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Database: PDB
Entry: 1XRE
LinkDB: 1XRE
Original site: 1XRE 
HEADER    OXIDOREDUCTASE                          14-OCT-04   1XRE              
TITLE     CRYSTAL STRUCTURE OF SODA-2 (BA5696) FROM BACILLUS                    
TITLE    2 ANTHRACIS AT 1.8A RESOLUTION.                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SODA-2;                                                     
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 1392;                                                
SOURCE   4 GENE: SODA2, SODA-2;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-YSBLIC                                
KEYWDS    SODA-2; SUPEROXIDE DISMUTASE; BACILLUS ANTHRACIS; BA5696;             
KEYWDS   2 SPINE, OXIDOREDUCTASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.W.BOUCHER,V.M.LEVDIKOV,E.V.BLAGOVA,M.J.FOGG,J.A.BRANNIGAN,          
AUTHOR   2 A.J.WILKINSON,K.S.WILSON                                             
REVDAT   2   24-FEB-09 1XRE    1       VERSN                                    
REVDAT   1   19-JUL-05 1XRE    0                                                
JRNL        AUTH   I.W.BOUCHER,A.K.KALLIOMAA,V.M.LEVDIKOV,E.V.BLAGOVA,          
JRNL        AUTH 2 M.J.FOGG,J.A.BRANNIGAN,K.S.WILSON,A.J.WILKINSON              
JRNL        TITL   STRUCTURES OF TWO SUPEROXIDE DISMUTASES FROM                 
JRNL        TITL 2 BACILLUS ANTHRACIS REVEAL A NOVEL ACTIVE CENTRE.             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  61   621 2005              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   16511113                                                     
JRNL        DOI    10.1107/S1744309105017380                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 29.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 35719                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1879                            
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) : 2526                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3284                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 374                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.09000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.334         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.611         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3388 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2866 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4606 ; 1.444 ; 1.932       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6698 ; 0.910 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   400 ; 6.410 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;38.477 ;24.889       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   538 ;15.443 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;12.473 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   482 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3798 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   690 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   713 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2806 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1649 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1670 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   225 ; 0.164 ; 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):    12 ; 0.168 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.249 ; 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):  2598 ; 1.883 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   816 ; 0.697 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3228 ; 2.488 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1688 ; 3.957 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1378 ; 5.077 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  7849 ; 3.293 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   375 ; 6.776 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6152 ; 2.851 ; 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   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1XRE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030677.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87000                            
REMARK 200  MONOCHROMATOR                  : SI MONOCHROMATOR                   
REMARK 200  OPTICS                         : RH COATED SI MIRROR                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37730                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.3300                            
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     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.940                              
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 1JR9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGCL2, TRIS, PH 8.0,           
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.93300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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     GLY A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     GLN A   206                                                      
REMARK 465     LYS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLN B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     GLN B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     HIS B   208                                                      
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 111      -55.64     71.08                                   
REMARK 500    ASN A 149     -126.88     57.42                                   
REMARK 500    GLN A 176     -129.00     48.78                                   
REMARK 500    GLU B  63      -19.84    -48.26                                   
REMARK 500    ASN B 111      -53.87     77.08                                   
REMARK 500    ASP B 138       75.35   -118.60                                   
REMARK 500    ASN B 149     -124.72     56.18                                   
REMARK 500    TYR B 171       -4.05   -144.16                                   
REMARK 500    GLN B 176     -128.37     45.92                                   
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 209  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   OD2                                                    
REMARK 620 2 HOH A 388   O    88.5                                              
REMARK 620 3 HIS A  28   NE2  88.0 175.7                                        
REMARK 620 4 HIS A  83   NE2 112.2  90.3  93.2                                  
REMARK 620 5 HIS A 169   NE2 120.5  89.3  90.5 127.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 209  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 165   OD2                                                    
REMARK 620 2 HOH B 212   O    89.7                                              
REMARK 620 3 HIS B  28   NE2  90.3 178.1                                        
REMARK 620 4 HIS B  83   NE2 108.0  84.5  93.7                                  
REMARK 620 5 HIS B 169   NE2 126.9  90.7  90.8 124.9                            
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 209                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 209                  
DBREF  1XRE A    1   208  UNP    Q81JK8   SODM2_BACAN      1    208             
DBREF  1XRE B    1   208  UNP    Q81JK8   SODM2_BACAN      1    208             
SEQADV 1XRE GLY A   -8  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE SER A   -7  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE SER A   -6  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A   -5  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A   -4  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A   -3  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A   -2  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A   -1  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS A    0  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE GLY B   -8  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE SER B   -7  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE SER B   -6  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B   -5  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B   -4  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B   -3  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B   -2  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B   -1  UNP  Q81JK8              EXPRESSION TAG                 
SEQADV 1XRE HIS B    0  UNP  Q81JK8              EXPRESSION TAG                 
SEQRES   1 A  217  GLY SER SER HIS HIS HIS HIS HIS HIS MET SER SER PHE          
SEQRES   2 A  217  GLN LEU PRO LYS LEU SER TYR ASP TYR ASP GLU LEU GLU          
SEQRES   3 A  217  PRO TYR ILE ASP SER ASN THR LEU SER ILE HIS HIS GLY          
SEQRES   4 A  217  LYS HIS HIS ALA THR TYR VAL ASN ASN LEU ASN ALA ALA          
SEQRES   5 A  217  LEU GLU ASN TYR SER GLU LEU HIS ASN LYS SER LEU GLU          
SEQRES   6 A  217  GLU LEU LEU CYS ASN LEU GLU THR LEU PRO LYS GLU ILE          
SEQRES   7 A  217  VAL THR ALA VAL ARG ASN ASN GLY GLY GLY HIS TYR CYS          
SEQRES   8 A  217  HIS SER LEU PHE TRP GLU VAL MET SER PRO ARG GLY GLY          
SEQRES   9 A  217  GLY GLU PRO ASN GLY ASP VAL ALA LYS VAL ILE ASP TYR          
SEQRES  10 A  217  TYR PHE ASN THR PHE ASP ASN LEU LYS ASP GLN LEU SER          
SEQRES  11 A  217  LYS ALA ALA ILE SER ARG PHE GLY SER GLY TYR GLY TRP          
SEQRES  12 A  217  LEU VAL LEU ASP GLY GLU GLU LEU SER VAL MET SER THR          
SEQRES  13 A  217  PRO ASN GLN ASP THR PRO LEU GLN GLU GLY LYS ILE PRO          
SEQRES  14 A  217  LEU LEU VAL ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 A  217  LYS TYR GLN ASN ARG ARG PRO GLU PHE VAL THR ASN TRP          
SEQRES  16 A  217  TRP HIS THR VAL ASN TRP ASP ARG VAL ASN GLU LYS TYR          
SEQRES  17 A  217  LEU GLN ALA ILE GLN SER GLN LYS HIS                          
SEQRES   1 B  217  GLY SER SER HIS HIS HIS HIS HIS HIS MET SER SER PHE          
SEQRES   2 B  217  GLN LEU PRO LYS LEU SER TYR ASP TYR ASP GLU LEU GLU          
SEQRES   3 B  217  PRO TYR ILE ASP SER ASN THR LEU SER ILE HIS HIS GLY          
SEQRES   4 B  217  LYS HIS HIS ALA THR TYR VAL ASN ASN LEU ASN ALA ALA          
SEQRES   5 B  217  LEU GLU ASN TYR SER GLU LEU HIS ASN LYS SER LEU GLU          
SEQRES   6 B  217  GLU LEU LEU CYS ASN LEU GLU THR LEU PRO LYS GLU ILE          
SEQRES   7 B  217  VAL THR ALA VAL ARG ASN ASN GLY GLY GLY HIS TYR CYS          
SEQRES   8 B  217  HIS SER LEU PHE TRP GLU VAL MET SER PRO ARG GLY GLY          
SEQRES   9 B  217  GLY GLU PRO ASN GLY ASP VAL ALA LYS VAL ILE ASP TYR          
SEQRES  10 B  217  TYR PHE ASN THR PHE ASP ASN LEU LYS ASP GLN LEU SER          
SEQRES  11 B  217  LYS ALA ALA ILE SER ARG PHE GLY SER GLY TYR GLY TRP          
SEQRES  12 B  217  LEU VAL LEU ASP GLY GLU GLU LEU SER VAL MET SER THR          
SEQRES  13 B  217  PRO ASN GLN ASP THR PRO LEU GLN GLU GLY LYS ILE PRO          
SEQRES  14 B  217  LEU LEU VAL ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 B  217  LYS TYR GLN ASN ARG ARG PRO GLU PHE VAL THR ASN TRP          
SEQRES  16 B  217  TRP HIS THR VAL ASN TRP ASP ARG VAL ASN GLU LYS TYR          
SEQRES  17 B  217  LEU GLN ALA ILE GLN SER GLN LYS HIS                          
HET     MN  A 209       1                                                       
HET     MN  B 209       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *374(H2 O)                                                    
HELIX    1   1 ASP A   21  LYS A   31  1                                  11    
HELIX    2   2 LYS A   31  GLU A   45  1                                  15    
HELIX    3   3 TYR A   47  HIS A   51  5                                   5    
HELIX    4   4 SER A   54  ASN A   61  1                                   8    
HELIX    5   5 LEU A   62  LEU A   65  5                                   4    
HELIX    6   6 ILE A   69  VAL A   89  1                                  21    
HELIX    7   7 ASN A   99  ASN A  111  1                                  13    
HELIX    8   8 THR A  112  SER A  126  1                                  15    
HELIX    9   9 THR A  152  GLY A  157  5                                   6    
HELIX   10  10 TRP A  167  ALA A  170  5                                   4    
HELIX   11  11 TYR A  171  GLN A  176  1                                   6    
HELIX   12  12 ARG A  178  TRP A  187  1                                  10    
HELIX   13  13 HIS A  188  VAL A  190  5                                   3    
HELIX   14  14 ASN A  191  ILE A  203  1                                  13    
HELIX   15  15 ASP B   21  LYS B   31  1                                  11    
HELIX   16  16 LYS B   31  GLU B   45  1                                  15    
HELIX   17  17 TYR B   47  HIS B   51  5                                   5    
HELIX   18  18 SER B   54  ASN B   61  1                                   8    
HELIX   19  19 LEU B   62  LEU B   65  5                                   4    
HELIX   20  20 ILE B   69  VAL B   89  1                                  21    
HELIX   21  21 ASN B   99  ASN B  111  1                                  13    
HELIX   22  22 THR B  112  ARG B  127  1                                  16    
HELIX   23  23 THR B  152  GLY B  157  5                                   6    
HELIX   24  24 TRP B  167  ALA B  170  5                                   4    
HELIX   25  25 TYR B  171  GLN B  176  1                                   6    
HELIX   26  26 ARG B  178  TRP B  187  1                                  10    
HELIX   27  27 HIS B  188  VAL B  190  5                                   3    
HELIX   28  28 ASN B  191  ILE B  203  1                                  13    
SHEET    1   A 3 GLU A 141  PRO A 148  0                                        
SHEET    2   A 3 GLY A 131  ASP A 138 -1  N  TRP A 134   O  MET A 145           
SHEET    3   A 3 ILE A 159  ASP A 165 -1  O  LEU A 161   N  LEU A 135           
SHEET    1   B 3 GLU B 141  PRO B 148  0                                        
SHEET    2   B 3 GLY B 131  ASP B 138 -1  N  ASP B 138   O  GLU B 141           
SHEET    3   B 3 ILE B 159  ASP B 165 -1  O  LEU B 161   N  LEU B 135           
LINK         OD2 ASP A 165                MN    MN A 209     1555   1555  1.92  
LINK         OD2 ASP B 165                MN    MN B 209     1555   1555  1.92  
LINK        MN    MN A 209                 O   HOH A 388     1555   1555  2.19  
LINK        MN    MN B 209                 O   HOH B 212     1555   1555  2.28  
LINK        MN    MN A 209                 NE2 HIS A  28     1555   1555  2.10  
LINK        MN    MN A 209                 NE2 HIS A  83     1555   1555  2.03  
LINK        MN    MN A 209                 NE2 HIS A 169     1555   1555  2.09  
LINK        MN    MN B 209                 NE2 HIS B  28     1555   1555  2.09  
LINK        MN    MN B 209                 NE2 HIS B  83     1555   1555  2.07  
LINK        MN    MN B 209                 NE2 HIS B 169     1555   1555  2.05  
CISPEP   1 GLU A   17    PRO A   18          0         6.14                     
CISPEP   2 GLU B   17    PRO B   18          0        -0.51                     
SITE     1 AC1  5 HIS A  28  HIS A  83  ASP A 165  HIS A 169                    
SITE     2 AC1  5 HOH A 388                                                     
SITE     1 AC2  5 HIS B  28  HIS B  83  ASP B 165  HIS B 169                    
SITE     2 AC2  5 HOH B 212                                                     
CRYST1   54.842   69.866   56.574  90.00 106.85  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018234  0.000000  0.005523        0.00000                         
SCALE2      0.000000  0.014313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018469        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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