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Database: PDB
Entry: 1IXB
LinkDB: 1IXB
Original site: 1IXB 
HEADER    OXIDOREDUCTASE                          18-JUN-02   1IXB              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI MANGANESE(II) SUPEROXIDE DISMUTASE   
TITLE    2 MUTANT Y174F AT 0.90 ANGSTROMS RESOLUTION.                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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_STRAIN: QC781;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDT1-5                                    
KEYWDS    MANGANESE(II) SUPEROXIDE DISMUTASE, Y174F MUTANT, HYDROGEN BOND       
KEYWDS   2 REACTIVITY, ULTRAHIGH RESOLUTION, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.F.ANDERSON,R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,       
AUTHOR   2 G.B.JAMESON                                                          
REVDAT   3   13-JUL-11 1IXB    1       VERSN                                    
REVDAT   2   24-FEB-09 1IXB    1       VERSN                                    
REVDAT   1   18-DEC-02 1IXB    0                                                
JRNL        AUTH   B.F.ANDERSON,R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,        
JRNL        AUTH 2 E.N.BAKER,G.B.JAMESON                                        
JRNL        TITL   STRUCTURES AT 0.90 A RESOLUTION OF THE OXIDISED AND REDUCED  
JRNL        TITL 2 FORMS OF THE Y174F MUTANT OF THE MANGANESE SUPEROXIDE        
JRNL        TITL 3 DISMUTASE FROM ESCHERICHIA COLI                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
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 ALTERS       
REMARK   1  TITL 3 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,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,           
REMARK   1  AUTH 2 G.B.JAMESON                                                  
REMARK   1  TITL   OUTER SPHERE MUTATIONS PERTURB METAL REACTIVITY IN MANGANESE 
REMARK   1  TITL 2 SUPEROXIDE DISMUTASE                                         
REMARK   1  REF    BIOCHEMISTRY                  V.  40    15 2001              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI0018943                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.9                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM SHELL                   
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.111                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.111                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.126                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 1.204                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3300                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 274173                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.104                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.104                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.119                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 1.207                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2876                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 238354                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3254                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 4                                             
REMARK   3   SOLVENT ATOMS      : 925                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3990.33                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2927.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 39                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 39423                   
REMARK   3   NUMBER OF RESTRAINTS                     : 47096                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.029                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.091                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.107                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.000                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.036                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.067                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: P.C.MOEWS & R.H.KRETSINGER, J.MOL.BIOL.91(1975)201-   
REMARK   3                228                                                   
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  NO ELECTRON DENSITY IS OBSERVED FOR A SECOND HYDROGEN ATOM          
REMARK   3  ON THE COORDINATED SOLVENT SPECIES IN EITHER CHAIN. THUS,           
REMARK   3  THE COORDINATED SOLVENT SPECIES IS ASSIGNED AS A HYDROXIDE          
REMARK   3  ION. HOWEVER, A SOFT VIBRATIONAL MODE INVOLVING A PUTATIVE          
REMARK   3  SECOND HYDROGEN ATOM COULD  RENDER THIS ATOM UNDETECTABLE           
REMARK   3  IN DIFFERENCE FOURIER MAPS.                                         
REMARK   3  THE CLOSE CONTACTS AND POOR GEOMETRY LISTED IN REMARK 500           
REMARK   3  ARE CAUSED BY PARTIAL OCCUPANCIES AND DISORDER.                     
REMARK   4                                                                      
REMARK   4 1IXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB005370.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91                               
REMARK 200  MONOCHROMATOR                  : BENT GERMANIUM SINGLE CRYSTAL      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 274173                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 56.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: MN-SOD FROM 1IOH                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG6000, 0.1M BICINE. CRYSTALS    
REMARK 280  WERE REDUCED JUST PRIOR TO FREEZING BY ADDITION OF 10% H2O2 (1      
REMARK 280  PART TO 40 PARTS MOTHER LIQUOR), PH 8.5, VAPOR DIFFUSION, SITTING   
REMARK 280  DROP, TEMPERATURE 293K                                              
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       22.91600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE A  18   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLU A  54   OE1 -  CD  -  OE2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP A  66   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A  66   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 180   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP B 110   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP B 136   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B 180   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG B 180   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  89      143.77   -175.15                                   
REMARK 500    ASN A 145     -126.45     55.63                                   
REMARK 500    GLN A 178     -126.12     55.83                                   
REMARK 500    LYS B  29      -68.19   -108.11                                   
REMARK 500    LYS B  89      131.73   -175.33                                   
REMARK 500    ASP B 136       14.24     50.08                                   
REMARK 500    ASN B 145     -125.61     57.27                                   
REMARK 500    GLN B 178     -124.83     54.97                                   
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 372        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A 439        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 448        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 463        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH A 471        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 474        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A 554        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH A 608        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 664        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A 669        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B 381        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 517        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH B 526        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 550        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH B 551        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH B 552        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH B 553        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH B 603        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B 620        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 640        DISTANCE =  6.18 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                             MH2 A 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 MH2 A 206   O1  172.3                                              
REMARK 620 3 HIS A  81   NE2  92.9  92.0                                        
REMARK 620 4 ASP A 167   OD2  85.9  86.7 112.8                                  
REMARK 620 5 HIS A 171   NE2  91.6  90.3 125.8 121.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MH2 B 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 MH2 B 206   O1  172.9                                              
REMARK 620 3 HIS B  81   NE2  92.6  91.7                                        
REMARK 620 4 ASP B 167   OD2  86.3  86.9 112.7                                  
REMARK 620 5 HIS B 171   NE2  91.4  90.4 128.2 119.1                            
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 MH2 A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MH2 B 206                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VEW   RELATED DB: PDB                                   
REMARK 900 1VEW CONTAINS THE NATIVE STRUCTURE OF THE SAME PROTEIN FROM          
REMARK 900 E. COLI                                                              
REMARK 900 RELATED ID: 1I0H   RELATED DB: PDB                                   
REMARK 900 1I0H CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN Y174F            
REMARK 900 MUTANT AT 1.35 ANGSTROMS RESOLUTION                                  
REMARK 900 RELATED ID: 1EN4   RELATED DB: PDB                                   
REMARK 900 1EN4 CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN Q146H            
REMARK 900 MUTANT                                                               
REMARK 900 RELATED ID: 1EN6   RELATED DB: PDB                                   
REMARK 900 1EN6 CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN Q146L            
REMARK 900 MUTANT                                                               
REMARK 900 RELATED ID: 1I08   RELATED DB: PDB                                   
REMARK 900 1I08 CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN H30A             
REMARK 900 MUTANT                                                               
REMARK 900 RELATED ID: 1MMM   RELATED DB: PDB                                   
REMARK 900 1MMM CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN FE-              
REMARK 900 SUBSTITUTED                                                          
REMARK 900 RELATED ID: 1IX9   RELATED DB: PDB                                   
REMARK 900 1IX9 CONTAINS CRYSTAL STRUCTURE OF THE SAME PROTEIN WITH             
REMARK 900 MANGANASE(III)                                                       
DBREF  1IXB A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1IXB B    1   205  UNP    P00448   SODM_ECOLI       1    205             
SEQADV 1IXB PHE A  174  UNP  P00448    TYR   174 ENGINEERED                     
SEQADV 1IXB PHE B  174  UNP  P00448    TYR   174 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 GLN 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 PHE 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 GLN 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 PHE 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                      
HET    MH2  A 206       2                                                       
HET    MH2  B 206       2                                                       
HETNAM     MH2 MANGANESE ION, 1 HYDROXYL COORDINATED                            
HETSYN     MH2 [MN(OH)]+                                                        
FORMUL   3  MH2    2(H MN O 2+)                                                 
FORMUL   5  HOH   *925(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 PRO A   64  ASP A   66  5                                   3    
HELIX    7   7 LYS A   67  GLY A   87  1                                  21    
HELIX    8   8 GLN A   95  GLY A  107  1                                  13    
HELIX    9   9 SER A  108  ARG A  123  1                                  16    
HELIX   10  10 SER A  148  MET A  151  5                                   4    
HELIX   11  11 GLY A  152  GLY A  157  1                                   6    
HELIX   12  12 TRP A  169  ALA A  172  5                                   4    
HELIX   13  13 TYR A  173  GLN A  178  1                                   6    
HELIX   14  14 ARG A  180  VAL A  192  1                                  13    
HELIX   15  15 ASN A  193  LYS A  205  1                                  13    
HELIX   16  16 ASP B   19  LYS B   29  1                                  11    
HELIX   17  17 LYS B   29  GLU B   43  1                                  15    
HELIX   18  18 LEU B   45  ASN B   50  1                                   6    
HELIX   19  19 PRO B   52  ILE B   57  1                                   6    
HELIX   20  20 THR B   58  LEU B   63  5                                   6    
HELIX   21  21 PRO B   64  ASP B   66  5                                   3    
HELIX   22  22 LYS B   67  GLY B   87  1                                  21    
HELIX   23  23 GLN B   95  GLY B  107  1                                  13    
HELIX   24  24 SER B  108  ARG B  123  1                                  16    
HELIX   25  25 SER B  148  MET B  151  5                                   4    
HELIX   26  26 GLY B  152  GLY B  157  1                                   6    
HELIX   27  27 TRP B  169  ALA B  172  5                                   4    
HELIX   28  28 TYR B  173  GLN B  178  1                                   6    
HELIX   29  29 ARG B  180  TRP B  189  1                                  10    
HELIX   30  30 ASN B  193  LYS B  205  1                                  13    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  N  TRP A 130   O  VAL A 141           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  O  LEU A 166   N  ALA A 129           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  N  TRP B 130   O  VAL B 141           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  O  ILE B 163   N  LEU B 131           
LINK        MN   MH2 A 206                 NE2 HIS A  26     1555   1555  2.18  
LINK        MN   MH2 A 206                 NE2 HIS A  81     1555   1555  2.13  
LINK        MN   MH2 A 206                 OD2 ASP A 167     1555   1555  2.05  
LINK        MN   MH2 A 206                 NE2 HIS A 171     1555   1555  2.14  
LINK        MN   MH2 B 206                 NE2 HIS B  26     1555   1555  2.18  
LINK        MN   MH2 B 206                 NE2 HIS B  81     1555   1555  2.15  
LINK        MN   MH2 B 206                 OD2 ASP B 167     1555   1555  2.04  
LINK        MN   MH2 B 206                 NE2 HIS B 171     1555   1555  2.13  
CISPEP   1 GLU A   15    PRO A   16          0         5.32                     
CISPEP   2 GLU B   15    PRO B   16          0         5.08                     
SITE     1 AC1  6 HIS A  26  HIS A  81  GLN A 146  ASP A 167                    
SITE     2 AC1  6 TRP A 169  HIS A 171                                          
SITE     1 AC2  6 HIS B  26  HIS B  81  GLN B 146  ASP B 167                    
SITE     2 AC2  6 TRP B 169  HIS B 171                                          
CRYST1   46.815   45.832   96.187  90.00  98.20  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      0.021361  0.000000  0.003078        0.00000                         
SCALE2      0.000000  0.021819  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010504        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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