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Database: PDB
Entry: 3DC6
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Original site: 3DC6 
HEADER    OXIDOREDUCTASE                          03-JUN-08   3DC6              
TITLE     CRYSTAL STRUCTURE OF A MANGANESE SUPEROXIDE DISMUTASES FROM           
TITLE    2 CAENORHABDITIS ELEGANS                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN] 1;                               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_COMMON: NEMATODE;                                           
SOURCE   4 ORGANISM_TAXID: 6239;                                                
SOURCE   5 GENE: SOD-2, SDM-1, F10D11.1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: OX326A;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRC-99A                                  
KEYWDS    ALPHA HAIRPIN N DOMAIN, ALPHA/BETA C DOMAIN, OXIDOREDUCTASE,          
KEYWDS   2 MANGANESE, METAL-BINDING, MITOCHONDRION, TRANSIT PEPTIDE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.TRINH,T.HUNTER,E.E.STEWART,S.E.V.PHILLIPS,G.J.HUNTER              
REVDAT   2   13-JUL-11 3DC6    1       VERSN                                    
REVDAT   1   09-JUN-09 3DC6    0                                                
JRNL        AUTH   C.H.TRINH,T.HUNTER,E.E.STEWART,S.E.PHILLIPS,G.J.HUNTER       
JRNL        TITL   PURIFICATION, CRYSTALLIZATION AND X-RAY STRUCTURES OF THE    
JRNL        TITL 2 TWO MANGANESE SUPEROXIDE DISMUTASES FROM CAENORHABDITIS      
JRNL        TITL 3 ELEGANS                                                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  64  1110 2008              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   19052361                                                     
JRNL        DOI    10.1107/S1744309108037056                                    
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) : 43.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 41573                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2105                            
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) : 2935                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.2080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3105                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 448                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 17.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.31000                                             
REMARK   3    B22 (A**2) : -0.31000                                             
REMARK   3    B33 (A**2) : 0.61000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.120         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.773         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3276 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4471 ; 1.109 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   410 ; 5.054 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   153 ;33.408 ;25.686       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   534 ;11.573 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ; 4.469 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   480 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2522 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1697 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2260 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   376 ; 0.150 ; 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):    59 ; 0.138 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    44 ; 0.200 ; 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):  2075 ; 0.605 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3224 ; 0.837 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1414 ; 1.472 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1244 ; 2.317 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1720   5.3940  -0.9700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0490 T22:   0.0176                                     
REMARK   3      T33:  -0.0115 T12:   0.0166                                     
REMARK   3      T13:   0.0023 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5920 L22:   0.6931                                     
REMARK   3      L33:   1.1730 L12:   0.1245                                     
REMARK   3      L13:  -0.3005 L23:  -0.4522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0452 S12:   0.0267 S13:  -0.0616                       
REMARK   3      S21:  -0.0464 S22:  -0.0066 S23:  -0.1059                       
REMARK   3      S31:   0.1675 S32:   0.0831 S33:   0.0518                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5080  -3.5180  14.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0016 T22:   0.2685                                     
REMARK   3      T33:  -0.0452 T12:   0.0691                                     
REMARK   3      T13:   0.0393 T23:   0.1226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5660 L22:   1.4318                                     
REMARK   3      L33:   3.1288 L12:  -0.8458                                     
REMARK   3      L13:   1.7219 L23:  -1.4417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1147 S12:  -0.7337 S13:  -0.1566                       
REMARK   3      S21:   0.1666 S22:   0.5027 S23:   0.3467                       
REMARK   3      S31:  -0.1798 S32:  -1.0738 S33:  -0.3879                       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3DC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047854.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.060                              
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41573                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
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) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.14400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: C. ELEGANS MNSOD3                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M AMMONIUM SULPHATE, 0.1M BICINE,       
REMARK 280  PH9.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.72200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.49000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.36100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.49000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.49000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.08300            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.49000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.49000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.36100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.49000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.49000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      103.08300            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.72200            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 204  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 200  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 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     LYS A 130    CG   CD   CE   NZ                                   
REMARK 470     LYS C  83    CG   CD   CE   NZ                                   
REMARK 470     ASP C  84    CG   OD1  OD2                                       
REMARK 470     GLU C  87    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 141     -125.30     52.23                                   
REMARK 500    TYR A 164      -12.33   -149.39                                   
REMARK 500    LYS A 169     -133.01     53.60                                   
REMARK 500    ASN C 141     -124.97     51.09                                   
REMARK 500    TYR C 164      -11.37   -149.05                                   
REMARK 500    LYS C 169     -132.29     52.55                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 305        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 333        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 436        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH A 444        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A 446        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C 285        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH C 343        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH C 356        DISTANCE =  5.02 ANGSTROMS                       
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 198  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 158   OD1                                                    
REMARK 620 2 HIS A  26   NE2  84.8                                              
REMARK 620 3 HIS A  74   NE2 113.9  90.1                                        
REMARK 620 4 HIS A 162   NE2 117.2  90.5 128.7                                  
REMARK 620 5 HOH A 202   O    92.2 176.6  92.4  89.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 198  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 158   OD1                                                    
REMARK 620 2 HIS C  26   NE2  84.2                                              
REMARK 620 3 HIS C  74   NE2 112.3  88.9                                        
REMARK 620 4 HIS C 162   NE2 121.6  89.6 125.6                                  
REMARK 620 5 HOH C 220   O    89.5 173.7  93.3  94.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 198                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 199                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 198                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 199                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DC5   RELATED DB: PDB                                   
REMARK 900 HOMOLOGOUS PROTEIN                                                   
DBREF  3DC6 A    1   197  UNP    P31161   SODM1_CAEEL     25    221             
DBREF  3DC6 C    1   197  UNP    P31161   SODM1_CAEEL     25    221             
SEQADV 3DC6 MET A    0  UNP  P31161              INITIATING METHIONINE          
SEQADV 3DC6 MET C    0  UNP  P31161              INITIATING METHIONINE          
SEQRES   1 A  198  MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR ALA          
SEQRES   2 A  198  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 A  198  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 A  198  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 A  198  GLY ASN VAL LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 A  198  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 A  198  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER ALA          
SEQRES   8 A  198  GLU LEU LEU THR ALA ILE LYS SER ASP PHE GLY SER LEU          
SEQRES   9 A  198  ASP ASN LEU GLN LYS GLN LEU SER ALA SER THR VAL ALA          
SEQRES  10 A  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS PRO          
SEQRES  11 A  198  LYS GLY LYS ILE LEU LYS VAL ALA THR CYS ALA ASN GLN          
SEQRES  12 A  198  ASP PRO LEU GLU ALA THR THR GLY LEU VAL PRO LEU PHE          
SEQRES  13 A  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 A  198  LYS ASN VAL ARG PRO ASP TYR VAL ASN ALA ILE TRP LYS          
SEQRES  15 A  198  ILE ALA ASN TRP LYS ASN VAL SER GLU ARG PHE ALA LYS          
SEQRES  16 A  198  ALA GLN GLN                                                  
SEQRES   1 C  198  MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR ALA          
SEQRES   2 C  198  ASP LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU          
SEQRES   3 C  198  HIS HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU          
SEQRES   4 C  198  ASN GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS          
SEQRES   5 C  198  GLY ASN VAL LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 C  198  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 C  198  TRP THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER ALA          
SEQRES   8 C  198  GLU LEU LEU THR ALA ILE LYS SER ASP PHE GLY SER LEU          
SEQRES   9 C  198  ASP ASN LEU GLN LYS GLN LEU SER ALA SER THR VAL ALA          
SEQRES  10 C  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS PRO          
SEQRES  11 C  198  LYS GLY LYS ILE LEU LYS VAL ALA THR CYS ALA ASN GLN          
SEQRES  12 C  198  ASP PRO LEU GLU ALA THR THR GLY LEU VAL PRO LEU PHE          
SEQRES  13 C  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 C  198  LYS ASN VAL ARG PRO ASP TYR VAL ASN ALA ILE TRP LYS          
SEQRES  15 C  198  ILE ALA ASN TRP LYS ASN VAL SER GLU ARG PHE ALA LYS          
SEQRES  16 C  198  ALA GLN GLN                                                  
HET     MN  A 198       1                                                       
HET    SO4  A 199       5                                                       
HET    SO4  A 200       5                                                       
HET     MN  C 198       1                                                       
HET    SO4  C 199       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *448(H2 O)                                                    
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   51  1                                  23    
HELIX    3   3 ASN A   53  LEU A   60  1                                   8    
HELIX    4   4 LEU A   60  ASN A   80  1                                  21    
HELIX    5   5 SER A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ALA A  116  1                                  15    
HELIX    7   7 PRO A  144  GLY A  150  1                                   7    
HELIX    8   8 TRP A  160  ALA A  163  5                                   4    
HELIX    9   9 TYR A  164  LYS A  169  1                                   6    
HELIX   10  10 VAL A  171  ILE A  179  1                                   9    
HELIX   11  11 TRP A  180  ALA A  183  5                                   4    
HELIX   12  12 ASN A  184  GLN A  196  1                                  13    
HELIX   13  13 SER C   19  LYS C   29  1                                  11    
HELIX   14  14 LYS C   29  GLY C   52  1                                  24    
HELIX   15  15 ASN C   53  LEU C   60  1                                   8    
HELIX   16  16 LEU C   60  ASN C   80  1                                  21    
HELIX   17  17 SER C   89  GLY C  101  1                                  13    
HELIX   18  18 SER C  102  ALA C  116  1                                  15    
HELIX   19  19 PRO C  144  GLY C  150  1                                   7    
HELIX   20  20 TRP C  160  ALA C  163  5                                   4    
HELIX   21  21 TYR C  164  LYS C  169  1                                   6    
HELIX   22  22 VAL C  171  ILE C  179  1                                   9    
HELIX   23  23 TRP C  180  ALA C  183  5                                   4    
HELIX   24  24 ASN C  184  GLN C  196  1                                  13    
SHEET    1   A 3 ILE A 133  ALA A 140  0                                        
SHEET    2   A 3 GLY A 121  CYS A 128 -1  N  GLY A 126   O  LYS A 135           
SHEET    3   A 3 VAL A 152  ASP A 158 -1  O  VAL A 152   N  TYR A 127           
SHEET    1   B 3 ILE C 133  ALA C 140  0                                        
SHEET    2   B 3 GLY C 121  CYS C 128 -1  N  TRP C 124   O  ALA C 137           
SHEET    3   B 3 VAL C 152  ASP C 158 -1  O  VAL C 152   N  TYR C 127           
LINK         OD1 ASP A 158                MN    MN A 198     1555   1555  2.01  
LINK         OD1 ASP C 158                MN    MN C 198     1555   1555  1.99  
LINK         NE2 HIS A  26                MN    MN A 198     1555   1555  2.15  
LINK         NE2 HIS C  26                MN    MN C 198     1555   1555  2.22  
LINK         NE2 HIS A  74                MN    MN A 198     1555   1555  2.16  
LINK         NE2 HIS C  74                MN    MN C 198     1555   1555  2.15  
LINK         NE2 HIS A 162                MN    MN A 198     1555   1555  2.19  
LINK         NE2 HIS C 162                MN    MN C 198     1555   1555  2.17  
LINK        MN    MN A 198                 O   HOH A 202     1555   1555  1.95  
LINK        MN    MN C 198                 O   HOH C 220     1555   1555  2.10  
CISPEP   1 GLU A   15    PRO A   16          0         4.26                     
CISPEP   2 GLU C   15    PRO C   16          0         9.14                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 158  HIS A 162                    
SITE     2 AC1  5 HOH A 202                                                     
SITE     1 AC2  6 TYR A  11  GLN A  24  GLN A  28  HOH A 323                    
SITE     2 AC2  6 LYS C   1  SER C   3                                          
SITE     1 AC3  5 HIS A   2  SER A   3  HIS A  71  HOH A 288                    
SITE     2 AC3  5 HOH A 419                                                     
SITE     1 AC4  5 HIS C  26  HIS C  74  ASP C 158  HIS C 162                    
SITE     2 AC4  5 HOH C 220                                                     
SITE     1 AC5  7 HIS C   2  SER C   3  HIS C  71  HOH C 262                    
SITE     2 AC5  7 HOH C 318  HOH C 321  HOH C 334                               
CRYST1   80.980   80.980  137.444  90.00  90.00  90.00 P 41 21 2    16          
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      0.012349  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007276        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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