HEADER LYASE (CARBON-CARBON) 20-APR-95 1PVD
TITLE CRYSTAL STRUCTURE OF THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE
TITLE 2 DECARBOXYLASE FROM THE YEAST SACCHAROMYCES CEREVISIAE AT 2.3
TITLE 3 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,P.ARJUNAN
REVDAT 5 21-FEB-24 1PVD 1 REMARK SEQADV LINK
REVDAT 4 14-AUG-19 1PVD 1 REMARK
REVDAT 3 17-JUL-19 1PVD 1 REMARK
REVDAT 2 24-FEB-09 1PVD 1 VERSN
REVDAT 1 31-JUL-95 1PVD 0
JRNL AUTH P.ARJUNAN,T.UMLAND,F.DYDA,S.SWAMINATHAN,W.FUREY,M.SAX,
JRNL AUTH 2 B.FARRENKOPF,Y.GAO,D.ZHANG,F.JORDAN
JRNL TITL CRYSTAL STRUCTURE OF THE THIAMIN DIPHOSPHATE-DEPENDENT
JRNL TITL 2 ENZYME PYRUVATE DECARBOXYLASE FROM THE YEAST SACCHAROMYCES
JRNL TITL 3 CEREVISIAE AT 2.3 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 256 590 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8604141
JRNL DOI 10.1006/JMBI.1996.0111
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.DYDA,W.FUREY,S.SWAMINATHAN,M.SAX,B.FARRENKOPF,F.JORDAN
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 S.HOHMANN
REMARK 1 TITL STRUCTURE AND EXPRESSION OF YEAST PYRUVATE DECARBOXYLASE
REMARK 1 TITL 2 STRUCTURAL GENES
REMARK 1 EDIT H.BISSWANGER, J.ULLRICH
REMARK 1 REF BIOCHEMISTRY AND PHYSIOLOGY 106 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 3
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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 46196
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.165
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 : 439
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:
REMARK 3 REFERENCE 1 DESCRIBES THE TRANSFORMATION TO THE MONOCLINIC
REMARK 3 FORM AND ROTATION FUNCTION RESULTS. (APPROPRIATE FOR BOTH
REMARK 3 SACCHAROMYCES UVARUM AND SACCHAROMYCES CEREVISIAE).
REMARK 3
REMARK 3 REFERENCE 3 DESCRIBES THE TRICLINIC CRYSTALS OF THE
REMARK 3 RELATED SACCHAROMYCES UVARUM FORM.
REMARK 4
REMARK 4 1PVD 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_1000175866.
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 : 46787
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
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 (%): 47.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
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 71.03000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.37500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.03000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.37500
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 (A AND B) ARE RELATED BY A
REMARK 300 NONCRYSTALLOGRAPHIC TWO-FOLD AXIS INCLINED BY 83.31 DEGREES
REMARK 300 TO THE B AXIS, AND WHOSE PROJECTION ON THE AC PLANE MAKES
REMARK 300 ANGLES OF 102.16 DEGREES WITH THE A AXIS, AND 14.23 DEGREES
REMARK 300 WITH THE C AXIS. THE NONCRYSTALLOGRAPHIC TWO-FOLD AXIS
REMARK 300 DOES NOT INTERSECT THE B AXIS, AS ITS CLOSEST APPROACH IS
REMARK 300 OFFSET BY 1.352 ANGSTROMS. THE TETRAMER THUS HAS ONLY
REMARK 300 APPROXIMATE 222 SYMMETRY, AS IT MUST INTERSECT THE B AXIS
REMARK 300 AND BE INCLINED TO IT BY 90 DEGREES FOR EXACT 222 SYMMETRY.
REMARK 300
REMARK 300 MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 A 2 .. 556 B 2 .. 556 1.282
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: 7600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 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 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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 416 N GLY A 416 CA 0.097
REMARK 500 SER B 253 CB SER B 253 OG 0.103
REMARK 500 ASN B 471 CB ASN B 471 CG 0.170
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 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 PHE A 23 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 28 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU A 31 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU A 33 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP A 35 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 35 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ALA A 49 CB - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 VAL A 95 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 SER A 103 C - N - CA ANGL. DEV. = 20.5 DEGREES
REMARK 500 HIS A 114 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 THR A 116 OG1 - CB - CG2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG A 127 CD - NE - CZ ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ALA A 137 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 141 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 THR A 144 CA - CB - CG2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 150 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 150 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 151 NH1 - CZ - NH2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 VAL A 176 N - CA - CB ANGL. DEV. = -16.2 DEGREES
REMARK 500 ASP A 186 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 219 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 224 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 LEU A 237 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU A 237 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 THR A 238 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 258 NH1 - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 VAL A 264 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 GLU A 271 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 280 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP A 312 OD1 - CG - OD2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 ASP A 312 CB - CG - OD1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 317 CD - NE - CZ ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG A 317 NE - CZ - NH1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 317 NE - CZ - NH2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 LEU A 330 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP A 339 CB - CG - OD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 SER A 362 CB - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 ASP A 382 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 144 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 SER A 103 5.02 -41.94
REMARK 500 ILE A 104 30.91 72.57
REMARK 500 HIS A 115 30.76 75.55
REMARK 500 ALA A 220 -61.49 -28.81
REMARK 500 CYS A 221 30.42 -89.60
REMARK 500 ASP A 226 -23.58 74.64
REMARK 500 LEU A 289 -167.37 47.66
REMARK 500 SER A 290 -62.20 -161.07
REMARK 500 THR A 303 92.54 -168.21
REMARK 500 LYS A 304 -84.12 -79.40
REMARK 500 ARG A 317 -125.25 60.03
REMARK 500 ILE A 415 -16.08 -47.65
REMARK 500 ASP A 433 118.39 -166.04
REMARK 500 ASP A 472 71.63 45.50
REMARK 500 LEU A 555 35.95 -83.44
REMARK 500 ILE B 104 106.85 -48.82
REMARK 500 ALA B 220 -68.03 -24.26
REMARK 500 ASP B 226 49.46 27.17
REMARK 500 VAL B 285 53.87 -110.05
REMARK 500 ALA B 287 -145.06 -144.13
REMARK 500 LEU B 288 164.22 -49.88
REMARK 500 LEU B 289 58.02 -99.25
REMARK 500 THR B 303 -177.85 58.72
REMARK 500 ARG B 317 -118.38 64.31
REMARK 500 LYS B 342 95.85 -64.87
REMARK 500 ASP B 433 113.77 -164.47
REMARK 500 HIS B 481 132.76 -172.46
REMARK 500 GLN B 552 -101.61 -76.72
REMARK 500 ALA B 553 -30.20 -31.39
REMARK 500 LEU B 555 50.74 -97.12
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 B 154 0.11 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 558 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 444 OD1
REMARK 620 2 ASN A 471 OD1 104.4
REMARK 620 3 GLY A 473 O 98.7 91.9
REMARK 620 4 TPP A 557 O1A 82.1 172.9 89.8
REMARK 620 5 TPP A 557 O3B 161.8 91.3 89.8 81.9
REMARK 620 6 HOH A 559 O 89.9 90.8 170.0 86.3 80.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 558 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 444 OD1
REMARK 620 2 ASN B 471 OD1 103.4
REMARK 620 3 GLY B 473 O 92.1 99.4
REMARK 620 4 TPP B 557 O3B 159.3 88.0 103.2
REMARK 620 5 TPP B 557 O1A 84.7 169.9 86.2 82.5
REMARK 620 6 HOH B 559 O 80.1 84.9 171.9 83.8 90.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: TPA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: TPB
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 558
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 558
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
DBREF 1PVD A 2 556 UNP P06169 PDC1_YEAST 1 555
DBREF 1PVD B 2 556 UNP P06169 PDC1_YEAST 1 555
SEQADV 1PVD ALA A 55 UNP P06169 ARG 54 CONFLICT
SEQADV 1PVD ALA A 143 UNP P06169 CYS 142 CONFLICT
SEQADV 1PVD ALA A 206 UNP P06169 VAL 205 CONFLICT
SEQADV 1PVD VAL A 208 UNP P06169 ALA 207 CONFLICT
SEQADV 1PVD ILE A 538 UNP P06169 VAL 537 CONFLICT
SEQADV 1PVD LYS A 551 UNP P06169 GLU 550 CONFLICT
SEQADV 1PVD ALA B 55 UNP P06169 ARG 54 CONFLICT
SEQADV 1PVD ALA B 143 UNP P06169 CYS 142 CONFLICT
SEQADV 1PVD ALA B 206 UNP P06169 VAL 205 CONFLICT
SEQADV 1PVD VAL B 208 UNP P06169 ALA 207 CONFLICT
SEQADV 1PVD ILE B 538 UNP P06169 VAL 537 CONFLICT
SEQADV 1PVD LYS B 551 UNP P06169 GLU 550 CONFLICT
SEQRES 1 A 555 SER GLU ILE THR LEU GLY LYS TYR LEU PHE GLU ARG LEU
SEQRES 2 A 555 LYS GLN VAL ASN VAL ASN THR VAL PHE GLY LEU PRO GLY
SEQRES 3 A 555 ASP PHE ASN LEU SER LEU LEU ASP LYS ILE TYR GLU VAL
SEQRES 4 A 555 GLU GLY MET ARG TRP ALA GLY ASN ALA ASN GLU LEU ASN
SEQRES 5 A 555 ALA ALA TYR ALA ALA ASP GLY TYR ALA ARG ILE LYS GLY
SEQRES 6 A 555 MET SER CYS ILE ILE THR THR PHE GLY VAL GLY GLU LEU
SEQRES 7 A 555 SER ALA LEU ASN GLY ILE ALA GLY SER TYR ALA GLU HIS
SEQRES 8 A 555 VAL GLY VAL LEU HIS VAL VAL GLY VAL PRO SER ILE SER
SEQRES 9 A 555 SER GLN ALA LYS GLN LEU LEU LEU HIS HIS THR LEU GLY
SEQRES 10 A 555 ASN GLY ASP PHE THR VAL PHE HIS ARG MET SER ALA ASN
SEQRES 11 A 555 ILE SER GLU THR THR ALA MET ILE THR ASP ILE ALA THR
SEQRES 12 A 555 ALA PRO ALA GLU ILE ASP ARG CYS ILE ARG THR THR TYR
SEQRES 13 A 555 VAL THR GLN ARG PRO VAL TYR LEU GLY LEU PRO ALA ASN
SEQRES 14 A 555 LEU VAL ASP LEU ASN VAL PRO ALA LYS LEU LEU GLN THR
SEQRES 15 A 555 PRO ILE ASP MET SER LEU LYS PRO ASN ASP ALA GLU SER
SEQRES 16 A 555 GLU LYS GLU VAL ILE ASP THR ILE LEU ALA LEU VAL LYS
SEQRES 17 A 555 ASP ALA LYS ASN PRO VAL ILE LEU ALA ASP ALA CYS CYS
SEQRES 18 A 555 SER ARG HIS ASP VAL LYS ALA GLU THR LYS LYS LEU ILE
SEQRES 19 A 555 ASP LEU THR GLN PHE PRO ALA PHE VAL THR PRO MET GLY
SEQRES 20 A 555 LYS GLY SER ILE SER GLU GLN HIS PRO ARG TYR GLY GLY
SEQRES 21 A 555 VAL TYR VAL GLY THR LEU SER LYS PRO GLU VAL LYS GLU
SEQRES 22 A 555 ALA VAL GLU SER ALA ASP LEU ILE LEU SER VAL GLY ALA
SEQRES 23 A 555 LEU LEU SER ASP PHE ASN THR GLY SER PHE SER TYR SER
SEQRES 24 A 555 TYR LYS THR LYS ASN ILE VAL GLU PHE HIS SER ASP HIS
SEQRES 25 A 555 MET LYS ILE ARG ASN ALA THR PHE PRO GLY VAL GLN MET
SEQRES 26 A 555 LYS PHE VAL LEU GLN LYS LEU LEU THR ASN ILE ALA ASP
SEQRES 27 A 555 ALA ALA LYS GLY TYR LYS PRO VAL ALA VAL PRO ALA ARG
SEQRES 28 A 555 THR PRO ALA ASN ALA ALA VAL PRO ALA SER THR PRO LEU
SEQRES 29 A 555 LYS GLN GLU TRP MET TRP ASN GLN LEU GLY ASN PHE LEU
SEQRES 30 A 555 GLN GLU GLY ASP VAL VAL ILE ALA GLU THR GLY THR SER
SEQRES 31 A 555 ALA PHE GLY ILE ASN GLN THR THR PHE PRO ASN ASN THR
SEQRES 32 A 555 TYR GLY ILE SER GLN VAL LEU TRP GLY SER ILE GLY PHE
SEQRES 33 A 555 THR THR GLY ALA THR LEU GLY ALA ALA PHE ALA ALA GLU
SEQRES 34 A 555 GLU ILE ASP PRO LYS LYS ARG VAL ILE LEU PHE ILE GLY
SEQRES 35 A 555 ASP GLY SER LEU GLN LEU THR VAL GLN GLU ILE SER THR
SEQRES 36 A 555 MET ILE ARG TRP GLY LEU LYS PRO TYR LEU PHE VAL LEU
SEQRES 37 A 555 ASN ASN ASP GLY TYR THR ILE GLU LYS LEU ILE HIS GLY
SEQRES 38 A 555 PRO LYS ALA GLN TYR ASN GLU ILE GLN GLY TRP ASP HIS
SEQRES 39 A 555 LEU SER LEU LEU PRO THR PHE GLY ALA LYS ASP TYR GLU
SEQRES 40 A 555 THR HIS ARG VAL ALA THR THR GLY GLU TRP ASP LYS LEU
SEQRES 41 A 555 THR GLN ASP LYS SER PHE ASN ASP ASN SER LYS ILE ARG
SEQRES 42 A 555 MET ILE GLU ILE MET LEU PRO VAL PHE ASP ALA PRO GLN
SEQRES 43 A 555 ASN LEU VAL LYS GLN ALA LYS LEU THR
SEQRES 1 B 555 SER GLU ILE THR LEU GLY LYS TYR LEU PHE GLU ARG LEU
SEQRES 2 B 555 LYS GLN VAL ASN VAL ASN THR VAL PHE GLY LEU PRO GLY
SEQRES 3 B 555 ASP PHE ASN LEU SER LEU LEU ASP LYS ILE TYR GLU VAL
SEQRES 4 B 555 GLU GLY MET ARG TRP ALA GLY ASN ALA ASN GLU LEU ASN
SEQRES 5 B 555 ALA ALA TYR ALA ALA ASP GLY TYR ALA ARG ILE LYS GLY
SEQRES 6 B 555 MET SER CYS ILE ILE THR THR PHE GLY VAL GLY GLU LEU
SEQRES 7 B 555 SER ALA LEU ASN GLY ILE ALA GLY SER TYR ALA GLU HIS
SEQRES 8 B 555 VAL GLY VAL LEU HIS VAL VAL GLY VAL PRO SER ILE SER
SEQRES 9 B 555 SER GLN ALA LYS GLN LEU LEU LEU HIS HIS THR LEU GLY
SEQRES 10 B 555 ASN GLY ASP PHE THR VAL PHE HIS ARG MET SER ALA ASN
SEQRES 11 B 555 ILE SER GLU THR THR ALA MET ILE THR ASP ILE ALA THR
SEQRES 12 B 555 ALA PRO ALA GLU ILE ASP ARG CYS ILE ARG THR THR TYR
SEQRES 13 B 555 VAL THR GLN ARG PRO VAL TYR LEU GLY LEU PRO ALA ASN
SEQRES 14 B 555 LEU VAL ASP LEU ASN VAL PRO ALA LYS LEU LEU GLN THR
SEQRES 15 B 555 PRO ILE ASP MET SER LEU LYS PRO ASN ASP ALA GLU SER
SEQRES 16 B 555 GLU LYS GLU VAL ILE ASP THR ILE LEU ALA LEU VAL LYS
SEQRES 17 B 555 ASP ALA LYS ASN PRO VAL ILE LEU ALA ASP ALA CYS CYS
SEQRES 18 B 555 SER ARG HIS ASP VAL LYS ALA GLU THR LYS LYS LEU ILE
SEQRES 19 B 555 ASP LEU THR GLN PHE PRO ALA PHE VAL THR PRO MET GLY
SEQRES 20 B 555 LYS GLY SER ILE SER GLU GLN HIS PRO ARG TYR GLY GLY
SEQRES 21 B 555 VAL TYR VAL GLY THR LEU SER LYS PRO GLU VAL LYS GLU
SEQRES 22 B 555 ALA VAL GLU SER ALA ASP LEU ILE LEU SER VAL GLY ALA
SEQRES 23 B 555 LEU LEU SER ASP PHE ASN THR GLY SER PHE SER TYR SER
SEQRES 24 B 555 TYR LYS THR LYS ASN ILE VAL GLU PHE HIS SER ASP HIS
SEQRES 25 B 555 MET LYS ILE ARG ASN ALA THR PHE PRO GLY VAL GLN MET
SEQRES 26 B 555 LYS PHE VAL LEU GLN LYS LEU LEU THR ASN ILE ALA ASP
SEQRES 27 B 555 ALA ALA LYS GLY TYR LYS PRO VAL ALA VAL PRO ALA ARG
SEQRES 28 B 555 THR PRO ALA ASN ALA ALA VAL PRO ALA SER THR PRO LEU
SEQRES 29 B 555 LYS GLN GLU TRP MET TRP ASN GLN LEU GLY ASN PHE LEU
SEQRES 30 B 555 GLN GLU GLY ASP VAL VAL ILE ALA GLU THR GLY THR SER
SEQRES 31 B 555 ALA PHE GLY ILE ASN GLN THR THR PHE PRO ASN ASN THR
SEQRES 32 B 555 TYR GLY ILE SER GLN VAL LEU TRP GLY SER ILE GLY PHE
SEQRES 33 B 555 THR THR GLY ALA THR LEU GLY ALA ALA PHE ALA ALA GLU
SEQRES 34 B 555 GLU ILE ASP PRO LYS LYS ARG VAL ILE LEU PHE ILE GLY
SEQRES 35 B 555 ASP GLY SER LEU GLN LEU THR VAL GLN GLU ILE SER THR
SEQRES 36 B 555 MET ILE ARG TRP GLY LEU LYS PRO TYR LEU PHE VAL LEU
SEQRES 37 B 555 ASN ASN ASP GLY TYR THR ILE GLU LYS LEU ILE HIS GLY
SEQRES 38 B 555 PRO LYS ALA GLN TYR ASN GLU ILE GLN GLY TRP ASP HIS
SEQRES 39 B 555 LEU SER LEU LEU PRO THR PHE GLY ALA LYS ASP TYR GLU
SEQRES 40 B 555 THR HIS ARG VAL ALA THR THR GLY GLU TRP ASP LYS LEU
SEQRES 41 B 555 THR GLN ASP LYS SER PHE ASN ASP ASN SER LYS ILE ARG
SEQRES 42 B 555 MET ILE GLU ILE MET LEU PRO VAL PHE ASP ALA PRO GLN
SEQRES 43 B 555 ASN LEU VAL LYS GLN ALA LYS LEU THR
HET MG A 558 1
HET TPP A 557 26
HET MG B 558 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 *439(H2 O)
HELIX 1 H1 LEU A 6 GLN A 16 1 11
HELIX 2 H2 LEU A 31 GLU A 39 1AND 5 9
HELIX 3 H3 GLU A 51 LYS A 65 1 15
HELIX 4 H4 VAL A 76 GLU A 91 1KINKED 16
HELIX 5 H5 VAL A 124 ILE A 132 1AND 5 9
HELIX 6 H6 ALA A 145 THR A 159 1 15
HELIX 7 H7 ASN A 170 ASP A 173 5 4
HELIX 8 H8 ALA A 178 GLN A 182 5 5
HELIX 9 H9 ALA A 194 ASP A 210 1 17
HELIX 10 A10 ALA A 220 CYS A 222 5 3
HELIX 11 A11 LYS A 228 THR A 238 1 11
HELIX 12 A12 PRO A 246 GLY A 248 5 3
HELIX 13 A13 PRO A 270 GLU A 277 1 8
HELIX 14 A14 MET A 326 ALA A 340 1 15
HELIX 15 A15 GLN A 367 LEU A 374 1 8
HELIX 16 A16 THR A 390 GLN A 397 1AND 5 8
HELIX 17 A17 PHE A 417 ILE A 432 1 16
HELIX 18 A18 ASP A 444 TRP A 460 1KINKED 17
HELIX 19 A19 THR A 475 LYS A 478 1 4
HELIX 20 A20 GLN A 486 ASN A 488 5 3
HELIX 21 A21 SER A 497 THR A 501 1 5
HELIX 22 A22 THR A 515 THR A 522 1 8
HELIX 23 A23 GLN A 547 LYS A 551 1 5
HELIX 24 B1 LEU B 6 GLN B 16 1 11
HELIX 25 B2 LEU B 31 GLU B 39 1AND 5 9
HELIX 26 B3 GLU B 51 LYS B 65 1 15
HELIX 27 B4 VAL B 76 GLU B 91 1KINKED 16
HELIX 28 B5 VAL B 124 ILE B 132 1AND 5 9
HELIX 29 B6 ALA B 145 THR B 159 1 15
HELIX 30 B7 ASN B 170 ASP B 173 5 4
HELIX 31 B8 ALA B 178 GLN B 182 5 5
HELIX 32 B9 ALA B 194 ASP B 210 1 17
HELIX 33 B10 ALA B 220 CYS B 222 5 3
HELIX 34 B11 LYS B 228 THR B 238 1 11
HELIX 35 B12 PRO B 246 GLY B 248 5 3
HELIX 36 B13 PRO B 270 GLU B 277 1 8
HELIX 37 B14 MET B 326 ALA B 340 1 15
HELIX 38 B15 GLN B 367 LEU B 374 1 8
HELIX 39 B16 THR B 390 GLN B 397 1AND 5 8
HELIX 40 B17 PHE B 417 ILE B 432 1 16
HELIX 41 B18 ASP B 444 TRP B 460 1KINKED 17
HELIX 42 B19 THR B 475 LYS B 478 1 4
HELIX 43 B20 GLN B 486 ASN B 488 5 3
HELIX 44 B21 SER B 497 THR B 501 1 5
HELIX 45 B22 THR B 515 THR B 522 1 8
HELIX 46 B23 GLN B 547 LYS B 551 1 5
SHEET 1 AS1 6 ARG A 44 ALA A 46 0
SHEET 2 AS1 6 ASN A 20 GLY A 24 1 O ASN A 20 N ARG A 44
SHEET 3 AS1 6 SER A 68 THR A 73 1 N ILE A 71 O PHE A 23
SHEET 4 AS1 6 VAL A 95 VAL A 101 1 O LEU A 96 N ILE A 70
SHEET 5 AS1 6 VAL A 163 PRO A 168 1 O VAL A 163 N HIS A 97
SHEET 6 AS1 6 THR A 135 MET A 138 1 N ALA A 137 O TYR A 164
SHEET 1 AS2 7 TYR A 259 VAL A 262 0
SHEET 2 AS2 7 ALA A 242 VAL A 244 1 O ALA A 242 N GLY A 260
SHEET 3 AS2 7 PRO A 214 ALA A 218 1 O ILE A 216 N PHE A 243
SHEET 4 AS2 7 LEU A 281 VAL A 285 1 O LEU A 283 N LEU A 217
SHEET 5 AS2 7 ASN A 305 HIS A 310 1 O VAL A 307 N SER A 284
SHEET 6 AS2 7 HIS A 313 ILE A 316 -1 O LYS A 315 N GLU A 308
SHEET 7 AS2 7 ALA A 319 PRO A 322 -1 O ALA A 319 N ILE A 316
SHEET 1 AS3 6 TYR A 405 SER A 408 0
SHEET 2 AS3 6 VAL A 383 GLU A 387 1 O VAL A 384 N ILE A 407
SHEET 3 AS3 6 VAL A 438 GLY A 443 1 O ILE A 439 N ILE A 385
SHEET 4 AS3 6 TYR A 465 ASN A 470 1 O TYR A 465 N LEU A 440
SHEET 5 AS3 6 ARG A 534 MET A 539 1 O ARG A 534 N LEU A 466
SHEET 6 AS3 6 THR A 509 VAL A 512 1 N HIS A 510 O MET A 535
SHEET 1 BS1 6 ARG B 44 ALA B 46 0
SHEET 2 BS1 6 ASN B 20 GLY B 24 1 O ASN B 20 N ARG B 44
SHEET 3 BS1 6 SER B 68 THR B 73 1 N ILE B 71 O PHE B 23
SHEET 4 BS1 6 VAL B 95 VAL B 101 1 O LEU B 96 N ILE B 70
SHEET 5 BS1 6 VAL B 163 PRO B 168 1 O VAL B 163 N HIS B 97
SHEET 6 BS1 6 THR B 135 MET B 138 1 N ALA B 137 O TYR B 164
SHEET 1 BS2 7 TYR B 259 VAL B 262 0
SHEET 2 BS2 7 ALA B 242 VAL B 244 1 O ALA B 242 N GLY B 260
SHEET 3 BS2 7 PRO B 214 ALA B 218 1 O ILE B 216 N PHE B 243
SHEET 4 BS2 7 LEU B 281 VAL B 285 1 O LEU B 283 N LEU B 217
SHEET 5 BS2 7 ASN B 305 HIS B 310 1 O VAL B 307 N SER B 284
SHEET 6 BS2 7 HIS B 313 ILE B 316 -1 O LYS B 315 N GLU B 308
SHEET 7 BS2 7 ALA B 319 PRO B 322 -1 O ALA B 319 N ILE B 316
SHEET 1 BS3 6 TYR B 405 SER B 408 0
SHEET 2 BS3 6 VAL B 383 GLU B 387 1 O VAL B 384 N ILE B 407
SHEET 3 BS3 6 VAL B 438 GLY B 443 1 O ILE B 439 N ILE B 385
SHEET 4 BS3 6 TYR B 465 ASN B 470 1 O TYR B 465 N LEU B 440
SHEET 5 BS3 6 ARG B 534 MET B 539 1 O ARG B 534 N LEU B 466
SHEET 6 BS3 6 THR B 509 VAL B 512 1 N HIS B 510 O MET B 535
LINK OD1 ASP A 444 MG MG A 558 1555 1555 2.25
LINK OD1 ASN A 471 MG MG A 558 1555 1555 2.10
LINK O GLY A 473 MG MG A 558 1555 1555 2.21
LINK O1A TPP A 557 MG MG A 558 1555 1555 2.31
LINK O3B TPP A 557 MG MG A 558 1555 1555 2.34
LINK MG MG A 558 O HOH A 559 1555 1555 2.22
LINK OD1 ASP B 444 MG MG B 558 1555 1555 2.19
LINK OD1 ASN B 471 MG MG B 558 1555 1555 2.27
LINK O GLY B 473 MG MG B 558 1555 1555 2.28
LINK O3B TPP B 557 MG MG B 558 1555 1555 2.05
LINK O1A TPP B 557 MG MG B 558 1555 1555 2.10
LINK MG MG B 558 O HOH B 559 1555 1555 2.22
SITE 1 TPA 20 GLY A 413 ILE A 415 THR A 388 THR A 390
SITE 2 TPA 20 SER A 446 ILE A 476 LEU A 469 ASN A 471
SITE 3 TPA 20 ASP A 444 GLY A 473 GLU A 477 LEU A 449
SITE 4 TPA 20 GLU B 51 ASP B 28 THR B 73 VAL B 76
SITE 5 TPA 20 ASN B 83 LEU B 25 HIS B 114 HIS B 115
SITE 1 TPB 20 GLY B 413 ILE B 415 THR B 388 THR B 390
SITE 2 TPB 20 SER B 446 ILE B 476 LEU B 469 ASN B 471
SITE 3 TPB 20 ASP B 444 GLY B 473 GLU B 477 LEU B 449
SITE 4 TPB 20 GLU A 51 ASP A 28 THR A 73 VAL A 76
SITE 5 TPB 20 ASN A 83 LEU A 25 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 559
SITE 1 AC2 5 ASP B 444 ASN B 471 GLY B 473 TPP B 557
SITE 2 AC2 5 HOH B 559
SITE 1 AC3 23 GLY A 389 THR A 390 GLY A 413 SER A 414
SITE 2 AC3 23 ILE A 415 GLY A 443 ASP A 444 GLY A 445
SITE 3 AC3 23 SER A 446 ASN A 471 GLY A 473 TYR A 474
SITE 4 AC3 23 THR A 475 ILE A 476 GLU A 477 MG A 558
SITE 5 AC3 23 HOH A 559 HOH A 583 HOH A 647 PRO B 26
SITE 6 AC3 23 GLY B 27 GLU B 51 VAL B 76
SITE 1 AC4 23 PRO A 26 GLU A 51 VAL A 76 GLY B 389
SITE 2 AC4 23 THR B 390 GLY B 413 SER B 414 ILE B 415
SITE 3 AC4 23 GLY B 443 ASP B 444 GLY B 445 SER B 446
SITE 4 AC4 23 ASN B 471 GLY B 473 TYR B 474 THR B 475
SITE 5 AC4 23 ILE B 476 GLU B 477 MG B 558 HOH B 559
SITE 6 AC4 23 HOH B 612 HOH B 791 HOH B 861
CRYST1 142.060 74.750 120.320 90.00 116.58 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 0.007039 0.000000 0.003522 0.00000
SCALE2 0.000000 0.013378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009293 0.00000
MTRIX1 1 -0.911500 -0.049300 -0.408400 1.83180 1
MTRIX2 1 -0.040300 -0.977300 0.207900 -1.42980 1
MTRIX3 1 -0.409400 0.205900 0.888800 0.46540 1
(ATOM LINES ARE NOT SHOWN.)
END
