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Database: PDB
Entry: 4B3E
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HEADER    OXIDOREDUCTASE                          23-JUL-12   4B3E              
TITLE     STRUCTURE OF COPPER-ZINC SUPEROXIDE DISMUTASE COMPLEXED WITH          
TITLE    2 BICARBONATE.                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1, HSOD1, CU-ZN SUPEROXIDE DISMUTASE;  
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.STRANGE,M.A.HOUGH,S.V.ANTONYUK,S.S.HASNAIN                        
REVDAT   1   26-SEP-12 4B3E    0                                                
JRNL        AUTH   R.W.STRANGE,M.A.HOUGH,S.V.ANTONYUK,S.S.HASNAIN               
JRNL        TITL   STRUCTURAL EVIDENCE FOR A COPPER-BOUND CARBONATE             
JRNL        TITL 2 INTERMEDIATE IN THE PEROXIDASE AND DISMUTASE ACTIVITIES OF   
JRNL        TITL 3 SUPEROXIDE DISMUTASE.                                        
JRNL        REF    PLOS ONE                      V.   7 44811 2012              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   22984565                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0044811                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.39                          
REMARK   3   NUMBER OF REFLECTIONS             : 118562                         
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) : 0.17670                         
REMARK   3   R VALUE            (WORKING SET) : 0.17467                         
REMARK   3   FREE R VALUE                     : 0.21496                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6298                            
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) : 2.148                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.203                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8365                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.210                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 436                          
REMARK   3   BIN FREE R VALUE                    : 0.250                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11138                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 85                                      
REMARK   3   SOLVENT ATOMS            : 1589                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.0                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.335                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09                                                 
REMARK   3    B22 (A**2) : -0.02                                                
REMARK   3    B33 (A**2) : -0.08                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.170         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.157         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.871         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11384 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7520 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15374 ; 1.334 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18494 ; 0.838 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1536 ; 6.461 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   484 ;40.829 ;25.661       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1860 ;12.586 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ; 9.432 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1695 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13142 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2058 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 122.4630  57.7300  53.0310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0997 T22:   0.1389                                     
REMARK   3      T33:   0.0898 T12:  -0.0567                                     
REMARK   3      T13:   0.0187 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6277 L22:   0.2869                                     
REMARK   3      L33:   0.7602 L12:   0.1846                                     
REMARK   3      L13:  -0.1527 L23:   0.0302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:   0.0422 S13:   0.0278                       
REMARK   3      S21:   0.0261 S22:  -0.0219 S23:   0.0317                       
REMARK   3      S31:   0.0961 S32:  -0.1182 S33:   0.0214                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 173.9530 118.2310  53.1330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3531 T22:   0.0106                                     
REMARK   3      T33:   0.0745 T12:  -0.0505                                     
REMARK   3      T13:  -0.1517 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6614 L22:   0.9860                                     
REMARK   3      L33:   1.2380 L12:  -0.1748                                     
REMARK   3      L13:   0.3824 L23:   0.0272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2899 S12:   0.0704 S13:   0.1050                       
REMARK   3      S21:  -0.0293 S22:   0.0187 S23:   0.0072                       
REMARK   3      S31:  -0.4628 S32:   0.0848 S33:   0.2712                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 201.9790  43.4510  52.9590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1011 T22:   0.1149                                     
REMARK   3      T33:   0.0958 T12:   0.0322                                     
REMARK   3      T13:  -0.0029 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7449 L22:   0.8135                                     
REMARK   3      L33:   0.3461 L12:  -0.6147                                     
REMARK   3      L13:  -0.1855 L23:  -0.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0120 S12:   0.0149 S13:  -0.0187                       
REMARK   3      S21:  -0.0048 S22:  -0.0177 S23:   0.0021                       
REMARK   3      S31:   0.0193 S32:   0.0457 S33:   0.0297                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 176.4660 149.4970  52.6620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0779 T22:   0.2169                                     
REMARK   3      T33:   0.0742 T12:  -0.1028                                     
REMARK   3      T13:  -0.0417 T23:   0.0713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7194 L22:   1.4986                                     
REMARK   3      L33:   0.6655 L12:   0.8694                                     
REMARK   3      L13:   0.6893 L23:   0.5272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1640 S12:   0.2899 S13:  -0.0157                       
REMARK   3      S21:  -0.0466 S22:   0.0682 S23:  -0.1309                       
REMARK   3      S31:  -0.1671 S32:   0.1773 S33:   0.0958                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 125.0360  87.7630  47.0270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1096 T22:   0.0539                                     
REMARK   3      T33:   0.1686 T12:   0.0039                                     
REMARK   3      T13:  -0.0294 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1824 L22:   2.9489                                     
REMARK   3      L33:   0.3181 L12:   0.1719                                     
REMARK   3      L13:   0.0418 L23:  -0.4208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0298 S12:  -0.0681 S13:   0.1003                       
REMARK   3      S21:  -0.3042 S22:  -0.0051 S23:   0.3065                       
REMARK   3      S31:   0.0748 S32:   0.0330 S33:  -0.0247                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 148.8530  66.6200  54.1970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1108 T22:   0.1088                                     
REMARK   3      T33:   0.0976 T12:  -0.0046                                     
REMARK   3      T13:   0.0035 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7404 L22:   0.2250                                     
REMARK   3      L33:   0.3784 L12:   0.1541                                     
REMARK   3      L13:  -0.0654 L23:  -0.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:   0.0028 S13:   0.0041                       
REMARK   3      S21:   0.0042 S22:   0.0043 S23:   0.0023                       
REMARK   3      S31:   0.0354 S32:  -0.0093 S33:   0.0062                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 169.5060  90.7540  54.1590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1276 T22:   0.0913                                     
REMARK   3      T33:   0.0965 T12:   0.0028                                     
REMARK   3      T13:  -0.0074 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2568 L22:   0.7697                                     
REMARK   3      L33:   0.5369 L12:   0.1688                                     
REMARK   3      L13:   0.1084 L23:  -0.0114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.0186 S13:   0.0138                       
REMARK   3      S21:   0.0169 S22:  -0.0111 S23:   0.0438                       
REMARK   3      S31:  -0.0574 S32:   0.0309 S33:   0.0388                       
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   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 180.2670  60.7770  54.2590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1052 T22:   0.1112                                     
REMARK   3      T33:   0.0982 T12:   0.0162                                     
REMARK   3      T13:   0.0065 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6377 L22:   0.7062                                     
REMARK   3      L33:   0.2472 L12:  -0.5522                                     
REMARK   3      L13:   0.0754 L23:   0.0366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0149 S12:   0.0035 S13:  -0.0085                       
REMARK   3      S21:  -0.0104 S22:  -0.0191 S23:   0.0264                       
REMARK   3      S31:  -0.0033 S32:  -0.0010 S33:   0.0341                       
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 :   J     1        J   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 130.0800 115.1230  49.3900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0987 T22:   0.0697                                     
REMARK   3      T33:   0.1351 T12:   0.0218                                     
REMARK   3      T13:  -0.0005 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4008 L22:   1.8780                                     
REMARK   3      L33:   0.2808 L12:   0.1485                                     
REMARK   3      L13:   0.0767 L23:  -0.0998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0209 S12:   0.0094 S13:  -0.0849                       
REMARK   3      S21:  -0.0457 S22:   0.0016 S23:   0.1215                       
REMARK   3      S31:  -0.0257 S32:   0.0513 S33:  -0.0225                       
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 :   I     1        I   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 150.3700 139.8300  52.2690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0845 T22:   0.1485                                     
REMARK   3      T33:   0.0812 T12:  -0.0052                                     
REMARK   3      T13:  -0.0188 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9268 L22:   0.2135                                     
REMARK   3      L33:   0.5915 L12:   0.2219                                     
REMARK   3      L13:   0.2016 L23:   0.1842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0760 S12:   0.0930 S13:   0.0166                       
REMARK   3      S21:   0.0259 S22:   0.0398 S23:  -0.0001                       
REMARK   3      S31:  -0.0717 S32:   0.0348 S33:   0.0362                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4B3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-53451.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-07                          
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               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124983                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 5.5                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SOS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULPHATE, 50 MM             
REMARK 280  TRIS PH 8.0 AND 50 MM NACL                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.19200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.19200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       82.99700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.55350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       82.99700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.55350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.19200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       82.99700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.55350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.19200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       82.99700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.55350            
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: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.1 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: 2060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.4 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: 2130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.7 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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.3 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: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.3 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     MET C     0                                                      
REMARK 465     MET D     0                                                      
REMARK 465     MET E     0                                                      
REMARK 465     MET F     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 465     MET I     0                                                      
REMARK 465     MET J     0                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS H   70   NZ                                                  
REMARK 480     LYS J   75   NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND1  HIS B    80    ZN     ZN B   155              1.63            
REMARK 500   OE1  GLN F   153     O    HOH E  2075              2.08            
REMARK 500   NE2  HIS H    63     O    HOH H  2065              2.12            
REMARK 500   NE2  HIS I    63     O    HOH I  2068              2.12            
REMARK 500  CU     CU H   154     O    HOH H  2065              1.31            
REMARK 500   S    SO4 J  1154     O    HOH J  2105              2.10            
REMARK 500   O4   SO4 J  1154     O    HOH J  2105              1.32            
REMARK 500   O4   SO4 J  1155     O    HOH I  2154              1.75            
REMARK 500   O    HOH A  2006     O    HOH A  2007              1.98            
REMARK 500   O    HOH A  2007     O    HOH F  2104              1.42            
REMARK 500   O    HOH A  2028     O    HOH A  2029              1.97            
REMARK 500   O    HOH A  2057     O    HOH A  2058              1.44            
REMARK 500   O    HOH A  2058     O    HOH A  2060              2.11            
REMARK 500   O    HOH A  2062     O    HOH A  2063              1.87            
REMARK 500   O    HOH A  2069     O    HOH A  2148              2.10            
REMARK 500   O    HOH A  2088     O    HOH A  2162              2.09            
REMARK 500   O    HOH A  2096     O    HOH A  2160              2.02            
REMARK 500   O    HOH A  2118     O    HOH A  2119              1.63            
REMARK 500   O    HOH A  2134     O    HOH A  2135              2.13            
REMARK 500   O    HOH A  2147     O    HOH A  2148              2.09            
REMARK 500   O    HOH B  2001     O    HOH B  2002              2.09            
REMARK 500   O    HOH B  2100     O    HOH B  2101              2.03            
REMARK 500   O    HOH C  2001     O    HOH C  2005              2.10            
REMARK 500   O    HOH C  2014     O    HOH C  2193              1.94            
REMARK 500   O    HOH C  2071     O    HOH C  2148              2.06            
REMARK 500   O    HOH C  2094     O    HOH C  2095              1.33            
REMARK 500   O    HOH C  2109     O    HOH C  2189              2.07            
REMARK 500   O    HOH C  2126     O    HOH C  2131              2.15            
REMARK 500   O    HOH C  2135     O    HOH C  2136              1.70            
REMARK 500   O    HOH E  2043     O    HOH E  2098              2.07            
REMARK 500   O    HOH E  2047     O    HOH E  2050              1.77            
REMARK 500   O    HOH F  2012     O    HOH F  2013              2.04            
REMARK 500   O    HOH F  2013     O    HOH A  2081              1.51            
REMARK 500   O    HOH F  2032     O    HOH F  2082              2.05            
REMARK 500   O    HOH F  2032     O    HOH F  2162              1.95            
REMARK 500   O    HOH F  2055     O    HOH F  2140              1.79            
REMARK 500   O    HOH F  2086     O    HOH F  2087              1.48            
REMARK 500   O    HOH F  2091     O    HOH F  2196              2.09            
REMARK 500   O    HOH F  2105     O    HOH F  2106              1.87            
REMARK 500   O    HOH F  2106     O    HOH F  2224              1.87            
REMARK 500   O    HOH F  2116     O    HOH F  2221              1.75            
REMARK 500   O    HOH F  2121     O    HOH F  2125              2.12            
REMARK 500   O    HOH F  2137     O    HOH F  2140              1.64            
REMARK 500   O    HOH F  2139     O    HOH F  2143              2.09            
REMARK 500   O    HOH G  2009     O    HOH G  2182              1.95            
REMARK 500   O    HOH G  2021     O    HOH H  2133              2.16            
REMARK 500   O    HOH G  2035     O    HOH G  2181              1.99            
REMARK 500   O    HOH G  2035     O    HOH G  2100              1.81            
REMARK 500   O    HOH G  2047     O    HOH G  2126              2.14            
REMARK 500   O    HOH G  2067     O    HOH G  2068              1.67            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN G    26     CD2  LEU G    67     3755     2.18            
REMARK 500   O2   SO4 J  1154     O    HOH C  2128     5455     1.90            
REMARK 500   O    HOH G  2006     O    HOH B  2023     4566     1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS H  70   CE    LYS H  70   NZ      0.158                       
REMARK 500    LYS J  75   CE    LYS J  75   NZ     -0.739                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS H  70   CD  -  CE  -  NZ  ANGL. DEV. =  40.9 DEGREES          
REMARK 500    LYS J  75   CD  -  CE  -  NZ  ANGL. DEV. =  39.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN B 131       36.83   -148.10                                   
REMARK 500    GLU B 132      -60.50     66.44                                   
REMARK 500    SER D  68       36.52     39.97                                   
REMARK 500    ASN E  65       62.63   -152.43                                   
REMARK 500    ALA F  55       51.19   -117.84                                   
REMARK 500    ASN H  65       58.78   -151.89                                   
REMARK 500    ASN I  65       59.84   -147.52                                   
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 J2121        DISTANCE =  5.59 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                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 ASP A  83   OD1  99.9                                              
REMARK 620 3 HIS A  63   ND1 106.0 109.4                                        
REMARK 620 4 HIS A  80   ND1 121.8 110.4 108.7                                  
REMARK 620 N                    1     2     3                                   
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 ASP B  83   OD1  97.6                                              
REMARK 620 3 HIS B  71   ND1 107.0 101.6                                        
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 105.3                                              
REMARK 620 3 HIS C  80   ND1 109.6 125.2                                        
REMARK 620 4 ASP C  83   OD1 103.6 100.6 110.3                                  
REMARK 620 N                    1     2     3                                   
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  80   ND1                                                    
REMARK 620 2 HIS D  63   ND1 112.7                                              
REMARK 620 3 HIS D  71   ND1 123.0 105.9                                        
REMARK 620 4 ASP D  83   OD1 111.7 106.2  95.0                                  
REMARK 620 N                    1     2     3                                   
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 106.9                                              
REMARK 620 3 HIS E  80   ND1 108.8 124.0                                        
REMARK 620 4 ASP E  83   OD1 106.9 101.1 108.0                                  
REMARK 620 N                    1     2     3                                   
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 ASP F  83   OD1 104.2                                              
REMARK 620 3 HIS F  80   ND1 107.8 111.5                                        
REMARK 620 4 HIS F  71   ND1 109.0 101.1 121.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  80   ND1                                                    
REMARK 620 2 HIS G  71   ND1 120.5                                              
REMARK 620 3 ASP G  83   OD1 111.8 100.9                                        
REMARK 620 4 HIS G  63   ND1 111.1 106.9 104.1                                  
REMARK 620 N                    1     2     3                                   
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 ASP H  83   OD1                                                    
REMARK 620 2 HIS H  80   ND1 109.4                                              
REMARK 620 3 HIS H  63   ND1 105.9 106.0                                        
REMARK 620 4 HIS H  71   ND1 101.4 123.0 109.9                                  
REMARK 620 N                    1     2     3                                   
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  71   ND1                                                    
REMARK 620 2 ASP I  83   OD1 100.7                                              
REMARK 620 3 HIS I  63   ND1 109.9 103.6                                        
REMARK 620 4 HIS I  80   ND1 123.9 111.6 105.5                                  
REMARK 620 N                    1     2     3                                   
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 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  80   ND1 115.8                                              
REMARK 620 3 HIS J  63   ND1 105.0 109.0                                        
REMARK 620 4 HIS J  71   ND1  98.8 121.1 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A 120   NE2 102.6                                              
REMARK 620 3 CO3 A 156   O1  113.9  83.7                                        
REMARK 620 4 HIS A  48   NE2 131.8 119.0  94.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HIS B  46   ND1 130.5                                              
REMARK 620 3 HIS B 120   NE2 121.8 103.8                                        
REMARK 620 4 CO3 B 156   O2   94.3 107.7  86.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  63   NE2  78.6                                              
REMARK 620 3 HIS C 120   NE2 102.9 138.2                                        
REMARK 620 4 HOH C2086   O   116.2  62.8  80.4                                  
REMARK 620 5 HIS C  48   NE2 139.6  90.6 110.5  91.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  48   NE2                                                    
REMARK 620 2 HIS D  46   ND1 128.1                                              
REMARK 620 3 HIS D 120   NE2 118.5  97.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  48   NE2                                                    
REMARK 620 2 HIS E 120   NE2 116.8                                              
REMARK 620 3 HIS E  46   ND1 132.8 102.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F 120   NE2 117.4                                              
REMARK 620 3 HIS F  46   ND1 137.7 101.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  46   ND1                                                    
REMARK 620 2 HIS G  63   NE2  79.4                                              
REMARK 620 3 HIS G 120   NE2 100.2 134.7                                        
REMARK 620 4 HIS G  48   NE2 143.3  94.3 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 145.1                                              
REMARK 620 3 HIS H 120   NE2 100.7 113.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  46   ND1                                                    
REMARK 620 2 HIS I  48   NE2 143.3                                              
REMARK 620 3 HIS I 120   NE2  98.2 117.0                                        
REMARK 620 4 HOH I2068   O    95.9  94.3  89.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  48   NE2                                                    
REMARK 620 2 HIS J 120   NE2 109.0                                              
REMARK 620 3 HIS J  46   ND1 145.7 100.3                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A 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 CO3 A 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 E 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 F 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU G 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 G 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU H 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 H 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU I 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN I 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 I 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU J 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN J 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 J 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1155                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                            
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE              
REMARK 900  DISMUTASE, NMR, 36 STRUCTURES                                       
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM                 
REMARK 900  OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE               
REMARK 900  SAMECHARGE AS THE NATIVE PROTEIN                                    
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY                
REMARK 900  GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY                  
REMARK 900   SER (K136E, C6A, C111S)                                            
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE                   
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE                  
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE                     
REMARK 900  SUPEROXIDEDISMUTASE                                                 
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC               
REMARK 900  SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION                          
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC                
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,             
REMARK 900  C111S                                                               
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT                                    
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE                       
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT                   
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A                  
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF                   
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A                  
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-                  
REMARK 900  ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A             
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE                    
REMARK 900  DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS)             
REMARK 900  MUTANT H43R                                                         
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE                       
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE:               
REMARK 900  ROLEOF METAL IONS IN PROTEIN FOLDING                                
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA              
REMARK 900   AND CYS 111 REPLACED BY SER (C6A, C111S)                           
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T MUTANT OF HUMAN SOD1                                          
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900  A4V MUTANT OF HUMAN SOD1                                            
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER                  
REMARK 900  DEPLETEDHUMAN SUPEROXIDE DISMUTASE                                  
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU               
REMARK 900  -ZN HUMAN SUPEROXIDE DISMUTASE                                      
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE               
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE             
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                 
REMARK 900   SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION                 
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                 
REMARK 900   SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION                
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                 
REMARK 900   SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION                
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.              
REMARK 900 RELATED ID: 2WYT   RELATED DB: PDB                                   
REMARK 900  1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                      
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH UMP                                 
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                            
REMARK 900 RELATED ID: 2WZ5   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.                       
REMARK 900 RELATED ID: 2WZ6   RELATED DB: PDB                                   
REMARK 900  G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.                        
REMARK 900 RELATED ID: 2XJK   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE                          
REMARK 900 RELATED ID: 2XJL   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU               
REMARK 900  LIGANDS                                                             
REMARK 900 RELATED ID: 4A7G   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -METHYLPIPERAZIN-1-YL)QUINAZOLINE IN THE P21 SPACE                  
REMARK 900  GROUP.                                                              
REMARK 900 RELATED ID: 4A7Q   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE IN THE                     
REMARK 900  P21 SPACE GROUP.                                                    
REMARK 900 RELATED ID: 4A7R   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL)                   
REMARK 900  QUINAZOLINE IN THE P21 SPACE GROUP                                  
REMARK 900 RELATED ID: 4A7S   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 5               
REMARK 900  -FLUOROURIDINE IN THE P21 SPACE GROUP                               
REMARK 900 RELATED ID: 4A7T   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH                 
REMARK 900  ISOPROTERANOL IN THE P21 SPACE GROUP                                
REMARK 900 RELATED ID: 4A7U   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 COMPLEXED WITH ADRENALINE             
REMARK 900   IN THE P21 SPACE GROUP.                                            
REMARK 900 RELATED ID: 4A7V   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH                 
REMARK 900  DOPAMINE IN THE P21 SPACE GROUP                                     
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED               
REMARK 900   BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S)                     
REMARK 900  WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO                 
REMARK 900  THE C-TERMINUS (THEORETICAL MODEL)                                  
DBREF  4B3E A    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E B    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E C    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E D    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E E    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E F    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E G    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E H    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E I    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  4B3E J    0   153  UNP    P00441   SODC_HUMAN       1    154             
SEQRES   1 A  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 E  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 E  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 E  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 E  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 E  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 E  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 E  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 E  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 E  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 E  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 E  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 E  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 G  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 G  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 G  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 G  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 G  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 G  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 G  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 G  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 G  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 G  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 G  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 G  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 H  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 H  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 H  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 H  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 H  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 H  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 H  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 H  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 H  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 H  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 H  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 H  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 I  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 I  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 I  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 I  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 I  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 I  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 I  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 I  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 I  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 I  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 I  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 I  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 J  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 J  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 J  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 J  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 J  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 J  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 J  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 J  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 J  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 J  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 J  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 J  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET    CO3  A 156       4                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET    CO3  B 156       4                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET    CO3  C 156       4                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET    CO3  D 156       4                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET    CO3  E 156       4                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET    CO3  F 156       4                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET    CO3  G 156       4                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET    CO3  H 156       4                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET    CO3  I 156       4                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET    CO3  J 156       4                                                       
HET    SO4  F1154       5                                                       
HET    SO4  G1154       5                                                       
HET    SO4  J1154       5                                                       
HET    SO4  J1155       5                                                       
HET    SO4  F1155       5                                                       
HETNAM     CO3 CARBONATE ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM      CU COPPER (II) ION                                                  
FORMUL  11  CO3    10(C O3 2-)                                                  
FORMUL  12  SO4    5(O4 S 2-)                                                   
FORMUL  13   ZN    10(ZN 2+)                                                    
FORMUL  14   CU    10(CU 2+)                                                    
FORMUL  15  HOH   *1589(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 GLU B  132  THR B  137  1                                   6    
HELIX    5   5 ALA C   55  GLY C   61  5                                   7    
HELIX    6   6 ALA D   55  GLY D   61  5                                   7    
HELIX    7   7 ASN D  131  GLY D  138  1                                   8    
HELIX    8   8 ALA E   55  GLY E   61  5                                   7    
HELIX    9   9 GLU E  133  GLY E  138  1                                   6    
HELIX   10  10 ALA F   55  GLY F   61  5                                   7    
HELIX   11  11 ALA G   55  GLY G   61  5                                   7    
HELIX   12  12 SER G  107  HIS G  110  5                                   4    
HELIX   13  13 GLU G  133  GLY G  138  1                                   6    
HELIX   14  14 ALA H   55  GLY H   61  5                                   7    
HELIX   15  15 GLU H  133  GLY H  138  1                                   6    
HELIX   16  16 ALA I   55  GLY I   61  5                                   7    
HELIX   17  17 ALA J   55  GLY J   61  5                                   7    
HELIX   18  18 GLU J  133  GLY J  138  1                                   6    
SHEET    1  AA 5 ALA A  95  ASP A 101  0                                        
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101           
SHEET    3  AA 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 THR A   2  LEU A   8 -1  O  THR A   2   N  GLN A  22           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 4 ASP A  83  ALA A  89  0                                        
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  BA 5 ALA B  95  ASP B 101  0                                        
SHEET    2  BA 5 VAL B  29  LYS B  36 -1  O  VAL B  29   N  ASP B 101           
SHEET    3  BA 5 GLN B  15  GLN B  22 -1  O  GLN B  15   N  LYS B  36           
SHEET    4  BA 5 THR B   2  LEU B   8 -1  O  THR B   2   N  GLN B  22           
SHEET    5  BA 5 GLY B 150  ALA B 152 -1  O  GLY B 150   N  VAL B   5           
SHEET    1  BB 4 ASP B  83  ALA B  89  0                                        
SHEET    2  BB 4 GLY B  41  HIS B  48 -1  O  GLY B  41   N  ALA B  89           
SHEET    3  BB 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4  BB 4 ARG B 143  VAL B 148 -1  N  LEU B 144   O  VAL B 119           
SHEET    1  CA 5 ALA C  95  ASP C 101  0                                        
SHEET    2  CA 5 VAL C  29  LYS C  36 -1  O  VAL C  29   N  ASP C 101           
SHEET    3  CA 5 GLN C  15  GLN C  22 -1  O  GLN C  15   N  LYS C  36           
SHEET    4  CA 5 THR C   2  LEU C   8 -1  O  THR C   2   N  GLN C  22           
SHEET    5  CA 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1  CB 4 ASP C  83  ALA C  89  0                                        
SHEET    2  CB 4 GLY C  41  HIS C  48 -1  O  GLY C  41   N  ALA C  89           
SHEET    3  CB 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4  CB 4 ARG C 143  VAL C 148 -1  N  LEU C 144   O  VAL C 119           
SHEET    1  DA 5 ALA D  95  ASP D 101  0                                        
SHEET    2  DA 5 VAL D  29  LYS D  36 -1  O  VAL D  29   N  ASP D 101           
SHEET    3  DA 5 GLN D  15  GLU D  21 -1  O  GLN D  15   N  LYS D  36           
SHEET    4  DA 5 LYS D   3  LEU D   8 -1  O  ALA D   4   N  PHE D  20           
SHEET    5  DA 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1  DB 4 ASP D  83  ALA D  89  0                                        
SHEET    2  DB 4 GLY D  41  HIS D  48 -1  O  GLY D  41   N  ALA D  89           
SHEET    3  DB 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4  DB 4 ARG D 143  VAL D 148 -1  N  LEU D 144   O  VAL D 119           
SHEET    1  EA 5 ALA E  95  ASP E 101  0                                        
SHEET    2  EA 5 VAL E  29  LYS E  36 -1  O  VAL E  29   N  ASP E 101           
SHEET    3  EA 5 GLN E  15  GLU E  21 -1  O  GLN E  15   N  LYS E  36           
SHEET    4  EA 5 LYS E   3  LYS E   9 -1  O  ALA E   4   N  PHE E  20           
SHEET    5  EA 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1  EB 4 ASP E  83  ALA E  89  0                                        
SHEET    2  EB 4 GLY E  41  HIS E  48 -1  O  GLY E  41   N  ALA E  89           
SHEET    3  EB 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4  EB 4 ARG E 143  VAL E 148 -1  N  LEU E 144   O  VAL E 119           
SHEET    1  FA 5 ALA F  95  ASP F 101  0                                        
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101           
SHEET    3  FA 5 GLN F  15  GLU F  21 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 LYS F   3  LYS F   9 -1  O  ALA F   4   N  PHE F  20           
SHEET    5  FA 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FB 4 ASP F  83  ALA F  89  0                                        
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SHEET    1  GA 5 ALA G  95  ASP G 101  0                                        
SHEET    2  GA 5 VAL G  29  LYS G  36 -1  O  VAL G  29   N  ASP G 101           
SHEET    3  GA 5 GLN G  15  GLU G  21 -1  O  GLN G  15   N  LYS G  36           
SHEET    4  GA 5 LYS G   3  LYS G   9 -1  O  ALA G   4   N  PHE G  20           
SHEET    5  GA 5 GLY G 150  ILE G 151 -1  O  GLY G 150   N  VAL G   5           
SHEET    1  GB 4 ASP G  83  ALA G  89  0                                        
SHEET    2  GB 4 GLY G  41  HIS G  48 -1  O  GLY G  41   N  ALA G  89           
SHEET    3  GB 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4  GB 4 ARG G 143  VAL G 148 -1  N  LEU G 144   O  VAL G 119           
SHEET    1  HA 5 ALA H  95  ASP H 101  0                                        
SHEET    2  HA 5 VAL H  29  LYS H  36 -1  O  VAL H  29   N  ASP H 101           
SHEET    3  HA 5 GLN H  15  GLU H  21 -1  O  GLN H  15   N  LYS H  36           
SHEET    4  HA 5 LYS H   3  LEU H   8 -1  O  ALA H   4   N  PHE H  20           
SHEET    5  HA 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1  HB 4 ASP H  83  ALA H  89  0                                        
SHEET    2  HB 4 GLY H  41  HIS H  48 -1  O  GLY H  41   N  ALA H  89           
SHEET    3  HB 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4  HB 4 ARG H 143  VAL H 148 -1  N  LEU H 144   O  VAL H 119           
SHEET    1  IA 5 ALA I  95  ASP I 101  0                                        
SHEET    2  IA 5 VAL I  29  LYS I  36 -1  O  VAL I  29   N  ASP I 101           
SHEET    3  IA 5 GLN I  15  GLU I  21 -1  O  GLN I  15   N  LYS I  36           
SHEET    4  IA 5 LYS I   3  LEU I   8 -1  O  ALA I   4   N  PHE I  20           
SHEET    5  IA 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1  IB 4 ASP I  83  ALA I  89  0                                        
SHEET    2  IB 4 GLY I  41  HIS I  48 -1  O  GLY I  41   N  ALA I  89           
SHEET    3  IB 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4  IB 4 ARG I 143  VAL I 148 -1  N  LEU I 144   O  VAL I 119           
SHEET    1  JA 5 ALA J  95  ASP J 101  0                                        
SHEET    2  JA 5 VAL J  29  LYS J  36 -1  O  VAL J  29   N  ASP J 101           
SHEET    3  JA 5 GLN J  15  GLU J  21 -1  O  GLN J  15   N  LYS J  36           
SHEET    4  JA 5 LYS J   3  LYS J   9 -1  O  ALA J   4   N  PHE J  20           
SHEET    5  JA 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1  JB 4 ASP J  83  ALA J  89  0                                        
SHEET    2  JB 4 GLY J  41  HIS J  48 -1  O  GLY J  41   N  ALA J  89           
SHEET    3  JB 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4  JB 4 ARG J 143  VAL J 148 -1  N  LEU J 144   O  VAL J 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.11  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.12  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.11  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.13  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.09  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.11  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.11  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.13  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.11  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.11  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.14  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.09  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.11  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.91  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  1.94  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.01  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.06  
LINK         O1  CO3 A 156                CU    CU A 154     1555   1555  2.28  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.06  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.00  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  2.09  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.85  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.13  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.06  
LINK         O2  CO3 B 156                CU    CU B 154     1555   1555  2.13  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  2.14  
LINK        CU    CU C 154                 NE2 HIS C  63     1555   1555  2.66  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  2.10  
LINK        CU    CU C 154                 O   HOH C2086     1555   1555  2.62  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  2.17  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.05  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.93  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.06  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.02  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  2.07  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  1.97  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.13  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.93  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.16  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.06  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.05  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.22  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  2.04  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.20  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  2.09  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.11  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.94  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.05  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  2.07  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.09  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.15  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.91  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  1.89  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.07  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.03  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.12  
LINK        CU    CU G 154                 NE2 HIS G  63     1555   1555  2.61  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  2.08  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  2.12  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.01  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.91  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.08  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  2.03  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  2.14  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  2.06  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  2.15  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.10  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  1.93  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  2.10  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.90  
LINK        CU    CU I 154                 O   HOH I2068     1555   1555  1.72  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  2.04  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  2.03  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  2.08  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.02  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  1.92  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  1.91  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.01  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  2.12  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.12  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.22  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.12  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  1.96  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.04  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.92  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 CO3 A 156                                                     
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  7 HIS A  48  HIS A  63  HIS A 120  THR A 137                    
SITE     2 AC3  7 ARG A 143   CU A 154  HOH A2166                               
SITE     1 AC4  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC4  5 CO3 B 156                                                     
SITE     1 AC5  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC6  9 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC6  9 THR B 137  ARG B 143   CU B 154  HOH B2120                    
SITE     3 AC6  9 HOH B2121                                                     
SITE     1 AC7  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC7  5 HOH C2086                                                     
SITE     1 AC8  5 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     2 AC8  5 LYS C 136                                                     
SITE     1 AC9  4 ARG C 143  HOH C2086  HOH C2187  HOH C2190                    
SITE     1 BC1  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 BC1  5 CO3 D 156                                                     
SITE     1 BC2  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 BC3  8 HIS D  48  HIS D  63  HIS D 120  THR D 137                    
SITE     2 BC3  8 ARG D 143   CU D 154  HOH D2069  HOH D2119                    
SITE     1 BC4  5 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     2 BC4  5 CO3 E 156                                                     
SITE     1 BC5  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC6  7 HIS E  48  HIS E  63  HIS E 120  THR E 137                    
SITE     2 BC6  7 ARG E 143   CU E 154  HOH E2108                               
SITE     1 BC7  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC7  5 HOH F2122                                                     
SITE     1 BC8  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC9  6 HIS F 120  GLY F 141  ARG F 143  HOH F2122                    
SITE     2 BC9  6 HOH F2218  HOH F2227                                          
SITE     1 CC1  5 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     2 CC1  5 HOH G2076                                                     
SITE     1 CC2  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 CC3  6 HIS G 120  GLY G 141  ARG G 143  HOH G2174                    
SITE     2 CC3  6 HOH G2180  HOH G2181                                          
SITE     1 CC4  5 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     2 CC4  5 HOH H2065                                                     
SITE     1 CC5  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 CC6  4 ARG H 143  HOH H2068  HOH H2130  HOH H2150                    
SITE     1 CC7  5 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     2 CC7  5 HOH I2068                                                     
SITE     1 CC8  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC9  4 ARG I 143  HOH I2092  HOH I2141  HOH I2161                    
SITE     1 DC1  5 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     2 DC1  5 HOH J2041                                                     
SITE     1 DC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 DC3  5 GLY J 141  ARG J 143  HOH J2041  HOH J2060                    
SITE     2 DC3  5 HOH J2115                                                     
SITE     1 DC4  7 LYS F  75  HOH F2205  HOH F2229  HOH F2231                    
SITE     2 DC4  7 HOH F2232  LYS G 128  LYS H 128                               
SITE     1 DC5  5 LYS G 122  ALA G 123  HOH G2072  HOH G2162                    
SITE     2 DC5  5 HOH G2186                                                     
SITE     1 DC6  7 LYS C 128  HOH C2128  LYS I 128  LYS J 128                    
SITE     2 DC6  7 SO4 J1155  HOH J2105  HOH J2106                               
SITE     1 DC7  8 LYS C 128  LYS I 128  HOH I2154  LEU J 126                    
SITE     2 DC7  8 LYS J 128  SO4 J1154  HOH J2099  HOH J2120                    
SITE     1 DC8  5 LYS F 128  HOH F2233  HOH F2234  LYS G 128                    
SITE     2 DC8  5 LYS H 128                                                     
CRYST1  165.994  203.107  144.384  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      0.006024  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004924  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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