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Entry: 1MFM
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HEADER    OXIDOREDUCTASE                          16-APR-99   1MFM              
TITLE     MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC                  
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (COPPER,ZINC SUPEROXIDE DISMUTASE);                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: Q133M2SOD;                                                  
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   6 GENE: SOD1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: TOPP 1 (STRATAGENE);                       
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PBR322;                               
SOURCE  12 EXPRESSION_SYSTEM_GENE: HSOD                                         
KEYWDS    OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR, MONOMERIC MUTANT                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FERRARONI,W.RYPNIEWSKI,K.S.WILSON,P.L.ORIOLI,M.S.VIEZZOLI,          
AUTHOR   2 L.BANCI,I.BERTINI,S.MANGANI                                          
REVDAT   5   24-FEB-09 1MFM    1       VERSN                                    
REVDAT   4   01-APR-03 1MFM    1       JRNL                                     
REVDAT   3   01-SEP-99 1MFM    1       SITE                                     
REVDAT   2   04-MAY-99 1MFM    1       JRNL                                     
REVDAT   1   21-APR-99 1MFM    0                                                
JRNL        AUTH   M.FERRARONI,W.RYPNIEWSKI,K.S.WILSON,M.S.VIEZZOLI,            
JRNL        AUTH 2 L.BANCI,I.BERTINI,S.MANGANI                                  
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE MONOMERIC HUMAN SOD             
JRNL        TITL 2 MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION. THE             
JRNL        TITL 3 ENZYME MECHANISM REVISITED.                                  
JRNL        REF    J.MOL.BIOL.                   V. 288   413 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10329151                                                     
JRNL        DOI    10.1006/JMBI.1999.2681                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-96                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.118                  
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) : 69839                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1152                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 13                                            
REMARK   3   SOLVENT ATOMS      : 283                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 19                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12921                   
REMARK   3   NUMBER OF RESTRAINTS                     : 15655                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.031                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.035                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.435                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.134                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.124                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.102                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.090                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.114                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000865.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.89                               
REMARK 200  MONOCHROMATOR                  : TRIANGULAR GE CRYSTAL              
REMARK 200  OPTICS                         : SEGMENTED MIRROR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 681833                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 1SOS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000 15%, CDCL2 200-400 MM,          
REMARK 280  TRIS 100MM, PH=8, PH 8.0                                            
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       17.49500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.54000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.05500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.54000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.49500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.05500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  77    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  78    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  91    CD   CE   NZ                                        
REMARK 470     LYS A 122    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    49     O    HOH A   218              2.03            
REMARK 500   O    HOH A   246     O    HOH A   287              2.06            
REMARK 500   O    HOH A   226     O    HOH A   430              2.08            
REMARK 500   OG   SER A   107     O    HOH A   267              2.10            
REMARK 500   O    HOH A   180     O    HOH A   326              2.11            
REMARK 500   O    HOH A   422     O    HOH A   433              2.11            
REMARK 500   O    PRO A    66     O    HOH A   187              2.12            
REMARK 500   O    HOH A   286     O    HOH A   378              2.14            
REMARK 500   O    HOH A   346     O    HOH A   422              2.15            
REMARK 500   O    HOH A   230     O    HOH A   411              2.15            
REMARK 500   O    HOH A   258     O    HOH A   264              2.16            
REMARK 500   OE2  GLU A    24     O    HOH A   435              2.16            
REMARK 500   O    HOH A   325     O    HOH A   344              2.16            
REMARK 500   CG   LYS A     9     O    HOH A   330              2.16            
REMARK 500   O    HOH A   183     O    HOH A   345              2.16            
REMARK 500   O    HOH A   276     O    HOH A   312              2.18            
REMARK 500   O    HOH A   231     O    HOH A   286              2.18            
REMARK 500   O    HOH A   211     O    HOH A   436              2.18            
REMARK 500   O    HOH A   179     O    HOH A   435              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   285     O    HOH A   293     4556     2.11            
REMARK 500   O    HOH A   186     O    HOH A   268     1455     2.16            
REMARK 500   OD2  ASP A    90    CD    CD  A   158     1455     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A  21   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    GLY A  56   C   -  N   -  CA  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    CYS A  57   CA  -  CB  -  SG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    CYS A  57   O   -  C   -  N   ANGL. DEV. =  10.3 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  53       56.79    -95.75                                   
REMARK 500    CYS A  57       45.25   -101.91                                   
REMARK 500    ASN A  65       59.78   -144.86                                   
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                              CD A 160  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  24   OE1                                                    
REMARK 620 2 GLU A  24   OE2  55.2                                              
REMARK 620 3 HOH A 179   O   152.7  97.6                                        
REMARK 620 4 HOH A 435   O   103.1  51.2  50.6                                  
REMARK 620 5 HOH A 319   O    86.0  88.1  91.8  73.1                            
REMARK 620 6 HOH A 228   O    86.5  78.7  89.9  98.2 166.8                      
REMARK 620 7 HOH A 200   O    96.5 151.3 110.8 156.0  94.9  96.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 164  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 103.9                                              
REMARK 620 3 HIS A  63   NE2  86.0 100.3                                        
REMARK 620 4 HIS A 120   NE2  87.3  91.8 167.3                                  
REMARK 620 5 HOH A 176   O    90.0 165.6  84.1  85.1                            
REMARK 620 6 HOH A 224   O   165.9  90.2  90.6  93.3  76.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 144.6                                              
REMARK 620 3 HIS A 120   NE2 103.2 104.2                                        
REMARK 620 4  CD A 164  CD    86.9  81.1  71.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 158  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  50   OE1                                                    
REMARK 620 2 GLU A  50   OE1  36.9                                              
REMARK 620 3 GLU A  50   OE2  30.5  51.8                                        
REMARK 620 4 ASP A  52   OD2  99.8 136.3  95.4                                  
REMARK 620 5 HOH A 186   O    76.5  86.2 104.1  73.8                            
REMARK 620 6 ASP A  90   OD2 112.1  94.1 141.8 101.7  50.5                      
REMARK 620 7 ASP A  92   OD1 105.0  72.3  95.7 147.8 131.8  87.7                
REMARK 620 8 ASP A  92   OD2 128.2 116.6  99.0  94.1 154.7 113.3  54.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 156  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  51   OE2                                                    
REMARK 620 2 GLU A  51   OE2  11.9                                              
REMARK 620 3 HOH A 178   O   110.6 101.5                                        
REMARK 620 4 ASP A  96   OD2  80.1  88.0  93.2                                  
REMARK 620 5 ALA A   1   O    80.3  89.7 168.8  86.4                            
REMARK 620 6 ASP A  96   OD1 130.2 140.0  89.4  52.7  81.4                      
REMARK 620 7 ALA A   1   N   116.1 113.5 105.9 146.9  69.7  99.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 106.9                                              
REMARK 620 3 HIS A  80   ND1 112.7 118.1                                        
REMARK 620 4 ASP A  83   OD1 104.4  97.6 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 161  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  76   OD1                                                    
REMARK 620 2 HOH A 234   O    91.4                                              
REMARK 620 3 HOH A 206   O   104.3  94.8                                        
REMARK 620 4 HOH A 384   O   165.8  93.2  88.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 162  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 109   O                                                      
REMARK 620 2 HIS A 110   ND1  83.8                                              
REMARK 620 3 HOH A 182   O    96.8  94.8                                        
REMARK 620 4 HOH A 339   O    83.7 163.1  75.4                                  
REMARK 620 5 GLN A 153   OXT  92.2  84.0 170.8 107.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 163  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 109   OD2                                                    
REMARK 620 2 HOH A 343   O   161.5                                              
REMARK 620 3 HOH A 419   O   101.2  62.9                                        
REMARK 620 4 HOH A 295   O   108.0  88.7 150.6                                  
REMARK 620 5 HOH A 209   O    86.4 103.7  94.6  83.9                            
REMARK 620 6 HOH A 376   O    81.6  99.2 124.6  64.6 140.4                      
REMARK 620 7 HOH A 421   O    64.2  99.3  67.5 129.2 140.0  64.6                
REMARK 620 8 HOH A 306   O    50.8 111.8  50.9 158.6  96.6 104.3  44.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 159  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 110   NE2                                                    
REMARK 620 2 HOH A 210   O   104.2                                              
REMARK 620 3 HOH A 396   O    79.5  88.0                                        
REMARK 620 4 HOH A 244   O    96.0  91.4 175.2                                  
REMARK 620 5 GLN A 153   OXT  90.6 163.8  88.2  93.6                            
REMARK 620 6 GLN A 153   O   142.4 109.4  85.2  99.5  54.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 157  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 121   OE1                                                    
REMARK 620 2 SER A 142   OG   84.3                                              
REMARK 620 3 HOH A 257   O    95.3 178.4                                        
REMARK 620 4 HOH A 275   O    89.2  83.7  94.7                                  
REMARK 620 5  CL A 165  CL    72.9  79.1 102.3 156.2                            
REMARK 620 6  CL A 166  CL   171.0  87.6  92.9  93.6 101.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZN                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE ZINC ION (ZN2+) IS                 
REMARK 800  COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID             
REMARK 800  RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED            
REMARK 800  THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1.      
REMARK 800  THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED       
REMARK 800  AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63,         
REMARK 800  HIS 71 AND HIS 80 ARE ALL HIS-E.                                    
REMARK 800 SITE_IDENTIFIER: CU                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CU BINDING SITE COPPER ION (CU2+) IS               
REMARK 800  COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED          
REMARK 800  THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120         
REMARK 800  METAL COORDINATED THROUGH NE2.                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 155                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 156                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 157                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 158                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 159                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 160                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 161                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 162                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 163                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 164                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 165                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 166                  
DBREF  1MFM A    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1MFM ALA A    6  UNP  P00441    CYS     6 ENGINEERED                     
SEQADV 1MFM GLU A   50  UNP  P00441    PHE    50 ENGINEERED                     
SEQADV 1MFM GLU A   51  UNP  P00441    GLY    51 ENGINEERED                     
SEQADV 1MFM SER A  111  UNP  P00441    CYS   111 ENGINEERED                     
SEQADV 1MFM GLN A  133  UNP  P00441    GLU   133 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU GLU GLU ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLN SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     ZN  A 154       1                                                       
HET     CU  A 155       1                                                       
HET     CD  A 156       1                                                       
HET     CD  A 157       1                                                       
HET     CD  A 158       1                                                       
HET     CD  A 159       1                                                       
HET     CD  A 160       1                                                       
HET     CD  A 161       1                                                       
HET     CD  A 162       1                                                       
HET     CD  A 163       1                                                       
HET     CD  A 164       1                                                       
HET     CL  A 165       1                                                       
HET     CL  A 166       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CU COPPER (II) ION                                                  
HETNAM      CD CADMIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CU    CU 2+                                                        
FORMUL   4   CD    9(CD 2+)                                                     
FORMUL  13   CL    2(CL 1-)                                                     
FORMUL  15  HOH   *283(H2 O)                                                    
HELIX    1   1 GLY A   56  THR A   58  5                                   3    
HELIX    2   2 GLU A  132  THR A  137  5                                   6    
SHEET    1   A 5 ILE A 149  ILE A 151  0                                        
SHEET    2   A 5 THR A   2  LEU A   8 -1  N  VAL A   5   O  GLY A 150           
SHEET    3   A 5 GLY A  16  GLN A  22 -1  N  GLN A  22   O  THR A   2           
SHEET    4   A 5 VAL A  29  ILE A  35 -1  N  TRP A  32   O  ASN A  19           
SHEET    5   A 5 ALA A  95  ASP A 101 -1  N  ASP A 101   O  VAL A  29           
SHEET    1   B 2 GLY A  41  GLY A  44  0                                        
SHEET    2   B 2 ASN A  86  ALA A  89 -1  N  ALA A  89   O  GLY A  41           
SHEET    1   C 3 PHE A  45  HIS A  48  0                                        
SHEET    2   C 3 THR A 116  HIS A 120 -1  N  VAL A 118   O  HIS A  46           
SHEET    3   C 3 ARG A 143  VAL A 148 -1  N  GLY A 147   O  LEU A 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  1.96  
LINK         OE1AGLU A  24                CD    CD A 160     1555   1555  2.30  
LINK         OE2AGLU A  24                CD    CD A 160     1555   1555  2.42  
LINK         ND1 HIS A  46                CD    CD A 164     1555   1555  2.49  
LINK         ND1 HIS A  46                CU    CU A 155     1555   1555  1.99  
LINK         NE2 HIS A  48                CD    CD A 164     1555   1555  2.39  
LINK         NE2 HIS A  48                CU    CU A 155     1555   1555  2.05  
LINK         OE1AGLU A  50                CD    CD A 158     1555   1555  2.05  
LINK         OE1BGLU A  50                CD    CD A 158     1555   1555  2.59  
LINK         OE2BGLU A  50                CD    CD A 158     1555   1555  2.38  
LINK         OE2AGLU A  51                CD    CD A 156     1555   1555  2.29  
LINK         OE2BGLU A  51                CD    CD A 156     1555   1555  2.20  
LINK         OD2 ASP A  52                CD    CD A 158     1555   1555  2.25  
LINK         ND1 HIS A  63                ZN    ZN A 154     1555   1555  2.00  
LINK         NE2 HIS A  63                CD    CD A 164     1555   1555  2.27  
LINK         ND1 HIS A  71                ZN    ZN A 154     1555   1555  2.03  
LINK         OD1 ASP A  76                CD    CD A 161     1555   1555  2.44  
LINK         ND1 HIS A  80                ZN    ZN A 154     1555   1555  2.00  
LINK         OD1 ASP A  83                ZN    ZN A 154     1555   1555  1.97  
LINK         O   ASP A 109                CD    CD A 162     1555   1555  2.51  
LINK         OD2 ASP A 109                CD    CD A 163     1555   1555  2.33  
LINK         ND1BHIS A 110                CD    CD A 162     1555   1555  2.52  
LINK         NE2AHIS A 110                CD    CD A 159     1555   1555  2.17  
LINK         NE2 HIS A 120                CD    CD A 164     1555   1555  2.27  
LINK         NE2 HIS A 120                CU    CU A 155     1555   1555  2.20  
LINK         OE1 GLU A 121                CD    CD A 157     1555   1555  2.33  
LINK         OG  SER A 142                CD    CD A 157     1555   1555  2.42  
LINK        CD    CD A 156                 O   HOH A 178     1555   1555  2.27  
LINK        CD    CD A 157                 O   HOH A 257     1555   1555  2.40  
LINK        CD    CD A 157                 O   HOH A 275     1555   1555  2.52  
LINK        CD    CD A 159                 O   HOH A 210     1555   1555  2.50  
LINK        CD    CD A 159                 O   HOH A 396     1555   1555  2.29  
LINK        CD    CD A 159                 O   HOH A 244     1555   1555  2.46  
LINK        CD    CD A 160                 O   HOH A 179     1555   1555  2.53  
LINK        CD    CD A 160                 O   HOH A 435     1555   1555  2.57  
LINK        CD    CD A 160                 O   HOH A 319     1555   1555  2.36  
LINK        CD    CD A 161                 O   HOH A 234     1555   1555  2.58  
LINK        CD    CD A 162                 O   HOH A 182     1555   1555  2.36  
LINK        CD    CD A 163                 O   HOH A 343     1555   1555  2.42  
LINK        CD    CD A 163                 O   HOH A 419     1555   1555  2.41  
LINK        CD    CD A 163                 O   HOH A 295     1555   1555  2.47  
LINK        CD    CD A 163                 O   HOH A 209     1555   1555  2.55  
LINK        CD    CD A 164                 O   HOH A 176     1555   1555  2.39  
LINK        CD    CD A 164                 O   HOH A 224     1555   1555  2.59  
LINK        CU    CU A 155                CD    CD A 164     1555   1555  1.60  
LINK        CD    CD A 157                CL    CL A 165     1555   1555  2.42  
LINK        CD    CD A 157                CL    CL A 166     1555   1555  2.50  
LINK        CD    CD A 161                 O   HOH A 206     1555   1555  2.61  
LINK        CD    CD A 161                 O   HOH A 384     1555   1555  2.65  
LINK        CD    CD A 162                 O   HOH A 339     1555   1555  2.81  
LINK        CD    CD A 163                 O   HOH A 376     1555   1555  2.63  
LINK        CD    CD A 163                 O   HOH A 421     1555   1555  3.00  
LINK        CD    CD A 163                 O   HOH A 306     1555   1555  2.89  
LINK        CD    CD A 156                 OD2 ASP A  96     1555   1655  2.28  
LINK        CD    CD A 156                 O   ALA A   1     1555   4556  2.50  
LINK        CD    CD A 156                 OD1 ASP A  96     1555   1655  2.50  
LINK        CD    CD A 156                 N   ALA A   1     1555   4556  2.25  
LINK        CD    CD A 158                 O   HOH A 186     1555   1655  3.07  
LINK        CD    CD A 158                 OD2 ASP A  90     1555   1655  2.16  
LINK        CD    CD A 158                 OD1 ASP A  92     1555   1655  2.38  
LINK        CD    CD A 158                 OD2 ASP A  92     1555   1655  2.37  
LINK        CD    CD A 159                 OXT GLN A 153     1555   4556  2.53  
LINK        CD    CD A 159                 O   GLN A 153     1555   4556  2.20  
LINK        CD    CD A 160                 O   HOH A 228     1555   4456  2.47  
LINK        CD    CD A 160                 O   HOH A 200     1555   4556  2.42  
LINK        CD    CD A 162                 OXT GLN A 153     1555   4556  2.69  
SITE     1  ZN  5  ZN A 154   CU A 155  HIS A  71  HIS A  80                    
SITE     2  ZN  5 ASP A  83                                                     
SITE     1  CU  4  CU A 155  HIS A  46  HIS A  48  HIS A 120                    
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  5  CD A 164                                                     
SITE     1 AC3  4 ALA A   1  GLU A  51  ASP A  96  HOH A 178                    
SITE     1 AC4  6 GLU A 121  SER A 142   CL A 165   CL A 166                    
SITE     2 AC4  6 HOH A 257  HOH A 275                                          
SITE     1 AC5  5 GLU A  50  ASP A  52  ASP A  90  ASP A  92                    
SITE     2 AC5  5 HOH A 186                                                     
SITE     1 AC6  6 HIS A 110  GLN A 153   CD A 162  HOH A 210                    
SITE     2 AC6  6 HOH A 244  HOH A 396                                          
SITE     1 AC7  7 GLU A  24  ASN A  53  HOH A 179  HOH A 200                    
SITE     2 AC7  7 HOH A 228  HOH A 319  HOH A 435                               
SITE     1 AC8  4 ASP A  76  HOH A 206  HOH A 234  HOH A 384                    
SITE     1 AC9  6 ASP A 109  HIS A 110  GLN A 153   CD A 159                    
SITE     2 AC9  6 HOH A 182  HOH A 339                                          
SITE     1 BC1  8 ASP A 109  HOH A 209  HOH A 295  HOH A 306                    
SITE     2 BC1  8 HOH A 343  HOH A 376  HOH A 419  HOH A 421                    
SITE     1 BC2  7 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 BC2  7  CU A 155  HOH A 176  HOH A 224                               
SITE     1 BC3  5 ARG A  69  GLU A 121  SER A 142   CD A 157                    
SITE     2 BC3  5 HOH A 322                                                     
SITE     1 BC4  5 ARG A  69  LYS A  70  GLU A  78  SER A 142                    
SITE     2 BC4  5  CD A 157                                                     
CRYST1   34.990   48.110   81.080  90.00  90.00  90.00 P 21 21 21    4          
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      0.028579  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012333        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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