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Database: PDB
Entry: 3G50
LinkDB: 3G50
Original site: 3G50 
HEADER    OXIDOREDUCTASE                          04-FEB-09   3G50              
TITLE     CRYSTAL STRUCTURE OF NISOD D3A MUTANT AT 1.9 A                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [NI];                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: NISOD (UNP RESIDUES 15 TO 131);                            
COMPND   5 SYNONYM: NISOD, NICKEL-CONTAINING SUPEROXIDE DISMUTASE;              
COMPND   6 EC: 1.15.1.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 GENE: 2SC7G11.16C, SCO5254, SOD1, SODN;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    NICKEL, HEXAMER, SUPEROXIDE DISMUTASE, NISOD, SOD, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, OXIDOREDUCTASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.GARMAN,A.I.GUCE,R.W.HERBST,P.A.BRYNGELSON,D.E.CABELLI,            
AUTHOR   2 K.A.HIGGINS,K.C.RYAN,M.J.MARONEY                                     
REVDAT   2   13-JUL-11 3G50    1       VERSN                                    
REVDAT   1   28-APR-09 3G50    0                                                
JRNL        AUTH   R.W.HERBST,A.GUCE,P.A.BRYNGELSON,K.A.HIGGINS,K.C.RYAN,       
JRNL        AUTH 2 D.E.CABELLI,S.C.GARMAN,M.J.MARONEY                           
JRNL        TITL   ROLE OF CONSERVED TYROSINE RESIDUES IN NISOD CATALYSIS: A    
JRNL        TITL 2 CASE OF CONVERGENT EVOLUTION                                 
JRNL        REF    BIOCHEMISTRY                  V.  48  3354 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19183068                                                     
JRNL        DOI    10.1021/BI802029T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 28277                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1519                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1990                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2753                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 291                                     
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) : 37.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.158         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.493         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2849 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3858 ; 1.564 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   347 ; 4.652 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   134 ;34.846 ;24.701       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   502 ;14.027 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.921 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   412 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2166 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1470 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1983 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   273 ; 0.189 ; 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):   118 ; 0.249 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.180 ; 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):  1743 ; 0.977 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2807 ; 1.717 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1106 ; 2.778 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1049 ; 4.568 ; 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  : 6                                          
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     7                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9398  21.0401  28.9185              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0825 T22:    .0574                                     
REMARK   3      T33:    .2727 T12:    .0492                                     
REMARK   3      T13:   -.0246 T23:   -.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3065 L22:   1.5926                                     
REMARK   3      L33:   2.5717 L12:  -2.2944                                     
REMARK   3      L13:  -2.8964 L23:   2.0068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0459 S12:   -.1587 S13:    .3548                       
REMARK   3      S21:   -.0031 S22:    .1477 S23:   -.2509                       
REMARK   3      S31:   -.0386 S32:    .1305 S33:   -.1936                       
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 :   A     8        A   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0432  24.3022  16.2586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0503 T22:    .0051                                     
REMARK   3      T33:    .0143 T12:   -.0058                                     
REMARK   3      T13:    .0110 T23:    .0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6644 L22:    .8542                                     
REMARK   3      L33:    .3175 L12:   -.5339                                     
REMARK   3      L13:   -.0506 L23:    .0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0201 S12:    .0428 S13:    .1308                       
REMARK   3      S21:   -.0765 S22:    .0088 S23:   -.0306                       
REMARK   3      S31:   -.1192 S32:    .0151 S33:   -.0289                       
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 :   B     4        B     7                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9011  -4.6629  28.5532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0648 T22:    .0590                                     
REMARK   3      T33:    .0515 T12:   -.0255                                     
REMARK   3      T13:   -.0121 T23:    .0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .7131 L22:   9.8514                                     
REMARK   3      L33:   2.3657 L12:   2.6481                                     
REMARK   3      L13:   1.2976 L23:   4.8275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0949 S12:   -.0398 S13:    .0599                       
REMARK   3      S21:    .4109 S22:   -.1876 S23:    .2132                       
REMARK   3      S31:    .2028 S32:   -.0863 S33:    .0927                       
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 :   B     8        B   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0589  -7.5989  16.3177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0224 T22:    .0147                                     
REMARK   3      T33:    .0107 T12:    .0046                                     
REMARK   3      T13:   -.0035 T23:   -.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3180 L22:    .8044                                     
REMARK   3      L33:    .9177 L12:    .7141                                     
REMARK   3      L13:   -.5392 L23:   -.3243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0403 S12:    .1058 S13:   -.0337                       
REMARK   3      S21:   -.0814 S22:    .0085 S23:    .0415                       
REMARK   3      S31:    .0856 S32:   -.0218 S33:    .0318                       
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 :   C     1        C     7                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5129   7.7102  46.6597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .3560 T22:    .1979                                     
REMARK   3      T33:    .2055 T12:    .0658                                     
REMARK   3      T13:    .0268 T23:    .0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .0017 L22:    .0007                                     
REMARK   3      L33:    .0081 L12:   -.0009                                     
REMARK   3      L13:   -.0027 L23:    .0022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0187 S12:   -.0054 S13:    .0087                       
REMARK   3      S21:    .0143 S22:    .0088 S23:    .0016                       
REMARK   3      S31:    .0533 S32:    .0124 S33:    .0100                       
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 :   C     8        C   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9710   8.5866  39.9301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0152 T22:    .0196                                     
REMARK   3      T33:    .0186 T12:   -.0045                                     
REMARK   3      T13:   -.0148 T23:    .0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .6370 L22:    .6094                                     
REMARK   3      L33:   1.3846 L12:   -.1622                                     
REMARK   3      L13:   -.4775 L23:    .3497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0071 S12:   -.0667 S13:    .0225                       
REMARK   3      S21:    .0899 S22:    .0034 S23:   -.1002                       
REMARK   3      S31:    .0346 S32:    .0967 S33:   -.0105                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3G50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051430.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-07                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29881                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.92900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH WITH ANOMALOUS               
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 550 MME, MGCL2, HEPES, PH 6.5,       
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.84750            
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       55.84750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       29.99400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.13700            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.99400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.13700            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.84750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.99400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.13700            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.84750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.99400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.13700            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.84750            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 182  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 121  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS B     1                                                      
REMARK 465     CYS B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B   117                                                      
REMARK 465     ALA C   117                                                      
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   NZ   LYS C    92     O    HOH C   260              2.03            
REMARK 500   O    HOH A   261     O    HOH A   262              2.11            
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    ARG A  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    CYS C   2       31.90   -179.57                                   
REMARK 500    ALA C   3       77.56     39.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B   8        22.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL C   8        22.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 151        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A 269        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B 126        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH B 276        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH C 249        DISTANCE =  5.51 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 201  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   1   N                                                      
REMARK 620 2 CYS A   2   N    69.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 203                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T6U   RELATED DB: PDB                                   
REMARK 900 NICKEL SUPEROXIDE DISMUTASE (NISOD) NATIVE AT 1.30 A                 
REMARK 900 RELATED ID: 3G4X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NISOD Y9F MUTANT AT 2.01 A                      
REMARK 900 RELATED ID: 3G4Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NISOD Y9F MUTANT AT 1.9 A                       
DBREF  3G50 A    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  3G50 B    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  3G50 C    1   117  UNP    P80735   SODN_STRCO      15    131             
SEQADV 3G50 ALA A    3  UNP  P80735    ASP    17 ENGINEERED                     
SEQADV 3G50 ALA B    3  UNP  P80735    ASP    17 ENGINEERED                     
SEQADV 3G50 ALA C    3  UNP  P80735    ASP    17 ENGINEERED                     
SEQRES   1 A  117  HIS CYS ALA LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 A  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 A  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 A  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 A  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 A  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 A  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 A  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 A  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 B  117  HIS CYS ALA LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 B  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 B  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 B  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 B  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 B  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 B  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 B  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 B  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 C  117  HIS CYS ALA LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 C  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 C  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 C  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 C  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 C  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 C  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 C  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 C  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
HET     NI  A 201       1                                                       
HET     NI  C 203       1                                                       
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   4   NI    2(NI 2+)                                                     
FORMUL   6  HOH   *291(H2 O)                                                    
HELIX    1   1 PRO A   11  ALA A   29  1                                  19    
HELIX    2   2 ASP A   33  TYR A   62  1                                  30    
HELIX    3   3 LYS A   64  TYR A   71  1                                   8    
HELIX    4   4 GLU A   73  GLY A   90  1                                  18    
HELIX    5   5 ASP A   93  LYS A  115  1                                  23    
HELIX    6   6 PRO B   11  ALA B   29  1                                  19    
HELIX    7   7 ASP B   33  TYR B   62  1                                  30    
HELIX    8   8 LYS B   64  TYR B   71  1                                   8    
HELIX    9   9 GLU B   73  GLY B   90  1                                  18    
HELIX   10  10 ASP B   93  LYS B  116  1                                  24    
HELIX   11  11 PRO C   11  ASN C   31  1                                  21    
HELIX   12  12 ASP C   33  TYR C   62  1                                  30    
HELIX   13  13 LYS C   64  TYR C   71  1                                   8    
HELIX   14  14 GLU C   73  GLY C   90  1                                  18    
HELIX   15  15 ASP C   93  LYS C  116  1                                  24    
LINK         N   HIS A   1                NI    NI A 201     1555   1555  2.33  
LINK         N   CYS A   2                NI    NI A 201     1555   1555  2.46  
LINK         N   HIS C   1                NI    NI C 203     1555   1555  2.14  
CISPEP   1 LEU A    4    PRO A    5          0        -0.30                     
CISPEP   2 LEU B    4    PRO B    5          0        -7.03                     
CISPEP   3 LEU C    4    PRO C    5          0         4.42                     
SITE     1 AC1  3 HIS A   1  CYS A   2  CYS A   6                               
SITE     1 AC2  3 HIS C   1  CYS C   2  CYS C   6                               
CRYST1   59.988  112.274  111.695  90.00  90.00  90.00 C 2 2 21     24          
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      0.016670  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008907  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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