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Database: PDB
Entry: 2CE4
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Original site: 2CE4 
HEADER    OXIDOREDUCTASE                          03-FEB-06   2CE4              
TITLE     MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM DEINOCOCCUS              
TITLE    2 RADIODURANS                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 ATCC: 13939;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)PLYSS;                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: GATEWAY PDEST17                            
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, DEINOCOCCUS RADIODURANS,              
KEYWDS   2 RADIATION RESISTANCE, OXIDOREDUCTASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,G.LEONARD,               
AUTHOR   2 S.MCSWEENEY                                                          
REVDAT   3   24-FEB-09 2CE4    1       VERSN                                    
REVDAT   2   05-APR-06 2CE4    1       JRNL                                     
REVDAT   1   13-FEB-06 2CE4    0                                                
JRNL        AUTH   R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,                
JRNL        AUTH 2 G.LEONARD,S.MCSWEENEY                                        
JRNL        TITL   STRUCTURE OF THE MANGANESE SUPEROXIDE DISMUTASE              
JRNL        TITL 2 FROM DEINOCOCCUS RADIODURANS IN TWO CRYSTAL FORMS.           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   325 2006              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   16582477                                                     
JRNL        DOI    10.1107/S1744309106008402                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.2  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19553                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 996                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1391                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3217                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 365                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.58000                                             
REMARK   3    B22 (A**2) : 2.34000                                              
REMARK   3    B33 (A**2) : -2.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.28000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.312         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.227         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.144         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3305 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2816 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4497 ; 1.308 ; 1.908       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6539 ; 0.846 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   404 ; 6.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   467 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3781 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   690 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   718 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3308 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1765 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   269 ; 0.154 ; 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):     8 ; 0.128 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    23 ; 0.267 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.214 ; 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):  2028 ; 0.642 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3225 ; 1.160 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1277 ; 1.624 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1272 ; 2.628 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A      45      6                      
REMARK   3           1     B      1       B      45      6                      
REMARK   3           2     A     46       A      90      6                      
REMARK   3           2     B     46       B      90      6                      
REMARK   3           3     A     97       A     210      6                      
REMARK   3           3     B     97       B     210      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2942 ;  0.38 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2942 ;  2.46 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS. ELECTRON DENSITY FOR RESIDUES A90-A95 AND         
REMARK   3  B91-B95 IS POOR. THEY ARE NOT INCLUDED IN THE MODEL.                
REMARK   4                                                                      
REMARK   4 2CE4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-FEB-06.                 
REMARK 100 THE PDBE ID CODE IS EBI-27551.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20567                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1VEW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM TRIS-HCL PH 8.5, 20MM              
REMARK 280  MNCL2, 30% PEG 4000                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       41.60500            
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE                                           
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     TYR A   -19                                                      
REMARK 465     TYR A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     GLN A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     GLN A    93                                                      
REMARK 465     ASN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     TYR B   -19                                                      
REMARK 465     TYR B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLU B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     LYS B    -4                                                      
REMARK 465     LYS B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     GLN B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     GLN B    93                                                      
REMARK 465     ASN B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  40    CD   CE   NZ                                        
REMARK 470     THR A  45    O                                                   
REMARK 470     ALA A  64    CB                                                  
REMARK 470     LEU A 104    CD1  CD2                                            
REMARK 470     LYS A 126    CE   NZ                                             
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     LEU B  -1    CD1  CD2                                            
REMARK 470     LYS B  40    CD   CE   NZ                                        
REMARK 470     GLU B  43    CD   OE1  OE2                                       
REMARK 470     LYS B  66    CE   NZ                                             
REMARK 470     LYS B 120    CE   NZ                                             
REMARK 470     LYS B 142    CG   CD   CE   NZ                                   
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 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    ARG A  61      -46.25    168.61                                   
REMARK 500    ASN A 150     -128.03     57.51                                   
REMARK 500    GLN A 183     -128.70     43.36                                   
REMARK 500    SER B 109      -72.01    -65.41                                   
REMARK 500    ASN B 150     -125.57     54.76                                   
REMARK 500    TYR B 178       -5.25   -146.54                                   
REMARK 500    GLN B 183     -125.37     50.73                                   
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 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 A1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  80   NE2  92.9                                              
REMARK 620 3 ASP A 172   OD2  86.2 110.0                                        
REMARK 620 4 HIS A 176   NE2  94.7 139.1 110.6                                  
REMARK 620 5 HOH A2198   O   167.7  94.3  82.0  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 172   OD2                                                    
REMARK 620 2 HIS B  26   NE2  85.1                                              
REMARK 620 3 HIS B 176   NE2 115.3  93.8                                        
REMARK 620 4 HOH B2167   O    83.8 168.9  90.6                                  
REMARK 620 5 HIS B  80   NE2 105.2  86.9 139.4  96.4                            
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 A1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B1211                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Y67   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE                           
REMARK 900  DISMUTASE FROMDEINOCOCCUS RADIODURANS                               
REMARK 900 RELATED ID: 2CDY   RELATED DB: PDB                                   
REMARK 900  MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM                        
REMARK 900  DEINOCOCCUS RADIODURANS                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE CRYSTALLISED CONTAINS AN N-TERMINAL                     
REMARK 999 PURIFICATION TAG. WHERE RESIDUES FROM THIS ARE SEEN IN THE           
REMARK 999 CRYSTAL THE NUMBERING IS -1, -2 ETC...                               
DBREF  2CE4 A  -21    -1  PDB    2CE4     2CE4           -21     -1             
DBREF  2CE4 A    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  2CE4 B  -21    -1  PDB    2CE4     2CE4           -21     -1             
DBREF  2CE4 B    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
SEQRES   1 A  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 A  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 A  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 A  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 A  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 A  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 A  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 A  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 A  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 A  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 A  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 A  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 A  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 A  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 A  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 A  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 A  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 A  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
SEQRES   1 B  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 B  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 B  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 B  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 B  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 B  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 B  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 B  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 B  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 B  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 B  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 B  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 B  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 B  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 B  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 B  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 B  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 B  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
HET     MN  A1211       1                                                       
HET     MN  B1211       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *365(H2 O1)                                                   
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 PRO A   51  ILE A   56  1                                   6    
HELIX    4   4 LYS A   66  ILE A   86  1                                  21    
HELIX    5   5 SER A  100  GLY A  112  1                                  13    
HELIX    6   6 SER A  113  THR A  127  1                                  15    
HELIX    7   7 ASN A  153  MET A  156  5                                   4    
HELIX    8   8 GLY A  157  GLY A  162  1                                   6    
HELIX    9   9 TRP A  174  ALA A  177  5                                   4    
HELIX   10  10 TYR A  178  GLN A  183  1                                   6    
HELIX   11  11 ARG A  185  TRP A  194  1                                  10    
HELIX   12  12 ASN A  198  LYS A  210  1                                  13    
HELIX   13  13 ASP B   19  LYS B   29  1                                  11    
HELIX   14  14 LYS B   29  GLU B   43  1                                  15    
HELIX   15  15 PRO B   51  ILE B   56  1                                   6    
HELIX   16  16 GLN B   57  VAL B   62  5                                   6    
HELIX   17  17 PRO B   63  ILE B   86  1                                  24    
HELIX   18  18 SER B  100  GLY B  112  1                                  13    
HELIX   19  19 SER B  113  THR B  127  1                                  15    
HELIX   20  20 ASN B  153  MET B  156  5                                   4    
HELIX   21  21 GLY B  157  GLY B  162  1                                   6    
HELIX   22  22 TRP B  174  ALA B  177  5                                   4    
HELIX   23  23 TYR B  178  GLN B  183  1                                   6    
HELIX   24  24 ARG B  185  TRP B  194  1                                  10    
HELIX   25  25 ASN B  198  LYS B  210  1                                  13    
SHEET    1  AA 3 LYS A 142  ALA A 149  0                                        
SHEET    2  AA 3 GLY A 132  LYS A 139 -1  O  TRP A 133   N  THR A 148           
SHEET    3  AA 3 THR A 166  ASP A 172 -1  O  THR A 166   N  VAL A 138           
SHEET    1  BA 3 LYS B 142  ALA B 149  0                                        
SHEET    2  BA 3 GLY B 132  LYS B 139 -1  O  TRP B 133   N  THR B 148           
SHEET    3  BA 3 THR B 166  ASP B 172 -1  O  THR B 166   N  VAL B 138           
LINK        MN    MN A1211                 NE2 HIS A  26     1555   1555  2.22  
LINK        MN    MN A1211                 NE2 HIS A  80     1555   1555  2.03  
LINK        MN    MN A1211                 OD2 ASP A 172     1555   1555  1.90  
LINK        MN    MN A1211                 NE2 HIS A 176     1555   1555  2.21  
LINK        MN    MN A1211                 O   HOH A2198     1555   1555  2.18  
LINK        MN    MN B1211                 NE2 HIS B  26     1555   1555  2.15  
LINK        MN    MN B1211                 NE2 HIS B 176     1555   1555  2.10  
LINK        MN    MN B1211                 O   HOH B2167     1555   1555  2.20  
LINK        MN    MN B1211                 NE2 HIS B  80     1555   1555  2.16  
LINK        MN    MN B1211                 OD2 ASP B 172     1555   1555  1.96  
CISPEP   1 GLU A   15    PRO A   16          0        -7.98                     
CISPEP   2 GLU B   15    PRO B   16          0        -2.08                     
SITE     1 AC1  5 HIS A  26  HIS A  80  ASP A 172  HIS A 176                    
SITE     2 AC1  5 HOH A2198                                                     
SITE     1 AC2  5 HIS B  26  HIS B  80  ASP B 172  HIS B 176                    
SITE     2 AC2  5 HOH B2167                                                     
CRYST1   44.280   83.210   59.520  90.00 110.18  90.00 P 1 21 1      4          
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      0.022584  0.000000  0.008300        0.00000                         
SCALE2      0.000000  0.012018  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017900        0.00000                         
MTRIX1   1  0.995000 -0.091000 -0.043000       42.89740    1                    
MTRIX2   1  0.088000  0.994000 -0.061000       17.99276    1                    
MTRIX3   1  0.048000  0.057000  0.997000       56.18528    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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