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Database: PDB
Entry: 1N18
LinkDB: 1N18
Original site: 1N18 
HEADER    OXIDOREDUCTASE                          16-OCT-02   1N18              
TITLE     THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,               
TITLE    2 C111S                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GREEK KEY BETA BARREL, OXIDOREDUCTASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.F.CARDOSO,M.M.THAYER,M.DIDONATO,T.P.LO,C.K.BRUNS,                 
AUTHOR   2 E.D.GETZOFF,J.A.TAINER                                               
REVDAT   2   24-FEB-09 1N18    1       VERSN                                    
REVDAT   1   27-NOV-02 1N18    0                                                
JRNL        AUTH   R.M.F.CARDOSO,M.M.THAYER,M.DIDONATO,T.P.LO,                  
JRNL        AUTH 2 C.K.BRUNS,E.D.GETZOFF,J.A.TAINER                             
JRNL        TITL   INSIGHTS INTO LOU GEHRIG'S DISEASE FROM THE                  
JRNL        TITL 2 STRUCTURE AND INSTABILITY OF THE A4V MUTANT OF               
JRNL        TITL 3 HUMAN CU,ZN SUPEROXIDE DISMUTASE.                            
JRNL        REF    J.MOL.BIOL.                   V. 324   247 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12441104                                                     
JRNL        DOI    10.1016/S0022-2836(02)01090-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.E.PARGE,R.A.HALLEWELL,J.A.TAINER                           
REMARK   1  TITL   ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE              
REMARK   1  TITL 2 MUTANT RECOMBINANT HUMAN CU,ZN SUPEROXIDE DISMUTASE          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  89  6109 1992              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 161466                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8091                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 25418                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1301                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11090                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 1389                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47000                                              
REMARK   3    B22 (A**2) : 5.25000                                              
REMARK   3    B33 (A**2) : -5.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.68                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.390 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.160 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.080 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.140 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 51.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N18 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162732                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41600                            
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, NACL, TRIS, EDTA,      
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.15000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.15000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      101.60000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.60000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      101.60000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.60000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.15000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      101.60000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       82.60000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.15000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      101.60000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       82.60000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     MET C     0                                                      
REMARK 465     MET D     0                                                      
REMARK 465     MET E     0                                                      
REMARK 465     MET F     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 465     MET I     0                                                      
REMARK 465     MET J     0                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ALA A    1   N     CA    CB                                      
REMARK 480     LYS A    9   CD                                                  
REMARK 480     LYS A   91   CE    NZ                                            
REMARK 480     GLU A  132   CD    OE1   OE2                                     
REMARK 480     LYS A  136   CD                                                  
REMARK 480     ALA B    1   N     CA    CB                                      
REMARK 480     LYS B   23   NZ                                                  
REMARK 480     LYS B   91   NZ                                                  
REMARK 480     ALA C    1   N     CA    CB                                      
REMARK 480     LYS C   23   CD    CE    NZ                                      
REMARK 480     LYS C   30   CD                                                  
REMARK 480     LYS C   36   CD                                                  
REMARK 480     ARG C   69   CB    CG                                            
REMARK 480     ASP C   76   CG    OD1   OD2                                     
REMARK 480     ARG C   79   CB                                                  
REMARK 480     LYS C   91   CD    CE    NZ                                      
REMARK 480     LYS C  122   CE    NZ                                            
REMARK 480     LYS C  136   CE    NZ                                            
REMARK 480     ALA D    1   N     CA    CB                                      
REMARK 480     LYS D   23   CD    CE    NZ                                      
REMARK 480     LYS D   36   NZ                                                  
REMARK 480     LYS D   70   CE    NZ                                            
REMARK 480     LYS D  136   CE    NZ                                            
REMARK 480     ALA E    1   N     CA    CB                                      
REMARK 480     LYS E    3   NZ                                                  
REMARK 480     LYS E   23   CG    CD    CE                                      
REMARK 480     LYS E   91   NZ                                                  
REMARK 480     LYS E  136   CE                                                  
REMARK 480     ALA F    1   N     CA    CB                                      
REMARK 480     LYS F   36   NZ                                                  
REMARK 480     LYS F   70   NZ                                                  
REMARK 480     GLU F   77   CD    OE1   OE2                                     
REMARK 480     ALA G    1   N     CA    CB                                      
REMARK 480     LYS G    3   CD                                                  
REMARK 480     LYS G   23   CB    CG    CD    CE    NZ                          
REMARK 480     GLU G   24   CD    OE1   OE2                                     
REMARK 480     ASN G   26   CB                                                  
REMARK 480     LYS G   30   CD    CE                                            
REMARK 480     ASN G   65   CA    CB                                            
REMARK 480     LEU G   67   CG    CD1   CD2                                     
REMARK 480     LYS G   75   CD                                                  
REMARK 480     GLU G   77   CB    CG    CD    OE1   OE2                         
REMARK 480     LYS G   91   CG    CE    NZ                                      
REMARK 480     SER G   98   OG                                                  
REMARK 480     LYS G  122   CE    NZ                                            
REMARK 480     GLU G  132   CD    OE1   OE2                                     
REMARK 480     LYS H    9   CE                                                  
REMARK 480     LYS H   23   CE    NZ                                            
REMARK 480     LYS H   91   CD    CE                                            
REMARK 480     ASP H  109   CB    CG    OD1                                     
REMARK 480     LYS H  122   CE    NZ                                            
REMARK 480     ALA I    1   N     CA    CB                                      
REMARK 480     LYS I    9   CD                                                  
REMARK 480     ASN I   26   CB    CG    OD1   ND2                               
REMARK 480     LYS I   70   CD                                                  
REMARK 480     GLU I   77   CG                                                  
REMARK 480     LYS I   91   CD    CE    NZ                                      
REMARK 480     ALA J    1   N     CA    CB                                      
REMARK 480     LYS J    9   CE                                                  
REMARK 480     LYS J   23   CE    NZ                                            
REMARK 480     GLU J   24   CG    CD    OE1   OE2                               
REMARK 480     SER J   25   O     OG                                            
REMARK 480     ASN J   26   CB    CG    OD1   ND2                               
REMARK 480     LYS J   36   NZ                                                  
REMARK 480     LYS J   70   CD                                                  
REMARK 480     LYS J   75   CD    CE    NZ                                      
REMARK 480     ASP J  109   CB                                                  
REMARK 480     GLU J  132   CG                                                  
REMARK 480     LYS J  136   CE                                                  
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   OD1  ASP C    76     O    HOH C   243              2.07            
REMARK 500   O    HOH A   213     O    HOH A   284              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D  1567     O    HOH D  1567     4555     1.44            
REMARK 500   NZ   LYS F    36     O    ASP G    92     3655     2.10            
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    SER B  25       -0.92    -43.96                                   
REMARK 500    ASN B  26      -16.35   -147.05                                   
REMARK 500    THR E   2      -36.97   -147.92                                   
REMARK 500    ASP E 109      -35.82    -37.56                                   
REMARK 500    LYS E 136      -56.52   -120.11                                   
REMARK 500    SER G  98       94.78   -160.54                                   
REMARK 500    ALA I  55       66.32   -115.98                                   
REMARK 500    LEU I 126       19.51     59.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 141.4                                              
REMARK 620 3 HIS A 120   NE2 102.2 116.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  71   ND1  91.0                                              
REMARK 620 3 HIS A  80   ND1 117.9 121.2                                        
REMARK 620 4 HIS A  63   ND1 101.7 107.9 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HIS B  46   ND1 140.8                                              
REMARK 620 3 HIS B 120   NE2 119.9  99.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 106.8                                              
REMARK 620 3 HIS B  80   ND1 108.8 122.3                                        
REMARK 620 4 ASP B  83   OD1 104.6  97.0 115.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  48   NE2                                                    
REMARK 620 2 HIS C  63   NE2  88.0                                              
REMARK 620 3 HIS C 120   NE2 116.7 113.5                                        
REMARK 620 4 HIS C  46   ND1 144.8  72.8  98.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  80   ND1                                                    
REMARK 620 2 HIS C  63   ND1 108.0                                              
REMARK 620 3 ASP C  83   OD1 122.6 109.8                                        
REMARK 620 4 HIS C  71   ND1 114.7 101.7  97.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D 120   NE2  97.2                                              
REMARK 620 3 HIS D  48   NE2 145.7 115.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  83   OD1                                                    
REMARK 620 2 HIS D  80   ND1 115.8                                              
REMARK 620 3 HIS D  71   ND1  99.8 121.8                                        
REMARK 620 4 HIS D  63   ND1 102.1 109.2 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 120   NE2                                                    
REMARK 620 2 HIS E  48   NE2 117.2                                              
REMARK 620 3 HIS E  46   ND1 100.0 142.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  71   ND1                                                    
REMARK 620 2 HIS E  80   ND1 122.1                                              
REMARK 620 3 HIS E  63   ND1 105.3 112.1                                        
REMARK 620 4 ASP E  83   OD1  90.9 116.0 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F 120   NE2  97.3                                              
REMARK 620 3 HIS F  48   NE2 143.8 118.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  63   ND1 103.6                                              
REMARK 620 3 HIS F  80   ND1 119.4 109.2                                        
REMARK 620 4 HIS F  71   ND1  94.9 104.2 123.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G 120   NE2                                                    
REMARK 620 2 HIS G  48   NE2 116.0                                              
REMARK 620 3 HIS G  46   ND1  97.8 145.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  80   ND1                                                    
REMARK 620 2 HIS G  71   ND1 125.8                                              
REMARK 620 3 ASP G  83   OD1 123.1  87.1                                        
REMARK 620 4 HIS G  63   ND1 110.4 100.7 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 120   NE2                                                    
REMARK 620 2 HIS H  48   NE2 120.4                                              
REMARK 620 3 HIS H  46   ND1  96.7 142.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  71   ND1                                                    
REMARK 620 2 ASP H  83   OD1 100.0                                              
REMARK 620 3 HIS H  80   ND1 127.8 114.2                                        
REMARK 620 4 HIS H  63   ND1 102.9 108.7 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 120   NE2                                                    
REMARK 620 2 HIS I  48   NE2 118.8                                              
REMARK 620 3 HIS I  46   ND1 100.3 140.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1 112.5                                              
REMARK 620 3 HIS I  80   ND1 105.2 122.7                                        
REMARK 620 4 ASP I  83   OD1 109.5  98.5 107.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  46   ND1                                                    
REMARK 620 2 HIS J 120   NE2  92.3                                              
REMARK 620 3 HIS J  48   NE2 148.6 118.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  80   ND1                                                    
REMARK 620 2 ASP J  83   OD1 118.6                                              
REMARK 620 3 HIS J  63   ND1 109.1 104.9                                        
REMARK 620 4 HIS J  71   ND1 119.3  96.7 106.5                                  
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 CU1 A 154                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 154                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 154                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 154                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 E 154                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 F 154                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 G 154                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 H 154                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 I 154                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 J 154                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1400                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M19   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT                                     
DBREF  1N18 A    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 B    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 C    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 D    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 E    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 F    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 G    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 H    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 I    0   153  UNP    P00441   SODC_HUMAN       0    153             
DBREF  1N18 J    0   153  UNP    P00441   SODC_HUMAN       0    153             
SEQADV 1N18 ALA A    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER A  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA B    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER B  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA C    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER C  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA D    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER D  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA E    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER E  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA F    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER F  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA G    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER G  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA H    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER H  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA I    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER I  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1N18 ALA J    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1N18 SER J  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQRES   1 A  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 E  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 E  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 E  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 E  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 E  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 E  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 E  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 E  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 E  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 E  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 E  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 E  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 G  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 G  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 G  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 G  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 G  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 G  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 G  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 G  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 G  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 G  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 G  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 G  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 H  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 H  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 H  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 H  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 H  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 H  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 H  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 H  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 H  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 H  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 H  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 H  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 I  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 I  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 I  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 I  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 I  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 I  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 I  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 I  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 I  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 I  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 I  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 I  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 J  154  MET ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 J  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 J  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 J  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 J  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 J  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 J  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 J  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 J  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 J  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 J  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 J  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET    CU1  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET    CU1  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET    CU1  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET    CU1  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET    CU1  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET    CU1  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET    CU1  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET    CU1  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET    CU1  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET    CU1  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET    SO4  D1400       5                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL  11  CU1    10(CU 1+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  SO4    O4 S 2-                                                      
FORMUL  32  HOH   *1389(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 ASN A  131  THR A  135  5                                   5    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 ALA C   55  GLY C   61  5                                   7    
HELIX    5   5 ASN C  131  THR C  137  1                                   7    
HELIX    6   6 CYS D   57  GLY D   61  5                                   5    
HELIX    7   7 GLU D  132  LYS D  136  5                                   5    
HELIX    8   8 ALA E   55  GLY E   61  5                                   7    
HELIX    9   9 GLU E  132  LYS E  136  5                                   5    
HELIX   10  10 ALA F   55  GLY F   61  5                                   7    
HELIX   11  11 ASN F  131  THR F  135  5                                   5    
HELIX   12  12 CYS G   57  GLY G   61  5                                   5    
HELIX   13  13 CYS H   57  GLY H   61  5                                   5    
HELIX   14  14 GLU H  132  LYS H  136  5                                   5    
HELIX   15  15 ALA I   55  GLY I   61  5                                   7    
HELIX   16  16 GLU I  132  LYS I  136  5                                   5    
HELIX   17  17 ALA J   55  GLY J   61  5                                   7    
HELIX   18  18 SER J  107  SER J  111  5                                   5    
HELIX   19  19 GLU J  132  LYS J  136  5                                   5    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  31   O  ILE A  99           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  VAL B  31   O  ILE B  99           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LYS B   9 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 LYS C   3  LEU C   8 -1  N  ALA C   6   O  ILE C  18           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  VAL D  29   O  ASP D 101           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1   I 5 ALA E  95  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    3   I 5 GLN E  15  GLU E  21 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 LYS E   3  LEU E   8 -1  N  LEU E   8   O  GLY E  16           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  GLY E 147   N  LEU E 117           
SHEET    1   K 5 ALA F  95  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  LYS F  36 -1  N  VAL F  31   O  ILE F  99           
SHEET    3   K 5 GLN F  15  GLU F  21 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 LYS F   3  LEU F   8 -1  N  ALA F   6   O  ILE F  18           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  GLY F 147   N  LEU F 117           
SHEET    1   M 5 ALA G  95  ASP G 101  0                                        
SHEET    2   M 5 VAL G  29  LYS G  36 -1  N  VAL G  31   O  ILE G  99           
SHEET    3   M 5 GLN G  15  GLU G  21 -1  N  ASN G  19   O  TRP G  32           
SHEET    4   M 5 LYS G   3  LEU G   8 -1  N  LEU G   8   O  GLY G  16           
SHEET    5   M 5 GLY G 150  ALA G 152 -1  O  GLY G 150   N  VAL G   5           
SHEET    1   N 4 ASP G  83  ALA G  89  0                                        
SHEET    2   N 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   N 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4   N 4 ARG G 143  VAL G 148 -1  O  ALA G 145   N  VAL G 119           
SHEET    1   O 5 ALA H  95  ASP H 101  0                                        
SHEET    2   O 5 VAL H  29  LYS H  36 -1  N  ILE H  35   O  ALA H  95           
SHEET    3   O 5 GLN H  15  GLU H  21 -1  N  ASN H  19   O  TRP H  32           
SHEET    4   O 5 LYS H   3  LEU H   8 -1  N  LEU H   8   O  GLY H  16           
SHEET    5   O 5 GLY H 150  GLN H 153 -1  O  ALA H 152   N  LYS H   3           
SHEET    1   P 4 ASP H  83  ALA H  89  0                                        
SHEET    2   P 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3   P 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4   P 4 ARG H 143  VAL H 148 -1  O  GLY H 147   N  LEU H 117           
SHEET    1   Q 5 ALA I  95  ASP I 101  0                                        
SHEET    2   Q 5 VAL I  29  LYS I  36 -1  N  VAL I  31   O  ILE I  99           
SHEET    3   Q 5 GLN I  15  GLN I  22 -1  N  ASN I  19   O  TRP I  32           
SHEET    4   Q 5 LYS I   3  LEU I   8 -1  N  ALA I   4   O  PHE I  20           
SHEET    5   Q 5 GLY I 150  ALA I 152 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   R 4 ASP I  83  ALA I  89  0                                        
SHEET    2   R 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   R 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4   R 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   S 5 ALA J  95  ASP J 101  0                                        
SHEET    2   S 5 VAL J  29  LYS J  36 -1  N  VAL J  31   O  ILE J  99           
SHEET    3   S 5 GLN J  15  GLU J  21 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   S 5 LYS J   3  LEU J   8 -1  N  ALA J   4   O  PHE J  20           
SHEET    5   S 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   T 4 ASP J  83  ALA J  89  0                                        
SHEET    2   T 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   T 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   T 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.05  
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  2.04  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.04  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.04  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.04  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.04  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.03  
LINK        CU   CU1 A 154                 ND1 HIS A  46     1555   1555  2.15  
LINK        CU   CU1 A 154                 NE2 HIS A  48     1555   1555  2.14  
LINK        CU   CU1 A 154                 NE2 HIS A 120     1555   1555  2.12  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.90  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.04  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.06  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.01  
LINK        CU   CU1 B 154                 NE2 HIS B  48     1555   1555  2.02  
LINK        CU   CU1 B 154                 ND1 HIS B  46     1555   1555  2.04  
LINK        CU   CU1 B 154                 NE2 HIS B 120     1555   1555  2.02  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.00  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.02  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.13  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.96  
LINK        CU   CU1 C 154                 NE2 HIS C  48     1555   1555  2.11  
LINK        CU   CU1 C 154                 NE2 HIS C  63     1555   1555  2.66  
LINK        CU   CU1 C 154                 NE2 HIS C 120     1555   1555  2.06  
LINK        CU   CU1 C 154                 ND1 HIS C  46     1555   1555  2.17  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.07  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.36  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.81  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.05  
LINK        CU   CU1 D 154                 ND1 HIS D  46     1555   1555  2.15  
LINK        CU   CU1 D 154                 NE2 HIS D 120     1555   1555  2.01  
LINK        CU   CU1 D 154                 NE2 HIS D  48     1555   1555  2.04  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.94  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.04  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.00  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  1.95  
LINK        CU   CU1 E 154                 NE2 HIS E 120     1555   1555  1.97  
LINK        CU   CU1 E 154                 NE2 HIS E  48     1555   1555  2.09  
LINK        CU   CU1 E 154                 ND1 HIS E  46     1555   1555  2.13  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.10  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  1.98  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.06  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.85  
LINK        CU   CU1 F 154                 ND1 HIS F  46     1555   1555  2.16  
LINK        CU   CU1 F 154                 NE2 HIS F 120     1555   1555  2.01  
LINK        CU   CU1 F 154                 NE2 HIS F  48     1555   1555  2.02  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.92  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  2.07  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.06  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.10  
LINK        CU   CU1 G 154                 NE2 HIS G 120     1555   1555  2.10  
LINK        CU   CU1 G 154                 NE2 HIS G  48     1555   1555  2.17  
LINK        CU   CU1 G 154                 ND1 HIS G  46     1555   1555  2.23  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  2.06  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.13  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.92  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.16  
LINK        CU   CU1 H 154                 NE2 HIS H 120     1555   1555  2.06  
LINK        CU   CU1 H 154                 NE2 HIS H  48     1555   1555  2.04  
LINK        CU   CU1 H 154                 ND1 HIS H  46     1555   1555  2.15  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.07  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.92  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  2.11  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.00  
LINK        CU   CU1 I 154                 NE2 HIS I 120     1555   1555  1.93  
LINK        CU   CU1 I 154                 NE2 HIS I  48     1555   1555  2.13  
LINK        CU   CU1 I 154                 ND1 HIS I  46     1555   1555  2.20  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  2.10  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  1.97  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.14  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  2.01  
LINK        CU   CU1 J 154                 ND1 HIS J  46     1555   1555  2.36  
LINK        CU   CU1 J 154                 NE2 HIS J 120     1555   1555  1.92  
LINK        CU   CU1 J 154                 NE2 HIS J  48     1555   1555  2.08  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.02  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.92  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  2.01  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  1.97  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC5  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 BC6  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC8  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC1  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC3  5 LYS B  75  LYS D 128  HOH D1429  HOH D1450                    
SITE     2 CC3  5 HOH D1515                                                     
CRYST1  203.200  165.200  144.300  90.00  90.00  90.00 C 2 2 21     80          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004921  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006053  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006930        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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