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Database: PDB
Entry: 1EN6
LinkDB: 1EN6
Original site: 1EN6 
HEADER    OXIDOREDUCTASE                          20-MAR-00   1EN6              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE E. COLI MANGANESE                   
TITLE    2 SUPEROXIDE DISMUTASE Q146L MUTANT                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PDT1-5                                    
KEYWDS    PROTON SHUTTLE, Q146L, MUTANT, MANGANESE SUPEROXIDE                   
KEYWDS   2 DISMUTASE, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.EDWARDS,M.M.WHITTAKER,E.N.BAKER,J.W.WHITTAKER,                    
AUTHOR   2 G.B.JAMESON                                                          
REVDAT   2   24-FEB-09 1EN6    1       VERSN                                    
REVDAT   1   27-JUN-01 1EN6    0                                                
JRNL        AUTH   R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,           
JRNL        AUTH 2 G.B.JAMESON                                                  
JRNL        TITL   OUTER SPHERE MUTATIONS PERTURB METAL REACTIVITY IN           
JRNL        TITL 2 MANGANESE SUPEROXIDE DISMUTASE.                              
JRNL        REF    BIOCHEMISTRY                  V.  40    15 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11141052                                                     
JRNL        DOI    10.1021/BI0018943                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,           
REMARK   1  AUTH 2 G.B.JAMESON                                                  
REMARK   1  TITL   REMOVING A HYDROGEN BOND IN THE DIMER INTERFACE OF           
REMARK   1  TITL 2 ESCHERICHIA COLI MANGANESE SUPEROXIDE DISMUTASE              
REMARK   1  TITL 3 ALTERS STRUCTURE AND REACTIVITY.                             
REMARK   1  REF    BIOCHEMISTRY                  V.  40  4622 2001              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI002403H                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.A.EDWARDS,H.M.BAKER,M.M.WHITTAKER,J.W.WHITTAKER,           
REMARK   1  AUTH 2 G.B.JAMESON,E.N.BAKER                                        
REMARK   1  TITL   CRYSTAL STRUCTURE OF ESCHERICHIA COLI MANGANESE              
REMARK   1  TITL 2 SUPEROXIDE DISMUTASE AT 2.1 A RESOLUTION                     
REMARK   1  REF    J.BIOL.INORG.CHEM.            V.   3   161 1998              
REMARK   1  REFN                   ISSN 0949-8257                               
REMARK   1  DOI    10.1007/S007750050217                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66366                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3261                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6632                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 340                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.60500                                             
REMARK   3    B22 (A**2) : -1.92800                                             
REMARK   3    B33 (A**2) : 6.53400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.22                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.333 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.085 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.075 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.154 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010742.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200B                      
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66399                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.4000                            
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) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG 6000, 0.05 M BICINE, PH      
REMARK 280  8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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       90.86100            
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       90.86100            
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       50.84900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.64850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.84900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.64850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.86100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.84900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.64850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.86100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.84900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.64850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 A 585  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  89      136.06   -176.29                                   
REMARK 500    ASP A 136       -3.05     71.25                                   
REMARK 500    ASN A 145     -121.52     42.30                                   
REMARK 500    TYR A 173       -5.01   -142.21                                   
REMARK 500    GLN A 178     -128.09     48.89                                   
REMARK 500    LYS A 204      -12.28     73.20                                   
REMARK 500    LYS B  29      -64.07   -109.39                                   
REMARK 500    LEU B  45       66.69   -119.27                                   
REMARK 500    LYS B  89      136.28   -178.96                                   
REMARK 500    ASN B 145     -118.85     45.31                                   
REMARK 500    TYR B 173       -2.53   -143.90                                   
REMARK 500    GLN B 178     -129.07     47.37                                   
REMARK 500    LYS C  89      138.15   -178.80                                   
REMARK 500    GLN C  95     -169.44   -165.61                                   
REMARK 500    ASN C 145     -119.43     43.55                                   
REMARK 500    GLN C 178     -127.47     50.40                                   
REMARK 500    LYS D  29      -64.33   -109.90                                   
REMARK 500    LYS D  89      136.07    172.44                                   
REMARK 500    GLN D  95     -169.85   -177.81                                   
REMARK 500    ASN D 145     -119.99     42.33                                   
REMARK 500    TYR D 173       -3.68   -145.86                                   
REMARK 500    GLN D 178     -129.53     51.52                                   
REMARK 500    LYS D 204       -2.33     63.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MN A 501  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 600   O                                                      
REMARK 620 2 HIS A  26   NE2 172.0                                              
REMARK 620 3 HIS A 171   NE2  90.6  93.0                                        
REMARK 620 4 HIS A  81   NE2  88.1  94.6 133.2                                  
REMARK 620 5 ASP A 167   OD2  83.3  88.7 115.2 111.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 502  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 591   O                                                      
REMARK 620 2 HIS B  26   NE2 173.1                                              
REMARK 620 3 HIS B 171   NE2  92.6  92.4                                        
REMARK 620 4 HIS B  81   NE2  90.5  89.8 131.3                                  
REMARK 620 5 ASP B 167   OD2  84.5  89.0 117.0 111.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 503  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 586   O                                                      
REMARK 620 2 ASP C 167   OD2  86.1                                              
REMARK 620 3 HIS C 171   NE2  94.8 113.9                                        
REMARK 620 4 HIS C  81   NE2  89.9 108.8 137.2                                  
REMARK 620 5 HIS C  26   NE2 173.6  87.7  88.8  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 504  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 577   O                                                      
REMARK 620 2 HIS D 171   NE2  94.0                                              
REMARK 620 3 ASP D 167   OD2  83.5 114.0                                        
REMARK 620 4 HIS D  26   NE2 170.6  89.8  87.1                                  
REMARK 620 5 HIS D  81   NE2  90.7 133.2 112.8  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 501                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 502                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 503                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VEW   RELATED DB: PDB                                   
REMARK 900 NATIVE CRYSTAL STRUCTURE                                             
REMARK 900 RELATED ID: 1MMM   RELATED DB: PDB                                   
REMARK 900 IRON-SUBSTITUTED NATIVE CRYSTAL STRUCTURE                            
REMARK 900 RELATED ID: 1EN4   RELATED DB: PDB                                   
REMARK 900 E. COLI MANGANESE SUPEROXIDE DISMUTASE Q146H MUTANT CRYSTAL          
REMARK 900 STRUCTURE                                                            
REMARK 900 RELATED ID: 1EN5   RELATED DB: PDB                                   
REMARK 900 E. COLI MANGANESE SUPEROXIDE DISMUTASE Y34F MUTANT CRYSTAL           
REMARK 900 STRUCTURE                                                            
DBREF  1EN6 A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1EN6 B    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1EN6 C    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1EN6 D    1   205  UNP    P00448   SODM_ECOLI       1    205             
SEQADV 1EN6 LEU A  146  UNP  P00448    GLN   146 ENGINEERED                     
SEQADV 1EN6 LEU B  146  UNP  P00448    GLN   146 ENGINEERED                     
SEQADV 1EN6 LEU C  146  UNP  P00448    GLN   146 ENGINEERED                     
SEQADV 1EN6 LEU D  146  UNP  P00448    GLN   146 ENGINEERED                     
SEQRES   1 A  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 A  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 A  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 A  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 A  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 A  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 A  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 A  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 A  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 A  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 A  205  ALA ASN LEU ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 A  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 A  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 A  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 A  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 B  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 B  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 B  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 B  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 B  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 B  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 B  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 B  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 B  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 B  205  ALA ASN LEU ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 B  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 B  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 B  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 B  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 C  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 C  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 C  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 C  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 C  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 C  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 C  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 C  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 C  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 C  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 C  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 C  205  ALA ASN LEU ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 C  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 C  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 C  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 C  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 D  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 D  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 D  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 D  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 D  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 D  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 D  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 D  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 D  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 D  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 D  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 D  205  ALA ASN LEU ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 D  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 D  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 D  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 D  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
HET     MN  A 501       1                                                       
HET     MN  B 502       1                                                       
HET     MN  C 503       1                                                       
HET     MN  D 504       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *344(H2 O)                                                    
HELIX    1   1 ASP A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLU A   43  1                                  15    
HELIX    3   3 LEU A   45  ASN A   50  1                                   6    
HELIX    4   4 PRO A   52  ILE A   57  1                                   6    
HELIX    5   5 THR A   58  LEU A   63  5                                   6    
HELIX    6   6 LYS A   67  GLY A   87  1                                  21    
HELIX    7   7 GLN A   95  GLY A  107  1                                  13    
HELIX    8   8 SER A  108  ARG A  123  1                                  16    
HELIX    9   9 SER A  148  MET A  151  5                                   4    
HELIX   10  10 GLY A  152  GLY A  157  1                                   6    
HELIX   11  11 TRP A  169  ALA A  172  5                                   4    
HELIX   12  12 TYR A  173  GLN A  178  1                                   6    
HELIX   13  13 ARG A  180  TRP A  189  1                                  10    
HELIX   14  14 ASN A  193  LYS A  204  1                                  12    
HELIX   15  15 ASP B   19  LYS B   29  1                                  11    
HELIX   16  16 LYS B   29  GLU B   43  1                                  15    
HELIX   17  17 LEU B   45  ASN B   50  1                                   6    
HELIX   18  18 PRO B   52  ILE B   57  1                                   6    
HELIX   19  19 THR B   58  LEU B   63  5                                   6    
HELIX   20  20 LYS B   67  GLY B   87  1                                  21    
HELIX   21  21 GLN B   95  GLY B  107  1                                  13    
HELIX   22  22 SER B  108  ARG B  123  1                                  16    
HELIX   23  23 SER B  148  MET B  151  5                                   4    
HELIX   24  24 GLY B  152  GLY B  157  1                                   6    
HELIX   25  25 TRP B  169  ALA B  172  5                                   4    
HELIX   26  26 TYR B  173  GLN B  178  1                                   6    
HELIX   27  27 ARG B  180  VAL B  192  1                                  13    
HELIX   28  28 ASN B  193  LYS B  204  1                                  12    
HELIX   29  29 ASP C   19  LYS C   29  1                                  11    
HELIX   30  30 LYS C   29  GLU C   43  1                                  15    
HELIX   31  31 LEU C   45  ASN C   50  1                                   6    
HELIX   32  32 PRO C   52  ILE C   57  1                                   6    
HELIX   33  33 THR C   58  LEU C   63  5                                   6    
HELIX   34  34 PRO C   64  GLY C   87  1                                  24    
HELIX   35  35 GLN C   95  GLY C  107  1                                  13    
HELIX   36  36 SER C  108  ARG C  123  1                                  16    
HELIX   37  37 SER C  148  MET C  151  5                                   4    
HELIX   38  38 GLY C  152  GLY C  157  1                                   6    
HELIX   39  39 TRP C  169  ALA C  172  5                                   4    
HELIX   40  40 TYR C  173  GLN C  178  1                                   6    
HELIX   41  41 ARG C  180  VAL C  192  1                                  13    
HELIX   42  42 ASN C  193  LYS C  204  1                                  12    
HELIX   43  43 ASP D   19  LYS D   29  1                                  11    
HELIX   44  44 LYS D   29  GLU D   43  1                                  15    
HELIX   45  45 GLU D   47  LEU D   51  5                                   5    
HELIX   46  46 PRO D   52  ILE D   57  1                                   6    
HELIX   47  47 THR D   58  LEU D   63  5                                   6    
HELIX   48  48 PRO D   64  GLY D   87  1                                  24    
HELIX   49  49 GLN D   95  GLY D  107  1                                  13    
HELIX   50  50 SER D  108  ARG D  123  1                                  16    
HELIX   51  51 SER D  148  MET D  151  5                                   4    
HELIX   52  52 GLY D  152  GLY D  157  1                                   6    
HELIX   53  53 TRP D  169  ALA D  172  5                                   4    
HELIX   54  54 TYR D  173  GLN D  178  1                                   6    
HELIX   55  55 ARG D  180  VAL D  192  1                                  13    
HELIX   56  56 ASN D  193  LYS D  204  1                                  12    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  O  TRP A 128   N  THR A 143           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  N  PHE A 161   O  LEU A 133           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  O  TRP B 128   N  THR B 143           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  N  PHE B 161   O  LEU B 133           
SHEET    1   C 3 LYS C 137  ALA C 144  0                                        
SHEET    2   C 3 GLY C 127  LYS C 134 -1  O  TRP C 128   N  THR C 143           
SHEET    3   C 3 PHE C 161  ASP C 167 -1  N  PHE C 161   O  LEU C 133           
SHEET    1   D 3 LYS D 137  ALA D 144  0                                        
SHEET    2   D 3 GLY D 127  LYS D 134 -1  O  TRP D 128   N  THR D 143           
SHEET    3   D 3 PHE D 161  ASP D 167 -1  N  PHE D 161   O  LEU D 133           
LINK        MN    MN A 501                 O   HOH A 600     1555   1555  2.27  
LINK        MN    MN B 502                 O   HOH B 591     1555   1555  2.31  
LINK        MN    MN C 503                 O   HOH C 586     1555   1555  2.30  
LINK        MN    MN D 504                 O   HOH D 577     1555   1555  2.31  
LINK        MN    MN A 501                 NE2 HIS A  26     1555   1555  2.23  
LINK        MN    MN A 501                 NE2 HIS A 171     1555   1555  2.24  
LINK        MN    MN A 501                 NE2 HIS A  81     1555   1555  2.24  
LINK        MN    MN A 501                 OD2 ASP A 167     1555   1555  2.00  
LINK        MN    MN B 502                 NE2 HIS B  26     1555   1555  2.25  
LINK        MN    MN B 502                 NE2 HIS B 171     1555   1555  2.24  
LINK        MN    MN B 502                 NE2 HIS B  81     1555   1555  2.22  
LINK        MN    MN B 502                 OD2 ASP B 167     1555   1555  1.95  
LINK        MN    MN C 503                 OD2 ASP C 167     1555   1555  1.99  
LINK        MN    MN C 503                 NE2 HIS C 171     1555   1555  2.17  
LINK        MN    MN C 503                 NE2 HIS C  81     1555   1555  2.24  
LINK        MN    MN C 503                 NE2 HIS C  26     1555   1555  2.23  
LINK        MN    MN D 504                 NE2 HIS D 171     1555   1555  2.17  
LINK        MN    MN D 504                 OD2 ASP D 167     1555   1555  2.02  
LINK        MN    MN D 504                 NE2 HIS D  26     1555   1555  2.26  
LINK        MN    MN D 504                 NE2 HIS D  81     1555   1555  2.22  
CISPEP   1 GLU A   15    PRO A   16          0         0.26                     
CISPEP   2 GLU B   15    PRO B   16          0         0.24                     
CISPEP   3 GLU C   15    PRO C   16          0        -0.02                     
CISPEP   4 GLU D   15    PRO D   16          0         0.24                     
SITE     1 AC1  5 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC1  5 HOH A 600                                                     
SITE     1 AC2  5 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC2  5 HOH B 591                                                     
SITE     1 AC3  5 HIS C  26  HIS C  81  ASP C 167  HIS C 171                    
SITE     2 AC3  5 HOH C 586                                                     
SITE     1 AC4  5 HIS D  26  HIS D  81  ASP D 167  HIS D 171                    
SITE     2 AC4  5 HOH D 577                                                     
CRYST1  101.698  109.297  181.722  90.00  90.00  90.00 C 2 2 21     32          
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      0.009833  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009149  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005503        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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