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Database: PDB
Entry: 1XUQ
LinkDB: 1XUQ
Original site: 1XUQ 
HEADER    OXIDOREDUCTASE                          26-OCT-04   1XUQ              
TITLE     CRYSTAL STRUCTURE OF SODA-1 (BA4499) FROM BACILLUS                    
TITLE    2 ANTHRACIS AT 1.8A RESOLUTION.                                        
CAVEAT     1XUQ    CHIRALITY ERROR AT ASN139B                                   
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: SODA1, SODA-1;                                                 
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-1; SUPEROXIDE DISMUTASE; BACILLUS ANTHRACIS; BA4499;             
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 1XUQ    1       VERSN                                    
REVDAT   1   19-JUL-05 1XUQ    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) : 31.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37842                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2001                            
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) : 2577                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 162                          
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3195                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 474                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.29000                                              
REMARK   3    B22 (A**2) : -0.98000                                             
REMARK   3    B33 (A**2) : 0.20000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.91000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.028         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3303 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2768 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4501 ; 1.449 ; 1.910       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6463 ; 0.980 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   406 ; 6.530 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;37.421 ;24.944       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   484 ;14.716 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;16.886 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   466 ; 0.155 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3791 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   685 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   702 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2701 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1567 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1603 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   308 ; 0.165 ; 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):     7 ; 0.135 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    22 ; 0.237 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.179 ; 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):  2574 ; 1.657 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   824 ; 0.299 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3207 ; 2.378 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1558 ; 6.466 ;66.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1291 ; 6.747 ;10.000       
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 : 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 1XUQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030784.                                      
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                             : 8.5                                
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   : 39919                              
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                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
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     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE TRIHYDRATE,      
REMARK 280  TRIS, PH 8.5, VAPOR DIFFUSION, SITTING 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       30.21950            
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     ALA A     2                                                      
REMARK 465     LYS A   203                                                      
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     ALA B     2                                                      
REMARK 465     LYS B   203                                                      
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    GLU A  49      -58.95    -27.24                                   
REMARK 500    ALA A  51        6.48    -69.35                                   
REMARK 500    ASN A  61       50.46   -117.26                                   
REMARK 500    ASN A 149     -124.23     55.20                                   
REMARK 500    GLN A 176     -121.60     42.41                                   
REMARK 500    ASN B  61       51.79   -118.71                                   
REMARK 500    ASN B 138      -68.25   -108.49                                   
REMARK 500    ASN B 139     -108.15    -56.43                                   
REMARK 500    ASN B 149     -121.88     56.32                                   
REMARK 500    GLN B 176     -126.53     43.55                                   
REMARK 500    GLU B 201       23.93    -76.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN B  139     GLY B  140                  118.31                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASN B 139       119.5                     ALPHA-CARBON           
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 204  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   OD2                                                    
REMARK 620 2 HOH A 365   O   174.5                                              
REMARK 620 3 HOH A 206   O    86.9  89.4                                        
REMARK 620 4 HIS A  28   NE2  85.6  98.1 172.4                                  
REMARK 620 5 HIS A  83   NE2 104.1  72.0  90.4  90.5                            
REMARK 620 6 HIS A 169   NE2 109.8  74.1  89.4  94.0 146.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 204  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 165   OD2                                                    
REMARK 620 2 HOH B 206   O    87.3                                              
REMARK 620 3 HIS B  28   NE2  86.0 172.4                                        
REMARK 620 4 HIS B  83   NE2 103.3  85.2  93.0                                  
REMARK 620 5 HIS B 169   NE2 109.6  92.4  93.2 146.9                            
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 B 204                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 204                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XRE   RELATED DB: PDB                                   
DBREF  1XUQ A    1   203  UNP    Q81LW0   SODM1_BACAN      1    203             
DBREF  1XUQ B    1   203  UNP    Q81LW0   SODM1_BACAN      1    203             
SEQADV 1XUQ GLY A   -8  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ SER A   -7  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ SER A   -6  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A   -5  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A   -4  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A   -3  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A   -2  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A   -1  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS A    0  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ GLY B   -8  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ SER B   -7  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ SER B   -6  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B   -5  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B   -4  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B   -3  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B   -2  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B   -1  UNP  Q81LW0              EXPRESSION TAG                 
SEQADV 1XUQ HIS B    0  UNP  Q81LW0              EXPRESSION TAG                 
SEQRES   1 A  212  GLY SER SER HIS HIS HIS HIS HIS HIS MET ALA LYS HIS          
SEQRES   2 A  212  GLU LEU PRO ASN LEU PRO TYR ALA TYR ASP ALA LEU GLU          
SEQRES   3 A  212  PRO HIS PHE ASP LYS GLU THR MET ASN ILE HIS HIS THR          
SEQRES   4 A  212  LYS HIS HIS ASN THR TYR ILE THR ASN LEU ASN ALA ALA          
SEQRES   5 A  212  LEU GLU GLY HIS ALA GLU LEU ALA ASP LYS SER VAL GLU          
SEQRES   6 A  212  GLU LEU VAL ALA ASN LEU ASN GLU VAL PRO GLU ALA ILE          
SEQRES   7 A  212  ARG THR ALA VAL ARG ASN ASN GLY GLY GLY HIS ALA ASN          
SEQRES   8 A  212  HIS THR PHE PHE TRP THR ILE LEU SER PRO ASN GLY GLY          
SEQRES   9 A  212  GLY GLN PRO VAL GLY GLU LEU ALA THR ALA ILE GLU ALA          
SEQRES  10 A  212  LYS PHE GLY SER PHE ASP ALA PHE LYS GLU GLU PHE ALA          
SEQRES  11 A  212  LYS ALA GLY ALA THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  12 A  212  LEU VAL VAL ASN ASN GLY GLU LEU GLU VAL THR SER THR          
SEQRES  13 A  212  PRO ASN GLN ASP SER PRO LEU THR GLU GLY LYS THR PRO          
SEQRES  14 A  212  VAL ILE GLY LEU ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 A  212  ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE GLY ALA PHE          
SEQRES  16 A  212  TRP ASN VAL VAL ASP TRP ASN ALA ALA GLU LYS ARG TYR          
SEQRES  17 A  212  GLN GLU ALA LYS                                              
SEQRES   1 B  212  GLY SER SER HIS HIS HIS HIS HIS HIS MET ALA LYS HIS          
SEQRES   2 B  212  GLU LEU PRO ASN LEU PRO TYR ALA TYR ASP ALA LEU GLU          
SEQRES   3 B  212  PRO HIS PHE ASP LYS GLU THR MET ASN ILE HIS HIS THR          
SEQRES   4 B  212  LYS HIS HIS ASN THR TYR ILE THR ASN LEU ASN ALA ALA          
SEQRES   5 B  212  LEU GLU GLY HIS ALA GLU LEU ALA ASP LYS SER VAL GLU          
SEQRES   6 B  212  GLU LEU VAL ALA ASN LEU ASN GLU VAL PRO GLU ALA ILE          
SEQRES   7 B  212  ARG THR ALA VAL ARG ASN ASN GLY GLY GLY HIS ALA ASN          
SEQRES   8 B  212  HIS THR PHE PHE TRP THR ILE LEU SER PRO ASN GLY GLY          
SEQRES   9 B  212  GLY GLN PRO VAL GLY GLU LEU ALA THR ALA ILE GLU ALA          
SEQRES  10 B  212  LYS PHE GLY SER PHE ASP ALA PHE LYS GLU GLU PHE ALA          
SEQRES  11 B  212  LYS ALA GLY ALA THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  12 B  212  LEU VAL VAL ASN ASN GLY GLU LEU GLU VAL THR SER THR          
SEQRES  13 B  212  PRO ASN GLN ASP SER PRO LEU THR GLU GLY LYS THR PRO          
SEQRES  14 B  212  VAL ILE GLY LEU ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 B  212  ASN TYR GLN ASN ARG ARG PRO ASP TYR ILE GLY ALA PHE          
SEQRES  16 B  212  TRP ASN VAL VAL ASP TRP ASN ALA ALA GLU LYS ARG TYR          
SEQRES  17 B  212  GLN GLU ALA LYS                                              
HET     MN  B 204       1                                                       
HET     MN  A 204       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *474(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 HIS A   47  ASP A   52  1                                   6    
HELIX    4   4 SER A   54  ASN A   61  1                                   8    
HELIX    5   5 LEU A   62  VAL A   65  5                                   4    
HELIX    6   6 PRO A   66  ILE A   89  1                                  24    
HELIX    7   7 VAL A   99  GLY A  111  1                                  13    
HELIX    8   8 SER A  112  ARG A  127  1                                  16    
HELIX    9   9 SER 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 ASP A  191  ALA A  202  1                                  12    
HELIX   14  14 ASP B   21  LYS B   31  1                                  11    
HELIX   15  15 LYS B   31  LEU B   44  1                                  14    
HELIX   16  16 GLU B   49  LYS B   53  5                                   5    
HELIX   17  17 SER B   54  ASN B   61  1                                   8    
HELIX   18  18 LEU B   62  VAL B   65  5                                   4    
HELIX   19  19 PRO B   66  THR B   88  1                                  23    
HELIX   20  20 VAL B   99  GLY B  111  1                                  13    
HELIX   21  21 SER B  112  ARG B  127  1                                  16    
HELIX   22  22 SER B  152  GLY B  157  5                                   6    
HELIX   23  23 TRP B  167  ALA B  170  5                                   4    
HELIX   24  24 TYR B  171  GLN B  176  1                                   6    
HELIX   25  25 ARG B  178  TRP B  187  1                                  10    
HELIX   26  26 ASP B  191  GLU B  201  1                                  11    
SHEET    1   A 3 GLU A 141  PRO A 148  0                                        
SHEET    2   A 3 GLY A 131  ASN A 138 -1  N  ASN A 138   O  GLU A 141           
SHEET    3   A 3 THR A 159  ASP A 165 -1  O  VAL A 161   N  LEU A 135           
SHEET    1   B 3 LEU B 142  PRO B 148  0                                        
SHEET    2   B 3 GLY B 131  VAL B 137 -1  N  VAL B 136   O  GLU B 143           
SHEET    3   B 3 THR B 159  ASP B 165 -1  O  VAL B 161   N  LEU B 135           
LINK         OD2 ASP A 165                MN    MN A 204     1555   1555  1.91  
LINK         OD2 ASP B 165                MN    MN B 204     1555   1555  1.94  
LINK        MN    MN B 204                 O   HOH B 206     1555   1555  2.06  
LINK        MN    MN A 204                 O   HOH A 365     1555   1555  2.24  
LINK        MN    MN A 204                 O   HOH A 206     1555   1555  2.19  
LINK        MN    MN A 204                 NE2 HIS A  28     1555   1555  2.03  
LINK        MN    MN A 204                 NE2 HIS A  83     1555   1555  2.08  
LINK        MN    MN A 204                 NE2 HIS A 169     1555   1555  2.08  
LINK        MN    MN B 204                 NE2 HIS B  28     1555   1555  2.04  
LINK        MN    MN B 204                 NE2 HIS B  83     1555   1555  2.04  
LINK        MN    MN B 204                 NE2 HIS B 169     1555   1555  2.07  
CISPEP   1 GLU A   17    PRO A   18          0         0.14                     
CISPEP   2 GLU B   17    PRO B   18          0         2.55                     
SITE     1 AC1  5 HIS B  28  HIS B  83  ASP B 165  HIS B 169                    
SITE     2 AC1  5 HOH B 206                                                     
SITE     1 AC2  6 HIS A  28  HIS A  83  ASP A 165  HIS A 169                    
SITE     2 AC2  6 HOH A 206  HOH A 365                                          
CRYST1   60.881   60.439   61.981  90.00 106.30  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      0.016425  0.000000  0.004803        0.00000                         
SCALE2      0.000000  0.016546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016810        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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