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Database: PDB
Entry: 1VAR
LinkDB: 1VAR
Original site: 1VAR 
HEADER    OXIDOREDUCTASE                          04-JAN-96   1VAR              
TITLE     MITOCHONDRIAL MANGANESE SUPEROXIDE DISMUTASE VARIANT WITH ILE 58      
TITLE    2 REPLACED BY THR                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: KIDNEY;                                                       
SOURCE   6 GENE: HUMAN KIDNEY SOD2;                                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SODASODB;                                  
SOURCE  10 EXPRESSION_SYSTEM_GENE: HUMAN KIDNEY SOD2                            
KEYWDS    OXIDOREDUCTASE, MANGANESE, MITOCHONDRION, TRANSIT PEPTIDE,            
KEYWDS   2 POLYMORPHISM                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.O.BORGSTAHL,H.E.PARGE,J.A.TAINER                                  
REVDAT   3   29-NOV-17 1VAR    1       HELIX                                    
REVDAT   2   24-FEB-09 1VAR    1       VERSN                                    
REVDAT   1   10-JUN-96 1VAR    0                                                
JRNL        AUTH   G.E.BORGSTAHL,H.E.PARGE,M.J.HICKEY,M.J.JOHNSON,M.BOISSINOT,  
JRNL        AUTH 2 R.A.HALLEWELL,J.R.LEPOCK,D.E.CABELLI,J.A.TAINER              
JRNL        TITL   HUMAN MITOCHONDRIAL MANGANESE SUPEROXIDE DISMUTASE           
JRNL        TITL 2 POLYMORPHIC VARIANT ILE58THR REDUCES ACTIVITY BY             
JRNL        TITL 3 DESTABILIZING THE TETRAMERIC INTERFACE.                      
JRNL        REF    BIOCHEMISTRY                  V.  35  4287 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8605177                                                      
JRNL        DOI    10.1021/BI951892W                                            
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 1992              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13431                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3144                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 175                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.864                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.765                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1VAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000177007.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13431                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       37.50000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.50000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.05000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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   HZ2  LYS A   108     H2   HOH A   364              1.21            
REMARK 500   H    SER B   121     H1   HOH A   205              1.31            
REMARK 500   H    ASN A    19    HE21  GLN A   168              1.33            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 154   C   -  N   -  CA  ANGL. DEV. =   9.0 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    PRO A   8       35.48    -90.60                                   
REMARK 500    TYR A  11        4.54    -53.20                                   
REMARK 500    LYS A  29      -68.27   -104.61                                   
REMARK 500    ASN A 142     -124.63     46.62                                   
REMARK 500    THR A 150      -24.13   -147.45                                   
REMARK 500    TYR A 165       -0.49   -156.25                                   
REMARK 500    GLN A 168      -61.24   -105.12                                   
REMARK 500    LYS A 170     -146.89     57.84                                   
REMARK 500    LYS A 197       61.72   -105.15                                   
REMARK 500    LYS B  29      -61.53   -100.60                                   
REMARK 500    ASN B  84       71.92   -109.84                                   
REMARK 500    PRO B  89     -168.37    -75.69                                   
REMARK 500    ASN B 142     -127.06     49.86                                   
REMARK 500    LEU B 146      -74.59    -47.18                                   
REMARK 500    TYR B 165       -3.96   -163.56                                   
REMARK 500    GLN B 168      -70.13   -115.37                                   
REMARK 500    LYS B 170     -137.32     55.19                                   
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                             MN3 A 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  86.0                                              
REMARK 620 3 ASP A 159   OD2  91.3  95.6                                        
REMARK 620 4 HIS A 163   NE2 101.4 150.8 112.2                                  
REMARK 620 5 HOH A 200   O   173.0  93.1  81.8  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MN3 B 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  74   NE2  86.9                                              
REMARK 620 3 ASP B 159   OD2  90.0 100.8                                        
REMARK 620 4 HIS B 163   NE2  99.6 145.2 113.2                                  
REMARK 620 5 HOH B 200   O   171.2  84.4  92.5  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: MNA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MNB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN3 A 199                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN3 B 199                 
DBREF  1VAR A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1VAR B    1   198  UNP    P04179   SODM_HUMAN      25    222             
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 THR 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 GLN          
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 THR 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 GLN          
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    MN3  A 199       1                                                       
HET    MN3  B 199       1                                                       
HETNAM     MN3 MANGANESE (III) ION                                              
FORMUL   3  MN3    2(MN 3+)                                                     
FORMUL   5  HOH   *175(H2 O)                                                    
HELIX    1 A1A ALA A   20  LEU A   49  1BENT AT SER 28                    30    
HELIX    2 A2A ASP A   53  ASN A   80  1                                  28    
HELIX    3 A3A GLY A   91  PHE A  101  1                                  11    
HELIX    4 A4A SER A  103  VAL A  116  1                                  14    
HELIX    5 A5A LEU A  146  GLY A  151  1                                   6    
HELIX    6 A6A ARG A  173  ILE A  180  1                                   8    
HELIX    7 A7A ASN A  185  LYS A  197  1                                  13    
HELIX    8 A1B ALA B   20  LEU B   49  1BENT AT SER 28                    30    
HELIX    9 A2B ASP B   53  ASN B   80  1                                  28    
HELIX   10 A3B GLY B   91  PHE B  101  1                                  11    
HELIX   11 A4B SER B  103  VAL B  116  1                                  14    
HELIX   12 A5B LEU B  146  GLY B  151  1                                   6    
HELIX   13 A6B ARG B  173  ILE B  180  1                                   8    
HELIX   14 A7B ASN B  185  LYS B  197  1                                  13    
SHEET    1 B1A 3 HIS A 134  PRO A 141  0                                        
SHEET    2 B1A 3 GLY A 122  ASN A 129 -1                                        
SHEET    3 B1A 3 LEU A 152  ASP A 159 -1                                        
SHEET    1 B1B 3 HIS B 134  PRO B 141  0                                        
SHEET    2 B1B 3 GLY B 122  ASN B 129 -1                                        
SHEET    3 B1B 3 LEU B 152  ASP B 159 -1                                        
LINK        MN   MN3 A 199                 NE2 HIS A  26     1555   1555  2.07  
LINK        MN   MN3 A 199                 NE2 HIS A  74     1555   1555  2.02  
LINK        MN   MN3 A 199                 OD2 ASP A 159     1555   1555  2.01  
LINK        MN   MN3 A 199                 NE2 HIS A 163     1555   1555  2.01  
LINK        MN   MN3 A 199                 O   HOH A 200     1555   1555  1.98  
LINK        MN   MN3 B 199                 NE2 HIS B  26     1555   1555  2.03  
LINK        MN   MN3 B 199                 NE2 HIS B  74     1555   1555  1.99  
LINK        MN   MN3 B 199                 OD2 ASP B 159     1555   1555  1.93  
LINK        MN   MN3 B 199                 NE2 HIS B 163     1555   1555  1.96  
LINK        MN   MN3 B 199                 O   HOH B 200     1555   1555  1.98  
CISPEP   1 GLU A   15    PRO A   16          0         0.04                     
CISPEP   2 GLU B   15    PRO B   16          0        -0.11                     
SITE     1 MNA  6 MN3 A 199  HIS A  26  HIS A  74  ASP A 159                    
SITE     2 MNA  6 HIS A 163  HOH A 200                                          
SITE     1 MNB  6 MN3 B 199  HIS B  26  HIS B  74  ASP B 159                    
SITE     2 MNB  6 HIS B 163  HOH B 200                                          
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A 200                                                     
SITE     1 AC2  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  5 HOH B 200                                                     
CRYST1   75.000   78.100   68.100  90.00  90.00  90.00 P 21 21 2     8          
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      0.013333  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012804  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014684        0.00000                         
MTRIX1   1  0.915800 -0.401600  0.000200        0.03500    1                    
MTRIX2   1 -0.401600 -0.915800  0.000900       -0.07100    1                    
MTRIX3   1 -0.000200 -0.000900 -1.000000      101.55600    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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