GenomeNet

Database: PDB
Entry: 4X9Q
LinkDB: 4X9Q
Original site: 4X9Q 
HEADER    OXIDOREDUCTASE                          11-DEC-14   4X9Q              
TITLE     MNSOD-3 ROOM TEMPERATURE STRUCTURE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN] 2, MITOCHONDRIAL;                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 25-218;                                       
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;                         
SOURCE   3 ORGANISM_TAXID: 6239;                                                
SOURCE   4 GENE: SOD-3, C08A9.1;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: OX326A                                     
KEYWDS    SUPEROXIDE, MANGANESE, OXIDOREDUCTASE, DISMUTASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.HUNTER,C.H.TRINH,T.HUNTER,R.BONETTA,E.E.STEWART                   
REVDAT   1   25-NOV-15 4X9Q    0                                                
JRNL        AUTH   G.J.HUNTER,C.H.TRINH,R.BONETTA,E.E.STEWART,D.E.CABELLI,      
JRNL        AUTH 2 T.HUNTER                                                     
JRNL        TITL   THE STRUCTURE OF THE CAENORHABDITIS ELEGANS MANGANESE        
JRNL        TITL 2 SUPEROXIDE DISMUTASE MNSOD-3-AZIDE COMPLEX.                  
JRNL        REF    PROTEIN SCI.                  V.  24  1777 2015              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   26257399                                                     
JRNL        DOI    10.1002/PRO.2768                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 43599                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2320                            
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) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3171                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 165                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 296                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
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): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.120         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3213 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3022 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4358 ; 1.493 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6947 ; 0.804 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   386 ; 5.653 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   158 ;30.951 ;24.937       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   541 ;13.271 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;14.915 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3664 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   774 ; 0.001 ; 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):  1550 ; 1.045 ; 1.544       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1549 ; 1.043 ; 1.543       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1934 ; 1.564 ; 2.306       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1935 ; 1.564 ; 2.307       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1663 ; 1.780 ; 1.759       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1657 ; 1.762 ; 1.742       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2418 ; 2.789 ; 2.521       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4004 ; 4.980 ;13.477       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3865 ; 4.844 ;12.947       
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   194                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7480   5.6500  -0.8200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0736 T22:   0.0226                                     
REMARK   3      T33:   0.0672 T12:   0.0244                                     
REMARK   3      T13:   0.0402 T23:   0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1057 L22:   1.4619                                     
REMARK   3      L33:   1.1208 L12:   0.1370                                     
REMARK   3      L13:   0.0008 L23:  -0.8114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:  -0.0564 S13:  -0.1092                       
REMARK   3      S21:  -0.2037 S22:  -0.1588 S23:  -0.2546                       
REMARK   3      S31:   0.2648 S32:   0.1205 S33:   0.1443                       
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     1        C   194                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5780  -2.3650  14.2150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0286 T22:   0.0909                                     
REMARK   3      T33:   0.0580 T12:  -0.0022                                     
REMARK   3      T13:   0.0296 T23:   0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8940 L22:   0.7790                                     
REMARK   3      L33:   0.9384 L12:  -0.1527                                     
REMARK   3      L13:   0.2347 L23:  -0.3438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0151 S12:  -0.1923 S13:  -0.0587                       
REMARK   3      S21:   0.1170 S22:   0.0621 S23:   0.1545                       
REMARK   3      S31:  -0.0529 S32:  -0.1772 S33:  -0.0773                       
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 4X9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205292.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45989                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1N0J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, BICINE, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       68.97950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.73250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.73250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.48975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.73250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.73250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.46925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.73250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.73250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       34.48975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.73250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.73250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      103.46925            
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       68.97950            
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: 8630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 327  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 320  LIES ON A SPECIAL POSITION.                          
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   1    CG   CD   CE   NZ                                   
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     LYS C 130    CG   CD   CE   NZ                                   
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  29      -62.33   -108.96                                   
REMARK 500    ASN A 141     -120.66     55.28                                   
REMARK 500    TYR A 161      -19.82   -143.00                                   
REMARK 500    LYS A 166     -131.86     52.02                                   
REMARK 500    LYS C  29      -61.74   -102.68                                   
REMARK 500    ASN C 141     -119.35     51.43                                   
REMARK 500    TYR C 161      -20.28   -145.84                                   
REMARK 500    LYS C 166     -136.25     54.46                                   
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  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  92.4                                              
REMARK 620 3 ASP A 155   OD2  84.7 110.3                                        
REMARK 620 4 HIS A 159   NE2  91.5 127.2 122.5                                  
REMARK 620 5 HOH A 353   O   171.0  93.4  86.8  90.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  74   NE2  91.9                                              
REMARK 620 3 ASP C 155   OD2  85.0 111.4                                        
REMARK 620 4 HIS C 159   NE2  93.7 128.5 120.1                                  
REMARK 620 5 HOH C 353   O   170.4  92.6  85.5  90.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 202                 
DBREF  4X9Q A    1   194  UNP    P41977   SODM2_CAEEL     25    218             
DBREF  4X9Q C    1   194  UNP    P41977   SODM2_CAEEL     25    218             
SEQRES   1 A  194  LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA ASP          
SEQRES   2 A  194  LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU HIS          
SEQRES   3 A  194  HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU ASN          
SEQRES   4 A  194  GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS GLY          
SEQRES   5 A  194  ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 A  194  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 A  194  THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS GLU          
SEQRES   8 A  194  LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU ASP          
SEQRES   9 A  194  ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA VAL          
SEQRES  10 A  194  GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS LYS LYS          
SEQRES  11 A  194  ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN GLN ASP          
SEQRES  12 A  194  PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP VAL          
SEQRES  13 A  194  TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL ARG          
SEQRES  14 A  194  PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN TRP          
SEQRES  15 A  194  LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN              
SEQRES   1 C  194  LYS HIS THR LEU PRO ASP LEU PRO PHE ASP TYR ALA ASP          
SEQRES   2 C  194  LEU GLU PRO VAL ILE SER HIS GLU ILE MET GLN LEU HIS          
SEQRES   3 C  194  HIS GLN LYS HIS HIS ALA THR TYR VAL ASN ASN LEU ASN          
SEQRES   4 C  194  GLN ILE GLU GLU LYS LEU HIS GLU ALA VAL SER LYS GLY          
SEQRES   5 C  194  ASN LEU LYS GLU ALA ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 C  194  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 C  194  THR ASN LEU ALA LYS ASP GLY GLY GLU PRO SER LYS GLU          
SEQRES   8 C  194  LEU MET ASP THR ILE LYS ARG ASP PHE GLY SER LEU ASP          
SEQRES   9 C  194  ASN LEU GLN LYS ARG LEU SER ASP ILE THR ILE ALA VAL          
SEQRES  10 C  194  GLN GLY SER GLY TRP GLY TRP LEU GLY TYR CYS LYS LYS          
SEQRES  11 C  194  ASP LYS ILE LEU LYS ILE ALA THR CYS ALA ASN GLN ASP          
SEQRES  12 C  194  PRO LEU GLU GLY MET VAL PRO LEU PHE GLY ILE ASP VAL          
SEQRES  13 C  194  TRP GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN VAL ARG          
SEQRES  14 C  194  PRO ASP TYR VAL HIS ALA ILE TRP LYS ILE ALA ASN TRP          
SEQRES  15 C  194  LYS ASN ILE SER GLU ARG PHE ALA ASN ALA ARG GLN              
HET     MN  A 201       1                                                       
HET    MLI  A 202       7                                                       
HET     MN  C 201       1                                                       
HET    SO4  C 202       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     MLI MALONATE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   4  MLI    C3 H2 O4 2-                                                  
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *296(H2 O)                                                    
HELIX    1 AA1 SER A   19  LYS A   29  1                                  11    
HELIX    2 AA2 LYS A   29  GLY A   52  1                                  24    
HELIX    3 AA3 ASN A   53  LEU A   60  1                                   8    
HELIX    4 AA4 LEU A   60  ASN A   80  1                                  21    
HELIX    5 AA5 SER A   89  GLY A  101  1                                  13    
HELIX    6 AA6 SER A  102  ALA A  116  1                                  15    
HELIX    7 AA7 TRP A  157  ALA A  160  5                                   4    
HELIX    8 AA8 TYR A  161  LYS A  166  1                                   6    
HELIX    9 AA9 VAL A  168  TRP A  177  1                                  10    
HELIX   10 AB1 LYS A  178  ALA A  180  5                                   3    
HELIX   11 AB2 ASN A  181  ARG A  193  1                                  13    
HELIX   12 AB3 SER C   19  LYS C   29  1                                  11    
HELIX   13 AB4 LYS C   29  GLY C   52  1                                  24    
HELIX   14 AB5 ASN C   53  LEU C   60  1                                   8    
HELIX   15 AB6 LEU C   60  ASN C   80  1                                  21    
HELIX   16 AB7 SER C   89  GLY C  101  1                                  13    
HELIX   17 AB8 SER C  102  ALA C  116  1                                  15    
HELIX   18 AB9 TRP C  157  ALA C  160  5                                   4    
HELIX   19 AC1 TYR C  161  LYS C  166  1                                   6    
HELIX   20 AC2 VAL C  168  TRP C  177  1                                  10    
HELIX   21 AC3 LYS C  178  ALA C  180  5                                   3    
HELIX   22 AC4 ASN C  181  ARG C  193  1                                  13    
SHEET    1 AA1 3 ILE A 133  ALA A 140  0                                        
SHEET    2 AA1 3 GLY A 121  CYS A 128 -1  N  TRP A 124   O  ALA A 137           
SHEET    3 AA1 3 VAL A 149  ASP A 155 -1  O  VAL A 149   N  TYR A 127           
SHEET    1 AA2 3 ILE C 133  ALA C 140  0                                        
SHEET    2 AA2 3 GLY C 121  CYS C 128 -1  N  CYS C 128   O  ILE C 133           
SHEET    3 AA2 3 VAL C 149  ASP C 155 -1  O  VAL C 149   N  TYR C 127           
LINK         NE2 HIS A  26                MN    MN A 201     1555   1555  2.21  
LINK         NE2 HIS A  74                MN    MN A 201     1555   1555  2.20  
LINK         OD2 ASP A 155                MN    MN A 201     1555   1555  2.05  
LINK         NE2 HIS A 159                MN    MN A 201     1555   1555  2.21  
LINK         NE2 HIS C  26                MN    MN C 201     1555   1555  2.22  
LINK         NE2 HIS C  74                MN    MN C 201     1555   1555  2.20  
LINK         OD2 ASP C 155                MN    MN C 201     1555   1555  2.03  
LINK         NE2 HIS C 159                MN    MN C 201     1555   1555  2.18  
LINK        MN    MN A 201                 O   HOH A 353     1555   1555  2.20  
LINK        MN    MN C 201                 O   HOH C 353     1555   1555  2.27  
CISPEP   1 GLU A   15    PRO A   16          0         4.23                     
CISPEP   2 GLU C   15    PRO C   16          0         4.94                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 155  HIS A 159                    
SITE     2 AC1  5 HOH A 353                                                     
SITE     1 AC2  9 ASN A 167  VAL A 168  HOH A 302  HOH A 304                    
SITE     2 AC2  9 HOH A 319  HOH A 320  HOH A 325  HOH A 331                    
SITE     3 AC2  9 HOH A 434                                                     
SITE     1 AC3  5 HIS C  26  HIS C  74  ASP C 155  HIS C 159                    
SITE     2 AC3  5 HOH C 353                                                     
SITE     1 AC4  3 LYS C  51  ASN C  53  HOH C 363                               
CRYST1   81.465   81.465  137.959  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      0.012275  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007249        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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