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Database: PDB
Entry: 6ELK
LinkDB: 6ELK
Original site: 6ELK 
HEADER    OXIDOREDUCTASE                          29-SEP-17   6ELK              
TITLE     C.ELEGANS MNSOD-3 MUTANT - Q142H                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN] 2, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 GENE: SOD-3, C08A9.1;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: OX326A                                     
KEYWDS    SUPEROXIDE DISMUTASE, MANGANESE, OXIDOREDUCTASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.HUNTER,C.H.TRINH,T.HUNTER                                         
REVDAT   2   18-APR-18 6ELK    1       JRNL                                     
REVDAT   1   06-DEC-17 6ELK    0                                                
JRNL        AUTH   T.HUNTER,R.BONETTA,A.SACCO,M.VELLA,P.M.SULTANA,C.H.TRINH,    
JRNL        AUTH 2 H.B.R.FADIA,T.BOROWSKI,R.GARCIA-FANDINO,T.STOCKNER,          
JRNL        AUTH 3 G.J.HUNTER                                                   
JRNL        TITL   A SINGLE MUTATION IS SUFFICIENT TO MODIFY THE METAL          
JRNL        TITL 2 SELECTIVITY AND SPECIFICITY OF A EUKARYOTIC MANGANESE        
JRNL        TITL 3 SUPEROXIDE DISMUTASE TO ENCOMPASS IRON.                      
JRNL        REF    CHEMISTRY                     V.  24  5303 2018              
JRNL        REFN                   ISSN 1521-3765                               
JRNL        PMID   29178484                                                     
JRNL        DOI    10.1002/CHEM.201704655                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 53555                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2869                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3762                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 206                          
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 303                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.42000                                             
REMARK   3    B22 (A**2) : -0.42000                                             
REMARK   3    B33 (A**2) : 0.84000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.092         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.413         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3294 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3096 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4472 ; 1.248 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7131 ; 0.752 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 5.438 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   164 ;32.335 ;24.817       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   564 ;11.730 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;14.812 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   469 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3728 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   793 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1561 ; 0.807 ; 1.626       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1560 ; 0.806 ; 1.625       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1951 ; 1.261 ; 2.434       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1952 ; 1.261 ; 2.435       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1733 ; 1.271 ; 1.830       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1733 ; 1.270 ; 1.830       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2519 ; 1.979 ; 2.683       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4060 ; 5.235 ;14.484       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3982 ; 5.121 ;14.106       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   194                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7480   5.6180  -0.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1187 T22:   0.0384                                     
REMARK   3      T33:   0.1202 T12:   0.0410                                     
REMARK   3      T13:   0.0688 T23:   0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4381 L22:   2.1594                                     
REMARK   3      L33:   2.0218 L12:  -0.0519                                     
REMARK   3      L13:   0.0339 L23:  -0.9425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:  -0.0744 S13:  -0.1438                       
REMARK   3      S21:  -0.2387 S22:  -0.2406 S23:  -0.4017                       
REMARK   3      S31:   0.4669 S32:   0.1870 S33:   0.2512                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   194                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6250  -2.2090  14.1470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0228 T22:   0.1371                                     
REMARK   3      T33:   0.0993 T12:   0.0013                                     
REMARK   3      T13:   0.0211 T23:   0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3737 L22:   1.2548                                     
REMARK   3      L33:   1.6967 L12:  -0.1551                                     
REMARK   3      L13:   0.3786 L23:  -0.6352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:  -0.3281 S13:  -0.0321                       
REMARK   3      S21:   0.1529 S22:   0.1120 S23:   0.2258                       
REMARK   3      S31:  -0.0886 S32:  -0.3166 S33:  -0.1226                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6ELK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006816.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.31                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56496                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.30                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049                                       
REMARK 200 STARTING MODEL: 4X9Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OCTAHEDRONS                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.9 M AMMONIUM SULPHATE, 0.1 M BICINE    
REMARK 280  PH 8.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       68.87500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.76500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.76500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.43750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.76500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.76500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.31250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.76500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.76500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.43750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.76500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.76500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      103.31250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.87500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 354  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 365  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET C     0                                                      
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  29      -60.74   -105.03                                   
REMARK 500    ASN A 141     -120.28     55.83                                   
REMARK 500    TYR A 161      -16.24   -143.40                                   
REMARK 500    LYS A 166     -129.71     51.78                                   
REMARK 500    LYS C  29      -60.78   -106.19                                   
REMARK 500    ASP C  84       77.20   -114.80                                   
REMARK 500    ASN C 141     -119.21     52.13                                   
REMARK 500    TYR C 161      -18.25   -141.42                                   
REMARK 500    LYS C 166     -136.28     55.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 445        DISTANCE =  6.54 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  89.7                                              
REMARK 620 3 ASP A 155   OD2  86.2 107.8                                        
REMARK 620 4 HIS A 159   NE2  89.3 133.7 118.3                                  
REMARK 620 5 HOH A 372   O   178.3  91.7  92.4  90.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  74   NE2  89.0                                              
REMARK 620 3 ASP C 155   OD2  87.0 113.8                                        
REMARK 620 4 HIS C 159   NE2  90.1 128.5 117.5                                  
REMARK 620 5 HOH C 393   O   176.2  87.3  95.2  91.6                            
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 205                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DC5   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE [MN] 2 AT 100K                                  
REMARK 900 RELATED ID: 4X9Q   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE [MN] 2 AT 293K                                  
DBREF  6ELK A    1   194  UNP    P41977   SODM2_CAEEL     25    218             
DBREF  6ELK C    1   194  UNP    P41977   SODM2_CAEEL     25    218             
SEQADV 6ELK MET A    0  UNP  P41977              INITIATING METHIONINE          
SEQADV 6ELK HIS A  142  UNP  P41977    GLN   166 ENGINEERED MUTATION            
SEQADV 6ELK MET C    0  UNP  P41977              INITIATING METHIONINE          
SEQADV 6ELK HIS C  142  UNP  P41977    GLN   166 ENGINEERED MUTATION            
SEQRES   1 A  195  MET LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA          
SEQRES   2 A  195  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 A  195  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 A  195  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 A  195  GLY ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 A  195  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 A  195  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS          
SEQRES   8 A  195  GLU LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU          
SEQRES   9 A  195  ASP ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA          
SEQRES  10 A  195  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS LYS          
SEQRES  11 A  195  LYS ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN HIS          
SEQRES  12 A  195  ASP PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP          
SEQRES  13 A  195  VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL          
SEQRES  14 A  195  ARG PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN          
SEQRES  15 A  195  TRP LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN          
SEQRES   1 C  195  MET LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA          
SEQRES   2 C  195  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 C  195  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 C  195  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 C  195  GLY ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 C  195  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 C  195  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS          
SEQRES   8 C  195  GLU LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU          
SEQRES   9 C  195  ASP ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA          
SEQRES  10 C  195  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS LYS          
SEQRES  11 C  195  LYS ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN HIS          
SEQRES  12 C  195  ASP PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP          
SEQRES  13 C  195  VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL          
SEQRES  14 C  195  ARG PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN          
SEQRES  15 C  195  TRP LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN          
HET     MN  A 201       1                                                       
HET    SO4  A 202       5                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET     MN  C 201       1                                                       
HET    SO4  C 202       5                                                       
HET    SO4  C 203       5                                                       
HET    SO4  C 204       5                                                       
HET    GOL  C 205       6                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   4  SO4    6(O4 S 2-)                                                   
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *303(H2 O)                                                    
HELIX    1 AA1 SER A   19  LYS A   29  1                                  11    
HELIX    2 AA2 LYS A   29  GLY A   52  1                                  24    
HELIX    3 AA3 ASN A   53  ASN A   80  1                                  28    
HELIX    4 AA4 SER A   89  GLY A  101  1                                  13    
HELIX    5 AA5 SER A  102  ALA A  116  1                                  15    
HELIX    6 AA6 TRP A  157  ALA A  160  5                                   4    
HELIX    7 AA7 TYR A  161  LYS A  166  1                                   6    
HELIX    8 AA8 VAL A  168  TRP A  177  1                                  10    
HELIX    9 AA9 LYS A  178  ALA A  180  5                                   3    
HELIX   10 AB1 ASN A  181  ARG A  193  1                                  13    
HELIX   11 AB2 SER C   19  LYS C   29  1                                  11    
HELIX   12 AB3 LYS C   29  GLY C   52  1                                  24    
HELIX   13 AB4 ASN C   53  LEU C   60  1                                   8    
HELIX   14 AB5 LEU C   60  ASN C   80  1                                  21    
HELIX   15 AB6 SER C   89  GLY C  101  1                                  13    
HELIX   16 AB7 SER C  102  ALA C  116  1                                  15    
HELIX   17 AB8 TRP C  157  ALA C  160  5                                   4    
HELIX   18 AB9 TYR C  161  LYS C  166  1                                   6    
HELIX   19 AC1 VAL C  168  TRP C  177  1                                  10    
HELIX   20 AC2 LYS C  178  ALA C  180  5                                   3    
HELIX   21 AC3 ASN C  181  ARG C  193  1                                  13    
SHEET    1 AA1 3 ILE A 133  ALA A 140  0                                        
SHEET    2 AA1 3 GLY A 121  CYS A 128 -1  N  TRP A 124   O  ALA A 137           
SHEET    3 AA1 3 VAL A 149  ASP A 155 -1  O  VAL A 149   N  TYR A 127           
SHEET    1 AA2 3 ILE C 133  ALA C 140  0                                        
SHEET    2 AA2 3 GLY C 121  CYS C 128 -1  N  CYS C 128   O  ILE C 133           
SHEET    3 AA2 3 VAL C 149  ASP C 155 -1  O  LEU C 151   N  LEU C 125           
LINK         NE2 HIS A  26                MN    MN A 201     1555   1555  2.24  
LINK         NE2 HIS A  74                MN    MN A 201     1555   1555  2.22  
LINK         OD2 ASP A 155                MN    MN A 201     1555   1555  2.01  
LINK         NE2 HIS A 159                MN    MN A 201     1555   1555  2.17  
LINK         NE2 HIS C  26                MN    MN C 201     1555   1555  2.19  
LINK         NE2 HIS C  74                MN    MN C 201     1555   1555  2.23  
LINK         OD2 ASP C 155                MN    MN C 201     1555   1555  1.98  
LINK         NE2 HIS C 159                MN    MN C 201     1555   1555  2.19  
LINK        MN    MN A 201                 O   HOH A 372     1555   1555  2.21  
LINK        MN    MN C 201                 O   HOH C 393     1555   1555  2.19  
CISPEP   1 GLU A   15    PRO A   16          0         8.91                     
CISPEP   2 GLU C   15    PRO C   16          0         5.21                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 155  HIS A 159                    
SITE     2 AC1  5 HOH A 372                                                     
SITE     1 AC2  4 PRO A  62  LYS A  65  HOH A 336  HOH A 342                    
SITE     1 AC3  5 HIS A   2  THR A   3  HIS A  71  HOH A 308                    
SITE     2 AC3  5 HOH A 397                                                     
SITE     1 AC4  4 ASN A 181  LYS A 183  HOH A 310  HOH A 399                    
SITE     1 AC5  5 HIS C  26  HIS C  74  ASP C 155  HIS C 159                    
SITE     2 AC5  5 HOH C 393                                                     
SITE     1 AC6  4 LYS C  29  ASN C 167  HOH C 323  HOH C 367                    
SITE     1 AC7  3 LYS C  51  ASN C  53  HOH C 346                               
SITE     1 AC8  3 ASN C 181  LYS C 183  HOH C 313                               
SITE     1 AC9  8 ASP A 131  ASP C  99  PHE C 100  ILE C 133                    
SITE     2 AC9  8 LEU C 134  LYS C 135  HOH C 303  HOH C 370                    
CRYST1   81.530   81.530  137.750  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012265  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012265  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007260        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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