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Database: PDB
Entry: 2GDS
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Original site: 2GDS 
HEADER    OXIDOREDUCTASE                          16-MAR-06   2GDS              
TITLE     INTERRUPTING THE HYDROGEN BONDING NETWORK AT THE ACTIVE               
TITLE    2 SITE OF HUMAN MANGANESE SUPEROXIDE DISMUTASE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
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 GENE: SOD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: QC774I (SOD--);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    HUMAN MANGANESE SUPEROXIDE DISMUTASE, H30N MUTATION,                  
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.PERRY                                                             
REVDAT   2   24-FEB-09 2GDS    1       VERSN                                    
REVDAT   1   28-MAR-06 2GDS    0                                                
JRNL        AUTH   C.A.RAMILO,V.LEVEQUE,Y.GUAN,J.R.LEPOCK,J.A.TAINER,           
JRNL        AUTH 2 H.S.NICK,D.N.SILVERMAN                                       
JRNL        TITL   INTERRUPTING THE HYDROGEN BOND NETWORK AT THE                
JRNL        TITL 2 ACTIVE SITE OF HUMAN MANGANESE SUPEROXIDE DISMUTASE          
JRNL        REF    J.BIOL.CHEM.                  V. 274 27711 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10488113                                                     
JRNL        DOI    10.1074/JBC.274.39.27711                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35154                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.300                           
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            : NULL                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : NULL                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.00                          
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 2GDS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036993.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(311) BENT        
REMARK 200                                   MON                                
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL              
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35154                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06400                            
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) : 2.30                     
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) : 0.36400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1QNM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19.3MG/ML PROTEIN, 25MM POTASSIUM        
REMARK 280  PHOSPHATE, 20% POLYETHYLENE GLYCOL 2000, MONOMETHYL ETHER, PH       
REMARK 280  7.80, VAPOR DIFFUSION, TEMPERATURE 298.0K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       36.85000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.78500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.85000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.78500            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER                        
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: 8320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 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       25.89    -77.18                                   
REMARK 500    LYS A  29      -72.52   -107.59                                   
REMARK 500    ASN A 142     -116.94     47.92                                   
REMARK 500    TYR A 165      -26.42   -158.37                                   
REMARK 500    LYS A 170     -133.92     51.41                                   
REMARK 500    ASN B  19      151.84    -48.66                                   
REMARK 500    ASN B 142     -118.87     52.07                                   
REMARK 500    LEU B 155      -52.85   -120.82                                   
REMARK 500    TYR B 165      -21.11   -153.77                                   
REMARK 500    LYS B 170     -124.64     58.52                                   
REMARK 500    ASN C 142     -129.19     54.07                                   
REMARK 500    TYR C 165      -33.00   -160.81                                   
REMARK 500    GLN C 168      -63.24   -107.98                                   
REMARK 500    LYS C 170     -136.62     54.94                                   
REMARK 500    SER D  82      138.83   -175.62                                   
REMARK 500    ASN D 142     -123.06     50.91                                   
REMARK 500    TYR D 165       -7.65   -156.92                                   
REMARK 500    LYS D 170     -144.22     53.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 249        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH D 365        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C 477        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH B 468        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH D 467        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH B 535        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH C 594        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A 542        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH D 599        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH D 600        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH A 563        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH D 642        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH C 677        DISTANCE =  7.75 ANGSTROMS                       
REMARK 525    HOH B 732        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH C 698        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH C 703        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 759        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH D 710        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH A 683        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 776        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH C 752        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH D 731        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A 694        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH D 742        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 701        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 702        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH D 750        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH A 709        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH C 779        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH B 830        DISTANCE =  8.25 ANGSTROMS                       
REMARK 525    HOH B 844        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH D 775        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH A 765        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH C 837        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A 799        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A 802        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 803        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH B 911        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH C 892        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A 808        DISTANCE =  8.96 ANGSTROMS                       
REMARK 525    HOH B 916        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH D 847        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 928        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH C 932        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH D 858        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH B 947        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 863        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A 910        DISTANCE =  6.63 ANGSTROMS                       
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 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  74   NE2                                                    
REMARK 620 2 HIS A 163   NE2 140.3                                              
REMARK 620 3 ASP A 159   OD1  90.3 128.2                                        
REMARK 620 4 HIS A  26   NE2  83.8  89.8  85.0                                  
REMARK 620 5 HOH A5011   O    94.9  99.6  81.5 166.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  74   NE2                                                    
REMARK 620 2 HIS B 163   NE2 146.5                                              
REMARK 620 3 ASP B 159   OD1  93.3 120.2                                        
REMARK 620 4 HIS B  26   NE2  91.8  87.2  95.0                                  
REMARK 620 5 HOH B5022   O    88.2  99.1  73.7 168.7                            
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  74   NE2                                                    
REMARK 620 2 HIS C 163   NE2 151.9                                              
REMARK 620 3 ASP C 159   OD1  93.7 114.3                                        
REMARK 620 4 HIS C  26   NE2  91.5  95.1  82.9                                  
REMARK 620 5 HOH C5033   O    89.6  87.9  88.7 171.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 202  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  74   NE2                                                    
REMARK 620 2 HIS D 163   NE2 131.9                                              
REMARK 620 3 ASP D 159   OD1 109.1 118.7                                        
REMARK 620 4 HIS D  26   NE2  85.6  92.4  85.6                                  
REMARK 620 5 HOH D5044   O   106.4  87.5  80.3 163.8                            
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 199                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 200                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 201                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 202                  
DBREF  2GDS A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2GDS B    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2GDS C    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  2GDS D    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 2GDS ASN A   30  UNP  P04179    HIS    54 ENGINEERED                     
SEQADV 2GDS ASN B   30  UNP  P04179    HIS    54 ENGINEERED                     
SEQADV 2GDS ASN C   30  UNP  P04179    HIS    54 ENGINEERED                     
SEQADV 2GDS ASN D   30  UNP  P04179    HIS    54 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 ASN 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 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 ASN 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 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                                                  
SEQRES   1 C  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 C  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 C  198  HIS SER LYS ASN HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 C  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 C  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 C  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 C  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 C  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 C  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 C  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 C  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 C  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 C  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 C  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 C  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 C  198  CYS LYS LYS                                                  
SEQRES   1 D  198  LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA          
SEQRES   2 D  198  LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS          
SEQRES   3 D  198  HIS SER LYS ASN HIS ALA ALA TYR VAL ASN ASN LEU ASN          
SEQRES   4 D  198  VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY          
SEQRES   5 D  198  ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS          
SEQRES   6 D  198  PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP          
SEQRES   7 D  198  THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY          
SEQRES   8 D  198  GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE          
SEQRES   9 D  198  ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY          
SEQRES  10 D  198  VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS          
SEQRES  11 D  198  GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN          
SEQRES  12 D  198  ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU          
SEQRES  13 D  198  GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN TYR          
SEQRES  14 D  198  LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN          
SEQRES  15 D  198  VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA          
SEQRES  16 D  198  CYS LYS LYS                                                  
HET     MN  A 199       1                                                       
HET     MN  B 200       1                                                       
HET     MN  C 201       1                                                       
HET     MN  D 202       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *745(H2 O)                                                    
HELIX    1   1 ASN A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  ALA A   50  1                                  22    
HELIX    3   3 ASP A   53  LEU A   60  1                                   8    
HELIX    4   4 LEU A   60  LEU A   81  1                                  22    
HELIX    5   5 GLY A   91  GLY A  102  1                                  12    
HELIX    6   6 SER A  103  GLY A  117  1                                  15    
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  182  ILE A  184  5                                   3    
HELIX   12  12 ASN A  185  LYS A  198  1                                  14    
HELIX   13  13 ASN B   19  LYS B   29  1                                  11    
HELIX   14  14 LYS B   29  GLY B   52  1                                  24    
HELIX   15  15 ASP B   53  LEU B   60  1                                   8    
HELIX   16  16 LEU B   60  LEU B   81  1                                  22    
HELIX   17  17 GLY B   91  GLY B  102  1                                  12    
HELIX   18  18 SER B  103  VAL B  118  1                                  16    
HELIX   19  19 PRO B  145  GLY B  151  1                                   7    
HELIX   20  20 TRP B  161  ALA B  164  5                                   4    
HELIX   21  21 TYR B  165  LYS B  170  1                                   6    
HELIX   22  22 VAL B  172  TRP B  181  1                                  10    
HELIX   23  23 ASN B  185  LYS B  198  1                                  14    
HELIX   24  24 ASN C   19  LYS C   29  1                                  11    
HELIX   25  25 LYS C   29  GLY C   52  1                                  24    
HELIX   26  26 ASP C   53  ASN C   80  1                                  28    
HELIX   27  27 GLY C   91  GLY C  102  1                                  12    
HELIX   28  28 SER C  103  VAL C  118  1                                  16    
HELIX   29  29 PRO C  145  THR C  150  1                                   6    
HELIX   30  30 TRP C  161  ALA C  164  5                                   4    
HELIX   31  31 TYR C  165  LYS C  170  1                                   6    
HELIX   32  32 VAL C  172  TRP C  181  1                                  10    
HELIX   33  33 ASN C  182  ILE C  184  5                                   3    
HELIX   34  34 ASN C  185  ALA C  195  1                                  11    
HELIX   35  35 ASP D   10  GLU D   15  5                                   6    
HELIX   36  36 ASN D   19  LYS D   29  1                                  11    
HELIX   37  37 LYS D   29  GLY D   52  1                                  24    
HELIX   38  38 ASP D   53  LEU D   60  1                                   8    
HELIX   39  39 LEU D   60  LEU D   81  1                                  22    
HELIX   40  40 GLY D   91  GLY D  102  1                                  12    
HELIX   41  41 SER D  103  VAL D  118  1                                  16    
HELIX   42  42 PRO D  145  GLY D  151  1                                   7    
HELIX   43  43 TRP D  161  ALA D  164  5                                   4    
HELIX   44  44 TYR D  165  LYS D  170  1                                   6    
HELIX   45  45 VAL D  172  TRP D  181  1                                  10    
HELIX   46  46 ASN D  182  ILE D  184  5                                   3    
HELIX   47  47 ASN D  185  ALA D  195  1                                  11    
SHEET    1   A 3 HIS A 134  PRO A 141  0                                        
SHEET    2   A 3 GLY A 122  ASN A 129 -1  N  ASN A 129   O  HIS A 134           
SHEET    3   A 3 ILE A 153  ASP A 159 -1  O  LEU A 155   N  LEU A 126           
SHEET    1   B 3 HIS B 134  PRO B 141  0                                        
SHEET    2   B 3 GLY B 122  ASN B 129 -1  N  ASN B 129   O  HIS B 134           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  O  LEU B 156   N  LEU B 126           
SHEET    1   C 3 HIS C 134  PRO C 141  0                                        
SHEET    2   C 3 GLY C 122  ASN C 129 -1  N  ASN C 129   O  HIS C 134           
SHEET    3   C 3 ILE C 153  ASP C 159 -1  O  LEU C 156   N  LEU C 126           
SHEET    1   D 3 HIS D 134  PRO D 141  0                                        
SHEET    2   D 3 GLY D 122  ASN D 129 -1  N  TRP D 125   O  ALA D 138           
SHEET    3   D 3 ILE D 153  ASP D 159 -1  O  LEU D 155   N  LEU D 126           
LINK         NE2 HIS A  74                MN    MN A 199     1555   1555  2.20  
LINK         NE2 HIS A 163                MN    MN A 199     1555   1555  2.08  
LINK         OD1 ASP A 159                MN    MN A 199     1555   1555  2.00  
LINK         NE2 HIS B  74                MN    MN B 200     1555   1555  2.14  
LINK         NE2 HIS B 163                MN    MN B 200     1555   1555  2.13  
LINK         OD1 ASP B 159                MN    MN B 200     1555   1555  1.97  
LINK         NE2 HIS C  74                MN    MN C 201     1555   1555  2.08  
LINK         NE2 HIS C 163                MN    MN C 201     1555   1555  2.13  
LINK         OD1 ASP C 159                MN    MN C 201     1555   1555  1.96  
LINK         NE2 HIS D  74                MN    MN D 202     1555   1555  2.15  
LINK         NE2 HIS D 163                MN    MN D 202     1555   1555  2.04  
LINK         OD1 ASP D 159                MN    MN D 202     1555   1555  2.06  
LINK         NE2 HIS A  26                MN    MN A 199     1555   1555  2.24  
LINK         NE2 HIS B  26                MN    MN B 200     1555   1555  2.21  
LINK         NE2 HIS C  26                MN    MN C 201     1555   1555  2.26  
LINK         NE2 HIS D  26                MN    MN D 202     1555   1555  2.22  
LINK        MN    MN A 199                 O   HOH A5011     1555   1555  1.95  
LINK        MN    MN B 200                 O   HOH B5022     1555   1555  2.32  
LINK        MN    MN C 201                 O   HOH C5033     1555   1555  2.29  
LINK        MN    MN D 202                 O   HOH D5044     1555   1555  2.06  
CISPEP   1 GLU A   15    PRO A   16          0        -0.08                     
CISPEP   2 GLU B   15    PRO B   16          0        -0.22                     
CISPEP   3 GLU C   15    PRO C   16          0         0.07                     
CISPEP   4 GLU D   15    PRO D   16          0         0.14                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A5011                                                     
SITE     1 AC2  6 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  6 HOH B 945  HOH B5022                                          
SITE     1 AC3  5 HIS C  26  HIS C  74  ASP C 159  HIS C 163                    
SITE     2 AC3  5 HOH C5033                                                     
SITE     1 AC4  5 HIS D  26  HIS D  74  ASP D 159  HIS D 163                    
SITE     2 AC4  5 HOH D5044                                                     
CRYST1   73.700   77.570  135.460  90.00  90.00  90.00 P 21 21 21   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      0.013569  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012892  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007382        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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