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Database: PDB
Entry: 5N56
LinkDB: 5N56
Original site: 5N56 
HEADER    OXIDOREDUCTASE                          13-FEB-17   5N56              
TITLE     STAPHYLOCOCCUS AUREUS MN-DEPENDENT SUPEROXIDE DISMUTASE SODA          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN/FE] 1;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN BOVINE RF122 /    
SOURCE   3 ET3-1);                                                              
SOURCE   4 ORGANISM_TAXID: 273036;                                              
SOURCE   5 STRAIN: BOVINE RF122 / ET3-1;                                        
SOURCE   6 GENE: SODA, SAB1425C;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUPEROXIDE DISMUTASE, MN-DEPENDENT, STAPHYLOCOCCUS AUREUS,            
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BARWINSKA-SENDRA,A.BASLE,K.WALDRON                                  
REVDAT   2   21-MAR-18 5N56    1       JRNL                                     
REVDAT   1   07-MAR-18 5N56    0                                                
JRNL        AUTH   A.BARWINSKA-SENDRA,A.BASLE,K.J.WALDRON,S.UN                  
JRNL        TITL   A CHARGE POLARIZATION MODEL FOR THE METAL-SPECIFIC ACTIVITY  
JRNL        TITL 2 OF SUPEROXIDE DISMUTASES.                                    
JRNL        REF    PHYS CHEM CHEM PHYS           V.  20  2363 2018              
JRNL        REFN                   ESSN 1463-9084                               
JRNL        PMID   29308487                                                     
JRNL        DOI    10.1039/C7CP06829H                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20774                          
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1070                            
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) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 879                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 51.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3202                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.68000                                              
REMARK   3    B22 (A**2) : -1.69000                                             
REMARK   3    B33 (A**2) : -2.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.94000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.183         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.220        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3292 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3022 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4480 ; 1.563 ; 1.923       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6970 ; 1.018 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 5.885 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;40.111 ;25.581       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   536 ;13.872 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ; 9.038 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   474 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3768 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   776 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1582 ; 4.254 ; 3.208       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1581 ; 4.252 ; 3.207       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1974 ; 5.327 ; 4.816       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1975 ; 5.329 ; 4.817       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1710 ; 4.405 ; 3.412       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1711 ; 4.404 ; 3.413       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2507 ; 5.280 ; 4.995       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3818 ; 5.860 ;37.082       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3803 ; 5.849 ;37.013       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6314 ; 2.874 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    88 ;44.011 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6278 ;26.596 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
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     2        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7780  -1.1000  -1.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0614 T22:   0.1657                                     
REMARK   3      T33:   0.1536 T12:   0.0018                                     
REMARK   3      T13:  -0.0657 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2202 L22:   0.0768                                     
REMARK   3      L33:   0.2417 L12:  -0.0060                                     
REMARK   3      L13:   0.0582 L23:  -0.0598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:   0.0477 S13:  -0.0027                       
REMARK   3      S21:   0.0092 S22:  -0.0020 S23:  -0.0023                       
REMARK   3      S31:   0.0092 S32:  -0.0043 S33:  -0.0003                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5N56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003530.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.881                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21845                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1IDS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 30 % PEG 4000, 0.1 M TRIS   
REMARK 280  PH 8.5, VAPOR DIFFUSION, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.17800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 100   CD    GLU A 100   OE2     0.072                       
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    ASP A 147   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 161   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 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                                                                      
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    ARG A  30      -60.71   -109.45                                   
REMARK 500    ASN A  91       57.65   -141.64                                   
REMARK 500    ASN A 145     -121.06     54.83                                   
REMARK 500    TYR A 167       -7.84   -140.49                                   
REMARK 500    GLN A 172     -123.35     46.31                                   
REMARK 500    ASN B  59       40.54   -108.54                                   
REMARK 500    ASN B 145     -114.74     54.51                                   
REMARK 500    GLN B 172     -129.72     52.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  27   NE2                                                    
REMARK 620 2 HIS A  81   NE2  95.1                                              
REMARK 620 3 ASP A 161   OD2  80.2 116.5                                        
REMARK 620 4 HIS A 165   NE2  89.6 131.1 112.3                                  
REMARK 620 5 HOH A 320   O   167.6  95.0  88.8  89.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  27   NE2                                                    
REMARK 620 2 HIS B  81   NE2  89.8                                              
REMARK 620 3 ASP B 161   OD2  83.3 107.6                                        
REMARK 620 4 HIS B 165   NE2  90.3 133.2 118.9                                  
REMARK 620 5 HOH B 336   O   171.1  92.7  87.7  94.2                            
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 201                  
DBREF  5N56 A    1   199  UNP    Q2YT26   SODM1_STAAB      1    199             
DBREF  5N56 B    1   199  UNP    Q2YT26   SODM1_STAAB      1    199             
SEQRES   1 A  199  MET ALA PHE GLU LEU PRO LYS LEU PRO TYR ALA PHE ASP          
SEQRES   2 A  199  ALA LEU GLU PRO HIS PHE ASP LYS GLU THR MET GLU ILE          
SEQRES   3 A  199  HIS HIS ASP ARG HIS HIS ASN THR TYR VAL THR LYS LEU          
SEQRES   4 A  199  ASN ALA ALA VAL GLU GLY THR ASP LEU GLU SER LYS SER          
SEQRES   5 A  199  ILE GLU GLU ILE VAL ALA ASN LEU ASP SER VAL PRO ALA          
SEQRES   6 A  199  ASN ILE GLN THR ALA VAL ARG ASN ASN GLY GLY GLY HIS          
SEQRES   7 A  199  LEU ASN HIS SER LEU PHE TRP GLU LEU LEU SER PRO ASN          
SEQRES   8 A  199  SER GLU GLU LYS GLY THR VAL VAL GLU LYS ILE LYS GLU          
SEQRES   9 A  199  GLN TRP GLY SER LEU GLU GLU PHE LYS LYS GLU PHE ALA          
SEQRES  10 A  199  ASP LYS ALA ALA ALA ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  199  LEU VAL VAL ASN ASN GLY GLN LEU GLU ILE VAL THR THR          
SEQRES  12 A  199  PRO ASN GLN ASP ASN PRO LEU THR GLU GLY LYS THR PRO          
SEQRES  13 A  199  ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 A  199  LYS TYR GLN ASN LYS ARG PRO ASP TYR ILE GLY ALA PHE          
SEQRES  15 A  199  TRP ASN VAL VAL ASN TRP GLU LYS VAL ASP GLU LEU TYR          
SEQRES  16 A  199  ASN ALA THR LYS                                              
SEQRES   1 B  199  MET ALA PHE GLU LEU PRO LYS LEU PRO TYR ALA PHE ASP          
SEQRES   2 B  199  ALA LEU GLU PRO HIS PHE ASP LYS GLU THR MET GLU ILE          
SEQRES   3 B  199  HIS HIS ASP ARG HIS HIS ASN THR TYR VAL THR LYS LEU          
SEQRES   4 B  199  ASN ALA ALA VAL GLU GLY THR ASP LEU GLU SER LYS SER          
SEQRES   5 B  199  ILE GLU GLU ILE VAL ALA ASN LEU ASP SER VAL PRO ALA          
SEQRES   6 B  199  ASN ILE GLN THR ALA VAL ARG ASN ASN GLY GLY GLY HIS          
SEQRES   7 B  199  LEU ASN HIS SER LEU PHE TRP GLU LEU LEU SER PRO ASN          
SEQRES   8 B  199  SER GLU GLU LYS GLY THR VAL VAL GLU LYS ILE LYS GLU          
SEQRES   9 B  199  GLN TRP GLY SER LEU GLU GLU PHE LYS LYS GLU PHE ALA          
SEQRES  10 B  199  ASP LYS ALA ALA ALA ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  199  LEU VAL VAL ASN ASN GLY GLN LEU GLU ILE VAL THR THR          
SEQRES  12 B  199  PRO ASN GLN ASP ASN PRO LEU THR GLU GLY LYS THR PRO          
SEQRES  13 B  199  ILE LEU GLY LEU ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 B  199  LYS TYR GLN ASN LYS ARG PRO ASP TYR ILE GLY ALA PHE          
SEQRES  15 B  199  TRP ASN VAL VAL ASN TRP GLU LYS VAL ASP GLU LEU TYR          
SEQRES  16 B  199  ASN ALA THR LYS                                              
HET     MN  A 201       1                                                       
HET     MN  B 201       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *140(H2 O)                                                    
HELIX    1 AA1 ASP A   20  ARG A   30  1                                  11    
HELIX    2 AA2 ARG A   30  GLU A   44  1                                  15    
HELIX    3 AA3 SER A   52  ASN A   59  1                                   8    
HELIX    4 AA4 LEU A   60  VAL A   63  5                                   4    
HELIX    5 AA5 PRO A   64  LEU A   87  1                                  24    
HELIX    6 AA6 GLY A   96  GLY A  107  1                                  12    
HELIX    7 AA7 SER A  108  ALA A  122  1                                  15    
HELIX    8 AA8 ASN A  148  GLY A  153  5                                   6    
HELIX    9 AA9 TRP A  163  ALA A  166  5                                   4    
HELIX   10 AB1 TYR A  167  GLN A  172  1                                   6    
HELIX   11 AB2 LYS A  174  TRP A  183  1                                  10    
HELIX   12 AB3 ASN A  184  VAL A  186  5                                   3    
HELIX   13 AB4 ASN A  187  ALA A  197  1                                  11    
HELIX   14 AB5 ASP B   20  ARG B   30  1                                  11    
HELIX   15 AB6 ARG B   30  GLU B   44  1                                  15    
HELIX   16 AB7 THR B   46  LYS B   51  5                                   6    
HELIX   17 AB8 SER B   52  ASN B   59  1                                   8    
HELIX   18 AB9 LEU B   60  VAL B   63  5                                   4    
HELIX   19 AC1 ILE B   67  LEU B   87  1                                  21    
HELIX   20 AC2 GLY B   96  GLY B  107  1                                  12    
HELIX   21 AC3 SER B  108  ARG B  123  1                                  16    
HELIX   22 AC4 ASN B  148  GLY B  153  5                                   6    
HELIX   23 AC5 TRP B  163  ALA B  166  5                                   4    
HELIX   24 AC6 TYR B  167  GLN B  172  1                                   6    
HELIX   25 AC7 LYS B  174  TRP B  183  1                                  10    
HELIX   26 AC8 ASN B  184  VAL B  186  5                                   3    
HELIX   27 AC9 ASN B  187  THR B  198  1                                  12    
SHEET    1 AA1 3 GLN A 137  PRO A 144  0                                        
SHEET    2 AA1 3 GLY A 127  ASN A 134 -1  N  ASN A 134   O  GLN A 137           
SHEET    3 AA1 3 THR A 155  ASP A 161 -1  O  LEU A 158   N  LEU A 131           
SHEET    1 AA2 3 GLN B 137  PRO B 144  0                                        
SHEET    2 AA2 3 GLY B 127  ASN B 134 -1  N  TRP B 130   O  VAL B 141           
SHEET    3 AA2 3 THR B 155  ASP B 161 -1  O  ILE B 157   N  LEU B 131           
LINK         NE2 HIS A  27                MN    MN A 201     1555   1555  2.36  
LINK         NE2 HIS A  81                MN    MN A 201     1555   1555  2.13  
LINK         OD2 ASP A 161                MN    MN A 201     1555   1555  2.12  
LINK         NE2 HIS A 165                MN    MN A 201     1555   1555  2.41  
LINK         NE2 HIS B  27                MN    MN B 201     1555   1555  2.38  
LINK         NE2 HIS B  81                MN    MN B 201     1555   1555  2.17  
LINK         OD2 ASP B 161                MN    MN B 201     1555   1555  2.06  
LINK         NE2 HIS B 165                MN    MN B 201     1555   1555  2.20  
LINK        MN    MN A 201                 O   HOH A 320     1555   1555  2.22  
LINK        MN    MN B 201                 O   HOH B 336     1555   1555  2.22  
CISPEP   1 GLU A   16    PRO A   17          0        13.06                     
CISPEP   2 GLU B   16    PRO B   17          0        10.29                     
SITE     1 AC1  5 HIS A  27  HIS A  81  ASP A 161  HIS A 165                    
SITE     2 AC1  5 HOH A 320                                                     
SITE     1 AC2  5 HIS B  27  HIS B  81  ASP B 161  HIS B 165                    
SITE     2 AC2  5 HOH B 336                                                     
CRYST1   51.275   68.356   56.724  90.00  99.45  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019503  0.000000  0.003247        0.00000                         
SCALE2      0.000000  0.014629  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017872        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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