOH S 314                                                     
SITE     1 AG2  5 HIS S  63  HIS S  71  HIS S  80  ASP S  83                    
SITE     2 AG2  5 LYS S 136                                                     
SITE     1 AG3  4 HIS T  46  HIS T  48  HIS T  63  HIS T 120                    
SITE     1 AG4  5 HIS T  63  HIS T  71  HIS T  80  ASP T  83                    
SITE     2 AG4  5 LYS T 136                                                     
SITE     1 AG5  4 HIS U  46  HIS U  48  HIS U  63  HIS U 120                    
SITE     1 AG6  5 HIS U  63  HIS U  71  HIS U  80  ASP U  83                    
SITE     2 AG6  5 LYS U 136                                                     
SITE     1 AG7  4 HIS V  46  HIS V  48  HIS V  63  HIS V 120                    
SITE     1 AG8  4 HIS V  63  HIS V  71  HIS V  80  ASP V  83                    
SITE     1 AG9  4 HIS W  46  HIS W  48  HIS W  63  HIS W 120                    
SITE     1 AH1  4 HIS W  63  HIS W  71  HIS W  80  ASP W  83                    
SITE     1 AH2  4 HIS X  46  HIS X  48  HIS X  63  HIS X 120                    
SITE     1 AH3  4 HIS X  63  HIS X  71  HIS X  80  ASP X  83                    
CRYST1  111.980  111.961  149.880  89.86  89.85  60.13 P 1          24          
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      0.008930 -0.005129 -0.000018        0.00000                         
SCALE2      0.000000  0.010300 -0.000013        0.00000                         
SCALE3      0.000000  0.000000  0.006672        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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