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Database: PDB
Entry: 1D5N
LinkDB: 1D5N
Original site: 1D5N 
HEADER    OXIDOREDUCTASE                          08-OCT-99   1D5N              
TITLE     CRYSTAL STRUCTURE OF E. COLI MNSOD AT 100K                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (MANGANESE SUPEROXIDE DISMUTASE);                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.O.BORGSTAHL,M.POKROSS,R.CHEHAB,A.SEKHER,E.H.SNELL                 
REVDAT   4   16-NOV-11 1D5N    1       VERSN  HETATM                            
REVDAT   3   24-FEB-09 1D5N    1       VERSN                                    
REVDAT   2   01-APR-03 1D5N    1       JRNL                                     
REVDAT   1   02-MAR-00 1D5N    0                                                
JRNL        AUTH   G.E.BORGSTAHL,M.POKROSS,R.CHEHAB,A.SEKHER,E.H.SNELL          
JRNL        TITL   CRYO-TRAPPING THE SIX-COORDINATE, DISTORTED-OCTAHEDRAL       
JRNL        TITL 2 ACTIVE SITE OF MANGANESE SUPEROXIDE DISMUTASE.               
JRNL        REF    J.MOL.BIOL.                   V. 296   951 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10686094                                                     
JRNL        DOI    10.1006/JMBI.1999.3506                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 114969                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5% RANDOM                       
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 6092                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 1085                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.21                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1D5N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009813.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135855                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.50                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.55500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.55500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.55500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.65000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.55500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.65000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.55500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.55500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.65000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.55500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.55500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.65000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2468  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C2461  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  89      132.38    175.80                                   
REMARK 500    ASN A 145     -117.86     47.13                                   
REMARK 500    TYR A 173       -5.11   -142.09                                   
REMARK 500    GLN A 178     -131.21     51.60                                   
REMARK 500    GLN B  95     -169.27   -172.64                                   
REMARK 500    ASN B 145     -120.51     48.29                                   
REMARK 500    GLN B 178     -130.47     52.85                                   
REMARK 500    HIS C  17      -60.12    -91.00                                   
REMARK 500    LEU C  45       70.46   -115.91                                   
REMARK 500    LYS C  89      135.25    176.92                                   
REMARK 500    ASN C 145     -114.69     46.69                                   
REMARK 500    TYR C 173       -0.32   -145.36                                   
REMARK 500    GLN C 178     -128.64     53.70                                   
REMARK 500    LYS D  89      136.19    177.49                                   
REMARK 500    ASN D 145     -120.82     49.52                                   
REMARK 500    TYR D 173       -0.57   -147.96                                   
REMARK 500    GLN D 178     -128.81     51.61                                   
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 A2421        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A2430        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH A2446        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A2447        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A2460        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH B2422        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH B2430        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH B2440        DISTANCE =  7.33 ANGSTROMS                       
REMARK 525    HOH B2446        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B2450        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH B2454        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH C2433        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH C2437        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH C2450        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH C2460        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH D2440        DISTANCE =  5.29 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 A2206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2479   O                                                      
REMARK 620 2 HOH A2478   O    87.7                                              
REMARK 620 3 HIS A  26   NE2 100.3 171.8                                        
REMARK 620 4 ASP A 167   OD2 166.6  86.1  86.6                                  
REMARK 620 5 HIS A  81   NE2  63.6  91.8  93.5 104.8                            
REMARK 620 6 HIS A 171   NE2  79.1  92.1  87.5 112.9 142.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2207  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2471   O                                                      
REMARK 620 2 HOH B2472   O    93.3                                              
REMARK 620 3 HIS B  26   NE2 169.6  94.5                                        
REMARK 620 4 HIS B  81   NE2  97.0  66.5  92.4                                  
REMARK 620 5 ASP B 167   OD2  84.8 176.1  87.8 110.3                            
REMARK 620 6 HIS B 171   NE2  88.9  69.9  87.4 136.3 113.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C2208  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2475   O                                                      
REMARK 620 2 HOH C2476   O    95.6                                              
REMARK 620 3 HIS C  81   NE2  92.2  69.2                                        
REMARK 620 4 HIS C 171   NE2  91.6  73.1 142.2                                  
REMARK 620 5 HIS C  26   NE2 171.4  92.9  92.3  89.3                            
REMARK 620 6 ASP C 167   OD2  85.8 176.3 107.3 110.4  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2209  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D2488   O                                                      
REMARK 620 2 HOH D2487   O    95.0                                              
REMARK 620 3 ASP D 167   OD2 173.5  84.9                                        
REMARK 620 4 HIS D 171   NE2  71.7  89.7 114.7                                  
REMARK 620 5 HIS D  26   NE2  93.4 171.2  87.0  90.6                            
REMARK 620 6 HIS D  81   NE2  65.2  90.5 108.3 136.8  95.3                      
REMARK 620 N                    1     2     3     4     5                       
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 2206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 2208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 2209                 
DBREF  1D5N A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1D5N B    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1D5N C    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1D5N D    1   205  UNP    P00448   SODM_ECOLI       1    205             
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 TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 A  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 A  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 B  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 B  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 B  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 B  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 B  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 B  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 B  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 B  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 B  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 B  205  ALA ASN 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 TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 B  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 B  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 C  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 C  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 C  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 C  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 C  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 C  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 C  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 C  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 C  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 C  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 C  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 C  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 C  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 C  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 C  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 C  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 D  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 D  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 D  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 D  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 D  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 D  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 D  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 D  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 D  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 D  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 D  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 D  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 D  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 D  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 D  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 D  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
HET     MN  A2206       1                                                       
HET     MN  B2207       1                                                       
HET     MN  C2208       1                                                       
HET     MN  D2209       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *1085(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  204  1                                  12    
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  VAL B  192  1                                  13    
HELIX   30  30 ASN B  193  LYS B  204  1                                  12    
HELIX   31  31 ASP C   19  LYS C   29  1                                  11    
HELIX   32  32 LYS C   29  GLU C   43  1                                  15    
HELIX   33  33 LEU C   45  ASN C   50  1                                   6    
HELIX   34  34 PRO C   52  ILE C   57  1                                   6    
HELIX   35  35 THR C   58  LEU C   63  5                                   6    
HELIX   36  36 PRO C   64  ASP C   66  5                                   3    
HELIX   37  37 LYS C   67  GLY C   87  1                                  21    
HELIX   38  38 GLN C   95  GLY C  107  1                                  13    
HELIX   39  39 SER C  108  ARG C  123  1                                  16    
HELIX   40  40 SER C  148  MET C  151  5                                   4    
HELIX   41  41 GLY C  152  GLY C  157  1                                   6    
HELIX   42  42 TRP C  169  ALA C  172  5                                   4    
HELIX   43  43 TYR C  173  GLN C  178  1                                   6    
HELIX   44  44 ARG C  180  VAL C  192  1                                  13    
HELIX   45  45 ASN C  193  LYS C  204  1                                  12    
HELIX   46  46 ASP D   19  LYS D   29  1                                  11    
HELIX   47  47 LYS D   29  GLU D   43  1                                  15    
HELIX   48  48 LEU D   45  ASN D   50  1                                   6    
HELIX   49  49 PRO D   52  ILE D   57  1                                   6    
HELIX   50  50 THR D   58  LEU D   63  5                                   6    
HELIX   51  51 LYS D   67  GLY D   87  1                                  21    
HELIX   52  52 GLN D   95  GLY D  107  1                                  13    
HELIX   53  53 SER D  108  ARG D  123  1                                  16    
HELIX   54  54 SER D  148  MET D  151  5                                   4    
HELIX   55  55 GLY D  152  GLY D  157  1                                   6    
HELIX   56  56 TRP D  169  ALA D  172  5                                   4    
HELIX   57  57 TYR D  173  GLN D  178  1                                   6    
HELIX   58  58 ARG D  180  VAL D  192  1                                  13    
HELIX   59  59 ASN D  193  LYS D  204  1                                  12    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  N  TRP A 128   O  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  N  TRP B 128   O  THR B 143           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  N  PHE B 161   O  LEU B 133           
SHEET    1   C 3 LYS C 137  ALA C 144  0                                        
SHEET    2   C 3 GLY C 127  LYS C 134 -1  O  TRP C 128   N  THR C 143           
SHEET    3   C 3 PHE C 161  ASP C 167 -1  N  PHE C 161   O  LEU C 133           
SHEET    1   D 3 LYS D 137  ALA D 144  0                                        
SHEET    2   D 3 GLY D 127  LYS D 134 -1  O  TRP D 128   N  THR D 143           
SHEET    3   D 3 PHE D 161  ASP D 167 -1  N  PHE D 161   O  LEU D 133           
LINK        MN    MN A2206                 O   HOH A2479     1555   1555  2.42  
LINK        MN    MN A2206                 O   HOH A2478     1555   1555  2.21  
LINK        MN    MN B2207                 O   HOH B2471     1555   1555  2.20  
LINK        MN    MN B2207                 O   HOH B2472     1555   1555  2.44  
LINK        MN    MN C2208                 O   HOH C2475     1555   1555  2.19  
LINK        MN    MN C2208                 O   HOH C2476     1555   1555  2.42  
LINK        MN    MN D2209                 O   HOH D2488     1555   1555  2.45  
LINK        MN    MN D2209                 O   HOH D2487     1555   1555  2.17  
LINK        MN    MN A2206                 NE2 HIS A  26     1555   1555  2.15  
LINK        MN    MN A2206                 OD2 ASP A 167     1555   1555  2.00  
LINK        MN    MN A2206                 NE2 HIS A  81     1555   1555  2.16  
LINK        MN    MN A2206                 NE2 HIS A 171     1555   1555  2.18  
LINK        MN    MN B2207                 NE2 HIS B  26     1555   1555  2.18  
LINK        MN    MN B2207                 NE2 HIS B  81     1555   1555  2.20  
LINK        MN    MN B2207                 OD2 ASP B 167     1555   1555  2.01  
LINK        MN    MN B2207                 NE2 HIS B 171     1555   1555  2.22  
LINK        MN    MN C2208                 NE2 HIS C  81     1555   1555  2.21  
LINK        MN    MN C2208                 NE2 HIS C 171     1555   1555  2.20  
LINK        MN    MN C2208                 NE2 HIS C  26     1555   1555  2.21  
LINK        MN    MN C2208                 OD2 ASP C 167     1555   1555  2.05  
LINK        MN    MN D2209                 OD2 ASP D 167     1555   1555  2.09  
LINK        MN    MN D2209                 NE2 HIS D 171     1555   1555  2.18  
LINK        MN    MN D2209                 NE2 HIS D  26     1555   1555  2.22  
LINK        MN    MN D2209                 NE2 HIS D  81     1555   1555  2.18  
CISPEP   1 GLU A   15    PRO A   16          0         0.02                     
CISPEP   2 GLU B   15    PRO B   16          0         0.59                     
CISPEP   3 GLU C   15    PRO C   16          0        -0.13                     
CISPEP   4 GLU D   15    PRO D   16          0         0.20                     
SITE     1 AC1  6 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC1  6 HOH A2478  HOH A2479                                          
SITE     1 AC2  6 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC2  6 HOH B2471  HOH B2472                                          
SITE     1 AC3  6 HIS C  26  HIS C  81  ASP C 167  HIS C 171                    
SITE     2 AC3  6 HOH C2475  HOH C2476                                          
SITE     1 AC4  6 HIS D  26  HIS D  81  ASP D 167  HIS D 171                    
SITE     2 AC4  6 HOH D2487  HOH D2488                                          
CRYST1   99.110  107.300  179.110  90.00  90.00  90.00 C 2 2 21     32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010090  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009320  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005583        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system