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Database: PDB
Entry: 3MDS
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HEADER    OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)     20-OCT-93   3MDS              
TITLE     MAGANESE SUPEROXIDE DISMUTASE FROM THERMUS THERMOPHILUS               
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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 274                                                  
KEYWDS    OXIDOREDUCTASE, OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.LUDWIG,A.L.METZGER,K.A.PATTRIDGE,W.C.STALLINGS                    
REVDAT   6   29-NOV-17 3MDS    1       HELIX                                    
REVDAT   5   13-JUL-11 3MDS    1       VERSN                                    
REVDAT   4   24-FEB-09 3MDS    1       VERSN                                    
REVDAT   3   01-APR-03 3MDS    1       JRNL                                     
REVDAT   2   05-APR-00 3MDS    1       HET    HETATM FORMUL                     
REVDAT   1   31-JAN-94 3MDS    0                                                
JRNL        AUTH   M.L.LUDWIG,A.L.METZGER,K.A.PATTRIDGE,W.C.STALLINGS           
JRNL        TITL   MANGANESE SUPEROXIDE DISMUTASE FROM THERMUS THERMOPHILUS. A  
JRNL        TITL 2 STRUCTURAL MODEL REFINED AT 1.8 A RESOLUTION.                
JRNL        REF    J.MOL.BIOL.                   V. 219   335 1991              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   2038060                                                      
JRNL        DOI    10.1016/0022-2836(91)90569-R                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.C.STALLINGS,C.BULL,J.A.FEE,M.S.LAH,M.L.LUDWIG              
REMARK   1  TITL   IRON AND MANGANESE SUPEROXIDE DISMUTASES: CATALYTIC          
REMARK   1  TITL 2 INFERENCES FROM THE STRUCTURES MOLECULAR BIOLOGY OF FREE     
REMARK   1  TITL 3 RADICAL SCAVENGING SYSTEMS                                   
REMARK   1  EDIT   J.G.SCANDALIOS                                               
REMARK   1  REF    MOLECULAR BIOLOGY OF FREE              193 1992              
REMARK   1  REF  2 RADICAL SCAVENGING SYSTEMS                                   
REMARK   1  PUBL   COLD SPRING HARBOR LAB.PRESS, PLAINVIEW,N.Y.                 
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.C.STALLINGS,A.L.METZGER,K.A.PATTRIDGE,J.A.FEE,M.L.LUDWIG   
REMARK   1  TITL   STRUCTURE-FUNCTION RELATIONSHIPS IN FE-AND MN-SUPEROXIDE     
REMARK   1  TITL 2 DISMUTASES                                                   
REMARK   1  REF    FREE RADICAL RES.COMMUN.      V.  12   259 1991              
REMARK   1  REFN                   ISSN 8755-0199                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   W.C.STALLINGS,K.A.PATTRIDGE,R.K.STRONG,M.L.LUDWIG            
REMARK   1  TITL   THE STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM THERMUS 
REMARK   1  TITL 2 THERMOPHILUS AT 2.4 ANGSTROMS RESOLUTION                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 260 16424 1985              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   W.C.STALLINGS,K.A.PATTRIDGE,R.K.STRONG,M.L.LUDWIG            
REMARK   1  TITL   MANGANESE AND IRON SUPEROXIDE DISMUTASES ARE STRUCTURAL      
REMARK   1  TITL 2 HOMOLOGS                                                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 259 10695 1984              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 54052                          
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 + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3282                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 187                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.020 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 2.035 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: THE SIDE CHAIN OF GLU 101 IS ILL          
REMARK   3  -DEFINED IN THE B CHAIN.                                            
REMARK   4                                                                      
REMARK   4 3MDS 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_1000179055.                                   
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) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
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) : 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                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.80000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       73.30000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       73.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       13.90000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       73.30000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       73.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.70000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       73.30000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       73.30000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       13.90000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       73.30000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       73.30000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.70000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       27.80000            
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 TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL   
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO          
REMARK 300 CHAIN *A*.                                                           
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: 6210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 166   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 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    ASN A 150     -123.08     51.04                                   
REMARK 500    TYR A 172       -3.94   -141.56                                   
REMARK 500    GLN A 177     -125.53     49.67                                   
REMARK 500    ASN B 150     -126.40     51.06                                   
REMARK 500    GLN B 177     -126.74     51.45                                   
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 204  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  28   NE2                                                    
REMARK 620 2 HIS A  83   NE2  92.3                                              
REMARK 620 3 ASP A 166   OD2  89.3 110.1                                        
REMARK 620 4 HIS A 170   NE2  90.2 130.9 118.9                                  
REMARK 620 5 HOH A 205   O   175.3  90.3  86.1  91.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MN3 B 204  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 170   NE2                                                    
REMARK 620 2 ASP B 166   OD2 117.9                                              
REMARK 620 3 HIS B  83   NE2 131.7 110.4                                        
REMARK 620 4 HOH B 205   O    89.1  87.1  92.9                                  
REMARK 620 5 HIS B  28   NE2  90.7  85.6  93.4 171.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE                  
REMARK 650 ALGORITHM OF KABSCH AND SANDER, WITH THE FOLLOWING                   
REMARK 650 EXCEPTIONS: HELICES START WITH THE FIRST RESIDUE HAVING              
REMARK 650 A HELICAL HYDROGEN BOND; SUCCESSIVE 3-10 TURNS ARE GIVEN             
REMARK 650 PRIORITY OVER SHORT 3-10 HELICES.                                    
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN3 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN3 B 204                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE ASSIGNS LYS RATHER THAN ILE AT POSITION 69;             
REMARK 999 THE FIT OF THIS RESIDUE WILL BE REINVESTIGATED.                      
DBREF  3MDS A    1   203  UNP    P61503   SODM_THET8       1    203             
DBREF  3MDS B    1   203  UNP    P61503   SODM_THET8       1    203             
SEQRES   1 A  203  PRO TYR PRO PHE LYS LEU PRO ASP LEU GLY TYR PRO TYR          
SEQRES   2 A  203  GLU ALA LEU GLU PRO HIS ILE ASP ALA LYS THR MET GLU          
SEQRES   3 A  203  ILE HIS HIS GLN LYS HIS HIS GLY ALA TYR VAL THR ASN          
SEQRES   4 A  203  LEU ASN ALA ALA LEU GLU LYS TYR PRO TYR LEU HIS GLY          
SEQRES   5 A  203  VAL GLU VAL GLU VAL LEU LEU ARG HIS LEU ALA ALA LEU          
SEQRES   6 A  203  PRO GLN ASP ILE GLN THR ALA VAL ARG ASN ASN GLY GLY          
SEQRES   7 A  203  GLY HIS LEU ASN HIS SER LEU PHE TRP ARG LEU LEU THR          
SEQRES   8 A  203  PRO GLY GLY ALA LYS GLU PRO VAL GLY GLU LEU LYS LYS          
SEQRES   9 A  203  ALA ILE ASP GLU GLN PHE GLY GLY PHE GLN ALA LEU LYS          
SEQRES  10 A  203  GLU LYS LEU THR GLN ALA ALA MET GLY ARG PHE GLY SER          
SEQRES  11 A  203  GLY TRP ALA TRP LEU VAL LYS ASP PRO PHE GLY LYS LEU          
SEQRES  12 A  203  HIS VAL LEU SER THR PRO ASN GLN ASP ASN PRO VAL MET          
SEQRES  13 A  203  GLU GLY PHE THR PRO ILE VAL GLY ILE ASP VAL TRP GLU          
SEQRES  14 A  203  HIS ALA TYR TYR LEU LYS TYR GLN ASN ARG ARG ALA ASP          
SEQRES  15 A  203  TYR LEU GLN ALA ILE TRP ASN VAL LEU ASN TRP ASP VAL          
SEQRES  16 A  203  ALA GLU GLU PHE PHE LYS LYS ALA                              
SEQRES   1 B  203  PRO TYR PRO PHE LYS LEU PRO ASP LEU GLY TYR PRO TYR          
SEQRES   2 B  203  GLU ALA LEU GLU PRO HIS ILE ASP ALA LYS THR MET GLU          
SEQRES   3 B  203  ILE HIS HIS GLN LYS HIS HIS GLY ALA TYR VAL THR ASN          
SEQRES   4 B  203  LEU ASN ALA ALA LEU GLU LYS TYR PRO TYR LEU HIS GLY          
SEQRES   5 B  203  VAL GLU VAL GLU VAL LEU LEU ARG HIS LEU ALA ALA LEU          
SEQRES   6 B  203  PRO GLN ASP ILE GLN THR ALA VAL ARG ASN ASN GLY GLY          
SEQRES   7 B  203  GLY HIS LEU ASN HIS SER LEU PHE TRP ARG LEU LEU THR          
SEQRES   8 B  203  PRO GLY GLY ALA LYS GLU PRO VAL GLY GLU LEU LYS LYS          
SEQRES   9 B  203  ALA ILE ASP GLU GLN PHE GLY GLY PHE GLN ALA LEU LYS          
SEQRES  10 B  203  GLU LYS LEU THR GLN ALA ALA MET GLY ARG PHE GLY SER          
SEQRES  11 B  203  GLY TRP ALA TRP LEU VAL LYS ASP PRO PHE GLY LYS LEU          
SEQRES  12 B  203  HIS VAL LEU SER THR PRO ASN GLN ASP ASN PRO VAL MET          
SEQRES  13 B  203  GLU GLY PHE THR PRO ILE VAL GLY ILE ASP VAL TRP GLU          
SEQRES  14 B  203  HIS ALA TYR TYR LEU LYS TYR GLN ASN ARG ARG ALA ASP          
SEQRES  15 B  203  TYR LEU GLN ALA ILE TRP ASN VAL LEU ASN TRP ASP VAL          
SEQRES  16 B  203  ALA GLU GLU PHE PHE LYS LYS ALA                              
HET    MN3  A 204       1                                                       
HET    MN3  B 204       1                                                       
HETNAM     MN3 MANGANESE (III) ION                                              
FORMUL   3  MN3    2(MN 3+)                                                     
FORMUL   5  HOH   *187(H2 O)                                                    
HELIX    1  A1 ASP A   21  GLU A   45  1                                  25    
HELIX    2  A2 GLU A   54  ARG A   60  1                                   7    
HELIX    3  A3 ILE A   69  LEU A   89  1                                  21    
HELIX    4  A4 GLY A  100  GLN A  109  1                                  10    
HELIX    5  A5 GLY A  112  GLY A  126  1                                  15    
HELIX    6  A6 ASN A  153  GLU A  157  5                                   5    
HELIX    7  A7 ARG A  179  ILE A  187  1                                   9    
HELIX    8  A8 ASN A  192  LYS A  202  1                                  11    
HELIX    9  B1 ASP B   21  GLU B   45  1                                  25    
HELIX   10  B2 GLU B   54  ARG B   60  1                                   7    
HELIX   11  B3 ILE B   69  LEU B   89  1                                  21    
HELIX   12  B4 GLY B  100  GLN B  109  1                                  10    
HELIX   13  B5 GLY B  112  GLY B  126  1                                  15    
HELIX   14  B6 ASN B  153  GLU B  157  5                                   5    
HELIX   15  B7 ARG B  179  ILE B  187  1                                   9    
HELIX   16  B8 ASN B  192  LYS B  202  1                                  11    
SHEET    1 B1A 3 GLY A 141  ASN A 150  0                                        
SHEET    2 B1A 3 SER A 130  ASP A 138 -1  O  TRP A 132   N  THR A 148           
SHEET    3 B1A 3 THR A 160  VAL A 167 -1  N  THR A 160   O  LYS A 137           
SHEET    1 B1B 3 GLY B 141  ASN B 150  0                                        
SHEET    2 B1B 3 SER B 130  ASP B 138 -1  O  TRP B 132   N  THR B 148           
SHEET    3 B1B 3 THR B 160  VAL B 167 -1  N  THR B 160   O  LYS B 137           
LINK        MN   MN3 A 204                 NE2 HIS A  28     1555   1555  2.14  
LINK        MN   MN3 A 204                 NE2 HIS A  83     1555   1555  2.11  
LINK        MN   MN3 A 204                 OD2 ASP A 166     1555   1555  1.80  
LINK        MN   MN3 A 204                 NE2 HIS A 170     1555   1555  2.15  
LINK        MN   MN3 A 204                 O   HOH A 205     1555   1555  2.07  
LINK        MN   MN3 B 204                 NE2 HIS B 170     1555   1555  2.18  
LINK        MN   MN3 B 204                 OD2 ASP B 166     1555   1555  1.78  
LINK        MN   MN3 B 204                 NE2 HIS B  83     1555   1555  2.08  
LINK        MN   MN3 B 204                 O   HOH B 205     1555   1555  2.09  
LINK        MN   MN3 B 204                 NE2 HIS B  28     1555   1555  2.14  
CISPEP   1 TYR A    2    PRO A    3          0        -3.46                     
CISPEP   2 GLU A   17    PRO A   18          0         1.80                     
CISPEP   3 TYR B    2    PRO B    3          0        -0.39                     
CISPEP   4 GLU B   17    PRO B   18          0         0.49                     
SITE     1 AC1  5 HIS A  28  HIS A  83  ASP A 166  HIS A 170                    
SITE     2 AC1  5 HOH A 205                                                     
SITE     1 AC2  5 HIS B  28  HIS B  83  ASP B 166  HIS B 170                    
SITE     2 AC2  5 HOH B 205                                                     
CRYST1  146.600  146.600   55.600  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006821  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006821  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017986        0.00000                         
MTRIX1   1 -0.059100 -0.938400  0.340300       72.79558    1                    
MTRIX2   1 -0.942600 -0.059800 -0.328500       72.95026    1                    
MTRIX3   1  0.328600 -0.340200 -0.881100        0.51355    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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