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Database: PDB
Entry: 2GBV
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HEADER    OXIDOREDUCTASE                          11-MAR-06   2GBV              
TITLE     C6A/C111A/C57A/C146A HOLO CUZN SUPEROXIDE DISMUTASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: CU/ZN SUPEROXIDE DISMUTASE;                                 
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACA                                      
KEYWDS    OXIDOREDUCTASE, HUMAN CU/ZN SUPEROXIDE DISMUTASE, CYSTEIN-FREE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG                         
REVDAT   3   13-JUL-11 2GBV    1       VERSN                                    
REVDAT   2   24-FEB-09 2GBV    1       VERSN                                    
REVDAT   1   02-JAN-07 2GBV    0                                                
JRNL        AUTH   A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG                
JRNL        TITL   THE COUPLING BETWEEN DISULPHIDE STATUS, METALLATION AND      
JRNL        TITL 2 DIMER INTERFACE STRENGTH IN CU/ZN SUPEROXIDE DISMUTASE       
JRNL        REF    J.MOL.BIOL.                   V. 365   333 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17070542                                                     
JRNL        DOI    10.1016/J.JMB.2006.09.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 162695                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8162                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11236                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 622                          
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11060                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 1498                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.83000                                              
REMARK   3    B22 (A**2) : -0.30000                                             
REMARK   3    B33 (A**2) : -0.53000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.129         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.274         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11240 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 10000 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15180 ; 1.055 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 23410 ; 0.669 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1520 ; 5.900 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   480 ;39.487 ;25.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1810 ;11.075 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ; 9.137 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1680 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13030 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2040 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1891 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10075 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5430 ; 0.158 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  6409 ; 0.079 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1166 ; 0.106 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    36 ; 0.092 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.111 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   107 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    65 ; 0.110 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9828 ; 0.519 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3280 ; 0.074 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11800 ; 0.577 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4580 ; 1.108 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3380 ; 1.501 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 123.7685  57.0514  52.8050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1565 T22:  -0.1304                                     
REMARK   3      T33:  -0.1666 T12:  -0.0909                                     
REMARK   3      T13:   0.0307 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8723 L22:   1.8405                                     
REMARK   3      L33:   2.1567 L12:   0.4257                                     
REMARK   3      L13:  -0.3616 L23:   0.1972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:   0.0074 S13:   0.0112                       
REMARK   3      S21:   0.0505 S22:  -0.0175 S23:   0.1181                       
REMARK   3      S31:   0.1542 S32:  -0.2172 S33:   0.0255                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 174.8075 117.6698  52.6607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3769 T22:  -0.1773                                     
REMARK   3      T33:  -0.0954 T12:  -0.0684                                     
REMARK   3      T13:  -0.1771 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7976 L22:   3.5328                                     
REMARK   3      L33:   5.3350 L12:   0.2352                                     
REMARK   3      L13:   1.1896 L23:   0.3349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4182 S12:   0.0533 S13:   0.2497                       
REMARK   3      S21:  -0.0511 S22:  -0.0118 S23:  -0.0506                       
REMARK   3      S31:  -1.3573 S32:   0.2656 S33:   0.4300                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 203.1679  43.4306  52.7197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1930 T22:  -0.1583                                     
REMARK   3      T33:  -0.1985 T12:   0.0541                                     
REMARK   3      T13:   0.0139 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9793 L22:   2.3628                                     
REMARK   3      L33:   1.7240 L12:  -0.9386                                     
REMARK   3      L13:   0.1342 L23:  -0.2282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0008 S12:  -0.0094 S13:  -0.0445                       
REMARK   3      S21:  -0.0402 S22:  -0.0224 S23:   0.0159                       
REMARK   3      S31:   0.0029 S32:   0.0012 S33:   0.0217                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 177.1731 149.2712  52.3769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1727 T22:  -0.0255                                     
REMARK   3      T33:  -0.1220 T12:  -0.0624                                     
REMARK   3      T13:  -0.0612 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8906 L22:   2.9873                                     
REMARK   3      L33:   2.5804 L12:   0.2814                                     
REMARK   3      L13:   0.1630 L23:   1.1632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1394 S12:   0.2329 S13:  -0.0188                       
REMARK   3      S21:   0.0164 S22:  -0.2443 S23:  -0.1403                       
REMARK   3      S31:  -0.1348 S32:  -0.0886 S33:   0.1050                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 126.5045  87.2157  46.5566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0623 T22:  -0.1301                                     
REMARK   3      T33:   0.0592 T12:   0.0006                                     
REMARK   3      T13:  -0.0011 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0663 L22:   4.8120                                     
REMARK   3      L33:   2.4590 L12:  -0.0665                                     
REMARK   3      L13:   0.4177 L23:  -1.0538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0011 S12:   0.1330 S13:   0.2743                       
REMARK   3      S21:  -0.4324 S22:   0.0379 S23:   0.2116                       
REMARK   3      S31:   0.0659 S32:  -0.1692 S33:  -0.0368                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 149.6225  66.3491  53.6764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1754 T22:  -0.1852                                     
REMARK   3      T33:  -0.2074 T12:  -0.0327                                     
REMARK   3      T13:   0.0252 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0635 L22:   1.9723                                     
REMARK   3      L33:   1.2139 L12:   0.1129                                     
REMARK   3      L13:   0.1755 L23:   0.4909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0046 S12:  -0.0009 S13:  -0.0581                       
REMARK   3      S21:   0.0088 S22:  -0.0482 S23:   0.1145                       
REMARK   3      S31:   0.1016 S32:  -0.0654 S33:   0.0528                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 170.7853  90.5000  53.7968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1784 T22:  -0.1932                                     
REMARK   3      T33:  -0.2036 T12:   0.0088                                     
REMARK   3      T13:  -0.0036 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7674 L22:   2.5523                                     
REMARK   3      L33:   1.8272 L12:   0.8352                                     
REMARK   3      L13:   0.4316 L23:  -0.2441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0682 S12:   0.0609 S13:   0.1245                       
REMARK   3      S21:   0.0453 S22:  -0.0596 S23:   0.0312                       
REMARK   3      S31:  -0.1314 S32:   0.0752 S33:   0.1278                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 181.3113  60.0120  53.9721              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1841 T22:  -0.1567                                     
REMARK   3      T33:  -0.2066 T12:   0.0357                                     
REMARK   3      T13:   0.0032 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2027 L22:   3.3402                                     
REMARK   3      L33:   1.4515 L12:  -1.3137                                     
REMARK   3      L13:  -0.2778 L23:   0.2039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:   0.0224 S13:   0.0222                       
REMARK   3      S21:  -0.1611 S22:  -0.0448 S23:  -0.0091                       
REMARK   3      S31:   0.0282 S32:   0.0137 S33:   0.0573                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 151.5285 139.2435  51.8282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1858 T22:  -0.0371                                     
REMARK   3      T33:  -0.1380 T12:   0.0054                                     
REMARK   3      T13:  -0.0532 T23:  -0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3519 L22:   2.3420                                     
REMARK   3      L33:   1.3321 L12:   0.1238                                     
REMARK   3      L13:  -0.2486 L23:   0.2032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1072 S12:   0.1049 S13:   0.1047                       
REMARK   3      S21:   0.0781 S22:   0.1780 S23:  -0.2531                       
REMARK   3      S31:  -0.0865 S32:   0.2432 S33:  -0.0709                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 130.8894 114.2553  48.9272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1166 T22:  -0.1457                                     
REMARK   3      T33:  -0.0561 T12:   0.0397                                     
REMARK   3      T13:   0.0005 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9529 L22:   4.1513                                     
REMARK   3      L33:   1.1308 L12:   0.8923                                     
REMARK   3      L13:  -0.0582 L23:   0.5932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0799 S12:   0.0841 S13:  -0.2938                       
REMARK   3      S21:  -0.0867 S22:   0.0277 S23:   0.2967                       
REMARK   3      S31:   0.0834 S32:  -0.0671 S33:   0.0522                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2GBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036932.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.080                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARXDS                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162729                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1N18                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M AMMONIUM SULPHATE, 50MM NAAC,       
REMARK 280  0.1M TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  291K                                                                
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       71.82000            
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       71.82000            
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       83.40000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.18500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       83.40000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.18500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.82000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       83.40000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.18500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.82000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       83.40000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.18500            
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: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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      HOH D1591  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA C  55       60.82   -116.82                                   
REMARK 500    ASN F  65       58.81   -145.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 801        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A1451        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A1834        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B1857        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH C1006        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH C1028        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH C1070        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH C1072        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C1532        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH C1900        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH D1585        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH E 158        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH F 640        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH G 257        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH G 274        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH G 435        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH G 609        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH G 619        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH G 623        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH G 624        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH G 625        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH G1751        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH G1853        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH H 277        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH H1676        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH H1750        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH I 156        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH I 170        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH I 300        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH I 308        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH J 165        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH J 179        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH J 254        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH J 256        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH J 285        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH J 289        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH J 290        DISTANCE =  7.51 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 144.1                                              
REMARK 620 3 HIS A 120   NE2 101.8 113.3                                        
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 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1  99.8                                              
REMARK 620 3 HIS A  80   ND1 110.1 123.2                                        
REMARK 620 4 ASP A  83   OD1 109.7  98.3 114.2                                  
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  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 145.2                                              
REMARK 620 3 HIS B 120   NE2  98.3 110.9                                        
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  95.5                                              
REMARK 620 3 HIS B  80   ND1 125.8 134.8                                        
REMARK 620 4 ASP B  83   OD1  83.1  69.0 127.0                                  
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  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 146.8                                              
REMARK 620 3 HIS C 120   NE2 106.0 106.9                                        
REMARK 620 N                    1     2                                         
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  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 100.0                                              
REMARK 620 3 HIS C  80   ND1 114.5 123.8                                        
REMARK 620 4 ASP C  83   OD1 102.6  97.0 115.5                                  
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  48   NE2 147.8                                              
REMARK 620 3 HIS D 120   NE2 102.0 110.1                                        
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 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 102.2                                              
REMARK 620 3 HIS D  80   ND1 113.1 121.5                                        
REMARK 620 4 ASP D  83   OD1 105.4  93.5 118.1                                  
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  46   ND1                                                    
REMARK 620 2 HIS E  48   NE2 150.4                                              
REMARK 620 3 HIS E 120   NE2  97.8 111.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1 102.2                                              
REMARK 620 3 HIS E  80   ND1 107.7 121.0                                        
REMARK 620 4 ASP E  83   OD1 110.0  97.8 116.9                                  
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  48   NE2 147.3                                              
REMARK 620 3 HIS F 120   NE2  98.5 114.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 104.1                                              
REMARK 620 3 HIS F  80   ND1 112.5 121.9                                        
REMARK 620 4 ASP F  83   OD1 104.4  96.9 114.7                                  
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  46   ND1                                                    
REMARK 620 2 HIS G  48   NE2 147.4                                              
REMARK 620 3 HIS G 120   NE2 105.1 107.4                                        
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  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 102.6                                              
REMARK 620 3 HIS G  80   ND1 112.1 122.9                                        
REMARK 620 4 ASP G  83   OD1 103.3  98.1 115.2                                  
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  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 148.7                                              
REMARK 620 3 HIS H 120   NE2 102.0 109.3                                        
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  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1  99.8                                              
REMARK 620 3 HIS H  80   ND1 111.6 123.9                                        
REMARK 620 4 ASP H  83   OD1 107.4  99.1 113.2                                  
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  48   NE2                                                    
REMARK 620 2 HIS I 120   NE2 112.0                                              
REMARK 620 3 HIS I  46   ND1 147.2 100.7                                        
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 100.2                                              
REMARK 620 3 HIS I  80   ND1 112.8 125.5                                        
REMARK 620 4 ASP I  83   OD1 105.4  96.1 114.0                                  
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  48   NE2                                                    
REMARK 620 2 HIS J 120   NE2 109.5                                              
REMARK 620 3 HIS J  46   ND1 147.1 103.3                                        
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  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 100.9                                              
REMARK 620 3 HIS J  80   ND1 112.3 123.6                                        
REMARK 620 4 ASP J  83   OD1 103.8 100.7 113.1                                  
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 G 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 H 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 I 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 J 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900 APO CUZN SUPEROXIDE DISMUTASE                                        
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900 C6A/C111S THERMOSTABLE MUTANT OF SUPEROXIDE DISMUTASE                
REMARK 900 RELATED ID: 2GBT   RELATED DB: PDB                                   
REMARK 900 C6A/C111A APO CUZN SUPEROXIDE DISMUTASE                              
REMARK 900 RELATED ID: 2GBU   RELATED DB: PDB                                   
REMARK 900 C6A/C111A/C57A/C146A APO CUZN SUPEROXIDE DISMUTASE                   
DBREF  2GBV A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBV J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 2GBV ALA A    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA A   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA A  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA A  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA B    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA B   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA B  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA B  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA C    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA C   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA C  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA C  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA D    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA D   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA D  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA D  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA E    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA E   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA E  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA E  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA F    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA F   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA F  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA F  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA G    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA G   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA G  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA G  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA H    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA H   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA H  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA H  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA I    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA I   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA I  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA I  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBV ALA J    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBV ALA J   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBV ALA J  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBV ALA J  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA ALA 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                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
FORMUL  11  CU1    10(CU 1+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  HOH   *1498(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  133  GLY A  138  1                                   6    
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 GLU C  133  GLY C  138  1                                   6    
HELIX    6   6 ALA D   55  GLY D   61  5                                   7    
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 ALA F   55  GLY F   61  5                                   7    
HELIX   10  10 ALA G   55  GLY G   61  5                                   7    
HELIX   11  11 ASN G  131  LYS G  136  5                                   6    
HELIX   12  12 ALA H   55  GLY H   61  5                                   7    
HELIX   13  13 GLU H  133  GLY H  138  1                                   6    
HELIX   14  14 ALA I   55  GLY I   61  5                                   7    
HELIX   15  15 ALA J   55  GLY J   61  5                                   7    
HELIX   16  16 ASN J  131  LYS J  136  5                                   6    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  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 THR A   2  LEU A   8 -1  N  THR A   2   O  GLN A  22           
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  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LEU B   8 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ALA B 152 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  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  GLN C  22 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 THR C   2  LEU C   8 -1  N  THR C   2   O  GLN C  22           
SHEET    5   E 5 GLY C 150  ALA C 152 -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  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLN D  22 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 THR D   2  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ALA D 152 -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  GLN E  22 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 THR E   2  LYS E   9 -1  N  ALA E   4   O  PHE E  20           
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  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 THR F   2  LEU F   8 -1  N  THR F   2   O  GLN F  22           
SHEET    5   K 5 GLY F 150  ALA F 152 -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  ILE G  35   O  ALA G  95           
SHEET    3   M 5 GLN G  15  GLN G  22 -1  N  ASN G  19   O  TRP G  32           
SHEET    4   M 5 THR G   2  LEU G   8 -1  N  ALA G   6   O  ILE G  18           
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  GLY G 147   N  LEU G 117           
SHEET    1   O 5 ALA H  95  ASP H 101  0                                        
SHEET    2   O 5 VAL H  29  LYS H  36 -1  N  VAL H  31   O  ILE H  99           
SHEET    3   O 5 GLN H  15  GLN H  22 -1  N  ASN H  19   O  TRP H  32           
SHEET    4   O 5 THR H   2  LEU H   8 -1  N  ALA H   6   O  ILE H  18           
SHEET    5   O 5 GLY H 150  ALA H 152 -1  O  GLY H 150   N  VAL H   5           
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  ILE I 151 -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  ILE J  35   O  ALA J  95           
SHEET    3   S 5 GLN J  15  GLN J  22 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   S 5 THR J   2  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           
LINK        CU   CU1 A 154                 ND1 HIS A  46     1555   1555  2.27  
LINK        CU   CU1 A 154                 NE2 HIS A  48     1555   1555  2.03  
LINK        CU   CU1 A 154                 NE2 HIS A 120     1555   1555  1.92  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.11  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.19  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.04  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.89  
LINK        CU   CU1 B 154                 ND1 HIS B  46     1555   1555  2.25  
LINK        CU   CU1 B 154                 NE2 HIS B  48     1555   1555  2.01  
LINK        CU   CU1 B 154                 NE2 HIS B 120     1555   1555  1.90  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.21  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.52  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.01  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.88  
LINK        CU   CU1 C 154                 ND1 HIS C  46     1555   1555  2.19  
LINK        CU   CU1 C 154                 NE2 HIS C  48     1555   1555  2.08  
LINK        CU   CU1 C 154                 NE2 HIS C 120     1555   1555  1.96  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.10  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.12  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.05  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.87  
LINK        CU   CU1 D 154                 ND1 HIS D  46     1555   1555  2.19  
LINK        CU   CU1 D 154                 NE2 HIS D  48     1555   1555  2.09  
LINK        CU   CU1 D 154                 NE2 HIS D 120     1555   1555  1.97  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.06  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.14  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.05  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.85  
LINK        CU   CU1 E 154                 ND1 HIS E  46     1555   1555  2.28  
LINK        CU   CU1 E 154                 NE2 HIS E  48     1555   1555  1.98  
LINK        CU   CU1 E 154                 NE2 HIS E 120     1555   1555  1.83  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.05  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.12  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  2.18  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.93  
LINK        CU   CU1 F 154                 ND1 HIS F  46     1555   1555  2.33  
LINK        CU   CU1 F 154                 NE2 HIS F  48     1555   1555  1.97  
LINK        CU   CU1 F 154                 NE2 HIS F 120     1555   1555  1.90  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  2.09  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.04  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.15  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.94  
LINK        CU   CU1 G 154                 ND1 HIS G  46     1555   1555  2.30  
LINK        CU   CU1 G 154                 NE2 HIS G  48     1555   1555  2.08  
LINK        CU   CU1 G 154                 NE2 HIS G 120     1555   1555  1.90  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.12  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.08  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  2.11  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.99  
LINK        CU   CU1 H 154                 ND1 HIS H  46     1555   1555  2.25  
LINK        CU   CU1 H 154                 NE2 HIS H  48     1555   1555  2.02  
LINK        CU   CU1 H 154                 NE2 HIS H 120     1555   1555  1.96  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.08  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.08  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  2.07  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.86  
LINK        CU   CU1 I 154                 NE2 HIS I  48     1555   1555  2.01  
LINK        CU   CU1 I 154                 NE2 HIS I 120     1555   1555  1.91  
LINK        CU   CU1 I 154                 ND1 HIS I  46     1555   1555  2.28  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  2.14  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.12  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.06  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  1.90  
LINK        CU   CU1 J 154                 NE2 HIS J  48     1555   1555  2.02  
LINK        CU   CU1 J 154                 NE2 HIS J 120     1555   1555  1.93  
LINK        CU   CU1 J 154                 ND1 HIS J  46     1555   1555  2.26  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  2.02  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.03  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.07  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.93  
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  5 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     2 AC4  5 LYS B 136                                                     
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC5  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 BC6  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC8  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC1  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
CRYST1  166.800  202.370  143.640  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      0.005990  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006960        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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