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Database: PDB
Entry: 2APS
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HEADER    SUPEROXIDE DISMUTASE                    11-FEB-99   2APS              
TITLE     CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS                        
TITLE    2 PLEUROPNEUMONIAE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CU,ZN SUPEROXIDE DISMUTASE);                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SOD;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: EACH ACTIVE SITE CONTAINS ONE COPPER AND              
COMPND   7 ONE ZINC.                                                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACTINOBACILLUS PLEUROPNEUMONIAE;                
SOURCE   3 ORGANISM_TAXID: 715;                                                 
SOURCE   4 CELLULAR_LOCATION: PERIPLASM;                                        
SOURCE   5 GENE: SODC;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: QC779;                                     
SOURCE   9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;                      
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PJSK157;                                  
SOURCE  11 EXPRESSION_SYSTEM_GENE: SODC                                         
KEYWDS    SUPEROXIDE DISMUTASE, SOD, WATER-MEDIATED DIMER, BETA BARREL          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.T.FOREST,P.R.LANGFORD,J.S.KROLL,E.D.GETZOFF                         
REVDAT   4   24-FEB-09 2APS    1       VERSN                                    
REVDAT   3   01-APR-03 2APS    1       JRNL                                     
REVDAT   2   07-FEB-00 2APS    1       JRNL                                     
REVDAT   1   25-FEB-99 2APS    0                                                
JRNL        AUTH   K.T.FOREST,P.R.LANGFORD,J.S.KROLL,E.D.GETZOFF                
JRNL        TITL   CU,ZN SUPEROXIDE DISMUTASE STRUCTURE FROM A                  
JRNL        TITL 2 MICROBIAL PATHOGEN ESTABLISHES A CLASS WITH A                
JRNL        TITL 3 CONSERVED DIMER INTERFACE.                                   
JRNL        REF    J.MOL.BIOL.                   V. 296   145 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10656823                                                     
JRNL        DOI    10.1006/JMBI.1999.3448                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 30219                          
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) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1534                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2549                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3430                       
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 146                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2321                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 25.80000                                             
REMARK   3    B22 (A**2) : 22.90000                                             
REMARK   3    B33 (A**2) : 16.50000                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 1.500                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.02                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : 1.500 ; 1.900                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; 3.100                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 3.100                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 4.700                
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  : PARHCSDX_SOD.PRO                               
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19.PEP                                     
REMARK   3  TOPOLOGY FILE  2   : TOPHCSDX_SOD.PRO                               
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: CHAIN B IS MUCH MORE WELL-ORDERED         
REMARK   3  THAN CHAIN A.                                                       
REMARK   4                                                                      
REMARK   4 2APS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000470.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUL-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
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   : 30234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 13.700                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1YAI                                       
REMARK 200                                                                      
REMARK 200 REMARK: SEARCH MODEL WAS A DIMER.                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.62500            
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       53.62500            
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       29.02500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.94000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.02500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.94000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.62500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.02500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       61.94000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.62500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.02500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       61.94000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CU    CU A 300  LIES ON A SPECIAL POSITION.                          
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     LYS A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     VAL B    12                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     LEU A  76    CG   CD1  CD2                                       
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    ASP A  23      100.41   -173.59                                   
REMARK 500    GLN A  63      -73.72    -57.48                                   
REMARK 500    PRO A  69     -176.65    -66.70                                   
REMARK 500    ASP A 145      112.34   -167.83                                   
REMARK 500    HIS B  48       69.98   -151.60                                   
REMARK 500    ASP B 145      109.01   -160.47                                   
REMARK 500    PRO B 159      156.20    -49.76                                   
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 A1266        DISTANCE =  7.04 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CU 300 AND CU 500 FORM CRYSTAL CONTACTS.                             
REMARK 600  CU 300 LIES ON A SPECIAL POSITION.                                  
REMARK 600 CU 402 AND CU 602 ARE IN  ACTIVE SITES.                              
REMARK 600                                                                      
REMARK 600 BOTH ZINC IONS ARE IN ACTIVE SITES.                                  
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 402  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  60   ND1                                                    
REMARK 620 2 HIS A  62   NE2 140.6                                              
REMARK 620 3 HIS A 141   NE2  89.7 126.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  85   ND1                                                    
REMARK 620 2 HIS A  94   ND1 104.7                                              
REMARK 620 3 HIS A 103   ND1 109.2 118.6                                        
REMARK 620 4 ASP A 106   OD1 111.8  98.8 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 500  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HIS B  50   NE2  95.7                                              
REMARK 620 3 HOH B1353   O    86.1  76.8                                        
REMARK 620 4 HIS B 114   NE2 161.9 102.1  94.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  60   ND1                                                    
REMARK 620 2 HIS B  62   NE2 140.1                                              
REMARK 620 3 HIS B 141   NE2 102.5 114.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 600  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  85   ND1                                                    
REMARK 620 2 HIS B  94   ND1 103.3                                              
REMARK 620 3 HIS B 103   ND1 106.7 124.9                                        
REMARK 620 4 ASP B 106   OD1 111.0  95.4 114.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 300  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 HIS A  50   NE2  83.1                                              
REMARK 620 3 HIS A  50   NE2 165.0 101.2                                        
REMARK 620 4 HIS A  48   NE2  96.6 162.4  83.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: COPPER AND ZINC ARE LIGATED BY THREE               
REMARK 800  CONSERVED HISTIDINES EACH IN THE ACTIVE SITE OF EACH SUBUNIT.       
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 300                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 500                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 402                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 600                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 602                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE IS NO LEADER PEPTIDE IN THE                                    
REMARK 999 PURIFIED PROTEIN (23 RESIDUES ARE                                    
REMARK 999 CLEAVED) AND THE FIRST 5 RESIDUES                                    
REMARK 999 OF THE EXPRESSED (MATURE) PROTEIN                                    
REMARK 999 HAVE APPARENTLY BEEN CLEAVED DURING                                  
REMARK 999 PURIFICATION. RESIDUES 6-12 ARE                                      
REMARK 999 PRESENT IN THE PROTEIN BUT NOT SEEN                                  
REMARK 999  IN THE ELECTRON DENSITY.                                            
DBREF  2APS A   13   167  UNP    P24702   SODC_ACTPL      29    190             
DBREF  2APS B   13   167  GB     1438120  X99396          29    190             
SEQRES   1 A  162  LYS ALA ASP ASN SER SER VAL GLU LYS LEU VAL VAL GLN          
SEQRES   2 A  162  VAL GLN GLN LEU ASP PRO VAL LYS GLY ASN LYS ASP VAL          
SEQRES   3 A  162  GLY THR VAL GLU ILE THR GLU SER ALA TYR GLY LEU VAL          
SEQRES   4 A  162  PHE THR PRO HIS LEU HIS GLY LEU ALA GLN GLY LEU HIS          
SEQRES   5 A  162  GLY PHE HIS ILE HIS GLN ASN PRO SER CYS GLU PRO LYS          
SEQRES   6 A  162  GLU LYS ASP GLY LYS LEU VAL ALA GLY LEU GLY ALA GLY          
SEQRES   7 A  162  GLY HIS TRP ASP PRO LYS GLU THR LYS GLN HIS GLY TYR          
SEQRES   8 A  162  PRO TRP SER ASP ASN ALA HIS LEU GLY ASP LEU PRO ALA          
SEQRES   9 A  162  LEU PHE VAL GLU HIS ASP GLY SER ALA THR ASN PRO VAL          
SEQRES  10 A  162  LEU ALA PRO ARG LEU LYS LYS LEU ASP GLU VAL LYS GLY          
SEQRES  11 A  162  HIS SER LEU MET ILE HIS GLU GLY GLY ASP ASN HIS SER          
SEQRES  12 A  162  ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO ARG MET          
SEQRES  13 A  162  ALA CYS GLY VAL ILE LYS                                      
SEQRES   1 B  162  LYS ALA ASP ASN SER SER VAL GLU LYS LEU VAL VAL GLN          
SEQRES   2 B  162  VAL GLN GLN LEU ASP PRO VAL LYS GLY ASN LYS ASP VAL          
SEQRES   3 B  162  GLY THR VAL GLU ILE THR GLU SER ALA TYR GLY LEU VAL          
SEQRES   4 B  162  PHE THR PRO HIS LEU HIS GLY LEU ALA GLN GLY LEU HIS          
SEQRES   5 B  162  GLY PHE HIS ILE HIS GLN ASN PRO SER CYS GLU PRO LYS          
SEQRES   6 B  162  GLU LYS ASP GLY LYS LEU VAL ALA GLY LEU GLY ALA GLY          
SEQRES   7 B  162  GLY HIS TRP ASP PRO LYS GLU THR LYS GLN HIS GLY TYR          
SEQRES   8 B  162  PRO TRP SER ASP ASN ALA HIS LEU GLY ASP LEU PRO ALA          
SEQRES   9 B  162  LEU PHE VAL GLU HIS ASP GLY SER ALA THR ASN PRO VAL          
SEQRES  10 B  162  LEU ALA PRO ARG LEU LYS LYS LEU ASP GLU VAL LYS GLY          
SEQRES  11 B  162  HIS SER LEU MET ILE HIS GLU GLY GLY ASP ASN HIS SER          
SEQRES  12 B  162  ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO ARG MET          
SEQRES  13 B  162  ALA CYS GLY VAL ILE LYS                                      
HET     CU  A 300       1                                                       
HET     CU  B 500       1                                                       
HET     ZN  A 400       1                                                       
HET     CU  A 402       1                                                       
HET     ZN  B 600       1                                                       
HET     CU  B 602       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   3   CU    4(CU 2+)                                                     
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   9  HOH   *126(H2 O)                                                    
HELIX    1   1 LEU A   80  ALA A   82  5                                   3    
HELIX    2   2 LEU A  130  VAL A  133  1                                   4    
HELIX    3   3 PRO A  153  GLY A  156  5                                   4    
HELIX    4   4 LEU B   80  ALA B   82  5                                   3    
HELIX    5   5 LEU B  130  VAL B  133  1                                   4    
HELIX    6   6 PRO B  153  GLY B  156  5                                   4    
SHEET    1   A 7 VAL A 122  ALA A 124  0                                        
SHEET    2   A 7 GLY A  42  LEU A  49 -1  N  PHE A  45   O  VAL A 122           
SHEET    3   A 7 LYS A  29  SER A  39 -1  N  SER A  39   O  GLY A  42           
SHEET    4   A 7 VAL A  16  GLN A  21 -1  N  GLN A  21   O  LYS A  29           
SHEET    5   A 7 ARG A 160  ILE A 166 -1  N  CYS A 163   O  GLN A  20           
SHEET    6   A 7 HIS A 136  HIS A 141 -1  N  ILE A 140   O  MET A 161           
SHEET    7   A 7 PHE A  59  HIS A  62 -1  N  HIS A  62   O  SER A 137           
SHEET    1   B 2 GLY A  55  HIS A  57  0                                        
SHEET    2   B 2 LEU A 110  VAL A 112 -1  N  VAL A 112   O  GLY A  55           
SHEET    1   C 2 LYS A  70  LYS A  72  0                                        
SHEET    1   D 4 VAL B 122  ALA B 124  0                                        
SHEET    2   D 4 GLY B  42  LEU B  49 -1  N  PHE B  45   O  VAL B 122           
SHEET    3   D 4 LYS B  29  SER B  39 -1  N  SER B  39   O  GLY B  42           
SHEET    4   D 4 LEU B  15  GLN B  21 -1  N  GLN B  21   O  LYS B  29           
SHEET    1   E 2 GLY B  55  HIS B  57  0                                        
SHEET    2   E 2 LEU B 110  VAL B 112 -1  N  VAL B 112   O  GLY B  55           
SHEET    1   F 3 PHE B  59  HIS B  62  0                                        
SHEET    2   F 3 HIS B 136  HIS B 141 -1  N  MET B 139   O  HIS B  60           
SHEET    3   F 3 ARG B 160  ILE B 166 -1  N  ILE B 166   O  HIS B 136           
SHEET    1   G 2 LYS B  70  LYS B  72  0                                        
SHEET    2   G 2 LYS B  75  VAL B  77 -1  N  VAL B  77   O  LYS B  70           
SSBOND   1 CYS A   67    CYS A  163                          1555   1555  2.04  
SSBOND   2 CYS B   67    CYS B  163                          1555   1555  2.05  
LINK         ND1 HIS A  60                CU    CU A 402     1555   1555  2.29  
LINK         NE2 HIS A  62                CU    CU A 402     1555   1555  2.24  
LINK         ND1 HIS A  85                ZN    ZN A 400     1555   1555  2.13  
LINK         ND1 HIS A  94                ZN    ZN A 400     1555   1555  2.10  
LINK         ND1 HIS A 103                ZN    ZN A 400     1555   1555  2.15  
LINK         OD1 ASP A 106                ZN    ZN A 400     1555   1555  2.00  
LINK         NE2 HIS A 141                CU    CU A 402     1555   1555  1.89  
LINK         NE2 HIS B  48                CU    CU B 500     1555   1555  2.28  
LINK         NE2 HIS B  50                CU    CU B 500     1555   1555  2.34  
LINK         ND1 HIS B  60                CU    CU B 602     1555   1555  1.99  
LINK         NE2 HIS B  62                CU    CU B 602     1555   1555  2.05  
LINK         ND1 HIS B  85                ZN    ZN B 600     1555   1555  2.08  
LINK         ND1 HIS B  94                ZN    ZN B 600     1555   1555  2.13  
LINK         ND1 HIS B 103                ZN    ZN B 600     1555   1555  2.01  
LINK         OD1 ASP B 106                ZN    ZN B 600     1555   1555  2.00  
LINK         NE2 HIS B 141                CU    CU B 602     1555   1555  2.14  
LINK        CU    CU A 300                 NE2 HIS A  48     1555   1555  1.71  
LINK        CU    CU A 300                 NE2 HIS A  50     1555   1555  1.65  
LINK        CU    CU B 500                 O   HOH B1353     1555   1555  1.51  
LINK        CU    CU A 300                 NE2 HIS A  50     1555   3655  1.64  
LINK        CU    CU A 300                 NE2 HIS A  48     1555   3655  1.71  
LINK        CU    CU B 500                 NE2 HIS B 114     1555   4566  1.98  
CISPEP   1 HIS A  150    PRO A  151          0         0.07                     
CISPEP   2 HIS B  150    PRO B  151          0         0.18                     
SITE     1 ACT 12 HIS A  60  HIS A  62  HIS A  85  HIS A  94                    
SITE     2 ACT 12 HIS A 103  HIS A 141  HIS B  60  HIS B  62                    
SITE     3 ACT 12 HIS B  85  HIS B  94  HIS B 103  HIS B 141                    
SITE     1 AC1  2 HIS A  48  HIS A  50                                          
SITE     1 AC2  4 HIS B  48  HIS B  50  HIS B 114  HOH B1353                    
SITE     1 AC3  4 HIS A  85  HIS A  94  HIS A 103  ASP A 106                    
SITE     1 AC4  4 HIS A  60  HIS A  62  HIS A  85  HIS A 141                    
SITE     1 AC5  4 HIS B  85  HIS B  94  HIS B 103  ASP B 106                    
SITE     1 AC6  4 HIS B  60  HIS B  62  HIS B  85  HIS B 141                    
CRYST1   58.050  123.880  107.250  90.00  90.00  90.00 C 2 2 21     16          
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      0.017226  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008072  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009324        0.00000                         
MTRIX1   1 -0.859000  0.506300 -0.076500       25.49200    1                    
MTRIX2   1  0.501500  0.801600 -0.325500       11.14300    1                    
MTRIX3   1 -0.103500 -0.318000 -0.942400      102.93800    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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