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Database: PDB
Entry: 3KKY
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Original site: 3KKY 
HEADER    METAL BINDING PROTEIN                   06-NOV-09   3KKY              
TITLE     STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM DEINOCOCCUS          
TITLE    2 RADIODURANS IN THE ORTHORHOMBIC SPACE GROUP P212121: A CASE STUDY OF 
TITLE    3 MISTAKEN IDENTITY                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 1299;                                                
SOURCE   4 GENE: SODA, DR_1279;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: QC774;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET31F1(-)                                
KEYWDS    SUPEROXIDE DISMUTASE, DEINOCOCCUS RADIODURANS, MANGANESE, METAL-      
KEYWDS   2 BINDING, OXIDOREDUCTASE, METAL BINDING PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.GOVINDASAMY,R.MIKULSKI,M.A.MCKENNA,D.N.SILVERMAN,R.MCKENNA          
REVDAT   1   03-NOV-10 3KKY    0                                                
JRNL        AUTH   L.GOVINDASAMY,R.MIKULSKI,M.A.MCKENNA,D.N.SILVERMAN,R.MCKENNA 
JRNL        TITL   STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM DEINOCOCCUS 
JRNL        TITL 2 RADIODURANS IN THE ORTHORHOMBIC SPACE GROUP P212121: A CASE  
JRNL        TITL 3 STUDY OF MISTAKEN IDENTITY                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 34999                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1758                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2434                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 127                          
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3228                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 162                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.132         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.208         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3359 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4577 ; 1.355 ; 1.917       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   416 ; 5.301 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;36.309 ;24.831       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   516 ;14.857 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.848 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   474 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2671 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1334 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2319 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   122 ; 0.103 ; 0.200       
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):    19 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.965 ; 0.200       
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):  2100 ; 0.994 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3270 ; 1.636 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1470 ; 2.468 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1303 ; 3.902 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3KKY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056121.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34999                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 24.800                             
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
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 2CE4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M K2PO4, 16% PEG, PH 7.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       30.07500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.70500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.70500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.07500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.12000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     GLN A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     GLN A    93                                                      
REMARK 465     ASN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     GLN B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     GLN B    93                                                      
REMARK 465     ASN B    94                                                      
REMARK 465     GLY B    95                                                      
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 150     -121.98     54.26                                   
REMARK 500    TYR A 178       -7.50   -142.65                                   
REMARK 500    GLN A 183     -128.74     51.94                                   
REMARK 500    ASN B 150     -122.38     56.45                                   
REMARK 500    GLN B 183     -129.06     43.08                                   
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 211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 172   OD2                                                    
REMARK 620 2 HOH A 292   O    85.6                                              
REMARK 620 3 HIS A  26   NE2  84.3 169.3                                        
REMARK 620 4 HIS A 176   NE2 118.2  90.7  91.2                                  
REMARK 620 5 HIS A  80   NE2 110.3  92.8  93.9 131.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 172   OD2                                                    
REMARK 620 2 HOH B 291   O    84.5                                              
REMARK 620 3 HIS B  26   NE2  87.2 171.8                                        
REMARK 620 4 HIS B 176   NE2 117.7  90.6  92.9                                  
REMARK 620 5 HIS B  80   NE2 111.3  91.9  91.5 131.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 211                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 211                  
DBREF  3KKY A    0   210  UNP    Q9RUV2   SODM_DEIRA       1    211             
DBREF  3KKY B    0   210  UNP    Q9RUV2   SODM_DEIRA       1    211             
SEQRES   1 A  211  MET ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR ASP          
SEQRES   2 A  211  ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU ILE          
SEQRES   3 A  211  HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN ALA          
SEQRES   4 A  211  ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU PRO          
SEQRES   5 A  211  VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO ALA          
SEQRES   6 A  211  ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 A  211  ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN GLY          
SEQRES   8 A  211  GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU LEU          
SEQRES   9 A  211  LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP ALA          
SEQRES  10 A  211  PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG PHE          
SEQRES  11 A  211  GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY LYS          
SEQRES  12 A  211  LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO LEU          
SEQRES  13 A  211  MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO ILE          
SEQRES  14 A  211  LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU ASN          
SEQRES  15 A  211  TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE TRP          
SEQRES  16 A  211  ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR ALA          
SEQRES  17 A  211  ALA ALA LYS                                                  
SEQRES   1 B  211  MET ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR ASP          
SEQRES   2 B  211  ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU ILE          
SEQRES   3 B  211  HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN ALA          
SEQRES   4 B  211  ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU PRO          
SEQRES   5 B  211  VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO ALA          
SEQRES   6 B  211  ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  211  ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN GLY          
SEQRES   8 B  211  GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU LEU          
SEQRES   9 B  211  LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP ALA          
SEQRES  10 B  211  PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG PHE          
SEQRES  11 B  211  GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY LYS          
SEQRES  12 B  211  LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO LEU          
SEQRES  13 B  211  MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO ILE          
SEQRES  14 B  211  LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU ASN          
SEQRES  15 B  211  TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE TRP          
SEQRES  16 B  211  ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR ALA          
SEQRES  17 B  211  ALA ALA LYS                                                  
HET     MN  A 211       1                                                       
HET     MN  B 211       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *162(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   51  ILE A   56  1                                   6    
HELIX    4   4 PRO A   63  ASP A   65  5                                   3    
HELIX    5   5 LYS A   66  ILE A   86  1                                  21    
HELIX    6   6 SER A  100  GLY A  112  1                                  13    
HELIX    7   7 SER A  113  ARG A  128  1                                  16    
HELIX    8   8 ASN A  153  MET A  156  5                                   4    
HELIX    9   9 GLY A  157  GLY A  162  1                                   6    
HELIX   10  10 TRP A  174  ALA A  177  5                                   4    
HELIX   11  11 TYR A  178  GLN A  183  1                                   6    
HELIX   12  12 ARG A  185  TRP A  194  1                                  10    
HELIX   13  13 ASN A  195  VAL A  197  5                                   3    
HELIX   14  14 ASN A  198  LYS A  210  1                                  13    
HELIX   15  15 ASP B   19  LYS B   29  1                                  11    
HELIX   16  16 LYS B   29  GLU B   43  1                                  15    
HELIX   17  17 PRO B   51  ILE B   56  1                                   6    
HELIX   18  18 GLN B   57  VAL B   62  5                                   6    
HELIX   19  19 LYS B   66  ILE B   86  1                                  21    
HELIX   20  20 SER B  100  GLY B  112  1                                  13    
HELIX   21  21 SER B  113  ARG B  128  1                                  16    
HELIX   22  22 ASN B  153  MET B  156  5                                   4    
HELIX   23  23 GLY B  157  GLY B  162  1                                   6    
HELIX   24  24 TRP B  174  ALA B  177  5                                   4    
HELIX   25  25 TYR B  178  GLN B  183  1                                   6    
HELIX   26  26 ARG B  185  TRP B  194  1                                  10    
HELIX   27  27 ASN B  195  VAL B  197  5                                   3    
HELIX   28  28 ASN B  198  LYS B  210  1                                  13    
SHEET    1   A 3 LYS A 142  ALA A 149  0                                        
SHEET    2   A 3 GLY A 132  LYS A 139 -1  N  TRP A 135   O  VAL A 146           
SHEET    3   A 3 THR A 166  ASP A 172 -1  O  ILE A 168   N  LEU A 136           
SHEET    1   B 3 LYS B 142  ALA B 149  0                                        
SHEET    2   B 3 GLY B 132  LYS B 139 -1  N  TRP B 135   O  VAL B 146           
SHEET    3   B 3 THR B 166  ASP B 172 -1  O  ILE B 168   N  LEU B 136           
LINK         OD2 ASP A 172                MN    MN A 211     1555   1555  2.02  
LINK         OD2 ASP B 172                MN    MN B 211     1555   1555  2.03  
LINK        MN    MN A 211                 O   HOH A 292     1555   1555  2.19  
LINK        MN    MN B 211                 O   HOH B 291     1555   1555  2.25  
LINK         NE2 HIS A  26                MN    MN A 211     1555   1555  2.15  
LINK         NE2 HIS B  26                MN    MN B 211     1555   1555  2.16  
LINK         NE2 HIS B 176                MN    MN B 211     1555   1555  2.17  
LINK         NE2 HIS B  80                MN    MN B 211     1555   1555  2.21  
LINK         NE2 HIS A 176                MN    MN A 211     1555   1555  2.23  
LINK         NE2 HIS A  80                MN    MN A 211     1555   1555  2.23  
CISPEP   1 GLU A   15    PRO A   16          0        -1.95                     
CISPEP   2 GLU B   15    PRO B   16          0         4.85                     
SITE     1 AC1  5 HIS A  26  HIS A  80  ASP A 172  HIS A 176                    
SITE     2 AC1  5 HOH A 292                                                     
SITE     1 AC2  5 HIS B  26  HIS B  80  ASP B 172  HIS B 176                    
SITE     2 AC2  5 HOH B 291                                                     
CRYST1   60.150   80.240   85.410  90.00  90.00  90.00 P 21 21 21    8          
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      0.016626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011709        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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