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Database: PDB
Entry: 1I0H
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HEADER    OXIDOREDUCTASE                          29-JAN-01   1I0H              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI MANGANESE SUPEROXIDE                 
TITLE    2 DISMUTASE MUTANT Y174F AT 1.35 ANGSTROMS RESOLUTION.                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE Y174F MUTANT;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PDT1-5 (CONTAINING SODA)                  
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, Y174F MUTANT, HYDROGEN BOND,          
KEYWDS   2 REACTIVITY, OXIDOREDUCTASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,                    
AUTHOR   2 G.B.JAMESON                                                          
REVDAT   4   24-FEB-09 1I0H    1       VERSN                                    
REVDAT   3   04-JUL-01 1I0H    1       REMARK                                   
REVDAT   2   25-APR-01 1I0H    1       JRNL                                     
REVDAT   1   28-FEB-01 1I0H    0                                                
JRNL        AUTH   R.A.EDWARDS,M.M.WHITTAKER,J.W.WHITTAKER,E.N.BAKER,           
JRNL        AUTH 2 G.B.JAMESON                                                  
JRNL        TITL   REMOVING A HYDROGEN BOND IN THE DIMER INTERFACE OF           
JRNL        TITL 2 ESCHERICHIA COLI MANGANESE SUPEROXIDE DISMUTASE              
JRNL        TITL 3 ALTERS STRUCTURE AND REACTIVITY.                             
JRNL        REF    BIOCHEMISTRY                  V.  40  4622 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11294629                                                     
JRNL        DOI    10.1021/BI002403H                                            
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   OUTER SPHERE MUTATIONS PERTURB METAL REACTIVITY IN           
REMARK   1  TITL 2 MANGANESE 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.    1.35 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) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.170                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.169                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.196                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4444                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 89092                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
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      : 498                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3667.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 17529                   
REMARK   3   NUMBER OF RESTRAINTS                     : 16393                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.004                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.015                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.391                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.066                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.066                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.044                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.024                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.042                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I0H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012752.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-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) : 0.9058                             
REMARK 200  MONOCHROMATOR                  : SINGLE-CRYSTAL GERMANIUM           
REMARK 200                                   TRIANGULAR MONOCHROMATOR           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
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   : 89109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.02700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 52.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 18.300                             
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG 6000, 0.1M BICINE PH          
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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       23.00850            
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: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17350 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   29   CD    CE    NZ                                      
REMARK 480     GLU A   43   CG    CD    OE1   OE2                               
REMARK 480     GLU A   47   CG    CD    OE1   OE2                               
REMARK 480     ASN A   50   CG    OD1   ND2                                     
REMARK 480     GLU A   54   CG    CD    OE1   OE2                               
REMARK 480     LEU A   56   CG    CD1   CD2                                     
REMARK 480     LYS A   59   CG    CD    CE    NZ                                
REMARK 480     ASP A   61   CG    OD1   OD2                                     
REMARK 480     GLN A   62   CD    OE1   NE2                                     
REMARK 480     LYS A   68   CG    CD    CE    NZ                                
REMARK 480     LYS A   86   CE    NZ                                            
REMARK 480     GLU A  117   CG    CD    OE1   OE2                               
REMARK 480     LYS A  118   CE    NZ                                            
REMARK 480     ASN A  179   CG    OD1   ND2                                     
REMARK 480     LYS A  186   CG    CD    CE    NZ                                
REMARK 480     LYS B   20   CG    CD    CE    NZ                                
REMARK 480     GLN B   21   CD    OE1   NE2                                     
REMARK 480     GLU B   24   CD    OE1   OE2                                     
REMARK 480     GLU B   54   CG    CD    OE1   OE2                               
REMARK 480     GLU B   55   CG    CD    OE1   OE2                               
REMARK 480     LYS B   86   CG    CD    CE    NZ                                
REMARK 480     ASP B  136   CB    CG    OD1   OD2                               
REMARK 480     GLN B  178   CG    CD    OE1   NE2                               
REMARK 480     LYS B  204   CD    CE    NZ                                      
REMARK 480     LYS B  205   CB    CG    CD    CE    NZ                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    54     O    HOH A   333              2.06            
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      142.52   -174.74                                   
REMARK 500    ASN A 145     -126.38     56.68                                   
REMARK 500    TYR A 173       -1.90   -142.35                                   
REMARK 500    GLN A 178     -123.03     52.33                                   
REMARK 500    LYS B  29      -68.06   -107.83                                   
REMARK 500    LYS B  89      132.67   -172.41                                   
REMARK 500    ASN B 145     -126.31     54.52                                   
REMARK 500    GLN B 178     -120.74     48.22                                   
REMARK 500    LYS B 204      -12.60     72.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 469   O                                                      
REMARK 620 2 HIS A  26   NE2 173.9                                              
REMARK 620 3 ASP A 167   OD2  87.8  86.3                                        
REMARK 620 4 HIS A 171   NE2  91.3  92.8 119.8                                  
REMARK 620 5 HIS A  81   NE2  90.2  90.9 114.4 125.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 443   O                                                      
REMARK 620 2 HIS B  81   NE2  92.2                                              
REMARK 620 3 ASP B 167   OD2  87.2 115.1                                        
REMARK 620 4 HIS B 171   NE2  92.4 127.5 117.3                                  
REMARK 620 5 HIS B  26   NE2 174.3  90.7  87.2  89.7                            
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 206                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 206                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VEW   RELATED DB: PDB                                   
REMARK 900 1VEW IS THE NATIVE STRUCTURE                                         
REMARK 900 RELATED ID: 1EN4   RELATED DB: PDB                                   
REMARK 900 1EN4 IS E. COLI MANGANESE SUPEROXIDE DISMUTASE Q146H MUTANT          
REMARK 900 RELATED ID: 1EN5   RELATED DB: PDB                                   
REMARK 900 IEN5 IS E. COLI MANGANESE SUPEROXIDE DISMUTASE Y34F MUTANT           
REMARK 900 RELATED ID: 1EN6   RELATED DB: PDB                                   
REMARK 900 1EN6 IS E. COLI MANGANESE SUPEROXIDE DISMUTASE Q146L MUTANT          
REMARK 900 RELATED ID: 1I08   RELATED DB: PDB                                   
REMARK 900 1I08 IS E. COLI MANGANESE SUPEROXIDE DISMUTASE H30A MUTANT           
REMARK 900 RELATED ID: 1MMM   RELATED DB: PDB                                   
REMARK 900 1MMM IS E. COLI FE-SUBSTITUTED MANGANESE SUPEROXIDE                  
REMARK 900 DISMUTASE                                                            
DBREF  1I0H A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1I0H B    1   205  UNP    P00448   SODM_ECOLI       1    205             
SEQADV 1I0H PHE A  174  UNP  P00448    TYR   174 ENGINEERED                     
SEQADV 1I0H 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     MN  A 206       1                                                       
HET     MN  B 206       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *500(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 PRO A   52  ILE A   57  1                                   6    
HELIX    4   4 THR A   58  LEU A   63  5                                   6    
HELIX    5   5 PRO A   64  ASP A   66  5                                   3    
HELIX    6   6 LYS A   67  GLY A   87  1                                  21    
HELIX    7   7 GLN A   95  GLY A  107  1                                  13    
HELIX    8   8 SER A  108  ARG A  123  1                                  16    
HELIX    9   9 SER A  148  MET A  151  5                                   4    
HELIX   10  10 GLY A  152  GLY A  157  1                                   6    
HELIX   11  11 TRP A  169  ALA A  172  5                                   4    
HELIX   12  12 TYR A  173  GLN A  178  1                                   6    
HELIX   13  13 ARG A  180  VAL A  192  1                                  13    
HELIX   14  14 ASN A  193  LYS A  205  1                                  13    
HELIX   15  15 ASP B   19  LYS B   29  1                                  11    
HELIX   16  16 LYS B   29  GLU B   43  1                                  15    
HELIX   17  17 LEU B   45  ASN B   50  1                                   6    
HELIX   18  18 PRO B   52  ILE B   57  1                                   6    
HELIX   19  19 THR B   58  LEU B   63  5                                   6    
HELIX   20  20 PRO B   64  ASP B   66  5                                   3    
HELIX   21  21 LYS B   67  GLY B   87  1                                  21    
HELIX   22  22 GLN B   95  GLY B  107  1                                  13    
HELIX   23  23 SER B  108  ARG B  123  1                                  16    
HELIX   24  24 SER B  148  MET B  151  5                                   4    
HELIX   25  25 GLY B  152  GLY B  157  1                                   6    
HELIX   26  26 TRP B  169  ALA B  172  5                                   4    
HELIX   27  27 TYR B  173  GLN B  178  1                                   6    
HELIX   28  28 ARG B  180  VAL B  192  1                                  13    
HELIX   29  29 ASN B  193  LYS B  204  1                                  12    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  O  TRP A 128   N  THR A 143           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  N  PHE A 161   O  LEU A 133           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  O  TRP B 128   N  THR B 143           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  N  PHE B 161   O  LEU B 133           
LINK        MN    MN A 206                 O   HOH A 469     1555   1555  2.23  
LINK        MN    MN B 206                 O   HOH B 443     1555   1555  2.24  
LINK        MN    MN A 206                 NE2 HIS A  26     1555   1555  2.18  
LINK        MN    MN A 206                 OD2 ASP A 167     1555   1555  2.02  
LINK        MN    MN A 206                 NE2 HIS A 171     1555   1555  2.13  
LINK        MN    MN A 206                 NE2 HIS A  81     1555   1555  2.18  
LINK        MN    MN B 206                 NE2 HIS B  81     1555   1555  2.18  
LINK        MN    MN B 206                 OD2 ASP B 167     1555   1555  2.01  
LINK        MN    MN B 206                 NE2 HIS B 171     1555   1555  2.16  
LINK        MN    MN B 206                 NE2 HIS B  26     1555   1555  2.14  
CISPEP   1 GLU A   15    PRO A   16          0         1.88                     
CISPEP   2 GLU B   15    PRO B   16          0         1.63                     
SITE     1 AC1  5 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC1  5 HOH A 469                                                     
SITE     1 AC2  5 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC2  5 HOH B 443                                                     
CRYST1   46.893   46.017   95.993  90.00  98.40  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      0.021325  0.000000  0.003149        0.00000                         
SCALE2      0.000000  0.021731  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010530        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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