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Database: PDB
Entry: 1DQ8
LinkDB: 1DQ8
Original site: 1DQ8 
HEADER    OXIDOREDUCTASE                          30-DEC-99   1DQ8              
TITLE     COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG  
TITLE    2 AND COA                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (HMG-COA REDUCTASE);                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC PORTION;                                         
COMPND   5 EC: 1.1.1.34;                                                        
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.ISTVAN,M.PALNITKAR,S.K.BUCHANAN,J.DEISENHOFER                     
REVDAT   4   14-MAR-18 1DQ8    1       SEQADV                                   
REVDAT   3   04-OCT-17 1DQ8    1       REMARK                                   
REVDAT   2   24-FEB-09 1DQ8    1       VERSN                                    
REVDAT   1   08-MAR-00 1DQ8    0                                                
JRNL        AUTH   E.S.ISTVAN,M.PALNITKAR,S.K.BUCHANAN,J.DEISENHOFER            
JRNL        TITL   CRYSTAL STRUCTURE OF THE CATALYTIC PORTION OF HUMAN HMG-COA  
JRNL        TITL 2 REDUCTASE: INSIGHTS INTO REGULATION OF ACTIVITY AND          
JRNL        TITL 3 CATALYSIS.                                                   
JRNL        REF    EMBO J.                       V.  19   819 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   10698924                                                     
JRNL        DOI    10.1093/EMBOJ/19.5.819                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MLF                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 96563                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1933                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15986                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 318                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12134                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 252                                     
REMARK   3   SOLVENT ATOMS            : 281                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.86000                                             
REMARK   3    B22 (A**2) : -4.48000                                             
REMARK   3    B33 (A**2) : 14.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.28000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.27                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.460                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.190 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.830 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.030 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 30.80                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  4  : LIG.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE ELECTRON DENSITY MAP SHOWS VERY POOR DENSITY                    
REMARK   3  FOR RESIDUES 439-478 AND AS A RESULT THEIR                          
REMARK   3  GEOMETRY MAY NOT HABE BEEN WELL DEFINED.                            
REMARK   4                                                                      
REMARK   4 1DQ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000010285.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.012                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101445                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
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) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT                       
REMARK 200 SOFTWARE USED: SNB V. 2.0                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMONIUM ACETATE, SODIUM        
REMARK 280  HEPES, GLYCEROL, DTT, HMG-COA, PH 7.50                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       65.09100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 51170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   422                                                      
REMARK 465     ALA A   423                                                      
REMARK 465     MET A   424                                                      
REMARK 465     ALA A   425                                                      
REMARK 465     SER A   426                                                      
REMARK 465     SER A   427                                                      
REMARK 465     VAL A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     VAL A   430                                                      
REMARK 465     THR A   431                                                      
REMARK 465     GLN A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     PRO A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     ILE A   436                                                      
REMARK 465     GLU A   437                                                      
REMARK 465     LEU A   438                                                      
REMARK 465     LEU A   452                                                      
REMARK 465     GLY A   453                                                      
REMARK 465     ASN A   454                                                      
REMARK 465     ALA A   455                                                      
REMARK 465     GLU A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     LYS A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     HIS A   866                                                      
REMARK 465     MET A   867                                                      
REMARK 465     ILE A   868                                                      
REMARK 465     HIS A   869                                                      
REMARK 465     ASN A   870                                                      
REMARK 465     ARG A   871                                                      
REMARK 465     SER A   872                                                      
REMARK 465     LYS A   873                                                      
REMARK 465     ILE A   874                                                      
REMARK 465     ASN A   875                                                      
REMARK 465     LEU A   876                                                      
REMARK 465     GLN A   877                                                      
REMARK 465     ASP A   878                                                      
REMARK 465     LEU A   879                                                      
REMARK 465     GLN A   880                                                      
REMARK 465     GLY A   881                                                      
REMARK 465     ALA A   882                                                      
REMARK 465     CYS A   883                                                      
REMARK 465     THR A   884                                                      
REMARK 465     LYS A   885                                                      
REMARK 465     LYS A   886                                                      
REMARK 465     THR A   887                                                      
REMARK 465     ALA A   888                                                      
REMARK 465     GLY B   422                                                      
REMARK 465     ALA B   423                                                      
REMARK 465     MET B   424                                                      
REMARK 465     ALA B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     SER B   427                                                      
REMARK 465     VAL B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     VAL B   430                                                      
REMARK 465     THR B   431                                                      
REMARK 465     GLN B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     PRO B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     ILE B   436                                                      
REMARK 465     GLU B   437                                                      
REMARK 465     LEU B   438                                                      
REMARK 465     PRO B   439                                                      
REMARK 465     ARG B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     PRO B   442                                                      
REMARK 465     ARG B   443                                                      
REMARK 465     PRO B   444                                                      
REMARK 465     ASN B   445                                                      
REMARK 465     GLU B   446                                                      
REMARK 465     GLU B   447                                                      
REMARK 465     CYS B   448                                                      
REMARK 465     LEU B   449                                                      
REMARK 465     GLN B   450                                                      
REMARK 465     ILE B   451                                                      
REMARK 465     LEU B   452                                                      
REMARK 465     GLY B   453                                                      
REMARK 465     ASN B   454                                                      
REMARK 465     ALA B   455                                                      
REMARK 465     GLU B   456                                                      
REMARK 465     LYS B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     ALA B   459                                                      
REMARK 465     LYS B   460                                                      
REMARK 465     HIS B   866                                                      
REMARK 465     MET B   867                                                      
REMARK 465     ILE B   868                                                      
REMARK 465     HIS B   869                                                      
REMARK 465     ASN B   870                                                      
REMARK 465     ARG B   871                                                      
REMARK 465     SER B   872                                                      
REMARK 465     LYS B   873                                                      
REMARK 465     ILE B   874                                                      
REMARK 465     ASN B   875                                                      
REMARK 465     LEU B   876                                                      
REMARK 465     GLN B   877                                                      
REMARK 465     ASP B   878                                                      
REMARK 465     LEU B   879                                                      
REMARK 465     GLN B   880                                                      
REMARK 465     GLY B   881                                                      
REMARK 465     ALA B   882                                                      
REMARK 465     CYS B   883                                                      
REMARK 465     THR B   884                                                      
REMARK 465     LYS B   885                                                      
REMARK 465     LYS B   886                                                      
REMARK 465     THR B   887                                                      
REMARK 465     ALA B   888                                                      
REMARK 465     GLY C   422                                                      
REMARK 465     ALA C   423                                                      
REMARK 465     MET C   424                                                      
REMARK 465     ALA C   425                                                      
REMARK 465     SER C   426                                                      
REMARK 465     SER C   427                                                      
REMARK 465     VAL C   428                                                      
REMARK 465     LEU C   429                                                      
REMARK 465     VAL C   430                                                      
REMARK 465     THR C   431                                                      
REMARK 465     GLN C   432                                                      
REMARK 465     GLU C   433                                                      
REMARK 465     PRO C   434                                                      
REMARK 465     GLU C   435                                                      
REMARK 465     ILE C   436                                                      
REMARK 465     GLU C   437                                                      
REMARK 465     LEU C   438                                                      
REMARK 465     PRO C   439                                                      
REMARK 465     ARG C   440                                                      
REMARK 465     GLU C   441                                                      
REMARK 465     PRO C   442                                                      
REMARK 465     ARG C   443                                                      
REMARK 465     PRO C   444                                                      
REMARK 465     ASN C   445                                                      
REMARK 465     GLU C   446                                                      
REMARK 465     GLU C   447                                                      
REMARK 465     CYS C   448                                                      
REMARK 465     LEU C   449                                                      
REMARK 465     GLN C   450                                                      
REMARK 465     ILE C   451                                                      
REMARK 465     LEU C   452                                                      
REMARK 465     GLY C   453                                                      
REMARK 465     ASN C   454                                                      
REMARK 465     ALA C   455                                                      
REMARK 465     GLU C   456                                                      
REMARK 465     LYS C   457                                                      
REMARK 465     GLY C   458                                                      
REMARK 465     ALA C   459                                                      
REMARK 465     LYS C   460                                                      
REMARK 465     PHE C   461                                                      
REMARK 465     LEU C   462                                                      
REMARK 465     SER C   463                                                      
REMARK 465     HIS C   866                                                      
REMARK 465     MET C   867                                                      
REMARK 465     ILE C   868                                                      
REMARK 465     HIS C   869                                                      
REMARK 465     ASN C   870                                                      
REMARK 465     ARG C   871                                                      
REMARK 465     SER C   872                                                      
REMARK 465     LYS C   873                                                      
REMARK 465     ILE C   874                                                      
REMARK 465     ASN C   875                                                      
REMARK 465     LEU C   876                                                      
REMARK 465     GLN C   877                                                      
REMARK 465     ASP C   878                                                      
REMARK 465     LEU C   879                                                      
REMARK 465     GLN C   880                                                      
REMARK 465     GLY C   881                                                      
REMARK 465     ALA C   882                                                      
REMARK 465     CYS C   883                                                      
REMARK 465     THR C   884                                                      
REMARK 465     LYS C   885                                                      
REMARK 465     LYS C   886                                                      
REMARK 465     THR C   887                                                      
REMARK 465     ALA C   888                                                      
REMARK 465     GLY D   422                                                      
REMARK 465     ALA D   423                                                      
REMARK 465     MET D   424                                                      
REMARK 465     ALA D   425                                                      
REMARK 465     SER D   426                                                      
REMARK 465     SER D   427                                                      
REMARK 465     VAL D   428                                                      
REMARK 465     LEU D   429                                                      
REMARK 465     VAL D   430                                                      
REMARK 465     THR D   431                                                      
REMARK 465     GLN D   432                                                      
REMARK 465     GLU D   433                                                      
REMARK 465     PRO D   434                                                      
REMARK 465     GLU D   435                                                      
REMARK 465     ILE D   436                                                      
REMARK 465     GLU D   437                                                      
REMARK 465     LEU D   438                                                      
REMARK 465     PRO D   439                                                      
REMARK 465     ARG D   440                                                      
REMARK 465     GLU D   441                                                      
REMARK 465     PRO D   442                                                      
REMARK 465     ARG D   443                                                      
REMARK 465     PRO D   444                                                      
REMARK 465     ASN D   445                                                      
REMARK 465     GLU D   446                                                      
REMARK 465     GLU D   447                                                      
REMARK 465     CYS D   448                                                      
REMARK 465     LEU D   449                                                      
REMARK 465     GLN D   450                                                      
REMARK 465     ILE D   451                                                      
REMARK 465     LEU D   452                                                      
REMARK 465     GLY D   453                                                      
REMARK 465     ASN D   454                                                      
REMARK 465     ALA D   455                                                      
REMARK 465     GLU D   456                                                      
REMARK 465     LYS D   457                                                      
REMARK 465     SER D   865                                                      
REMARK 465     HIS D   866                                                      
REMARK 465     MET D   867                                                      
REMARK 465     ILE D   868                                                      
REMARK 465     HIS D   869                                                      
REMARK 465     ASN D   870                                                      
REMARK 465     ARG D   871                                                      
REMARK 465     SER D   872                                                      
REMARK 465     LYS D   873                                                      
REMARK 465     ILE D   874                                                      
REMARK 465     ASN D   875                                                      
REMARK 465     LEU D   876                                                      
REMARK 465     GLN D   877                                                      
REMARK 465     ASP D   878                                                      
REMARK 465     LEU D   879                                                      
REMARK 465     GLN D   880                                                      
REMARK 465     GLY D   881                                                      
REMARK 465     ALA D   882                                                      
REMARK 465     CYS D   883                                                      
REMARK 465     THR D   884                                                      
REMARK 465     LYS D   885                                                      
REMARK 465     LYS D   886                                                      
REMARK 465     THR D   887                                                      
REMARK 465     ALA D   888                                                      
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 441   N   -  CA  -  C   ANGL. DEV. = -21.1 DEGREES          
REMARK 500    PRO A 442   C   -  N   -  CA  ANGL. DEV. =   9.3 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    GLU A 441       97.15    161.66                                   
REMARK 500    PRO A 442      114.06    -29.64                                   
REMARK 500    LEU A 449       96.68    -58.27                                   
REMARK 500    GLN A 450      -98.78    -41.04                                   
REMARK 500    LEU A 462      174.06     62.41                                   
REMARK 500    HIS A 475       70.07   -119.18                                   
REMARK 500    TYR A 514      -26.13   -155.89                                   
REMARK 500    ALA A 525      -30.17   -147.74                                   
REMARK 500    CYS A 561      -15.12     82.00                                   
REMARK 500    SER A 651       34.24   -149.11                                   
REMARK 500    LYS A 735      -67.64    -97.76                                   
REMARK 500    LEU A 737      -66.96   -103.38                                   
REMARK 500    TYR A 749       53.46    -93.89                                   
REMARK 500    HIS A 752       46.11   -154.83                                   
REMARK 500    CYS A 777      138.29   -170.46                                   
REMARK 500    SER A 799       55.60   -146.51                                   
REMARK 500    ASN A 830       77.15   -151.16                                   
REMARK 500    LYS B 474       85.50    -27.98                                   
REMARK 500    HIS B 475      -41.79   -136.04                                   
REMARK 500    PRO B 477      108.23     26.58                                   
REMARK 500    ALA B 478      -49.65    -22.29                                   
REMARK 500    GLU B 486      -75.57    -56.95                                   
REMARK 500    PRO B 506      -33.36    -39.93                                   
REMARK 500    TYR B 514      -28.17   -156.13                                   
REMARK 500    ALA B 525      -45.79   -144.56                                   
REMARK 500    CYS B 561      -19.40     84.99                                   
REMARK 500    SER B 651       40.21   -160.08                                   
REMARK 500    LYS B 735      -65.39   -100.35                                   
REMARK 500    LEU B 737      -64.37   -108.20                                   
REMARK 500    TYR B 749       58.30    -92.61                                   
REMARK 500    HIS B 752       46.04   -153.89                                   
REMARK 500    ASP B 829      -16.74     96.10                                   
REMARK 500    ASN B 830       70.60   -162.72                                   
REMARK 500    LYS C 474     -171.52    -63.09                                   
REMARK 500    ILE C 476       86.35   -150.91                                   
REMARK 500    TYR C 514      -16.23   -156.10                                   
REMARK 500    ALA C 525      -27.22   -148.37                                   
REMARK 500    CYS C 561      -14.51     80.14                                   
REMARK 500    SER C 651       30.24   -155.24                                   
REMARK 500    LYS C 735      -61.37   -104.38                                   
REMARK 500    LEU C 737      -65.45   -100.95                                   
REMARK 500    TYR C 749       54.64    -94.91                                   
REMARK 500    HIS C 752       44.64   -150.62                                   
REMARK 500    SER C 799       59.11   -142.42                                   
REMARK 500    ASN C 830       70.82   -162.94                                   
REMARK 500    ALA D 473      -73.59    -48.92                                   
REMARK 500    HIS D 475       75.14     47.79                                   
REMARK 500    ALA D 478      -37.57    113.55                                   
REMARK 500    LEU D 484      -73.88    -69.73                                   
REMARK 500    TYR D 514      -26.84   -158.57                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH D 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 302                 
DBREF  1DQ8 A  422   888  UNP    P04035   HMDH_HUMAN     422    888             
DBREF  1DQ8 B  422   888  UNP    P04035   HMDH_HUMAN     422    888             
DBREF  1DQ8 C  422   888  UNP    P04035   HMDH_HUMAN     422    888             
DBREF  1DQ8 D  422   888  UNP    P04035   HMDH_HUMAN     422    888             
SEQADV 1DQ8 ILE A  485  UNP  P04035    MET   485 ENGINEERED MUTATION            
SEQADV 1DQ8 ILE B  485  UNP  P04035    MET   485 ENGINEERED MUTATION            
SEQADV 1DQ8 ILE C  485  UNP  P04035    MET   485 ENGINEERED MUTATION            
SEQADV 1DQ8 ILE D  485  UNP  P04035    MET   485 ENGINEERED MUTATION            
SEQRES   1 A  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 A  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 A  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 A  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 A  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 A  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 A  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 A  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 A  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 A  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 A  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 A  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 A  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 A  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 A  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 A  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 A  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 A  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 A  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 A  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 A  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 A  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 A  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 A  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 A  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 A  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 A  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 A  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 A  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 A  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 A  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 A  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 A  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 A  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 A  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 A  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 B  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 B  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 B  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 B  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 B  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 B  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 B  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 B  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 B  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 B  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 B  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 B  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 B  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 B  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 B  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 B  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 B  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 B  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 B  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 B  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 B  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 B  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 B  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 B  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 B  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 B  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 B  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 B  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 B  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 B  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 B  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 B  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 B  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 B  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 B  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 B  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 C  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 C  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 C  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 C  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 C  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 C  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 C  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 C  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 C  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 C  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 C  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 C  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 C  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 C  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 C  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 C  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 C  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 C  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 C  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 C  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 C  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 C  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 C  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 C  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 C  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 C  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 C  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 C  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 C  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 C  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 C  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 C  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 C  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 C  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 C  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 C  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 D  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 D  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 D  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 D  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 D  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 D  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 D  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 D  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 D  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 D  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 D  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 D  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 D  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 D  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 D  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 D  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 D  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 D  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 D  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 D  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 D  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 D  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 D  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 D  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 D  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 D  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 D  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 D  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 D  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 D  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 D  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 D  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 D  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 D  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 D  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 D  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
HET    COA  A 100      48                                                       
HET    MAH  A 200      11                                                       
HET    COA  B 101      48                                                       
HET    MAH  B 201      11                                                       
HET    DTT  B 302       8                                                       
HET    COA  C 102      48                                                       
HET    DTT  C 301       8                                                       
HET    COA  D 103      48                                                       
HET    MAH  D 202      11                                                       
HET    MAH  D 203      11                                                       
HETNAM     COA COENZYME A                                                       
HETNAM     MAH 3-HYDROXY-3-METHYL-GLUTARIC ACID                                 
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   5  COA    4(C21 H36 N7 O16 P3 S)                                       
FORMUL   6  MAH    4(C6 H10 O5)                                                 
FORMUL   9  DTT    2(C4 H10 O2 S2)                                              
FORMUL  15  HOH   *281(H2 O)                                                    
HELIX    1   1 PRO A  444  LEU A  449  1                                   6    
HELIX    2   2 SER A  463  LYS A  474  1                                  12    
HELIX    3   3 PRO A  477  TYR A  479  5                                   3    
HELIX    4   4 LYS A  480  ILE A  485  1                                   6    
HELIX    5   5 THR A  487  LYS A  501  1                                  15    
HELIX    6   6 GLU A  505  LEU A  512  5                                   8    
HELIX    7   7 CYS A  561  LEU A  575  1                                  15    
HELIX    8   8 ARG A  598  GLU A  610  1                                  13    
HELIX    9   9 THR A  611  SER A  624  1                                  14    
HELIX   10  10 GLY A  656  PHE A  675  1                                  20    
HELIX   11  11 ALA A  694  GLY A  701  1                                   8    
HELIX   12  12 PRO A  713  VAL A  720  1                                   8    
HELIX   13  13 THR A  724  LEU A  737  1                                  14    
HELIX   14  14 LEU A  737  ALA A  743  1                                   7    
HELIX   15  15 HIS A  752  CYS A  764  1                                  13    
HELIX   16  16 ASP A  767  ALA A  769  5                                   3    
HELIX   17  17 GLN A  770  SER A  775  1                                   6    
HELIX   18  18 GLY A  806  ASN A  810  5                                   5    
HELIX   19  19 LEU A  811  LEU A  821  1                                  11    
HELIX   20  20 GLY A  832  GLY A  860  1                                  29    
HELIX   21  21 SER B  463  ALA B  473  1                                  11    
HELIX   22  22 PRO B  477  TYR B  479  5                                   3    
HELIX   23  23 LYS B  480  ILE B  485  1                                   6    
HELIX   24  24 THR B  487  LYS B  501  1                                  15    
HELIX   25  25 GLU B  505  GLN B  510  5                                   6    
HELIX   26  26 ASN B  518  VAL B  522  5                                   5    
HELIX   27  27 CYS B  561  GLY B  576  1                                  16    
HELIX   28  28 ARG B  598  GLU B  610  1                                  13    
HELIX   29  29 THR B  611  SER B  624  1                                  14    
HELIX   30  30 GLY B  656  PHE B  675  1                                  20    
HELIX   31  31 ALA B  694  GLY B  701  1                                   8    
HELIX   32  32 PRO B  713  VAL B  720  1                                   8    
HELIX   33  33 THR B  724  LEU B  737  1                                  14    
HELIX   34  34 LEU B  737  ALA B  743  1                                   7    
HELIX   35  35 HIS B  752  CYS B  764  1                                  13    
HELIX   36  36 ASP B  767  ALA B  769  5                                   3    
HELIX   37  37 GLN B  770  SER B  775  1                                   6    
HELIX   38  38 GLY B  806  ASN B  810  5                                   5    
HELIX   39  39 LEU B  811  GLY B  822  1                                  12    
HELIX   40  40 GLY B  832  GLY B  860  1                                  29    
HELIX   41  41 ALA C  465  ALA C  473  1                                   9    
HELIX   42  42 PRO C  477  TYR C  479  5                                   3    
HELIX   43  43 LYS C  480  ILE C  485  1                                   6    
HELIX   44  44 THR C  487  LYS C  501  1                                  15    
HELIX   45  45 SER C  507  LEU C  512  5                                   6    
HELIX   46  46 CYS C  561  GLY C  576  1                                  16    
HELIX   47  47 ARG C  598  THR C  611  1                                  14    
HELIX   48  48 THR C  611  SER C  624  1                                  14    
HELIX   49  49 GLY C  656  PHE C  675  1                                  20    
HELIX   50  50 ALA C  694  GLY C  701  1                                   8    
HELIX   51  51 PRO C  713  VAL C  720  1                                   8    
HELIX   52  52 THR C  724  LEU C  737  1                                  14    
HELIX   53  53 LEU C  737  ALA C  743  1                                   7    
HELIX   54  54 HIS C  752  CYS C  764  1                                  13    
HELIX   55  55 ASP C  767  ALA C  769  5                                   3    
HELIX   56  56 GLN C  770  SER C  775  1                                   6    
HELIX   57  57 GLY C  806  ASN C  810  5                                   5    
HELIX   58  58 LEU C  811  LEU C  821  1                                  11    
HELIX   59  59 GLY C  832  ALA C  859  1                                  28    
HELIX   60  60 SER D  463  LYS D  474  1                                  12    
HELIX   61  61 LYS D  480  ILE D  485  1                                   6    
HELIX   62  62 THR D  487  LYS D  501  1                                  15    
HELIX   63  63 CYS D  561  GLY D  576  1                                  16    
HELIX   64  64 ARG D  598  GLU D  610  1                                  13    
HELIX   65  65 THR D  611  SER D  624  1                                  14    
HELIX   66  66 GLY D  656  PHE D  675  1                                  20    
HELIX   67  67 ALA D  694  GLY D  701  1                                   8    
HELIX   68  68 PRO D  713  VAL D  720  1                                   8    
HELIX   69  69 THR D  724  LEU D  737  1                                  14    
HELIX   70  70 LEU D  737  ALA D  743  1                                   7    
HELIX   71  71 HIS D  752  CYS D  764  1                                  13    
HELIX   72  72 ASP D  767  ALA D  769  5                                   3    
HELIX   73  73 GLN D  770  SER D  775  1                                   6    
HELIX   74  74 GLY D  806  ASN D  810  5                                   5    
HELIX   75  75 LEU D  811  LEU D  821  1                                  11    
HELIX   76  76 GLY D  832  GLY D  860  1                                  29    
SHEET    1   A 4 LYS A 549  ALA A 556  0                                        
SHEET    2   A 4 VAL A 530  LEU A 546 -1  N  GLY A 539   O  MET A 555           
SHEET    3   A 4 VAL B 530  LEU B 546 -1  N  ILE B 531   O  VAL A 538           
SHEET    4   A 4 LYS B 549  ALA B 556 -1  O  LYS B 549   N  LEU B 546           
SHEET    1   B 8 GLY A 748  TYR A 749  0                                        
SHEET    2   B 8 CYS A 777  SER A 784  1  O  CYS A 777   N  TYR A 749           
SHEET    3   B 8 ASP A 790  ILE A 800 -1  O  ASP A 790   N  SER A 784           
SHEET    4   B 8 GLY A 703  ILE A 712 -1  N  LYS A 704   O  ILE A 800           
SHEET    5   B 8 SER A 580  ARG A 590 -1  N  SER A 580   O  GLU A 709           
SHEET    6   B 8 ASN A 642  ARG A 650 -1  N  PHE A 647   O  ARG A 590           
SHEET    7   B 8 VAL A 593  ARG A 595 -1  N  VAL A 594   O  LEU A 643           
SHEET    8   B 8 GLN A 679  ALA A 682 -1  N  GLN A 679   O  ARG A 595           
SHEET    1   C 7 GLY A 748  TYR A 749  0                                        
SHEET    2   C 7 CYS A 777  SER A 784  1  O  CYS A 777   N  TYR A 749           
SHEET    3   C 7 ASP A 790  ILE A 800 -1  O  ASP A 790   N  SER A 784           
SHEET    4   C 7 GLY A 703  ILE A 712 -1  N  LYS A 704   O  ILE A 800           
SHEET    5   C 7 SER A 580  ARG A 590 -1  N  SER A 580   O  GLU A 709           
SHEET    6   C 7 ASN A 642  ARG A 650 -1  N  PHE A 647   O  ARG A 590           
SHEET    7   C 7 ARG A 630  ALA A 639 -1  O  ARG A 630   N  ARG A 650           
SHEET    1   D 7 ALA B 629  ALA B 639  0                                        
SHEET    2   D 7 ASN B 642  SER B 651 -1  O  ASN B 642   N  ALA B 639           
SHEET    3   D 7 SER B 580  ARG B 590 -1  O  MET B 588   N  SER B 649           
SHEET    4   D 7 GLY B 703  ILE B 712 -1  N  GLY B 703   O  GLY B 587           
SHEET    5   D 7 ASP B 790  ILE B 800 -1  O  LEU B 791   N  ILE B 712           
SHEET    6   D 7 CYS B 777  SER B 784 -1  O  ILE B 778   N  THR B 796           
SHEET    7   D 7 GLY B 748  TYR B 749  1  O  TYR B 749   N  THR B 779           
SHEET    1   E 4 ALA B 629  ALA B 639  0                                        
SHEET    2   E 4 ASN B 642  SER B 651 -1  O  ASN B 642   N  ALA B 639           
SHEET    3   E 4 VAL B 593  ARG B 595 -1  N  VAL B 594   O  LEU B 643           
SHEET    4   E 4 GLN B 679  ALA B 682 -1  N  GLN B 679   O  ARG B 595           
SHEET    1   F 4 LYS C 549  ALA C 556  0                                        
SHEET    2   F 4 VAL C 530  LEU C 546 -1  N  GLY C 539   O  MET C 555           
SHEET    3   F 4 VAL D 530  LEU D 546 -1  N  ILE D 531   O  VAL C 538           
SHEET    4   F 4 LYS D 549  ALA D 556 -1  O  LYS D 549   N  LEU D 546           
SHEET    1   G 8 GLY C 748  TYR C 749  0                                        
SHEET    2   G 8 CYS C 777  SER C 784  1  O  CYS C 777   N  TYR C 749           
SHEET    3   G 8 ASP C 790  ILE C 800 -1  N  ASP C 790   O  SER C 784           
SHEET    4   G 8 GLY C 703  ILE C 712 -1  N  LYS C 704   O  ILE C 800           
SHEET    5   G 8 SER C 580  ARG C 590 -1  N  SER C 580   O  GLU C 709           
SHEET    6   G 8 ASN C 642  ARG C 650 -1  N  PHE C 647   O  ARG C 590           
SHEET    7   G 8 VAL C 593  ARG C 595 -1  N  VAL C 594   O  LEU C 643           
SHEET    8   G 8 GLN C 679  ALA C 682 -1  N  GLN C 679   O  ARG C 595           
SHEET    1   H 7 GLY C 748  TYR C 749  0                                        
SHEET    2   H 7 CYS C 777  SER C 784  1  O  CYS C 777   N  TYR C 749           
SHEET    3   H 7 ASP C 790  ILE C 800 -1  N  ASP C 790   O  SER C 784           
SHEET    4   H 7 GLY C 703  ILE C 712 -1  N  LYS C 704   O  ILE C 800           
SHEET    5   H 7 SER C 580  ARG C 590 -1  N  SER C 580   O  GLU C 709           
SHEET    6   H 7 ASN C 642  ARG C 650 -1  N  PHE C 647   O  ARG C 590           
SHEET    7   H 7 ARG C 630  ALA C 639 -1  O  ARG C 630   N  ARG C 650           
SHEET    1   I 8 GLY D 748  TYR D 749  0                                        
SHEET    2   I 8 CYS D 777  SER D 784  1  O  CYS D 777   N  TYR D 749           
SHEET    3   I 8 ASP D 790  ILE D 800 -1  O  ASP D 790   N  SER D 784           
SHEET    4   I 8 GLY D 703  ILE D 712 -1  N  LYS D 704   O  ILE D 800           
SHEET    5   I 8 SER D 580  ARG D 590 -1  N  SER D 580   O  GLU D 709           
SHEET    6   I 8 ASN D 642  ARG D 650 -1  N  PHE D 647   O  ARG D 590           
SHEET    7   I 8 VAL D 593  ARG D 595 -1  N  VAL D 594   O  LEU D 643           
SHEET    8   I 8 GLN D 679  ALA D 682 -1  N  GLN D 679   O  ARG D 595           
SHEET    1   J 7 GLY D 748  TYR D 749  0                                        
SHEET    2   J 7 CYS D 777  SER D 784  1  O  CYS D 777   N  TYR D 749           
SHEET    3   J 7 ASP D 790  ILE D 800 -1  O  ASP D 790   N  SER D 784           
SHEET    4   J 7 GLY D 703  ILE D 712 -1  N  LYS D 704   O  ILE D 800           
SHEET    5   J 7 SER D 580  ARG D 590 -1  N  SER D 580   O  GLU D 709           
SHEET    6   J 7 ASN D 642  ARG D 650 -1  N  PHE D 647   O  ARG D 590           
SHEET    7   J 7 ARG D 630  ALA D 639 -1  O  ARG D 630   N  ARG D 650           
CISPEP   1 GLY A  542    PRO A  543          0         0.62                     
CISPEP   2 CYS A  688    THR A  689          0        -0.75                     
CISPEP   3 GLY B  542    PRO B  543          0         0.58                     
CISPEP   4 CYS B  688    THR B  689          0        -0.91                     
CISPEP   5 GLY C  542    PRO C  543          0         1.51                     
CISPEP   6 CYS C  688    THR C  689          0         0.14                     
CISPEP   7 GLY D  542    PRO D  543          0        -0.36                     
CISPEP   8 CYS D  688    THR D  689          0        -1.48                     
SITE     1 AC1 17 MAH A 200  GLU A 559  GLY A 560  LEU A 562                    
SITE     2 AC1 17 ALA A 564  SER A 565  ASN A 567  ARG A 568                    
SITE     3 AC1 17 ARG A 571  VAL A 720  LYS A 722  HIS A 752                    
SITE     4 AC1 17 SER A 852  LEU A 853  HOH A2093  TYR B 479                    
SITE     5 AC1 17 GLU B 528                                                     
SITE     1 AC2 17 PRO A 477  TYR A 479  GLU A 528  GLU B 559                    
SITE     2 AC2 17 GLY B 560  LEU B 562  ALA B 564  SER B 565                    
SITE     3 AC2 17 ASN B 567  ARG B 568  ARG B 571  VAL B 720                    
SITE     4 AC2 17 LYS B 722  HIS B 752  SER B 852  LEU B 853                    
SITE     5 AC2 17 ALA B 856                                                     
SITE     1 AC3 20 GLU C 559  GLY C 560  CYS C 561  LEU C 562                    
SITE     2 AC3 20 ALA C 564  SER C 565  ASN C 567  ARG C 568                    
SITE     3 AC3 20 ARG C 571  VAL C 720  LYS C 722  HIS C 752                    
SITE     4 AC3 20 ASN C 755  SER C 852  LEU C 853  ALA C 856                    
SITE     5 AC3 20 LEU C 862  SER C 865  PRO D 477  TYR D 479                    
SITE     1 AC4 17 TYR C 479  GLU D 559  GLY D 560  LEU D 562                    
SITE     2 AC4 17 ALA D 564  SER D 565  ASN D 567  ARG D 568                    
SITE     3 AC4 17 ARG D 571  VAL D 720  LYS D 722  HIS D 752                    
SITE     4 AC4 17 SER D 852  LEU D 853  ALA D 856  LEU D 862                    
SITE     5 AC4 17 HOH D2274                                                     
SITE     1 AC5 12 COA A 100  GLU A 559  LYS A 735  ALA A 751                    
SITE     2 AC5 12 ASN A 755  LEU A 853  HOH A2005  ARG B 590                    
SITE     3 AC5 12 SER B 684  ASP B 690  LYS B 691  LYS B 692                    
SITE     1 AC6 12 ARG A 590  MET A 657  SER A 684  ASP A 690                    
SITE     2 AC6 12 LYS A 691  LYS A 692  GLU B 559  LYS B 735                    
SITE     3 AC6 12 ALA B 751  ASN B 755  LEU B 853  HOH B2052                    
SITE     1 AC7 12 GLU C 559  LYS C 735  ALA C 751  ASN C 755                    
SITE     2 AC7 12 LEU C 853  ARG D 590  SER D 684  ASP D 690                    
SITE     3 AC7 12 LYS D 691  LYS D 692  HOH D2088  HOH D2266                    
SITE     1 AC8 11 ARG C 590  SER C 684  ASP C 690  LYS C 691                    
SITE     2 AC8 11 LYS C 692  GLU D 559  LYS D 735  ALA D 751                    
SITE     3 AC8 11 ASN D 755  LEU D 853  HOH D2090                               
SITE     1 AC9 10 GLY C 765  GLN C 766  ASP C 767  GLY C 806                    
SITE     2 AC9 10 GLY C 807  GLY C 808  HOH C2095  HOH C2117                    
SITE     3 AC9 10 THR D 558  GLU D 559                                          
SITE     1 BC1  6 GLY A 765  GLN A 766  ASP A 767  GLY A 808                    
SITE     2 BC1  6 THR B 558  GLU B 559                                          
CRYST1   75.297  130.182   92.547  90.00 106.48  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013281  0.000000  0.003929        0.00000                         
SCALE2      0.000000  0.007682  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011268        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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