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Database: PDB
Entry: 1VEW
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Original site: 1VEW 
HEADER    OXIDOREDUCTASE                          20-JAN-98   1VEW              
TITLE     MANGANESE SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MNSOD, MNSD;                                                
COMPND   5 EC: 1.15.1.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: AB2463/PDT1-5                                                
KEYWDS    SUPEROXIDE DISMUTASE, MANGANESE ENZYME, METALLOPROTEIN, DNA           
KEYWDS   2 BINDING, OXIDOREDUCTASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.EDWARDS,H.M.BAKER,M.M.WHITTAKER,J.W.WHITTAKER,                    
AUTHOR   2 G.B.JAMESON,E.N.BAKER                                                
REVDAT   2   24-FEB-09 1VEW    1       VERSN                                    
REVDAT   1   27-MAY-98 1VEW    0                                                
JRNL        AUTH   R.A.EDWARDS,H.M.BAKER,M.M.WHITTAKER,J.W.WHITTAKER,           
JRNL        AUTH 2 G.B.JAMESON,E.N.BAKER                                        
JRNL        TITL   CRYSTAL STRUCTURE OF ESCHERICHIA COLI MANGANESE              
JRNL        TITL 2 SUPEROXIDE DISMUTASE AT 2.1-ANGSTROM RESOLUTION.             
JRNL        REF    J.BIOL.INORG.CHEM.            V.   3   161 1998              
JRNL        REFN                   ISSN 0949-8257                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-E                                           
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53872                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2874                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1860                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1880                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.218                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2874                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 53872                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6532                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 411                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 23.300                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.010 ; 0.400 ; 6716            
REMARK   3   BOND ANGLES            (DEGREES) : 1.200 ; 0.600 ; 9072            
REMARK   3   TORSION ANGLES         (DEGREES) : 15.600; 1.200 ; 3892            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.015 ; 0.650 ; 180             
REMARK   3   GENERAL PLANES               (A) : 0.016 ; 2.200 ; 968             
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : 1.600 ; 3.400 ; 6700            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.114 ; 2.000 ; 2157            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : MOEWS AND KRETSINGER (J.MOL.BIOL.(1975)91, 201-      
REMARK   3                 228)                                                 
REMARK   3   KSOL        : 0.83                                                 
REMARK   3   BSOL        : 130.00                                               
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT CSDX-PROTGEO                                 
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1VEW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUL-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-C                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : 0.3MM DIAMETER COLLIMATOR          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56890                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 0.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.19100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1MNG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT ROOM              
REMARK 280  TEMPERATURE USING THE HANGING DROP METHOD. THE HANGING DROPS        
REMARK 280  WERE SUSPENDED OVER 0.75ML OF WELL SOLUTION (16-30% PEG6000         
REMARK 280  AND 0.05M BICINE TITRATED TO PH8.5) AND CONSISTED OF 2UL OF         
REMARK 280  WELL SOLUTION AND 2UL OF PROTEIN SOLUTION (MNSOD AT 12MG/ML IN      
REMARK 280  WATER)., VAPOR DIFFUSION - HANGING DROP                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       91.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.42000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.45500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.42000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.45500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       91.05000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.42000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.45500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       91.05000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.42000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.45500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 214  LIES ON A SPECIAL POSITION.                          
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   47   CG    CD    OE1   OE2                               
REMARK 480     ASN A   50   CG    OD1   ND2                                     
REMARK 480     LYS A  137   CG    CD    CE    NZ                                
REMARK 480     LYS A  186   CG    CD    CE    NZ                                
REMARK 480     LYS A  205   CG    CD    CE    NZ    OXT                         
REMARK 480     GLU B   47   CG    CD    OE1   OE2                               
REMARK 480     ASN B   50   CG    OD1   ND2                                     
REMARK 480     ASP B   61   CG    OD1   OD2                                     
REMARK 480     LYS B  137   CG    CD    CE    NZ                                
REMARK 480     LYS B  186   CG    CD    CE    NZ                                
REMARK 480     LYS B  205   CG    CD    CE    NZ    OXT                         
REMARK 480     GLU C   47   CG    CD    OE1   OE2                               
REMARK 480     ASN C   50   CG    OD1   ND2                                     
REMARK 480     LYS C  137   CG    CD    CE    NZ                                
REMARK 480     LYS C  186   CG    CD    CE    NZ                                
REMARK 480     LYS C  205   CG    CD    CE    NZ    OXT                         
REMARK 480     GLU D   47   CG    CD    OE1   OE2                               
REMARK 480     ASN D   50   CG    OD1   ND2                                     
REMARK 480     LYS D  137   CG    CD    CE    NZ                                
REMARK 480     LYS D  186   CG    CD    CE    NZ                                
REMARK 480     LYS D  205   CG    CD    CE    NZ    OXT                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  89      139.96   -178.19                                   
REMARK 500    ASN A 145     -112.73     49.11                                   
REMARK 500    GLN A 178     -125.53     57.77                                   
REMARK 500    LYS A 204      -12.14     71.05                                   
REMARK 500    LEU B  45       77.40   -115.84                                   
REMARK 500    LYS B  89      139.50   -174.99                                   
REMARK 500    ASN B 145     -113.21     50.21                                   
REMARK 500    TYR B 173       -5.25   -141.86                                   
REMARK 500    GLN B 178     -126.98     57.75                                   
REMARK 500    LYS B 204      -10.51     70.58                                   
REMARK 500    LYS C  29      -60.04   -108.64                                   
REMARK 500    LYS C  89      141.28   -176.81                                   
REMARK 500    ASN C 145     -113.12     49.90                                   
REMARK 500    TYR C 173       -6.64   -140.14                                   
REMARK 500    GLN C 178     -126.27     58.18                                   
REMARK 500    LYS C 204      -13.02     70.64                                   
REMARK 500    LYS D  89      141.21   -174.16                                   
REMARK 500    ASN D 145     -113.16     49.48                                   
REMARK 500    TYR D 173       -5.75   -141.70                                   
REMARK 500    GLN D 178     -124.94     59.30                                   
REMARK 500    LYS D 204       -8.08     69.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  81   NE2  91.2                                              
REMARK 620 3 ASP A 167   OD2  92.5 107.7                                        
REMARK 620 4 HIS A 171   NE2  93.7 129.4 122.3                                  
REMARK 620 5  OH A 207   O   176.0  91.4  83.8  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  81   NE2  93.2                                              
REMARK 620 3 ASP B 167   OD2  93.3 108.3                                        
REMARK 620 4 HIS B 171   NE2  94.9 129.7 120.7                                  
REMARK 620 5  OH B 207   O   173.1  90.9  80.2  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  81   NE2  91.3                                              
REMARK 620 3 ASP C 167   OD2  90.5 108.3                                        
REMARK 620 4 HIS C 171   NE2  93.0 130.3 121.1                                  
REMARK 620 5  OH C 207   O   174.8  90.7  84.4  89.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 206  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  26   NE2                                                    
REMARK 620 2 HIS D  81   NE2  91.8                                              
REMARK 620 3 ASP D 167   OD2  92.8 105.9                                        
REMARK 620 4 HIS D 171   NE2  93.8 131.0 122.3                                  
REMARK 620 5  OH D 207   O   176.3  90.2  83.7  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: MN1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: MANGANESE-BOUND ACTIVE SITE ON CHAIN A.            
REMARK 800  CATALYTIC REDOX CENTER.                                             
REMARK 800 SITE_IDENTIFIER: MN2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: MANGANESE-BOUND ACTIVE SITE ON CHAIN B.            
REMARK 800  CATALYTIC REDOX CENTER.                                             
REMARK 800 SITE_IDENTIFIER: MN3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: MANGANESE-BOUND ACTIVE SITE ON CHAIN C.            
REMARK 800  CATALYTIC REDOX CENTER.                                             
REMARK 800 SITE_IDENTIFIER: MN4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: MANGANESE-BOUND ACTIVE SITE ON CHAIN D.            
REMARK 800  CATALYTIC REDOX CENTER.                                             
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 206                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 207                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 206                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH B 207                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 206                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH C 207                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 206                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH D 207                  
DBREF  1VEW A    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1VEW B    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1VEW C    1   205  UNP    P00448   SODM_ECOLI       1    205             
DBREF  1VEW D    1   205  UNP    P00448   SODM_ECOLI       1    205             
SEQRES   1 A  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 A  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 A  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 A  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 A  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 A  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 A  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 A  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 A  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 A  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 A  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 A  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 A  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 A  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 A  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 B  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 B  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 B  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 B  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 B  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 B  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 B  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 B  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 B  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 B  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 B  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 B  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 B  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 B  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 C  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 C  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 C  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 C  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 C  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 C  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 C  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 C  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 C  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 C  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 C  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 C  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 C  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 C  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 C  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 C  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 D  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 D  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 D  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 D  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 D  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 D  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 D  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 D  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 D  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 D  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 D  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 D  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 D  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 D  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 D  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 D  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
HET     MN  A 206       1                                                       
HET     OH  A 207       1                                                       
HET     MN  B 206       1                                                       
HET     OH  B 207       1                                                       
HET     MN  C 206       1                                                       
HET     OH  C 207       1                                                       
HET     MN  D 206       1                                                       
HET     OH  D 207       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      OH HYDROXIDE ION                                                    
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   6   OH    4(H O 1-)                                                    
FORMUL  13  HOH   *411(H2 O)                                                    
HELIX    1   1 LYS A   20  THR A   28  1                                   9    
HELIX    2   2 HIS A   30  SER A   44  1                                  15    
HELIX    3   3 PRO A   46  ALA A   49  1                                   4    
HELIX    4   4 VAL A   53  THR A   58  1                                   6    
HELIX    5   5 LEU A   60  GLN A   62  5                                   3    
HELIX    6   6 ALA A   65  LYS A   86  1                                  22    
HELIX    7   7 GLY A   96  PHE A  106  1                                  11    
HELIX    8   8 VAL A  109  SER A  122  1                                  14    
HELIX    9   9 PRO A  149  MET A  151  5                                   3    
HELIX   10  10 GLU A  153  SER A  156  1                                   4    
HELIX   11  11 GLU A  170  ALA A  172  5                                   3    
HELIX   12  12 TYR A  174  PHE A  177  1                                   4    
HELIX   13  13 ARG A  181  ASN A  190  1                                  10    
HELIX   14  14 TRP A  194  ALA A  203  1                                  10    
HELIX   15  15 LYS B   20  THR B   28  1                                   9    
HELIX   16  16 HIS B   30  LEU B   42  1                                  13    
HELIX   17  17 PRO B   46  ALA B   49  1                                   4    
HELIX   18  18 VAL B   53  THR B   58  1                                   6    
HELIX   19  19 LEU B   60  GLN B   62  5                                   3    
HELIX   20  20 ALA B   65  LYS B   86  1                                  22    
HELIX   21  21 GLY B   96  PHE B  106  1                                  11    
HELIX   22  22 VAL B  109  SER B  122  1                                  14    
HELIX   23  23 PRO B  149  MET B  151  5                                   3    
HELIX   24  24 GLU B  153  SER B  156  1                                   4    
HELIX   25  25 GLU B  170  ALA B  172  5                                   3    
HELIX   26  26 TYR B  174  PHE B  177  1                                   4    
HELIX   27  27 ARG B  181  ASN B  190  1                                  10    
HELIX   28  28 TRP B  194  ALA B  203  1                                  10    
HELIX   29  29 LYS C   20  THR C   28  1                                   9    
HELIX   30  30 HIS C   30  SER C   44  1                                  15    
HELIX   31  31 PRO C   46  ALA C   49  1                                   4    
HELIX   32  32 VAL C   53  THR C   58  1                                   6    
HELIX   33  33 LEU C   60  GLN C   62  5                                   3    
HELIX   34  34 ALA C   65  LYS C   86  1                                  22    
HELIX   35  35 GLY C   96  PHE C  106  1                                  11    
HELIX   36  36 VAL C  109  SER C  122  1                                  14    
HELIX   37  37 PRO C  149  MET C  151  5                                   3    
HELIX   38  38 GLU C  153  SER C  156  1                                   4    
HELIX   39  39 GLU C  170  ALA C  172  5                                   3    
HELIX   40  40 TYR C  174  PHE C  177  1                                   4    
HELIX   41  41 ARG C  181  ASN C  190  1                                  10    
HELIX   42  42 TRP C  194  ALA C  203  1                                  10    
HELIX   43  43 LYS D   20  THR D   28  1                                   9    
HELIX   44  44 HIS D   30  LEU D   42  1                                  13    
HELIX   45  45 PRO D   46  ALA D   49  1                                   4    
HELIX   46  46 VAL D   53  THR D   58  1                                   6    
HELIX   47  47 LEU D   60  GLN D   62  5                                   3    
HELIX   48  48 ALA D   65  LYS D   86  1                                  22    
HELIX   49  49 GLY D   96  PHE D  106  1                                  11    
HELIX   50  50 VAL D  109  SER D  122  1                                  14    
HELIX   51  51 PRO D  149  MET D  151  5                                   3    
HELIX   52  52 GLU D  153  SER D  156  1                                   4    
HELIX   53  53 GLU D  170  ALA D  172  5                                   3    
HELIX   54  54 TYR D  174  PHE D  177  1                                   4    
HELIX   55  55 ARG D  181  ASN D  190  1                                  10    
HELIX   56  56 TRP D  194  ALA D  203  1                                  10    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  N  LYS A 134   O  LYS A 137           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  N  LEU A 166   O  ALA A 129           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  N  LYS B 134   O  LYS B 137           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  N  LEU B 166   O  ALA B 129           
SHEET    1   C 3 LYS C 137  ALA C 144  0                                        
SHEET    2   C 3 GLY C 127  LYS C 134 -1  N  LYS C 134   O  LYS C 137           
SHEET    3   C 3 PHE C 161  ASP C 167 -1  N  LEU C 166   O  ALA C 129           
SHEET    1   D 3 LYS D 137  ALA D 144  0                                        
SHEET    2   D 3 GLY D 127  LYS D 134 -1  N  LYS D 134   O  LYS D 137           
SHEET    3   D 3 PHE D 161  ASP D 167 -1  N  LEU D 166   O  ALA D 129           
LINK        MN    MN A 206                 NE2 HIS A  26     1555   1555  2.15  
LINK        MN    MN A 206                 NE2 HIS A  81     1555   1555  2.22  
LINK        MN    MN A 206                 OD2 ASP A 167     1555   1555  2.01  
LINK        MN    MN A 206                 NE2 HIS A 171     1555   1555  2.16  
LINK        MN    MN A 206                 O    OH A 207     1555   1555  2.16  
LINK        MN    MN B 206                 NE2 HIS B  26     1555   1555  2.09  
LINK        MN    MN B 206                 NE2 HIS B  81     1555   1555  2.21  
LINK        MN    MN B 206                 OD2 ASP B 167     1555   1555  2.03  
LINK        MN    MN B 206                 NE2 HIS B 171     1555   1555  2.17  
LINK        MN    MN B 206                 O    OH B 207     1555   1555  2.18  
LINK        MN    MN C 206                 NE2 HIS C  26     1555   1555  2.20  
LINK        MN    MN C 206                 NE2 HIS C  81     1555   1555  2.20  
LINK        MN    MN C 206                 OD2 ASP C 167     1555   1555  2.02  
LINK        MN    MN C 206                 NE2 HIS C 171     1555   1555  2.15  
LINK        MN    MN C 206                 O    OH C 207     1555   1555  2.28  
LINK        MN    MN D 206                 NE2 HIS D  26     1555   1555  2.12  
LINK        MN    MN D 206                 NE2 HIS D  81     1555   1555  2.21  
LINK        MN    MN D 206                 OD2 ASP D 167     1555   1555  2.01  
LINK        MN    MN D 206                 NE2 HIS D 171     1555   1555  2.18  
LINK        MN    MN D 206                 O    OH D 207     1555   1555  2.20  
HYDBND       O    OH A  207                 OD1 ASP A  167 1555    1555         
HYDBND       OH  TYR A   34                 NE2 GLN A  146 1555    1555         
HYDBND       O    OH A  207                 NE2 GLN A  146 1555    1555         
HYDBND       OE1 GLN A  146                 ND2 ASN A   80 1555    1555         
HYDBND       OE1 GLN A  146                 NE1 TRP A  128 1555    1555         
HYDBND       O    OH B  207                 OD1 ASP B  167 1555    1555         
HYDBND       OH  TYR B   34                 NE2 GLN B  146 1555    1555         
HYDBND       O    OH B  207                 NE2 GLN B  146 1555    1555         
HYDBND       OE1 GLN B  146                 ND2 ASN B   80 1555    1555         
HYDBND       OE1 GLN B  146                 NE1 TRP B  128 1555    1555         
HYDBND       O    OH C  207                 OD1 ASP C  167 1555    1555         
HYDBND       OH  TYR C   34                 NE2 GLN C  146 1555    1555         
HYDBND       O    OH C  207                 NE2 GLN C  146 1555    1555         
HYDBND       OE1 GLN C  146                 ND2 ASN C   80 1555    1555         
HYDBND       OE1 GLN C  146                 NE1 TRP C  128 1555    1555         
HYDBND       O    OH D  207                 OD1 ASP D  167 1555    1555         
HYDBND       OH  TYR D   34                 NE2 GLN D  146 1555    1555         
HYDBND       O    OH D  207                 NE2 GLN D  146 1555    1555         
HYDBND       OE1 GLN D  146                 ND2 ASN D   80 1555    1555         
HYDBND       OE1 GLN D  146                 NE1 TRP D  128 1555    1555         
CISPEP   1 GLU A   15    PRO A   16          0         3.25                     
CISPEP   2 GLU B   15    PRO B   16          0         3.50                     
CISPEP   3 GLU C   15    PRO C   16          0         4.02                     
CISPEP   4 GLU D   15    PRO D   16          0         3.91                     
SITE     1 MN1  6  MN A 206  HIS A  26  HIS A  81  ASP A 167                    
SITE     2 MN1  6 HIS A 171   OH A 207                                          
SITE     1 MN2  6  MN B 206  HIS B  26  HIS B  81  ASP B 167                    
SITE     2 MN2  6 HIS B 171   OH B 207                                          
SITE     1 MN3  6  MN C 206  HIS C  26  HIS C  81  ASP C 167                    
SITE     2 MN3  6 HIS C 171   OH C 207                                          
SITE     1 MN4  6  MN D 206  HIS D  26  HIS D  81  ASP D 167                    
SITE     2 MN4  6 HIS D 171   OH D 207                                          
SITE     1 AC1  5 HIS A  26  HIS A  81  ASP A 167  HIS A 171                    
SITE     2 AC1  5  OH A 207                                                     
SITE     1 AC2  6 HIS A  81  GLN A 146  ASP A 167  TRP A 169                    
SITE     2 AC2  6 HIS A 171   MN A 206                                          
SITE     1 AC3  5 HIS B  26  HIS B  81  ASP B 167  HIS B 171                    
SITE     2 AC3  5  OH B 207                                                     
SITE     1 AC4  6 HIS B  81  GLN B 146  ASP B 167  TRP B 169                    
SITE     2 AC4  6 HIS B 171   MN B 206                                          
SITE     1 AC5  5 HIS C  26  HIS C  81  ASP C 167  HIS C 171                    
SITE     2 AC5  5  OH C 207                                                     
SITE     1 AC6  6 HIS C  81  GLN C 146  ASP C 167  TRP C 169                    
SITE     2 AC6  6 HIS C 171   MN C 206                                          
SITE     1 AC7  5 HIS D  26  HIS D  81  ASP D 167  HIS D 171                    
SITE     2 AC7  5  OH D 207                                                     
SITE     1 AC8  6 HIS D  81  GLN D 146  ASP D 167  TRP D 169                    
SITE     2 AC8  6 HIS D 171   MN D 206                                          
CRYST1  100.840  108.910  182.100  90.00  90.00  90.00 C 2 2 21     32          
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      0.009917  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009182  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005491        0.00000                         
MTRIX1   1 -0.134086  0.977846  0.160742       10.10900    1                    
MTRIX2   1  0.977948  0.104362  0.180905      -12.66800    1                    
MTRIX3   1  0.160122  0.181454 -0.970276       22.89400    1                    
MTRIX1   2 -0.079286 -0.996480  0.027237      103.40800    1                    
MTRIX2   2 -0.996167  0.080214  0.034875       51.43100    1                    
MTRIX3   2 -0.036937 -0.024368 -0.999020       46.99400    1                    
MTRIX1   3 -0.956616 -0.172522 -0.234782      115.99900    1                    
MTRIX2   3  0.217210 -0.959375 -0.180053       41.21000    1                    
MTRIX3   3 -0.194181 -0.223239  0.955227       24.59400    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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