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Database: PDB
Entry: 2CDY
LinkDB: 2CDY
Original site: 2CDY 
HEADER    OXIDOREDUCTASE                          31-JAN-06   2CDY              
TITLE     MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM DEINOCOCCUS              
TITLE    2 RADIODURANS                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 ATCC: 13939;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)PLYSS;                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: GATEWAY PDEST17                            
KEYWDS    MANGANESE SUPEROXIDE DISMUTASE, DEINOCOCCUS RADIODURANS,              
KEYWDS   2 RADIATION RESISTANCE, OXIDOREDUCTASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,G.LEONARD,               
AUTHOR   2 S.MCSWEENEY                                                          
REVDAT   3   24-FEB-09 2CDY    1       VERSN                                    
REVDAT   2   05-APR-06 2CDY    1       JRNL                                     
REVDAT   1   13-FEB-06 2CDY    0                                                
JRNL        AUTH   R.DENNIS,E.MICOSSI,J.MCCARTHY,E.MOE,E.GORDON,                
JRNL        AUTH 2 G.LEONARD,S.MCSWEENEY                                        
JRNL        TITL   STRUCTURE OF THE MANGANESE SUPEROXIDE DISMUTASE              
JRNL        TITL 2 FROM DEINOCOCCUS RADIODURANS IN TWO CRYSTAL FORMS.           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   325 2006              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   16582477                                                     
JRNL        DOI    10.1107/S1744309106008402                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 45779                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2483                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1600                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.2310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6478                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 567                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : 0.51000                                              
REMARK   3    B33 (A**2) : -1.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.92000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.238         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.833         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6657 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5710 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9060 ; 1.142 ; 1.914       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13266 ; 0.797 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   820 ; 5.705 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   342 ;37.011 ;24.737       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   988 ;13.426 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.988 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   946 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7620 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1384 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1534 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5744 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3273 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3392 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   489 ; 0.141 ; 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):     6 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    34 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.135 ; 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):  4224 ; 0.712 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6522 ; 1.161 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2875 ; 1.513 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2538 ; 2.321 ; 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   : 1.20                                          
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. DUE TO POOR ELECTRON DENSITY THE SIDE CHAINS      
REMARK   3  OF THE FOLLOWING RESIDUES HAVE BEEN TRUNCATED AT CB LYS A142,       
REMARK   3  LYS A210, GLU B46, ASP B105, GLN B91, LYS C210, LYS D139 DUE        
REMARK   3  TO POOR ELECTRON DENSITY THE SIDE CHAIN OF GLU D158 HAS BEEN        
REMARK   3  TRUNCATED AT CG. DUE TO POOR ELECTRON DENSITY THE SIDE CHAIN        
REMARK   3  OF MET B23 HAS BEEN TRUNCATED AT SD. DUE TO POOR ELECTRON           
REMARK   3  DENSITY THE SIDE CHAIN OF ASN C94 HAS BEEN TRUNCATED AT CA.         
REMARK   4                                                                      
REMARK   4 2CDY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-27479.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 41.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2CE4 (MONOMER A)                           
REMARK 200                                                                      
REMARK 200 REMARK: DATA COMPLETENESS OF RANGE 41.2-2.25A IS 95.4%               
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       43.55000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 GENERATING THE BIOMOLECULE                                           
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  3                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  4                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     TYR A   -19                                                      
REMARK 465     TYR A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     GLN A    93                                                      
REMARK 465     ASN A    94                                                      
REMARK 465     GLY A    95                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     TYR B   -19                                                      
REMARK 465     TYR B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLU B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     LYS B    -4                                                      
REMARK 465     LYS B    -3                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     GLN B    93                                                      
REMARK 465     ASN B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     ALA B    96                                                      
REMARK 465     MET C   -21                                                      
REMARK 465     SER C   -20                                                      
REMARK 465     TYR C   -19                                                      
REMARK 465     TYR C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     LEU C   -11                                                      
REMARK 465     GLU C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     THR C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     TYR C    -5                                                      
REMARK 465     LYS C    -4                                                      
REMARK 465     LYS C    -3                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     GLY C    92                                                      
REMARK 465     GLN C    93                                                      
REMARK 465     MET D   -21                                                      
REMARK 465     SER D   -20                                                      
REMARK 465     TYR D   -19                                                      
REMARK 465     TYR D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     LEU D   -11                                                      
REMARK 465     GLU D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     THR D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     TYR D    -5                                                      
REMARK 465     LYS D    -4                                                      
REMARK 465     LYS D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 465     GLY D    92                                                      
REMARK 465     GLN D    93                                                      
REMARK 465     ASN D    94                                                      
REMARK 465     GLY D    95                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  53    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 102    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     MET B  23    CE                                                  
REMARK 470     LYS B  40    CG   CD   CE   NZ                                   
REMARK 470     GLU B  46    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 105    CG   OD1  OD2                                       
REMARK 470     GLU B 158    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  -1    CG   CD1  CD2                                       
REMARK 470     GLN C   6    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  46    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  91    CG   CD   OE1  NE2                                  
REMARK 470     ASN C  94    CB   CG   OD1  ND2                                  
REMARK 470     LYS C 210    CG   CD   CE   NZ                                   
REMARK 470     LEU D  -1    CG   CD1  CD2                                       
REMARK 470     GLN D   6    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 139    CD   CE   NZ                                        
REMARK 470     GLU D 158    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SD   MET D    82  -  O    HOH D  2128              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  29      -63.19   -107.63                                   
REMARK 500    ASN A 150     -123.73     56.32                                   
REMARK 500    TYR A 178       -4.64   -140.68                                   
REMARK 500    GLN A 183     -123.95     44.47                                   
REMARK 500    PRO B   8        1.51    -69.37                                   
REMARK 500    LYS B  29      -60.81   -109.71                                   
REMARK 500    ASN B 150     -124.27     56.36                                   
REMARK 500    GLN B 183     -124.64     47.52                                   
REMARK 500    ALA C   1     -137.98     79.61                                   
REMARK 500    LYS C  29      -60.19   -107.55                                   
REMARK 500    ALA C  96       84.69     75.15                                   
REMARK 500    ASN C 150     -127.67     55.67                                   
REMARK 500    TYR C 178       -5.14   -143.56                                   
REMARK 500    GLN C 183     -131.40     48.01                                   
REMARK 500    TYR D   2      131.08     15.54                                   
REMARK 500    ASN D 150     -123.45     51.56                                   
REMARK 500    TYR D 178       -6.18   -141.38                                   
REMARK 500    GLN D 183     -131.71     43.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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 A1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 176   NE2                                                    
REMARK 620 2 HOH A2183   O    87.8                                              
REMARK 620 3 HIS A  26   NE2  92.2 173.0                                        
REMARK 620 4 HIS A  80   NE2 138.9  91.9  92.7                                  
REMARK 620 5 ASP A 172   OD2 114.2  86.7  86.8 106.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  80   NE2                                                    
REMARK 620 2 HIS B  26   NE2  91.9                                              
REMARK 620 3 ASP B 172   OD2 108.9  90.2                                        
REMARK 620 4 HIS B 176   NE2 135.9  91.8 115.0                                  
REMARK 620 5 HOH B2100   O    92.5 172.8  82.9  89.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C 176   NE2  93.6                                              
REMARK 620 3 ASP C 172   OD2  84.6 115.7                                        
REMARK 620 4 HIS C  80   NE2  91.4 137.0 107.3                                  
REMARK 620 5 HOH C2120   O   170.2  93.0  86.0  88.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D1211  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  26   NE2                                                    
REMARK 620 2 ASP D 172   OD2  85.8                                              
REMARK 620 3 HIS D 176   NE2  91.7 113.4                                        
REMARK 620 4 HIS D  80   NE2  93.2 112.1 134.4                                  
REMARK 620 5 HOH D2164   O   173.2  88.4  87.5  92.1                            
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 A1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN C1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D1211                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Y67   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE                           
REMARK 900  DISMUTASE FROMDEINOCOCCUS RADIODURANS                               
REMARK 900 RELATED ID: 2CE4   RELATED DB: PDB                                   
REMARK 900  MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM                        
REMARK 900  DEINOCOCCUS RADIODURANS                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE CRYSTALLISED CONTAINS AN N-TERMINAL                     
REMARK 999 PURIFICATION TAG. WHERE RESIDUES FROM THIS ARE SEEN IN THE           
REMARK 999 CRYSTAL THE NUMBERING IS -1, -2 ETC...                               
DBREF  2CDY A  -21    -1  PDB    2CDY     2CDY           -21     -1             
DBREF  2CDY A    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  2CDY B  -21    -1  PDB    2CDY     2CDY           -21     -1             
DBREF  2CDY B    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  2CDY C  -21    -1  PDB    2CDY     2CDY           -21     -1             
DBREF  2CDY C    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  2CDY D  -21    -1  PDB    2CDY     2CDY           -21     -1             
DBREF  2CDY D    1   210  UNP    Q9RUV2   SODM_DEIRA       1    210             
SEQRES   1 A  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 A  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 A  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 A  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 A  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 A  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 A  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 A  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 A  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 A  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 A  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 A  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 A  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 A  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 A  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 A  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 A  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 A  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
SEQRES   1 B  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 B  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 B  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 B  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 B  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 B  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 B  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 B  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 B  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 B  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 B  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 B  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 B  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 B  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 B  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 B  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 B  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 B  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
SEQRES   1 C  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 C  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 C  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 C  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 C  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 C  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 C  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 C  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 C  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 C  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 C  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 C  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 C  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 C  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 C  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 C  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 C  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 C  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
SEQRES   1 D  231  MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER          
SEQRES   2 D  231  THR SER LEU TYR LYS LYS ALA LEU ALA TYR THR LEU PRO          
SEQRES   3 D  231  GLN LEU PRO TYR ALA TYR ASP ALA LEU GLU PRO HIS ILE          
SEQRES   4 D  231  ASP ALA ARG THR MET GLU ILE HIS HIS THR LYS HIS HIS          
SEQRES   5 D  231  GLN THR TYR VAL ASP ASN ALA ASN LYS ALA LEU GLU GLY          
SEQRES   6 D  231  THR GLU PHE ALA ASP LEU PRO VAL GLU GLN LEU ILE GLN          
SEQRES   7 D  231  GLN LEU ASP ARG VAL PRO ALA ASP LYS LYS GLY ALA LEU          
SEQRES   8 D  231  ARG ASN ASN ALA GLY GLY HIS ALA ASN HIS SER MET PHE          
SEQRES   9 D  231  TRP GLN ILE MET GLY GLN GLY GLN GLY GLN ASN GLY ALA          
SEQRES  10 D  231  ASN GLN PRO SER GLY GLU LEU LEU ASP ALA ILE ASN SER          
SEQRES  11 D  231  ALA PHE GLY SER PHE ASP ALA PHE LYS GLN LYS PHE GLU          
SEQRES  12 D  231  ASP ALA ALA LYS THR ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  13 D  231  LEU VAL VAL LYS ASP GLY LYS LEU ASP VAL VAL SER THR          
SEQRES  14 D  231  ALA ASN GLN ASP ASN PRO LEU MET GLY GLU ALA ILE ALA          
SEQRES  15 D  231  GLY VAL SER GLY THR PRO ILE LEU GLY VAL ASP VAL TRP          
SEQRES  16 D  231  GLU HIS ALA TYR TYR LEU ASN TYR GLN ASN ARG ARG PRO          
SEQRES  17 D  231  ASP TYR LEU ALA ALA PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  18 D  231  GLU VAL SER LYS ARG TYR ALA ALA ALA LYS                      
HET     MN  A1211       1                                                       
HET     MN  B1211       1                                                       
HET     MN  C1211       1                                                       
HET     MN  D1211       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *567(H2 O1)                                                   
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 GLN A   57  VAL A   62  5                                   6    
HELIX    5   5 PRO A   63  ASP A   65  5                                   3    
HELIX    6   6 LYS A   66  ILE A   86  1                                  21    
HELIX    7   7 SER A  100  GLY A  112  1                                  13    
HELIX    8   8 SER A  113  ARG A  128  1                                  16    
HELIX    9   9 ASN A  153  MET A  156  5                                   4    
HELIX   10  10 GLY A  157  GLY A  162  1                                   6    
HELIX   11  11 TRP A  174  ALA A  177  5                                   4    
HELIX   12  12 TYR A  178  GLN A  183  1                                   6    
HELIX   13  13 ARG A  185  TRP A  194  1                                  10    
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 PRO B   63  ILE B   86  1                                  24    
HELIX   19  19 GLY B  101  GLY B  112  1                                  12    
HELIX   20  20 SER B  113  THR B  127  1                                  15    
HELIX   21  21 ASN B  153  MET B  156  5                                   4    
HELIX   22  22 GLY B  157  GLY B  162  1                                   6    
HELIX   23  23 TRP B  174  ALA B  177  5                                   4    
HELIX   24  24 TYR B  178  GLN B  183  1                                   6    
HELIX   25  25 ARG B  185  TRP B  194  1                                  10    
HELIX   26  26 ASN B  198  ALA B  208  1                                  11    
HELIX   27  27 ASP C   19  LYS C   29  1                                  11    
HELIX   28  28 LYS C   29  GLU C   43  1                                  15    
HELIX   29  29 PRO C   51  ILE C   56  1                                   6    
HELIX   30  30 LYS C   66  ILE C   86  1                                  21    
HELIX   31  31 SER C  100  GLY C  112  1                                  13    
HELIX   32  32 SER C  113  ARG C  128  1                                  16    
HELIX   33  33 ASN C  153  MET C  156  5                                   4    
HELIX   34  34 GLY C  157  GLY C  162  1                                   6    
HELIX   35  35 TRP C  174  ALA C  177  5                                   4    
HELIX   36  36 TYR C  178  GLN C  183  1                                   6    
HELIX   37  37 ARG C  185  TRP C  194  1                                  10    
HELIX   38  38 ASN C  198  LYS C  210  1                                  13    
HELIX   39  39 ASP D   19  LYS D   29  1                                  11    
HELIX   40  40 LYS D   29  GLU D   43  1                                  15    
HELIX   41  41 PRO D   51  ILE D   56  1                                   6    
HELIX   42  42 PRO D   63  ASP D   65  5                                   3    
HELIX   43  43 LYS D   66  MET D   87  1                                  22    
HELIX   44  44 SER D  100  GLY D  112  1                                  13    
HELIX   45  45 SER D  113  ARG D  128  1                                  16    
HELIX   46  46 ASN D  153  MET D  156  5                                   4    
HELIX   47  47 GLY D  157  GLY D  162  1                                   6    
HELIX   48  48 TRP D  174  ALA D  177  5                                   4    
HELIX   49  49 TYR D  178  GLN D  183  1                                   6    
HELIX   50  50 ARG D  185  TRP D  194  1                                  10    
HELIX   51  51 ASN D  198  LYS D  210  1                                  13    
SHEET    1  AA 3 LYS A 142  ALA A 149  0                                        
SHEET    2  AA 3 GLY A 132  LYS A 139 -1  O  TRP A 133   N  THR A 148           
SHEET    3  AA 3 THR A 166  ASP A 172 -1  O  THR A 166   N  VAL A 138           
SHEET    1  BA 3 LYS B 142  ALA B 149  0                                        
SHEET    2  BA 3 GLY B 132  LYS B 139 -1  O  TRP B 133   N  THR B 148           
SHEET    3  BA 3 THR B 166  ASP B 172 -1  O  THR B 166   N  VAL B 138           
SHEET    1  CA 3 LYS C 142  ALA C 149  0                                        
SHEET    2  CA 3 GLY C 132  LYS C 139 -1  O  TRP C 133   N  THR C 148           
SHEET    3  CA 3 THR C 166  ASP C 172 -1  O  THR C 166   N  VAL C 138           
SHEET    1  DA 3 LYS D 142  ALA D 149  0                                        
SHEET    2  DA 3 GLY D 132  LYS D 139 -1  O  TRP D 133   N  THR D 148           
SHEET    3  DA 3 THR D 166  ASP D 172 -1  O  THR D 166   N  VAL D 138           
LINK        MN    MN A1211                 NE2 HIS A 176     1555   1555  2.24  
LINK        MN    MN A1211                 O   HOH A2183     1555   1555  2.26  
LINK        MN    MN A1211                 NE2 HIS A  26     1555   1555  2.24  
LINK        MN    MN A1211                 NE2 HIS A  80     1555   1555  2.15  
LINK        MN    MN A1211                 OD2 ASP A 172     1555   1555  1.92  
LINK        MN    MN B1211                 NE2 HIS B  80     1555   1555  2.11  
LINK        MN    MN B1211                 NE2 HIS B  26     1555   1555  2.17  
LINK        MN    MN B1211                 OD2 ASP B 172     1555   1555  1.93  
LINK        MN    MN B1211                 NE2 HIS B 176     1555   1555  2.31  
LINK        MN    MN B1211                 O   HOH B2100     1555   1555  2.21  
LINK        MN    MN C1211                 NE2 HIS C 176     1555   1555  2.20  
LINK        MN    MN C1211                 OD2 ASP C 172     1555   1555  1.93  
LINK        MN    MN C1211                 NE2 HIS C  80     1555   1555  2.13  
LINK        MN    MN C1211                 O   HOH C2120     1555   1555  2.20  
LINK        MN    MN C1211                 NE2 HIS C  26     1555   1555  2.21  
LINK        MN    MN D1211                 OD2 ASP D 172     1555   1555  1.98  
LINK        MN    MN D1211                 NE2 HIS D 176     1555   1555  2.31  
LINK        MN    MN D1211                 NE2 HIS D  80     1555   1555  2.12  
LINK        MN    MN D1211                 O   HOH D2164     1555   1555  2.25  
LINK        MN    MN D1211                 NE2 HIS D  26     1555   1555  2.21  
CISPEP   1 GLU A   15    PRO A   16          0        -5.73                     
CISPEP   2 GLU B   15    PRO B   16          0        -6.56                     
CISPEP   3 GLU C   15    PRO C   16          0        -0.68                     
CISPEP   4 GLU D   15    PRO D   16          0        -1.45                     
SITE     1 AC1  5 HIS A  26  HIS A  80  ASP A 172  HIS A 176                    
SITE     2 AC1  5 HOH A2183                                                     
SITE     1 AC2  5 HIS B  26  HIS B  80  ASP B 172  HIS B 176                    
SITE     2 AC2  5 HOH B2100                                                     
SITE     1 AC3  5 HIS C  26  HIS C  80  ASP C 172  HIS C 176                    
SITE     2 AC3  5 HOH C2120                                                     
SITE     1 AC4  5 HIS D  26  HIS D  80  ASP D 172  HIS D 176                    
SITE     2 AC4  5 HOH D2164                                                     
CRYST1   43.577   87.100  116.418  90.00  92.10  90.00 P 1 21 1      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      0.022948  0.000000  0.000841        0.00000                         
SCALE2      0.000000  0.011481  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008595        0.00000                         
MTRIX1   1  0.795000  0.139000 -0.590000       51.55883    1                    
MTRIX2   1  0.136000 -0.990000 -0.049000       75.63525    1                    
MTRIX3   1 -0.591000 -0.041000 -0.806000      174.25024    1                    
MTRIX1   2  0.990000  0.141000  0.025000      -29.81303    1                    
MTRIX2   2 -0.099000  0.804000 -0.587000       60.49112    1                    
MTRIX3   2 -0.103000  0.578000  0.809000      -59.54546    1                    
MTRIX1   3  0.791000 -0.059000 -0.608000       38.20346    1                    
MTRIX2   3  0.329000 -0.798000  0.505000       14.55108    1                    
MTRIX3   3 -0.515000 -0.600000 -0.612000      119.46127    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system