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Entry: 2GBU
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HEADER    OXIDOREDUCTASE                          11-MAR-06   2GBU              
TITLE     C6A/C111A/C57A/C146A APO CUZN SUPEROXIDE DISMUTASE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CU/ZN SUPEROXIDE DISMUTASE;                                 
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACA                                      
KEYWDS    OXIDOREDUCTASE, HUMAN CU/ZN SUPEROXIDE DISMUTASE, CYSTEIN-FREE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG                         
REVDAT   3   13-JUL-11 2GBU    1       VERSN                                    
REVDAT   2   24-FEB-09 2GBU    1       VERSN                                    
REVDAT   1   02-JAN-07 2GBU    0                                                
JRNL        AUTH   A.HORNBERG,D.T.LOGAN,S.L.MARKLUND,M.OLIVEBERG                
JRNL        TITL   THE COUPLING BETWEEN DISULPHIDE STATUS, METALLATION AND      
JRNL        TITL 2 DIMER INTERFACE STRENGTH IN CU/ZN SUPEROXIDE DISMUTASE       
JRNL        REF    J.MOL.BIOL.                   V. 365   333 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17070542                                                     
JRNL        DOI    10.1016/J.JMB.2006.09.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 38832                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1953                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2649                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4002                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 259                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.87000                                             
REMARK   3    B22 (A**2) : 6.28000                                              
REMARK   3    B33 (A**2) : -3.76000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.79000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.205         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.178         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.747        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4066 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3645 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5496 ; 1.061 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8510 ; 0.660 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   545 ; 6.050 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   171 ;38.654 ;25.556       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   643 ;11.962 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;11.012 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   620 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4678 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   739 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   621 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3563 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1946 ; 0.159 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2408 ; 0.079 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   235 ; 0.125 ; 0.200       
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):    11 ; 0.063 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    34 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.113 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3549 ; 0.499 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1182 ; 0.068 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4271 ; 0.585 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1668 ; 0.961 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1225 ; 1.345 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9308  -2.9374  20.9595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0960 T22:  -0.1532                                     
REMARK   3      T33:  -0.0897 T12:  -0.0608                                     
REMARK   3      T13:   0.0136 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8461 L22:   1.4835                                     
REMARK   3      L33:   4.8554 L12:   0.3183                                     
REMARK   3      L13:   1.2102 L23:  -0.2165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0357 S12:   0.0680 S13:  -0.1595                       
REMARK   3      S21:  -0.0364 S22:  -0.0626 S23:  -0.0535                       
REMARK   3      S31:   0.1502 S32:  -0.2909 S33:   0.0268                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8552   3.2768  46.0547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1228 T22:  -0.1002                                     
REMARK   3      T33:  -0.0978 T12:  -0.0203                                     
REMARK   3      T13:  -0.0036 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0144 L22:   0.8733                                     
REMARK   3      L33:   3.8579 L12:  -0.0563                                     
REMARK   3      L13:  -0.2020 L23:  -0.0266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0533 S12:  -0.2574 S13:  -0.0581                       
REMARK   3      S21:   0.0639 S22:   0.0062 S23:   0.0227                       
REMARK   3      S31:   0.0877 S32:  -0.0706 S33:  -0.0595                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3538  11.3719  30.2515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1128 T22:  -0.1633                                     
REMARK   3      T33:  -0.0889 T12:  -0.0319                                     
REMARK   3      T13:   0.0047 T23:  -0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2341 L22:   1.2707                                     
REMARK   3      L33:   4.6151 L12:   0.5718                                     
REMARK   3      L13:  -0.5285 L23:   0.3502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0748 S12:  -0.3906 S13:   0.2998                       
REMARK   3      S21:  -0.0761 S22:   0.0483 S23:  -0.0432                       
REMARK   3      S31:  -0.2085 S32:   0.2498 S33:  -0.1232                       
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     2        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0829   5.0498   8.3130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0701 T22:  -0.2004                                     
REMARK   3      T33:  -0.0737 T12:  -0.0304                                     
REMARK   3      T13:  -0.0074 T23:   0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3333 L22:   2.1571                                     
REMARK   3      L33:   7.0345 L12:  -0.5038                                     
REMARK   3      L13:  -0.0658 L23:   0.5773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0315 S12:   0.4811 S13:  -0.1582                       
REMARK   3      S21:  -0.0645 S22:  -0.0340 S23:   0.0916                       
REMARK   3      S31:   0.0302 S32:  -0.1055 S33:   0.0025                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2GBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036931.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.092                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38835                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1HL4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4000, 0.1M NA CACODYLATE, 50MM    
REMARK 280  NAAC, 1MM EDTA, 1MM NAN3, PH 6.5, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.30700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.21350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.30700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.21350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER C    68                                                      
REMARK 465     ARG C    69                                                      
REMARK 465     LYS C    70                                                      
REMARK 465     HIS C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     PRO C    74                                                      
REMARK 465     LYS C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     GLU C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     ARG C    79                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     LEU C   126                                                      
REMARK 465     GLY C   127                                                      
REMARK 465     LYS C   128                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     ASN C   131                                                      
REMARK 465     GLU C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     SER C   134                                                      
REMARK 465     THR C   135                                                      
REMARK 465     LYS C   136                                                      
REMARK 465     THR C   137                                                      
REMARK 465     GLY C   138                                                      
REMARK 465     ASN C   139                                                      
REMARK 465     ALA C   140                                                      
REMARK 465     GLY C   141                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     LEU D    67                                                      
REMARK 465     SER D    68                                                      
REMARK 465     ARG D    69                                                      
REMARK 465     LYS D    70                                                      
REMARK 465     HIS D    71                                                      
REMARK 465     GLY D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     LYS D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     GLU D    78                                                      
REMARK 465     ASP D   125                                                      
REMARK 465     LEU D   126                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     LYS D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     GLY D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     GLU D   132                                                      
REMARK 465     GLU D   133                                                      
REMARK 465     SER D   134                                                      
REMARK 465     THR D   135                                                      
REMARK 465     LYS D   136                                                      
REMARK 465     THR D   137                                                      
REMARK 465     GLY D   138                                                      
REMARK 465     ASN D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     GLY D   141                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  11       38.76    -86.55                                   
REMARK 500    SER A  98       86.87   -152.12                                   
REMARK 500    SER B  98       87.53   -151.12                                   
REMARK 500    ASN C  65       77.56   -155.11                                   
REMARK 500    PRO C  66     -166.35    -70.53                                   
REMARK 500    ASN D  65       67.85   -151.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900 APO CUZN SUPEROXIDE DISMUTASE                                        
REMARK 900 RELATED ID: 2GBT   RELATED DB: PDB                                   
REMARK 900 C6A/C111A APO CUZN SUPEROXIDE DISMUTASE                              
REMARK 900 RELATED ID: 2GBV   RELATED DB: PDB                                   
REMARK 900 C6A/C111A/C57A/C146A HOLO CUZN SUPEROXIDE DISMUTASE                  
DBREF  2GBU A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBU B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBU C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  2GBU D    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 2GBU ALA A    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBU ALA A   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBU ALA A  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBU ALA A  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBU ALA B    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBU ALA B   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBU ALA B  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBU ALA B  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBU ALA C    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBU ALA C   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBU ALA C  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBU ALA C  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQADV 2GBU ALA D    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 2GBU ALA D   57  UNP  P00441    CYS    57 ENGINEERED                     
SEQADV 2GBU ALA D  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 2GBU ALA D  146  UNP  P00441    CYS   146 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY ALA THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA ALA GLY VAL ILE GLY ILE ALA GLN                      
FORMUL   5  HOH   *259(H2 O)                                                    
HELIX    1   1 GLU A  133  GLY A  138  1                                   6    
HELIX    2   2 GLU B  133  GLY B  138  1                                   6    
HELIX    3   3 ALA C   55  GLY C   61  5                                   7    
HELIX    4   4 ALA D   55  GLY D   61  5                                   7    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LEU B   8 -1  N  ALA B   4   O  PHE B  20           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  PHE B  45   O  GLY B  85           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  LEU B 144   N  VAL B 119           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 THR C   2  LEU C   8 -1  N  THR C   2   O  GLN C  22           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  ALA D   6   O  ILE D  18           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
CRYST1  156.614   34.427  114.461  90.00 112.17  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006380  0.000000  0.002600        0.00000                         
SCALE2      0.000000  0.029050  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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