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Database: PDB
Entry: 3K9S
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Original site: 3K9S 
HEADER    OXIDOREDUCTASE                          16-OCT-09   3K9S              
TITLE     CRYSTAL STRUCTURE OF THE PEROXIDE-BOUND MANGANESE SUPEROXIDE          
TITLE    2 DISMUTASE.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B3908, JW3879, SODA;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: OX326A.1;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTTQA10                                   
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, PEROXIDE-BOUND, MANGANESE, METAL-     
KEYWDS   2 BINDING, OXIDOREDUCTASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.PORTA,A.VAHEDI-FARIDI,G.E.O.BORGSTAHL                             
REVDAT   2   18-AUG-10 3K9S    1       JRNL                                     
REVDAT   1   12-MAY-10 3K9S    0                                                
JRNL        AUTH   J.PORTA,A.VAHEDI-FARIDI,G.E.BORGSTAHL                        
JRNL        TITL   STRUCTURAL ANALYSIS OF PEROXIDE-SOAKED MNSOD CRYSTALS        
JRNL        TITL 2 REVEALS SIDE-ON BINDING OF PEROXIDE TO ACTIVE-SITE           
JRNL        TITL 3 MANGANESE.                                                   
JRNL        REF    J.MOL.BIOL.                   V. 399   377 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20417642                                                     
JRNL        DOI    10.1016/J.JMB.2010.04.031                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 118082                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6254                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6479                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 373                          
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
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          : 10                                      
REMARK   3   SOLVENT ATOMS            : 478                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 6.29                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : 0.83000                                              
REMARK   3    B33 (A**2) : -0.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.133         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.072         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.316         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.862                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.830                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6725 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9091 ; 1.323 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   818 ; 5.874 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   324 ;34.302 ;24.568       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1085 ;14.158 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;10.799 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   949 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5200 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4089 ; 0.783 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6510 ; 1.110 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2636 ; 1.809 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2580 ; 2.408 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6725 ; 1.106 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   481 ; 4.733 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6523 ; 2.264 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3K9S COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055725.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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) : 1.08                               
REMARK 200  MONOCHROMATOR                  : VERTICAL FOCUSING MIRROR SINGLE    
REMARK 200                                   CRYSTAL (SI111) BENT               
REMARK 200                                   MONOCHROMATOR (HORIZONTAL          
REMARK 200                                   FOCUSING)                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139669                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08220                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
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) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1D5N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BICINE PH 8.5, 25% PEG 6000,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
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       90.02200            
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       90.02200            
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       50.42450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.70900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.42450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.70900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.02200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.42450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.70900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.02200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.42450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.70900            
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: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17580 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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17410 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 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   O    ALA B   203     N    LYS B   205              1.26            
REMARK 500   O    ASP B    97     N    LYS B    99              1.28            
REMARK 500   C    PRO B    64     O    HOH B   244              1.80            
REMARK 500   CD1  LEU C    14     CE   MET C    23              1.84            
REMARK 500   OD1  ASP C    61     O    HOH C   429              1.96            
REMARK 500   N    ALA B    65     O    HOH B   244              1.98            
REMARK 500   CD1  LEU D     4     O    HOH D   365              2.08            
REMARK 500   O    ALA B   203     O    LYS B   205              2.09            
REMARK 500   OE1  GLU B   117     O    HOH B   243              2.13            
REMARK 500   O    HOH C   265     O    HOH C   472              2.15            
REMARK 500   O    ALA D   202     CD   LYS D   204              2.17            
REMARK 500   CG   GLU D    47     O    HOH D   253              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C   447     O    HOH C   447     3755     1.24            
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    ASN A 145     -120.29     57.50                                   
REMARK 500    TYR A 173       -7.86   -142.90                                   
REMARK 500    GLN A 178     -130.25     40.82                                   
REMARK 500    LYS A 204       -6.93     75.80                                   
REMARK 500    HIS B  17      -63.24    -90.74                                   
REMARK 500    LYS B  29      -60.20   -109.48                                   
REMARK 500    ALA B  65      -61.95     29.37                                   
REMARK 500    LYS B  89      139.18    179.63                                   
REMARK 500    GLN B  95     -163.87   -168.04                                   
REMARK 500    LEU B  98       25.28    -27.98                                   
REMARK 500    ILE B 102      -76.59    -61.62                                   
REMARK 500    GLU B 103       37.22    -83.45                                   
REMARK 500    ASP B 105      -31.91   -134.53                                   
REMARK 500    PHE B 106     -161.42   -117.24                                   
REMARK 500    LYS B 137      112.84    150.18                                   
REMARK 500    ASN B 145     -125.37     55.95                                   
REMARK 500    TYR B 173       -5.04   -141.52                                   
REMARK 500    GLN B 178     -128.71     39.34                                   
REMARK 500    PHE B 201      -11.36    -42.50                                   
REMARK 500    ALA B 203        0.58    -59.60                                   
REMARK 500    LYS B 204      -38.03     14.10                                   
REMARK 500    LYS C  29      -64.41   -107.68                                   
REMARK 500    LYS C  89      136.97   -173.40                                   
REMARK 500    ASN C 145     -125.46     54.93                                   
REMARK 500    TYR C 173       -1.57   -141.85                                   
REMARK 500    GLN C 178     -124.48     46.71                                   
REMARK 500    HIS D  17      -60.39    -91.01                                   
REMARK 500    LYS D  29      -63.24   -109.74                                   
REMARK 500    ASN D 145     -122.38     55.76                                   
REMARK 500    TYR D 173       -4.99   -146.84                                   
REMARK 500    GLN D 178     -126.54     34.52                                   
REMARK 500    ARG D 180       57.75    -90.09                                   
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 ASP A 167   OD2                                                    
REMARK 620 2 HOH A 207   O   170.1                                              
REMARK 620 3 HOH A 208   O    88.8  99.0                                        
REMARK 620 4 HIS A  26   NE2  89.5  83.3 174.0                                  
REMARK 620 5 HIS A  81   NE2  98.2  75.6  90.8  95.1                            
REMARK 620 6 HIS A 171   NE2 109.9  76.3  90.8  84.3 151.8                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP B 167   OD2                                                    
REMARK 620 2 PEO B 207   O1   85.0                                              
REMARK 620 3 HOH B 208   O    92.7   8.9                                        
REMARK 620 4 HIS B 171   NE2 111.3  86.7  87.9                                  
REMARK 620 5 HIS B  81   NE2 106.3  99.4  93.1 142.3                            
REMARK 620 6 HIS B  26   NE2  85.9 169.0 177.7  90.9  89.1                      
REMARK 620 7 PEO B 207   O2  119.8  34.8  27.6  73.8  90.1 153.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 167   OD2                                                    
REMARK 620 2 PEO C 207   O2   78.3                                              
REMARK 620 3 PEO C 207   O1   92.3  40.6                                        
REMARK 620 4 HOH C 209   O    83.2  27.0  14.6                                  
REMARK 620 5 HOH C 208   O   176.2  98.2  84.1  93.0                            
REMARK 620 6 HIS C 171   NE2 109.9 115.5  75.0  88.8  70.4                      
REMARK 620 7 HIS C  81   NE2 103.5  71.8 105.0  96.1  76.4 146.7                
REMARK 620 8 HIS C  26   NE2  86.3 154.0 162.8 168.1  97.4  89.4  91.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 167   OD2                                                    
REMARK 620 2 PEO D 208   O2  119.1                                              
REMARK 620 3 PEO D 208   O1   83.1  36.0                                        
REMARK 620 4 HOH D 209   O    88.2  31.0   5.1                                  
REMARK 620 5 HIS D  26   NE2  88.8 151.6 168.5 170.5                            
REMARK 620 6 HIS D 171   NE2 116.2  78.6  91.7  88.7  84.5                      
REMARK 620 7 HIS D  81   NE2 106.5  82.9  95.5  94.9  94.6 137.2                
REMARK 620 N                    1     2     3     4     5     6                 
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO B 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO C 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO D 208                 
DBREF  3K9S A    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3K9S B    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3K9S C    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3K9S D    1   205  UNP    P00448   SODM_ECOLI       2    206             
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  A 206       1                                                       
HET     MN  B 206       1                                                       
HET    PEO  B 207       2                                                       
HET     MN  C 206       1                                                       
HET    PEO  C 207       2                                                       
HET     MN  D 206       1                                                       
HET    PEO  D 208       2                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PEO HYDROGEN PEROXIDE                                                
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  PEO    3(H2 O2)                                                     
FORMUL  12  HOH   *478(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 LYS A   67  GLY A   87  1                                  21    
HELIX    6   6 GLN A   95  GLY A  107  1                                  13    
HELIX    7   7 SER A  108  ARG A  123  1                                  16    
HELIX    8   8 SER A  148  MET A  151  5                                   4    
HELIX    9   9 GLY A  152  GLY A  157  1                                   6    
HELIX   10  10 TRP A  169  ALA A  172  5                                   4    
HELIX   11  11 TYR A  173  GLN A  178  1                                   6    
HELIX   12  12 ARG A  180  TRP A  189  1                                  10    
HELIX   13  13 ASN A  193  LYS A  204  1                                  12    
HELIX   14  14 ASP B   19  LYS B   29  1                                  11    
HELIX   15  15 LYS B   29  GLU B   43  1                                  15    
HELIX   16  16 LEU B   45  ASN B   50  1                                   6    
HELIX   17  17 PRO B   52  ILE B   57  1                                   6    
HELIX   18  18 THR B   58  LEU B   63  5                                   6    
HELIX   19  19 PRO B   64  ASP B   66  5                                   3    
HELIX   20  20 LYS B   67  GLY B   87  1                                  21    
HELIX   21  21 SER B  108  ARG B  123  1                                  16    
HELIX   22  22 SER B  148  MET B  151  5                                   4    
HELIX   23  23 GLY B  152  GLY B  157  1                                   6    
HELIX   24  24 TRP B  169  ALA B  172  5                                   4    
HELIX   25  25 TYR B  173  GLN B  178  1                                   6    
HELIX   26  26 ARG B  180  VAL B  192  1                                  13    
HELIX   27  27 ASN B  193  LYS B  204  1                                  12    
HELIX   28  28 ASP C   19  LYS C   29  1                                  11    
HELIX   29  29 LYS C   29  GLU C   43  1                                  15    
HELIX   30  30 LEU C   45  ASN C   50  1                                   6    
HELIX   31  31 PRO C   52  ILE C   57  1                                   6    
HELIX   32  32 THR C   58  LEU C   63  5                                   6    
HELIX   33  33 PRO C   64  ASP C   66  5                                   3    
HELIX   34  34 LYS C   67  GLY C   87  1                                  21    
HELIX   35  35 GLN C   95  GLY C  107  1                                  13    
HELIX   36  36 SER C  108  ARG C  123  1                                  16    
HELIX   37  37 SER C  148  MET C  151  5                                   4    
HELIX   38  38 GLY C  152  GLY C  157  1                                   6    
HELIX   39  39 TRP C  169  ALA C  172  5                                   4    
HELIX   40  40 TYR C  173  GLN C  178  1                                   6    
HELIX   41  41 ARG C  180  VAL C  192  1                                  13    
HELIX   42  42 ASN C  193  LYS C  204  1                                  12    
HELIX   43  43 ASP D   19  LYS D   29  1                                  11    
HELIX   44  44 LYS D   29  GLU D   43  1                                  15    
HELIX   45  45 LEU D   45  ASN D   50  1                                   6    
HELIX   46  46 PRO D   52  ILE D   57  1                                   6    
HELIX   47  47 THR D   58  LEU D   63  5                                   6    
HELIX   48  48 PRO D   64  ASP D   66  5                                   3    
HELIX   49  49 LYS D   67  GLY D   87  1                                  21    
HELIX   50  50 GLN D   95  GLY D  107  1                                  13    
HELIX   51  51 SER D  108  ARG D  123  1                                  16    
HELIX   52  52 SER D  148  MET D  151  5                                   4    
HELIX   53  53 GLY D  152  GLY D  157  1                                   6    
HELIX   54  54 TRP D  169  ALA D  172  5                                   4    
HELIX   55  55 TYR D  173  GLN D  178  1                                   6    
HELIX   56  56 ARG D  180  TRP D  189  1                                  10    
HELIX   57  57 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 130   O  VAL A 141           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  O  ILE A 163   N  LEU A 131           
SHEET    1   B 3 LEU B 138  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LEU B 133 -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           
SHEET    1   C 3 LYS C 137  ALA C 144  0                                        
SHEET    2   C 3 GLY C 127  LYS C 134 -1  N  VAL C 132   O  ALA C 139           
SHEET    3   C 3 PHE C 161  ASP C 167 -1  O  ILE C 163   N  LEU C 131           
SHEET    1   D 3 LYS D 137  ALA D 144  0                                        
SHEET    2   D 3 GLY D 127  LYS D 134 -1  N  TRP D 130   O  VAL D 141           
SHEET    3   D 3 PHE D 161  ASP D 167 -1  O  ILE D 163   N  LEU D 131           
LINK         OD2 ASP A 167                MN    MN A 206     1555   1555  1.95  
LINK         OD2 ASP B 167                MN    MN B 206     1555   1555  1.96  
LINK         OD2 ASP C 167                MN    MN C 206     1555   1555  1.94  
LINK         OD2 ASP D 167                MN    MN D 206     1555   1555  1.95  
LINK        MN    MN B 206                 O1  PEO B 207     1555   1555  2.09  
LINK        MN    MN C 206                 O2  PEO C 207     1555   1555  2.10  
LINK        MN    MN C 206                 O1  PEO C 207     1555   1555  2.09  
LINK        MN    MN D 206                 O2  PEO D 208     1555   1555  2.49  
LINK        MN    MN D 206                 O1  PEO D 208     1555   1555  2.09  
LINK        MN    MN A 206                 O   HOH A 207     1555   1555  2.23  
LINK        MN    MN A 206                 O   HOH A 208     1555   1555  2.37  
LINK        MN    MN B 206                 O   HOH B 208     1555   1555  2.11  
LINK        MN    MN C 206                 O   HOH C 209     1555   1555  2.25  
LINK        MN    MN C 206                 O   HOH C 208     1555   1555  2.35  
LINK        MN    MN D 206                 O   HOH D 209     1555   1555  2.21  
LINK         NE2 HIS D  26                MN    MN D 206     1555   1555  2.06  
LINK         NE2 HIS A  26                MN    MN A 206     1555   1555  2.06  
LINK         NE2 HIS D 171                MN    MN D 206     1555   1555  2.07  
LINK         NE2 HIS D  81                MN    MN D 206     1555   1555  2.07  
LINK         NE2 HIS B 171                MN    MN B 206     1555   1555  2.07  
LINK         NE2 HIS A  81                MN    MN A 206     1555   1555  2.07  
LINK         NE2 HIS B  81                MN    MN B 206     1555   1555  2.08  
LINK         NE2 HIS C 171                MN    MN C 206     1555   1555  2.09  
LINK         NE2 HIS C  81                MN    MN C 206     1555   1555  2.09  
LINK         NE2 HIS C  26                MN    MN C 206     1555   1555  2.09  
LINK         NE2 HIS B  26                MN    MN B 206     1555   1555  2.10  
LINK         NE2 HIS A 171                MN    MN A 206     1555   1555  2.11  
LINK        MN    MN B 206                 O2  PEO B 207     1555   1555  2.58  
CISPEP   1 GLU A   15    PRO A   16          0         3.78                     
CISPEP   2 GLU B   15    PRO B   16          0         1.22                     
CISPEP   3 GLU C   15    PRO C   16          0         4.27                     
CISPEP   4 GLU D   15    PRO D   16          0         3.88                     
SITE     1 AC1  6 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC1  6 HOH A 207  HOH A 208                                          
SITE     1 AC2  6 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC2  6 PEO B 207  HOH B 208                                          
SITE     1 AC3  8 TYR B  34  HIS B  81  GLN B 146  ASP B 167                    
SITE     2 AC3  8 TRP B 169  HIS B 171   MN B 206  HOH B 208                    
SITE     1 AC4  7 HIS C  26  HIS C  81  ASP C 167  HIS C 171                    
SITE     2 AC4  7 PEO C 207  HOH C 208  HOH C 209                               
SITE     1 AC5  9 HIS C  81  TRP C 128  GLN C 146  ASP C 167                    
SITE     2 AC5  9 TRP C 169  HIS C 171   MN C 206  HOH C 208                    
SITE     3 AC5  9 HOH C 209                                                     
SITE     1 AC6  6 HIS D  26  HIS D  81  ASP D 167  HIS D 171                    
SITE     2 AC6  6 PEO D 208  HOH D 209                                          
SITE     1 AC7  8 TYR D  34  HIS D  81  GLN D 146  ASP D 167                    
SITE     2 AC7  8 TRP D 169  HIS D 171   MN D 206  HOH D 209                    
CRYST1  100.849  107.418  180.044  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      0.009916  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009309  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005554        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system