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Database: PDB
Entry: 1EM1
LinkDB: 1EM1
Original site: 1EM1 
HEADER    OXIDOREDUCTASE                          14-MAR-00   1EM1              
TITLE     X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE,     
TITLE    2 Q143A                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HMNSOD;                                                     
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGANELLE: MITOCHONDRIA;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SODASODB;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PHMNSOD4 (ATCC#59947)                      
KEYWDS    ALPHA-BETA PROTEIN, METALLOENZYME, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.LEVEQUE,M.E.STROUPE,J.R.LEPOCK,D.E.CABELLI,J.A.TAINER,H.S.NICK,     
AUTHOR   2 D.N.SILVERMAN                                                        
REVDAT   5   04-OCT-17 1EM1    1       REMARK                                   
REVDAT   4   13-JUL-11 1EM1    1       VERSN                                    
REVDAT   3   24-FEB-09 1EM1    1       VERSN                                    
REVDAT   2   01-SEP-00 1EM1    1       JRNL                                     
REVDAT   1   24-MAR-00 1EM1    0                                                
JRNL        AUTH   V.J.LEVEQUE,M.E.STROUPE,J.R.LEPOCK,D.E.CABELLI,J.A.TAINER,   
JRNL        AUTH 2 H.S.NICK,D.N.SILVERMAN                                       
JRNL        TITL   MULTIPLE REPLACEMENTS OF GLUTAMINE 143 IN HUMAN MANGANESE    
JRNL        TITL 2 SUPEROXIDE DISMUTASE: EFFECTS ON STRUCTURE, STABILITY, AND   
JRNL        TITL 3 CATALYSIS.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  39  7131 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10852710                                                     
JRNL        DOI    10.1021/BI9929958                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.E.BORGSTAHL,H.E.PARGE,M.J.HICKEY,W.F.BEYER JUNIOR,         
REMARK   1  AUTH 2 R.A.HALLEWELL,J.A.TAINER                                     
REMARK   1  TITL   THE STRUCTURE OF HUMAN MITOCHONDRIAL MANGANESE SUPEROXIDE    
REMARK   1  TITL 2 DISMUTASE REVEALS A NOVEL TETRAMERIC INTERFACE OF TWO        
REMARK   1  TITL 3 4-HELIX BUNDLES                                              
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  71   107 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/0092-8674(92)90270-M                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3778026.940                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 89153                          
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 SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2574                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.12                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3625                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 390                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3138                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 293                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.26000                                              
REMARK   3    B22 (A**2) : 4.26000                                              
REMARK   3    B33 (A**2) : -8.52000                                             
REMARK   3    B12 (A**2) : 5.15000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.250 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.470 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.190 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 0.330 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 52.94                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ALL.PARAM                                      
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ALL2.TOP                                       
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000010714.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89153                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.330                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, IMIDAZOLE/MALATE, PH   
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-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       80.54733            
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      161.09467            
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      120.82100            
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      201.36833            
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       40.27367            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       80.54733            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      161.09467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      201.36833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      120.82100            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.27367            
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 350   BIOMT1   2  0.500000 -0.866025  0.000000       39.82150            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       68.97286            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      201.36833            
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 B 691  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    92     O    HOH A   613              2.04            
REMARK 500   OH   TYR B    34     O    HOH B   695              2.06            
REMARK 500   O    ILE B   137     O    HOH B   725              2.09            
REMARK 500   NZ   LYS B     1     O    HOH B   722              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   709     O    HOH A   709    10665     1.25            
REMARK 500   OD2  ASP A    10     OD1  ASN B    84     1655     2.18            
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  29      -61.18   -108.34                                   
REMARK 500    ASN A 142     -121.11     45.66                                   
REMARK 500    TYR A 165      -17.77   -153.34                                   
REMARK 500    LYS A 170     -137.63     55.18                                   
REMARK 500    ASN B 142     -123.77     45.39                                   
REMARK 500    TYR B 165      -18.11   -152.66                                   
REMARK 500    LYS B 170     -131.98     56.05                                   
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 600  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 763   O                                                      
REMARK 620 2 HIS A  26   NE2 170.7                                              
REMARK 620 3 HIS A 163   NE2  95.2  90.0                                        
REMARK 620 4 HIS A  74   NE2  93.6  88.2 134.1                                  
REMARK 620 5 ASP A 159   OD1  84.3  86.5 114.9 110.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 601  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 731   O                                                      
REMARK 620 2 ASP B 159   OD1  85.2                                              
REMARK 620 3 HIS B  74   NE2  88.8 111.3                                        
REMARK 620 4 HIS B 163   NE2  97.9 116.1 132.5                                  
REMARK 620 5 HIS B  26   NE2 168.9  85.3  89.5  91.4                            
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 SO4 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 601                  
DBREF  1EM1 A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1EM1 B    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 1EM1 ALA A  143  UNP  P04179    GLN   167 ENGINEERED                     
SEQADV 1EM1 ALA B  143  UNP  P04179    GLN   167 ENGINEERED                     
SEQRES   1 A  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 A  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 A  198  HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 A  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 A  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 A  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 A  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 A  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 A  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 A  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 A  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN ALA          
SEQRES  12 A  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 A  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 A  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 A  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 A  198  CYS LYS LYS                                                  
SEQRES   1 B  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 B  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 B  198  HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 B  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 B  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 B  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 B  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 B  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 B  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 B  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 B  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN ALA          
SEQRES  12 B  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 B  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 B  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 B  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 B  198  CYS LYS LYS                                                  
HET    SO4  A 501       5                                                       
HET     MN  A 600       1                                                       
HET    SO4  B 500       5                                                       
HET     MN  B 601       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4   MN    2(MN 2+)                                                     
FORMUL   7  HOH   *293(H2 O)                                                    
HELIX    1   1 ASN A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLY A   52  1                                  24    
HELIX    3   3 ASP A   53  LEU A   60  1                                   8    
HELIX    4   4 LEU A   60  ASN A   80  1                                  21    
HELIX    5   5 LYS A   90  GLY A  102  1                                  13    
HELIX    6   6 SER A  103  VAL A  118  1                                  16    
HELIX    7   7 PRO A  145  GLY A  151  1                                   7    
HELIX    8   8 TRP A  161  ALA A  164  5                                   4    
HELIX    9   9 TYR A  165  LYS A  170  1                                   6    
HELIX   10  10 VAL A  172  TRP A  181  1                                  10    
HELIX   11  11 ASN A  185  CYS A  196  1                                  12    
HELIX   12  12 ASN B   19  LYS B   29  1                                  11    
HELIX   13  13 LYS B   29  GLY B   52  1                                  24    
HELIX   14  14 ASP B   53  LEU B   60  1                                   8    
HELIX   15  15 LEU B   60  ASN B   80  1                                  21    
HELIX   16  16 LYS B   90  GLY B  102  1                                  13    
HELIX   17  17 SER B  103  GLY B  117  1                                  15    
HELIX   18  18 PRO B  145  GLY B  151  1                                   7    
HELIX   19  19 TRP B  161  ALA B  164  5                                   4    
HELIX   20  20 TYR B  165  LYS B  170  1                                   6    
HELIX   21  21 VAL B  172  TRP B  181  1                                  10    
HELIX   22  22 ASN B  185  LYS B  197  1                                  13    
SHEET    1   A 3 HIS A 134  PRO A 141  0                                        
SHEET    2   A 3 GLY A 122  ASN A 129 -1  O  TRP A 123   N  CYS A 140           
SHEET    3   A 3 ILE A 153  ASP A 159 -1  N  ILE A 153   O  PHE A 128           
SHEET    1   B 3 HIS B 134  PRO B 141  0                                        
SHEET    2   B 3 GLY B 122  ASN B 129 -1  N  TRP B 123   O  CYS B 140           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  N  ILE B 153   O  PHE B 128           
LINK        MN    MN A 600                 O   HOH A 763     1555   1555  2.20  
LINK        MN    MN B 601                 O   HOH B 731     1555   1555  2.29  
LINK        MN    MN A 600                 NE2 HIS A  26     1555   1555  2.13  
LINK        MN    MN A 600                 NE2 HIS A 163     1555   1555  2.09  
LINK        MN    MN A 600                 NE2 HIS A  74     1555   1555  2.11  
LINK        MN    MN A 600                 OD1 ASP A 159     1555   1555  2.13  
LINK        MN    MN B 601                 OD1 ASP B 159     1555   1555  2.04  
LINK        MN    MN B 601                 NE2 HIS B  74     1555   1555  2.28  
LINK        MN    MN B 601                 NE2 HIS B 163     1555   1555  2.22  
LINK        MN    MN B 601                 NE2 HIS B  26     1555   1555  2.23  
CISPEP   1 GLU A   15    PRO A   16          0        -0.56                     
CISPEP   2 GLU B   15    PRO B   16          0        -0.62                     
SITE     1 AC1  5 LYS A 178  HIS B   2  SER B   3  HIS B  71                    
SITE     2 AC1  5 HOH B 703                                                     
SITE     1 AC2  5 LYS A   1  HIS A   2  SER A   3  HIS A  71                    
SITE     2 AC2  5 HOH A 708                                                     
SITE     1 AC3  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC3  5 HOH A 763                                                     
SITE     1 AC4  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC4  5 HOH B 731                                                     
CRYST1   79.643   79.643  241.642  90.00  90.00 120.00 P 61 2 2     24          
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      0.012556  0.007249  0.000000        0.00000                         
SCALE2      0.000000  0.014498  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004138        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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