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Database: PDB
Entry: 5N57
LinkDB: 5N57
Original site: 5N57 
HEADER    OXIDOREDUCTASE                          13-FEB-17   5N57              
TITLE     STAPHYLOCOCCUS AUREUS CAMBIALISTIC SUPEROXIDE DISMUTASE SODM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
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;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: SODA, SODM, A4U86_04870, BN1321_40056, ERS072738_00830,        
SOURCE   5 ERS072840_00559, ERS073147_02394, ERS073767_02269, ERS074020_00889,  
SOURCE   6 ERS1058648_00955, FORC27_0128, HMPREF3211_00238, SAMEA2298760_02426; 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUPEROXIDE DISMUTASE, CAMBIALISTIC, STAPHYLOCOCCUS AUREUS,            
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BARWINSKA-SENDRA,A.BASLE,K.WALDRON                                  
REVDAT   2   21-MAR-18 5N57    1       JRNL                                     
REVDAT   1   07-MAR-18 5N57    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22975                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1146                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1666                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3242                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.57000                                              
REMARK   3    B22 (A**2) : 0.57000                                              
REMARK   3    B33 (A**2) : -1.84000                                             
REMARK   3    B12 (A**2) : 0.28000                                              
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): 0.267         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.213         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.206         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.214        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3338 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3052 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4540 ; 1.695 ; 1.921       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7032 ; 1.031 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 6.675 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;38.379 ;25.287       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   548 ;14.269 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;24.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   476 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3802 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   806 ; 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 ; 2.334 ; 3.242       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1581 ; 2.334 ; 3.240       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1974 ; 3.469 ; 4.853       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1975 ; 3.468 ; 4.856       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1756 ; 2.714 ; 3.447       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1757 ; 2.713 ; 3.450       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2567 ; 4.264 ; 5.054       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3797 ; 5.675 ;36.410       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3782 ; 5.675 ;36.382       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    199       B     2    199   13106  0.08  0.05     
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   199                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7870  -2.5170  16.7450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4208 T22:   2.0240                                     
REMARK   3      T33:   2.3017 T12:  -0.5835                                     
REMARK   3      T13:  -0.5522 T23:   0.1587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8107 L22:   3.2129                                     
REMARK   3      L33:   0.8275 L12:  -0.1758                                     
REMARK   3      L13:  -0.8078 L23:   0.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3170 S12:  -1.2511 S13:   0.1850                       
REMARK   3      S21:   0.6149 S22:  -0.2639 S23:  -2.7086                       
REMARK   3      S31:  -0.3075 S32:   1.2816 S33:  -0.0532                       
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 5N57 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_1200003531.                                   
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) : 1.282                              
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   : 24136                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 2RCV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M KSCN, 34 % PEG 2K MME, VAPOR      
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       15.47533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.95067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       23.21300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.68833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        7.73767            
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: 2130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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  55   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LYS A 174   CD  -  CE  -  NZ  ANGL. DEV. =  14.2 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    LYS A  30      -66.33    -99.81                                   
REMARK 500    ASP A 135       42.90     70.08                                   
REMARK 500    ASN A 145     -113.31     51.64                                   
REMARK 500    GLN A 172     -122.93     51.39                                   
REMARK 500    LYS B  30      -64.84   -102.97                                   
REMARK 500    ASN B  91       76.70   -117.82                                   
REMARK 500    ASP B 135     -112.91     75.76                                   
REMARK 500    ASN B 145     -116.23     54.39                                   
REMARK 500    GLN B 172     -121.98     49.18                                   
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  91.1                                              
REMARK 620 3 ASP A 161   OD2  87.4 120.0                                        
REMARK 620 4 HIS A 165   NE2  89.3 124.7 115.2                                  
REMARK 620 5 HOH A 323   O   174.3  84.2  92.1  96.1                            
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  91.4                                              
REMARK 620 3 ASP B 161   OD2  89.4 122.5                                        
REMARK 620 4 HIS B 165   NE2  87.5 121.5 116.0                                  
REMARK 620 5 HOH B 319   O   172.3  95.7  84.3  91.3                            
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  5N57 A    1   199  UNP    W8UU58   W8UU58_STAAU     1    199             
DBREF  5N57 B    1   199  UNP    W8UU58   W8UU58_STAAU     1    199             
SEQRES   1 A  199  MET ALA PHE LYS LEU PRO ASN LEU PRO TYR ALA TYR ASP          
SEQRES   2 A  199  ALA LEU GLU PRO TYR ILE ASP GLN ARG THR MET GLU PHE          
SEQRES   3 A  199  HIS HIS ASP LYS HIS HIS ASN THR TYR VAL THR LYS LEU          
SEQRES   4 A  199  ASN ALA THR VAL GLU GLY THR GLU LEU GLU HIS GLN SER          
SEQRES   5 A  199  LEU ALA ASP MET ILE ALA ASN LEU ASP LYS VAL PRO GLU          
SEQRES   6 A  199  ALA MET ARG MET SER VAL ARG ASN ASN GLY GLY GLY HIS          
SEQRES   7 A  199  PHE ASN HIS SER LEU PHE TRP GLU ILE LEU SER PRO ASN          
SEQRES   8 A  199  SER GLU GLU LYS GLY GLY VAL ILE ASP ASP ILE LYS ALA          
SEQRES   9 A  199  GLN TRP GLY THR LEU ASP GLU PHE LYS ASN GLU PHE ALA          
SEQRES  10 A  199  ASN LYS ALA THR THR LEU PHE GLY SER GLY TRP THR TRP          
SEQRES  11 A  199  LEU VAL VAL ASN ASP GLY LYS 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 LEU PHE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 A  199  LYS TYR GLN ASN LYS ARG PRO ASP TYR MET THR ALA PHE          
SEQRES  15 A  199  TRP ASN ILE VAL ASN TRP LYS LYS VAL ASP GLU LEU TYR          
SEQRES  16 A  199  GLN ALA ALA LYS                                              
SEQRES   1 B  199  MET ALA PHE LYS LEU PRO ASN LEU PRO TYR ALA TYR ASP          
SEQRES   2 B  199  ALA LEU GLU PRO TYR ILE ASP GLN ARG THR MET GLU PHE          
SEQRES   3 B  199  HIS HIS ASP LYS HIS HIS ASN THR TYR VAL THR LYS LEU          
SEQRES   4 B  199  ASN ALA THR VAL GLU GLY THR GLU LEU GLU HIS GLN SER          
SEQRES   5 B  199  LEU ALA ASP MET ILE ALA ASN LEU ASP LYS VAL PRO GLU          
SEQRES   6 B  199  ALA MET ARG MET SER VAL ARG ASN ASN GLY GLY GLY HIS          
SEQRES   7 B  199  PHE ASN HIS SER LEU PHE TRP GLU ILE LEU SER PRO ASN          
SEQRES   8 B  199  SER GLU GLU LYS GLY GLY VAL ILE ASP ASP ILE LYS ALA          
SEQRES   9 B  199  GLN TRP GLY THR LEU ASP GLU PHE LYS ASN GLU PHE ALA          
SEQRES  10 B  199  ASN LYS ALA THR THR LEU PHE GLY SER GLY TRP THR TRP          
SEQRES  11 B  199  LEU VAL VAL ASN ASP GLY LYS 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 LEU PHE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 B  199  LYS TYR GLN ASN LYS ARG PRO ASP TYR MET THR ALA PHE          
SEQRES  15 B  199  TRP ASN ILE VAL ASN TRP LYS LYS VAL ASP GLU LEU TYR          
SEQRES  16 B  199  GLN ALA ALA 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   *121(H2 O)                                                    
HELIX    1 AA1 ASP A   20  LYS A   30  1                                  11    
HELIX    2 AA2 LYS A   30  GLU A   44  1                                  15    
HELIX    3 AA3 THR A   46  GLN A   51  5                                   6    
HELIX    4 AA4 SER A   52  ASN A   59  1                                   8    
HELIX    5 AA5 LEU A   60  VAL A   63  5                                   4    
HELIX    6 AA6 PRO A   64  ILE A   87  1                                  24    
HELIX    7 AA7 GLY A   96  GLY A  107  1                                  12    
HELIX    8 AA8 THR A  108  THR A  122  1                                  15    
HELIX    9 AA9 ASN A  148  GLY A  153  5                                   6    
HELIX   10 AB1 TRP A  163  ALA A  166  5                                   4    
HELIX   11 AB2 TYR A  167  GLN A  172  1                                   6    
HELIX   12 AB3 LYS A  174  ASN A  184  1                                  11    
HELIX   13 AB4 ASN A  187  LYS A  199  1                                  13    
HELIX   14 AB5 ASP B   20  LYS B   30  1                                  11    
HELIX   15 AB6 LYS B   30  GLU B   44  1                                  15    
HELIX   16 AB7 SER B   52  ASN B   59  1                                   8    
HELIX   17 AB8 LEU B   60  VAL B   63  5                                   4    
HELIX   18 AB9 PRO B   64  ILE B   87  1                                  24    
HELIX   19 AC1 GLY B   96  GLY B  107  1                                  12    
HELIX   20 AC2 THR B  108  THR B  122  1                                  15    
HELIX   21 AC3 ASN B  148  GLY B  153  5                                   6    
HELIX   22 AC4 TRP B  163  ALA B  166  5                                   4    
HELIX   23 AC5 TYR B  167  GLN B  172  1                                   6    
HELIX   24 AC6 LYS B  174  TRP B  183  1                                  10    
HELIX   25 AC7 ASN B  184  VAL B  186  5                                   3    
HELIX   26 AC8 ASN B  187  LYS B  199  1                                  13    
SHEET    1 AA1 3 LYS A 137  PRO A 144  0                                        
SHEET    2 AA1 3 GLY A 127  ASN A 134 -1  N  VAL A 132   O  GLU A 139           
SHEET    3 AA1 3 THR A 155  ASP A 161 -1  O  ILE A 157   N  LEU A 131           
SHEET    1 AA2 3 LYS B 137  PRO B 144  0                                        
SHEET    2 AA2 3 GLY B 127  ASN B 134 -1  N  VAL B 132   O  GLU B 139           
SHEET    3 AA2 3 THR B 155  ASP B 161 -1  O  LEU B 158   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  2.33  
LINK         OD2 ASP A 161                MN    MN A 201     1555   1555  1.97  
LINK         NE2 HIS A 165                MN    MN A 201     1555   1555  2.30  
LINK         NE2 HIS B  27                MN    MN B 201     1555   1555  2.35  
LINK         NE2 HIS B  81                MN    MN B 201     1555   1555  2.33  
LINK         OD2 ASP B 161                MN    MN B 201     1555   1555  1.91  
LINK         NE2 HIS B 165                MN    MN B 201     1555   1555  2.34  
LINK        MN    MN A 201                 O   HOH A 323     1555   1555  2.21  
LINK        MN    MN B 201                 O   HOH B 319     1555   1555  2.14  
CISPEP   1 GLU A   16    PRO A   17          0        -5.89                     
CISPEP   2 GLU B   16    PRO B   17          0        -2.08                     
SITE     1 AC1  5 HIS A  27  HIS A  81  ASP A 161  HIS A 165                    
SITE     2 AC1  5 HOH A 323                                                     
SITE     1 AC2  5 HIS B  27  HIS B  81  ASP B 161  HIS B 165                    
SITE     2 AC2  5 HOH B 319                                                     
CRYST1  142.225  142.225   46.426  90.00  90.00 120.00 P 61         12          
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      0.007031  0.004059  0.000000        0.00000                         
SCALE2      0.000000  0.008119  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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