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Database: PDB
Entry: 1PYD
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HEADER    LYASE(CARBON-CARBON)                    23-MAR-93   1PYD              
TITLE     CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE
TITLE    2 DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE DECARBOXYLASE;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932                                                 
KEYWDS    LYASE(CARBON-CARBON)                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.FUREY,F.DYDA                                                        
REVDAT   6   14-FEB-24 1PYD    1       REMARK                                   
REVDAT   5   04-AUG-21 1PYD    1       COMPND REMARK SEQADV HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   14-AUG-19 1PYD    1       REMARK                                   
REVDAT   3   17-JUL-19 1PYD    1       REMARK                                   
REVDAT   2   24-FEB-09 1PYD    1       VERSN                                    
REVDAT   1   30-APR-94 1PYD    0                                                
JRNL        AUTH   F.DYDA,W.FUREY,S.SWAMINATHAN,M.SAX,B.FARRENKOPF,F.JORDAN     
JRNL        TITL   CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT       
JRNL        TITL 2 ENZYME PYRUVATE DECARBOXYLASE AT 2.4-A RESOLUTION.           
JRNL        REF    BIOCHEMISTRY                  V.  32  6165 1993              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8512926                                                      
JRNL        DOI    10.1021/BI00075A008                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.DYDA,W.FUREY,S.SWAMINATHAN,M.SAX,F.JORDAN,B.FARRENKOPF     
REMARK   1  TITL   MULTIPLE CRYSTAL FORMS OF BREWERS' YEAST PYRUVATE            
REMARK   1  TITL 2 DECARBOXYLASE: CHARACTERIZATION AND PRELIMINARY              
REMARK   1  TITL 3 CRYSTALLOGRAPHIC ANALYSIS                                    
REMARK   1  EDIT   H.BISSWANGER, J.ULLRICH                                      
REMARK   1  REF    BIOCHEMISTRY AND PHYSIOLOGY            115 1991              
REMARK   1  REF  2 OF THIAMIN DIPHOSPHATE                                       
REMARK   1  REF  3 ENZYMES                                                      
REMARK   1  PUBL   VCH VERLAGSGESELLSCHAFT,WEINHEIM; VCH PUBLISHERS,NEW YORK    
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.DYDA,W.FUREY,S.SWAMINATHAN,M.SAX,B.FARRENKOPF,F.JORDAN     
REMARK   1  TITL   PRELIMINARY CRYSTALLOGRAPHIC DATA FOR THE THIAMIN            
REMARK   1  TITL 2 DIPHOSPHATE-DEPENDENT ENZYME PYRUVATE DECARBOXYLASE FROM     
REMARK   1  TITL 3 BREWERS' YEAST                                               
REMARK   1  REF    J.BIOL.CHEM.                  V. 265 17413 1990              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : GPRLSA                                               
REMARK   3   AUTHORS     : FUREY                                                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8260                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000175877.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       70.97500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.33500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.97500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.33500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE UNIT CELL CONTAINS TWO TETRAMERS, WITH ONE DIMER IN THE  
REMARK 300 ASYMMETRIC UNIT.  IN TERMS OF THE CRYSTAL AXES, THE TWO              
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT (CHAINS *A* AND *B*) ARE             
REMARK 300 RELATED BY A NONCRYSTALLOGRAPHIC TWO-FOLD AXIS INCLINED BY           
REMARK 300 83.31 DEGREES TO THE B AXIS, AND WHOSE PROJECTION ON THE AC          
REMARK 300 PLANE MAKES ANGLES OF 102.16 DEGREES WITH THE A AXIS AND             
REMARK 300 14.23 DEGREES WITH THE C AXIS.  THIS TRANSFORMATION IS               
REMARK 300 PRESENTED ON *MTRIX* RECORDS BELOW.  THE COMPLETE TETRAMER           
REMARK 300 IS FORMED BY THE SUBMITTED DIMER AND ITS                             
REMARK 300 CRYSTALLOGRAPHICALLY RELATED MATE OBTAINED BY TWO-FOLD               
REMARK 300 ROTATION ABOUT THE B AXIS.  THE NONCRYSTALLOGRAPHIC                  
REMARK 300 TWO-FOLD AXIS DOES NOT INTERSECT THE B AXIS, AS ITS CLOSEST          
REMARK 300 APPROACH IS OFFSET BY 1.352 ANGSTROMS.  THE TETRAMER THUS            
REMARK 300 HAS ONLY APPROXIMATE 222 SYMMETRY, AS IT MUST INTERSECT THE          
REMARK 300 B AXIS AND BE INCLINED TO IT BY 90 DEGREES FOR EXACT 222             
REMARK 300 SYMMETRY.                                                            
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE CATALYTIC CENTERS ARE LOCATED AT THE INTERFACE BETWEEN           
REMARK 400 MONOMERS WITHIN EACH DIMER, WITH TWO SITES PER DIMER AND             
REMARK 400 FOUR PER TETRAMER.                                                   
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     MET A     1                                                      
REMARK 465     SER A   106                                                      
REMARK 465     GLN A   107                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     LEU A   113                                                      
REMARK 465     PHE A   292                                                      
REMARK 465     ASN A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     SER A   296                                                      
REMARK 465     PHE A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     TYR A   299                                                      
REMARK 465     SER A   300                                                      
REMARK 465     TYR A   301                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B   106                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     ALA B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     LEU B   111                                                      
REMARK 465     LEU B   112                                                      
REMARK 465     LEU B   113                                                      
REMARK 465     PHE B   292                                                      
REMARK 465     ASN B   293                                                      
REMARK 465     THR B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     SER B   296                                                      
REMARK 465     PHE B   297                                                      
REMARK 465     SER B   298                                                      
REMARK 465     TYR B   299                                                      
REMARK 465     SER B   300                                                      
REMARK 465     TYR B   301                                                      
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   NH1  ARG A   317     OE2  GLU B   199     2555     2.08            
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    SER A   2   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ILE A   4   CA  -  CB  -  CG2 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    GLU A  12   OE1 -  CD  -  OE2 ANGL. DEV. =  14.9 DEGREES          
REMARK 500    GLU A  12   CG  -  CD  -  OE1 ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU A  31   CB  -  CG  -  CD1 ANGL. DEV. =  11.9 DEGREES          
REMARK 500    LEU A  33   C   -  N   -  CA  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ASP A  35   CB  -  CG  -  OD2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    TYR A  38   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    TYR A  38   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    GLU A  41   CA  -  CB  -  CG  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    GLU A  41   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG A  44   CD  -  NE  -  CZ  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ARG A  44   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ALA A  49   CB  -  CA  -  C   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    TYR A  56   CA  -  CB  -  CG  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    TYR A  61   CB  -  CG  -  CD1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  63   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LEU A  79   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ALA A  86   N   -  CA  -  CB  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    VAL A 101   N   -  CA  -  CB  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    HIS A 115   N   -  CA  -  CB  ANGL. DEV. =  12.5 DEGREES          
REMARK 500    LEU A 117   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ARG A 127   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ASP A 141   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    GLU A 148   OE1 -  CD  -  OE2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ASP A 150   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    TYR A 157   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 161   CD  -  NE  -  CZ  ANGL. DEV. =  32.5 DEGREES          
REMARK 500    ARG A 161   NE  -  CZ  -  NH1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    VAL A 176   N   -  CA  -  CB  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LYS A 179   CA  -  CB  -  CG  ANGL. DEV. =  21.1 DEGREES          
REMARK 500    ASP A 186   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A 202   CB  -  CG  -  OD2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    LYS A 209   CA  -  CB  -  CG  ANGL. DEV. =  22.5 DEGREES          
REMARK 500    ASP A 219   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ASP A 219   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP A 226   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLU A 230   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP A 236   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    MET A 247   N   -  CA  -  CB  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    SER A 251   CA  -  CB  -  OG  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    GLN A 255   O   -  C   -  N   ANGL. DEV. = -11.1 DEGREES          
REMARK 500    ARG A 258   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    VAL A 264   CA  -  CB  -  CG2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    VAL A 264   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ALA A 275   CB  -  CA  -  C   ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ASP A 280   CB  -  CG  -  OD1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ASP A 280   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     184 ANGLE DEVIATIONS.                             
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    PHE A  74      122.41    -33.47                                   
REMARK 500    HIS A  92       64.23     69.26                                   
REMARK 500    SER A 103       41.95    -46.95                                   
REMARK 500    HIS A 115       32.84     82.94                                   
REMARK 500    LEU A 117       24.23    -76.23                                   
REMARK 500    ALA A 220      -65.99    -26.77                                   
REMARK 500    ASP A 226      -42.80     79.45                                   
REMARK 500    VAL A 227        3.54    -45.96                                   
REMARK 500    PRO A 270      -39.20    -39.23                                   
REMARK 500    LEU A 288       49.18   -140.18                                   
REMARK 500    SER A 290      -60.82    -96.47                                   
REMARK 500    LYS A 304     -109.53    -51.00                                   
REMARK 500    ARG A 317     -130.45     65.50                                   
REMARK 500    LYS A 342       -7.90    -58.30                                   
REMARK 500    THR A 353      123.98    -38.23                                   
REMARK 500    ALA A 355      161.63    -48.37                                   
REMARK 500    PHE A 417      -67.16    -21.01                                   
REMARK 500    ASP A 433      109.04   -164.11                                   
REMARK 500    LYS A 463       55.09   -114.20                                   
REMARK 500    ASN A 471       18.04   -141.23                                   
REMARK 500    SER B 103      159.35    -48.30                                   
REMARK 500    ILE B 104       87.16    -56.48                                   
REMARK 500    HIS B 115       33.16     83.20                                   
REMARK 500    TYR B 157      -70.02    -55.99                                   
REMARK 500    ALA B 220      -50.83    -29.80                                   
REMARK 500    HIS B 225       43.57    -98.08                                   
REMARK 500    ASP B 226       42.32     36.45                                   
REMARK 500    VAL B 264       25.12   -140.73                                   
REMARK 500    VAL B 285       50.81    -96.62                                   
REMARK 500    ALA B 287     -155.68   -166.21                                   
REMARK 500    LEU B 288       88.11    -18.60                                   
REMARK 500    LEU B 289       49.70    -49.53                                   
REMARK 500    THR B 303      172.87     55.87                                   
REMARK 500    ASN B 305       67.43    -69.31                                   
REMARK 500    ARG B 317     -122.71     52.61                                   
REMARK 500    LYS B 342       88.22    -63.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 352         0.13    SIDE CHAIN                              
REMARK 500    ARG B 154         0.09    SIDE CHAIN                              
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                              MG A 559  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 444   OD1                                                    
REMARK 620 2 ASN A 471   OD1 108.4                                              
REMARK 620 3 GLY A 473   O    80.6  85.8                                        
REMARK 620 4 TPP A 557   O2A  83.4 162.7  83.8                                  
REMARK 620 5 TPP A 557   O3B 158.9  89.6  90.2  76.8                            
REMARK 620 6 HOH A 560   O    97.4  98.1 176.1  92.7  90.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 559  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 444   OD1                                                    
REMARK 620 2 ASN B 471   OD1 101.4                                              
REMARK 620 3 GLY B 473   O   100.2 101.3                                        
REMARK 620 4 TPP B 557   O3B 154.6  94.3  96.1                                  
REMARK 620 5 TPP B 557   O2A  85.9 171.0  82.3  77.1                            
REMARK 620 6 HOH B 560   O    79.5  81.9 176.8  83.1  94.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: TD1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TD2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 559                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 559                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 557                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 557                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SINCE THE SEQUENCE FOR PDC FROM SACCHAROMYCES UVARUM IS              
REMARK 999 NOT KNOWN, THE MODEL WAS BUILT ASSUMING THE HOMOLOGOUS               
REMARK 999 SACCHAROMYCES CEREVISIAE PDC1 SEQUENCE WAS APPROPRIATE.              
REMARK 999 THE CEREVISIAE SEQUENCE INDEED FIT THE ELECTRON DENSITY              
REMARK 999 EXTREMELY WELL, AND ONLY TWO DIFFERENCES ARE REFLECTED IN            
REMARK 999 THE DEPOSITED COORDINATES:  ARG 55 - ALA 55 AND VAL 538 -            
REMARK 999 ILE 538.  THE CEREVISIAE SEQUENCE USED WAS REPORTED EARLIER          
REMARK 999 BY HOHMANN, EG "STRUCTURE AND EXPRESSION OF YEAST PYRUVATE           
REMARK 999 DECARBOXYLASE STRUCTURAL GENES", HOHMANN, S. (1991) IN               
REMARK 999 BIOCHEMISTRY AND PHYSIOLOGY OF THIAMIN DIPHOSPHATE                   
REMARK 999 ENZYMES" (BISSWANGER, H. & ULLRICH, J., EDS.) PP106 - 114,           
REMARK 999 VCH PUBLISHERS, NEW YORK.                                            
DBREF  1PYD A    2   556  UNP    P06169   PDC1_YEAST       1    555             
DBREF  1PYD B    2   556  UNP    P06169   PDC1_YEAST       1    555             
SEQADV 1PYD ALA A   55  UNP  P06169    ARG    54 CONFLICT                       
SEQADV 1PYD ALA A  143  UNP  P06169    CYS   142 CONFLICT                       
SEQADV 1PYD ALA A  206  UNP  P06169    VAL   205 CONFLICT                       
SEQADV 1PYD VAL A  208  UNP  P06169    ALA   207 CONFLICT                       
SEQADV 1PYD ILE A  538  UNP  P06169    VAL   537 CONFLICT                       
SEQADV 1PYD LYS A  551  UNP  P06169    GLU   550 CONFLICT                       
SEQADV 1PYD ALA B   55  UNP  P06169    ARG    54 CONFLICT                       
SEQADV 1PYD ALA B  143  UNP  P06169    CYS   142 CONFLICT                       
SEQADV 1PYD ALA B  206  UNP  P06169    VAL   205 CONFLICT                       
SEQADV 1PYD VAL B  208  UNP  P06169    ALA   207 CONFLICT                       
SEQADV 1PYD ILE B  538  UNP  P06169    VAL   537 CONFLICT                       
SEQADV 1PYD LYS B  551  UNP  P06169    GLU   550 CONFLICT                       
SEQRES   1 A  556  MET SER GLU ILE THR LEU GLY LYS TYR LEU PHE GLU ARG          
SEQRES   2 A  556  LEU LYS GLN VAL ASN VAL ASN THR VAL PHE GLY LEU PRO          
SEQRES   3 A  556  GLY ASP PHE ASN LEU SER LEU LEU ASP LYS ILE TYR GLU          
SEQRES   4 A  556  VAL GLU GLY MET ARG TRP ALA GLY ASN ALA ASN GLU LEU          
SEQRES   5 A  556  ASN ALA ALA TYR ALA ALA ASP GLY TYR ALA ARG ILE LYS          
SEQRES   6 A  556  GLY MET SER CYS ILE ILE THR THR PHE GLY VAL GLY GLU          
SEQRES   7 A  556  LEU SER ALA LEU ASN GLY ILE ALA GLY SER TYR ALA GLU          
SEQRES   8 A  556  HIS VAL GLY VAL LEU HIS VAL VAL GLY VAL PRO SER ILE          
SEQRES   9 A  556  SER SER GLN ALA LYS GLN LEU LEU LEU HIS HIS THR LEU          
SEQRES  10 A  556  GLY ASN GLY ASP PHE THR VAL PHE HIS ARG MET SER ALA          
SEQRES  11 A  556  ASN ILE SER GLU THR THR ALA MET ILE THR ASP ILE ALA          
SEQRES  12 A  556  THR ALA PRO ALA GLU ILE ASP ARG CYS ILE ARG THR THR          
SEQRES  13 A  556  TYR VAL THR GLN ARG PRO VAL TYR LEU GLY LEU PRO ALA          
SEQRES  14 A  556  ASN LEU VAL ASP LEU ASN VAL PRO ALA LYS LEU LEU GLN          
SEQRES  15 A  556  THR PRO ILE ASP MET SER LEU LYS PRO ASN ASP ALA GLU          
SEQRES  16 A  556  SER GLU LYS GLU VAL ILE ASP THR ILE LEU ALA LEU VAL          
SEQRES  17 A  556  LYS ASP ALA LYS ASN PRO VAL ILE LEU ALA ASP ALA CYS          
SEQRES  18 A  556  CYS SER ARG HIS ASP VAL LYS ALA GLU THR LYS LYS LEU          
SEQRES  19 A  556  ILE ASP LEU THR GLN PHE PRO ALA PHE VAL THR PRO MET          
SEQRES  20 A  556  GLY LYS GLY SER ILE SER GLU GLN HIS PRO ARG TYR GLY          
SEQRES  21 A  556  GLY VAL TYR VAL GLY THR LEU SER LYS PRO GLU VAL LYS          
SEQRES  22 A  556  GLU ALA VAL GLU SER ALA ASP LEU ILE LEU SER VAL GLY          
SEQRES  23 A  556  ALA LEU LEU SER ASP PHE ASN THR GLY SER PHE SER TYR          
SEQRES  24 A  556  SER TYR LYS THR LYS ASN ILE VAL GLU PHE HIS SER ASP          
SEQRES  25 A  556  HIS MET LYS ILE ARG ASN ALA THR PHE PRO GLY VAL GLN          
SEQRES  26 A  556  MET LYS PHE VAL LEU GLN LYS LEU LEU THR ASN ILE ALA          
SEQRES  27 A  556  ASP ALA ALA LYS GLY TYR LYS PRO VAL ALA VAL PRO ALA          
SEQRES  28 A  556  ARG THR PRO ALA ASN ALA ALA VAL PRO ALA SER THR PRO          
SEQRES  29 A  556  LEU LYS GLN GLU TRP MET TRP ASN GLN LEU GLY ASN PHE          
SEQRES  30 A  556  LEU GLN GLU GLY ASP VAL VAL ILE ALA GLU THR GLY THR          
SEQRES  31 A  556  SER ALA PHE GLY ILE ASN GLN THR THR PHE PRO ASN ASN          
SEQRES  32 A  556  THR TYR GLY ILE SER GLN VAL LEU TRP GLY SER ILE GLY          
SEQRES  33 A  556  PHE THR THR GLY ALA THR LEU GLY ALA ALA PHE ALA ALA          
SEQRES  34 A  556  GLU GLU ILE ASP PRO LYS LYS ARG VAL ILE LEU PHE ILE          
SEQRES  35 A  556  GLY ASP GLY SER LEU GLN LEU THR VAL GLN GLU ILE SER          
SEQRES  36 A  556  THR MET ILE ARG TRP GLY LEU LYS PRO TYR LEU PHE VAL          
SEQRES  37 A  556  LEU ASN ASN ASP GLY TYR THR ILE GLU LYS LEU ILE HIS          
SEQRES  38 A  556  GLY PRO LYS ALA GLN TYR ASN GLU ILE GLN GLY TRP ASP          
SEQRES  39 A  556  HIS LEU SER LEU LEU PRO THR PHE GLY ALA LYS ASP TYR          
SEQRES  40 A  556  GLU THR HIS ARG VAL ALA THR THR GLY GLU TRP ASP LYS          
SEQRES  41 A  556  LEU THR GLN ASP LYS SER PHE ASN ASP ASN SER LYS ILE          
SEQRES  42 A  556  ARG MET ILE GLU ILE MET LEU PRO VAL PHE ASP ALA PRO          
SEQRES  43 A  556  GLN ASN LEU VAL LYS GLN ALA LYS LEU THR                      
SEQRES   1 B  556  MET SER GLU ILE THR LEU GLY LYS TYR LEU PHE GLU ARG          
SEQRES   2 B  556  LEU LYS GLN VAL ASN VAL ASN THR VAL PHE GLY LEU PRO          
SEQRES   3 B  556  GLY ASP PHE ASN LEU SER LEU LEU ASP LYS ILE TYR GLU          
SEQRES   4 B  556  VAL GLU GLY MET ARG TRP ALA GLY ASN ALA ASN GLU LEU          
SEQRES   5 B  556  ASN ALA ALA TYR ALA ALA ASP GLY TYR ALA ARG ILE LYS          
SEQRES   6 B  556  GLY MET SER CYS ILE ILE THR THR PHE GLY VAL GLY GLU          
SEQRES   7 B  556  LEU SER ALA LEU ASN GLY ILE ALA GLY SER TYR ALA GLU          
SEQRES   8 B  556  HIS VAL GLY VAL LEU HIS VAL VAL GLY VAL PRO SER ILE          
SEQRES   9 B  556  SER SER GLN ALA LYS GLN LEU LEU LEU HIS HIS THR LEU          
SEQRES  10 B  556  GLY ASN GLY ASP PHE THR VAL PHE HIS ARG MET SER ALA          
SEQRES  11 B  556  ASN ILE SER GLU THR THR ALA MET ILE THR ASP ILE ALA          
SEQRES  12 B  556  THR ALA PRO ALA GLU ILE ASP ARG CYS ILE ARG THR THR          
SEQRES  13 B  556  TYR VAL THR GLN ARG PRO VAL TYR LEU GLY LEU PRO ALA          
SEQRES  14 B  556  ASN LEU VAL ASP LEU ASN VAL PRO ALA LYS LEU LEU GLN          
SEQRES  15 B  556  THR PRO ILE ASP MET SER LEU LYS PRO ASN ASP ALA GLU          
SEQRES  16 B  556  SER GLU LYS GLU VAL ILE ASP THR ILE LEU ALA LEU VAL          
SEQRES  17 B  556  LYS ASP ALA LYS ASN PRO VAL ILE LEU ALA ASP ALA CYS          
SEQRES  18 B  556  CYS SER ARG HIS ASP VAL LYS ALA GLU THR LYS LYS LEU          
SEQRES  19 B  556  ILE ASP LEU THR GLN PHE PRO ALA PHE VAL THR PRO MET          
SEQRES  20 B  556  GLY LYS GLY SER ILE SER GLU GLN HIS PRO ARG TYR GLY          
SEQRES  21 B  556  GLY VAL TYR VAL GLY THR LEU SER LYS PRO GLU VAL LYS          
SEQRES  22 B  556  GLU ALA VAL GLU SER ALA ASP LEU ILE LEU SER VAL GLY          
SEQRES  23 B  556  ALA LEU LEU SER ASP PHE ASN THR GLY SER PHE SER TYR          
SEQRES  24 B  556  SER TYR LYS THR LYS ASN ILE VAL GLU PHE HIS SER ASP          
SEQRES  25 B  556  HIS MET LYS ILE ARG ASN ALA THR PHE PRO GLY VAL GLN          
SEQRES  26 B  556  MET LYS PHE VAL LEU GLN LYS LEU LEU THR ASN ILE ALA          
SEQRES  27 B  556  ASP ALA ALA LYS GLY TYR LYS PRO VAL ALA VAL PRO ALA          
SEQRES  28 B  556  ARG THR PRO ALA ASN ALA ALA VAL PRO ALA SER THR PRO          
SEQRES  29 B  556  LEU LYS GLN GLU TRP MET TRP ASN GLN LEU GLY ASN PHE          
SEQRES  30 B  556  LEU GLN GLU GLY ASP VAL VAL ILE ALA GLU THR GLY THR          
SEQRES  31 B  556  SER ALA PHE GLY ILE ASN GLN THR THR PHE PRO ASN ASN          
SEQRES  32 B  556  THR TYR GLY ILE SER GLN VAL LEU TRP GLY SER ILE GLY          
SEQRES  33 B  556  PHE THR THR GLY ALA THR LEU GLY ALA ALA PHE ALA ALA          
SEQRES  34 B  556  GLU GLU ILE ASP PRO LYS LYS ARG VAL ILE LEU PHE ILE          
SEQRES  35 B  556  GLY ASP GLY SER LEU GLN LEU THR VAL GLN GLU ILE SER          
SEQRES  36 B  556  THR MET ILE ARG TRP GLY LEU LYS PRO TYR LEU PHE VAL          
SEQRES  37 B  556  LEU ASN ASN ASP GLY TYR THR ILE GLU LYS LEU ILE HIS          
SEQRES  38 B  556  GLY PRO LYS ALA GLN TYR ASN GLU ILE GLN GLY TRP ASP          
SEQRES  39 B  556  HIS LEU SER LEU LEU PRO THR PHE GLY ALA LYS ASP TYR          
SEQRES  40 B  556  GLU THR HIS ARG VAL ALA THR THR GLY GLU TRP ASP LYS          
SEQRES  41 B  556  LEU THR GLN ASP LYS SER PHE ASN ASP ASN SER LYS ILE          
SEQRES  42 B  556  ARG MET ILE GLU ILE MET LEU PRO VAL PHE ASP ALA PRO          
SEQRES  43 B  556  GLN ASN LEU VAL LYS GLN ALA LYS LEU THR                      
HET     MG  A 559       1                                                       
HET    TPP  A 557      26                                                       
HET     MG  B 559       1                                                       
HET    TPP  B 557      26                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  TPP    2(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL   7  HOH   *2(H2 O)                                                      
HELIX    1  1A LEU A    6  GLN A   16  1                                  11    
HELIX    2  2A LEU A   31  GLU A   39  1ALSO CLASS 5                       9    
HELIX    3  3A GLU A   51  LYS A   65  1                                  15    
HELIX    4  4A VAL A   76  GLU A   91  1KINKED                            16    
HELIX    5  5A VAL A  124  ILE A  132  1ALSO CLASS 5                       9    
HELIX    6  6A ALA A  145  THR A  159  1                                  15    
HELIX    7  7A ASN A  170  ASP A  173  5                                   4    
HELIX    8  8A ALA A  178  GLN A  182  5                                   5    
HELIX    9  9A ALA A  194  ASP A  210  1                                  17    
HELIX   10 10A ALA A  220  CYS A  222  5                                   3    
HELIX   11 11A LYS A  228  THR A  238  1                                  11    
HELIX   12 12A PRO A  246  GLY A  248  5                                   3    
HELIX   13 13A PRO A  270  GLU A  277  1                                   8    
HELIX   14 14A MET A  326  ALA A  340  1                                  15    
HELIX   15 15A GLN A  367  LEU A  374  1                                   8    
HELIX   16 16A THR A  390  GLN A  397  1ALSO CLASS 5                       8    
HELIX   17 17A PHE A  417  ILE A  432  1                                  16    
HELIX   18 18A ASP A  444  TRP A  460  1KINKED                            17    
HELIX   19 19A THR A  475  LYS A  478  1                                   4    
HELIX   20 20A GLN A  486  ASN A  488  5                                   3    
HELIX   21 21A SER A  497  THR A  501  1                                   5    
HELIX   22 22A THR A  515  THR A  522  1                                   8    
HELIX   23 23A GLN A  547  LYS A  551  1                                   5    
HELIX   24  1B LEU B    6  GLN B   16  1                                  11    
HELIX   25  2B LEU B   31  GLU B   39  1ALSO CLASS 5                       9    
HELIX   26  3B GLU B   51  LYS B   65  1                                  15    
HELIX   27  4B VAL B   76  GLU B   91  1KINKED                            16    
HELIX   28  5B VAL B  124  ILE B  132  1ALSO CLASS 5                       9    
HELIX   29  6B ALA B  145  THR B  159  1                                  15    
HELIX   30  7B ASN B  170  ASP B  173  5                                   4    
HELIX   31  8B ALA B  178  GLN B  182  5                                   5    
HELIX   32  9B ALA B  194  ASP B  210  1                                  17    
HELIX   33 10B ALA B  220  CYS B  222  5                                   3    
HELIX   34 11B LYS B  228  THR B  238  1                                  11    
HELIX   35 12B PRO B  246  GLY B  248  5                                   3    
HELIX   36 13B PRO B  270  GLU B  277  1                                   8    
HELIX   37 14B MET B  326  ALA B  340  1                                  15    
HELIX   38 15B GLN B  367  LEU B  374  1                                   8    
HELIX   39 16B THR B  390  GLN B  397  1ALSO CLASS 5                       8    
HELIX   40 17B PHE B  417  ILE B  432  1                                  16    
HELIX   41 18B ASP B  444  TRP B  460  1KINKED                            17    
HELIX   42 19B THR B  475  LYS B  478  1                                   4    
HELIX   43 20B GLN B  486  ASN B  488  5                                   3    
HELIX   44 21B SER B  497  THR B  501  1                                   5    
HELIX   45 22B THR B  515  THR B  522  1                                   8    
HELIX   46 23B GLN B  547  LYS B  551  1                                   5    
SHEET    1 S1A 6 ARG A  44  ALA A  46  0                                        
SHEET    2 S1A 6 ASN A  20  GLY A  24  1  O  ASN A  20   N  ARG A  44           
SHEET    3 S1A 6 SER A  68  THR A  73  1  N  ILE A  71   O  PHE A  23           
SHEET    4 S1A 6 VAL A  95  VAL A 101  1  O  LEU A  96   N  ILE A  70           
SHEET    5 S1A 6 VAL A 163  PRO A 168  1  O  VAL A 163   N  HIS A  97           
SHEET    6 S1A 6 THR A 135  MET A 138  1  N  ALA A 137   O  TYR A 164           
SHEET    1 S2A 7 TYR A 259  VAL A 262  0                                        
SHEET    2 S2A 7 ALA A 242  VAL A 244  1  O  ALA A 242   N  GLY A 260           
SHEET    3 S2A 7 PRO A 214  ALA A 218  1  O  ILE A 216   N  PHE A 243           
SHEET    4 S2A 7 LEU A 281  VAL A 285  1  O  LEU A 283   N  LEU A 217           
SHEET    5 S2A 7 ASN A 305  HIS A 310  1  O  VAL A 307   N  SER A 284           
SHEET    6 S2A 7 HIS A 313  ILE A 316 -1  O  LYS A 315   N  GLU A 308           
SHEET    7 S2A 7 ALA A 319  PRO A 322 -1  O  ALA A 319   N  ILE A 316           
SHEET    1 S3A 6 TYR A 405  SER A 408  0                                        
SHEET    2 S3A 6 VAL A 383  GLU A 387  1  O  VAL A 384   N  ILE A 407           
SHEET    3 S3A 6 VAL A 438  GLY A 443  1  O  ILE A 439   N  ILE A 385           
SHEET    4 S3A 6 TYR A 465  ASN A 470  1  O  TYR A 465   N  LEU A 440           
SHEET    5 S3A 6 ARG A 534  MET A 539  1  O  ARG A 534   N  LEU A 466           
SHEET    6 S3A 6 THR A 509  VAL A 512  1  N  HIS A 510   O  MET A 535           
SHEET    1 S1B 6 ARG B  44  ALA B  46  0                                        
SHEET    2 S1B 6 ASN B  20  GLY B  24  1  O  ASN B  20   N  ARG B  44           
SHEET    3 S1B 6 SER B  68  THR B  73  1  N  ILE B  71   O  PHE B  23           
SHEET    4 S1B 6 VAL B  95  VAL B 101  1  O  LEU B  96   N  ILE B  70           
SHEET    5 S1B 6 VAL B 163  PRO B 168  1  O  VAL B 163   N  HIS B  97           
SHEET    6 S1B 6 THR B 135  MET B 138  1  N  ALA B 137   O  TYR B 164           
SHEET    1 S2B 7 TYR B 259  VAL B 262  0                                        
SHEET    2 S2B 7 ALA B 242  VAL B 244  1  O  ALA B 242   N  GLY B 260           
SHEET    3 S2B 7 PRO B 214  ALA B 218  1  O  ILE B 216   N  PHE B 243           
SHEET    4 S2B 7 LEU B 281  VAL B 285  1  O  LEU B 283   N  LEU B 217           
SHEET    5 S2B 7 ASN B 305  HIS B 310  1  O  VAL B 307   N  SER B 284           
SHEET    6 S2B 7 HIS B 313  ILE B 316 -1  O  LYS B 315   N  GLU B 308           
SHEET    7 S2B 7 ALA B 319  PRO B 322 -1  O  ALA B 319   N  ILE B 316           
SHEET    1 S3B 6 TYR B 405  SER B 408  0                                        
SHEET    2 S3B 6 VAL B 383  GLU B 387  1  O  VAL B 384   N  ILE B 407           
SHEET    3 S3B 6 VAL B 438  GLY B 443  1  O  ILE B 439   N  ILE B 385           
SHEET    4 S3B 6 TYR B 465  ASN B 470  1  O  TYR B 465   N  LEU B 440           
SHEET    5 S3B 6 ARG B 534  MET B 539  1  O  ARG B 534   N  LEU B 466           
SHEET    6 S3B 6 THR B 509  VAL B 512  1  N  HIS B 510   O  MET B 535           
LINK         OD1 ASP A 444                MG    MG A 559     1555   1555  2.01  
LINK         OD1 ASN A 471                MG    MG A 559     1555   1555  2.04  
LINK         O   GLY A 473                MG    MG A 559     1555   1555  2.20  
LINK         O2A TPP A 557                MG    MG A 559     1555   1555  2.17  
LINK         O3B TPP A 557                MG    MG A 559     1555   1555  2.15  
LINK        MG    MG A 559                 O   HOH A 560     1555   1555  1.99  
LINK         OD1 ASP B 444                MG    MG B 559     1555   1555  2.27  
LINK         OD1 ASN B 471                MG    MG B 559     1555   1555  1.94  
LINK         O   GLY B 473                MG    MG B 559     1555   1555  2.09  
LINK         O3B TPP B 557                MG    MG B 559     1555   1555  2.19  
LINK         O2A TPP B 557                MG    MG B 559     1555   1555  2.43  
LINK        MG    MG B 559                 O   HOH B 560     1555   1555  2.26  
SITE     1 TD1 20 THR A 388  THR A 390  GLY A 413  ILE A 415                    
SITE     2 TD1 20 ASP A 444  SER A 446  LEU A 449  LEU A 469                    
SITE     3 TD1 20 ASN A 471  ILE A 476  GLY A 473  GLU A 477                    
SITE     4 TD1 20 LEU B  25  ASP B  28  GLU B  51  THR B  73                    
SITE     5 TD1 20 VAL B  76  ASN B  83  HIS B 114  HIS B 115                    
SITE     1 TD2 20 THR B 388  THR B 390  GLY B 413  ILE B 415                    
SITE     2 TD2 20 ASP B 444  SER B 446  LEU B 449  LEU B 469                    
SITE     3 TD2 20 ASN B 471  ILE B 476  GLY B 473  GLU B 477                    
SITE     4 TD2 20 LEU A  25  ASP A  28  GLU A  51  THR A  73                    
SITE     5 TD2 20 VAL A  76  ASN A  83  HIS A 114  HIS A 115                    
SITE     1 AC1  5 ASP A 444  ASN A 471  GLY A 473  TPP A 557                    
SITE     2 AC1  5 HOH A 560                                                     
SITE     1 AC2  5 ASP B 444  ASN B 471  GLY B 473  TPP B 557                    
SITE     2 AC2  5 HOH B 560                                                     
SITE     1 AC3 19 THR A 390  GLY A 413  ILE A 415  GLY A 443                    
SITE     2 AC3 19 ASP A 444  GLY A 445  SER A 446  ASN A 471                    
SITE     3 AC3 19 GLY A 473  TYR A 474  THR A 475  ILE A 476                    
SITE     4 AC3 19 GLU A 477   MG A 559  HOH A 560  PRO B  26                    
SITE     5 AC3 19 GLY B  27  GLU B  51  VAL B  76                               
SITE     1 AC4 20 PRO A  26  GLY A  27  GLU A  51  VAL A  76                    
SITE     2 AC4 20 GLY B 389  THR B 390  GLY B 413  ILE B 415                    
SITE     3 AC4 20 GLY B 443  ASP B 444  GLY B 445  SER B 446                    
SITE     4 AC4 20 ASN B 471  GLY B 473  TYR B 474  THR B 475                    
SITE     5 AC4 20 ILE B 476  GLU B 477   MG B 559  HOH B 560                    
CRYST1  141.950   74.670  119.950  90.00 116.39  90.00 C 1 2 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      0.007045  0.000000  0.003496        0.00000                         
SCALE2      0.000000  0.013392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009307        0.00000                         
MTRIX1   1 -0.912290 -0.045160 -0.407040        2.16400    1                    
MTRIX2   1 -0.045160 -0.976750  0.209580       -1.49200    1                    
MTRIX3   1 -0.407040  0.209580  0.889040        0.63200    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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