HEADER TRANSFERASE 03-NOV-00 1G69
TITLE THIAMIN PHOSPHATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIAMIN PHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: COMPLEXED WITH 2-METHYL-5-METHYLENE-5H-PYRIMIDIN-4-
COMPND 8 YLIDENEAMINE, 4-METHYL-5-HYDROXYETHYLTHIAZOLE PHOSPHATE AND
COMPND 9 PYROPHOSPHATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: THIC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SG13009 WITH PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PYZC6927
KEYWDS THIAMIN BIOSYNTHESIS, TIM BARREL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.PEAPUS,H.-J.CHIU,N.CAMPOBASSO,J.J.REDDICK,T.P.BEGLEY,S.E.EALICK
REVDAT 5 09-AUG-23 1G69 1 REMARK
REVDAT 4 27-OCT-21 1G69 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1G69 1 VERSN
REVDAT 2 01-APR-03 1G69 1 JRNL
REVDAT 1 26-SEP-01 1G69 0
JRNL AUTH D.H.PEAPUS,H.J.CHIU,N.CAMPOBASSO,J.J.REDDICK,T.P.BEGLEY,
JRNL AUTH 2 S.E.EALICK
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE ENZYME-SUBSTRATE,
JRNL TITL 2 ENZYME-INTERMEDIATE, AND ENZYME-PRODUCT COMPLEXES OF THIAMIN
JRNL TITL 3 PHOSPHATE SYNTHASE.
JRNL REF BIOCHEMISTRY V. 40 10103 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11513589
JRNL DOI 10.1021/BI0104726
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.-J.CHIU,J.J.REDDICK,T.P.BEGLEY,S.E.EALICK
REMARK 1 TITL CRYSTAL STRUCTURE OF THIAMIN PHOSPHATE SYNTHASE FROM
REMARK 1 TITL 2 BACILLUS SUBTILIS AT 1.25A RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 38 6460 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI982903Z
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.ZHANG,S.V.TAYLOR,H.-J.CHIU,T.P.BEGLEY
REMARK 1 TITL CHARACTERIZATION OF THE BACILLUS SUBTILIS THIC OPERON
REMARK 1 TITL 2 INVOLVED IN THIAMINE BIOSYNTHESIS
REMARK 1 REF J.BACTERIOL. V. 179 3030 1997
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD FUNCTION
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2362308.320
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 61893
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3120
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7026
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 369
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3402
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.09
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.08
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.740 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.940 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 37.98
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : N2.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : N2.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61893
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 42.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1G4E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 75MM TRIS-HCL, 75 MM MGCL2, 21-22%
REMARK 280 PEG4000, PH 7.5, HANGING DROP VAPOR DIFFUSION WITH MICRO SEEDING,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 69.94000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.24000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.24000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 104.91000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.24000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.24000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.97000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.24000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.24000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 104.91000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.24000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.24000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.97000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.94000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HIS A 8
REMARK 465 HIS A 9
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 ASP A 93 -49.38 63.31
REMARK 500 ASP A 112 -138.36 -60.16
REMARK 500 ALA A 113 -149.48 -94.98
REMARK 500 ILE A 208 -79.71 -116.93
REMARK 500 ASP B1093 -50.79 62.61
REMARK 500 ASP B1094 96.42 -69.43
REMARK 500 ASP B1112 -167.18 -70.94
REMARK 500 ILE B1208 -80.15 -117.60
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 A2007 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 93 OD2 45.0
REMARK 620 3 ASP A 112 OD2 64.0 95.0
REMARK 620 4 POP A2003 O2 155.3 158.6 96.1
REMARK 620 5 POP A2003 O5 100.3 84.3 155.7 93.0
REMARK 620 6 HOH A2101 O 70.3 100.5 91.9 97.5 64.5
REMARK 620 7 HOH A2102 O 120.4 88.8 92.6 72.4 111.7 169.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2008 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1093 OD1
REMARK 620 2 ASP B1093 OD2 48.6
REMARK 620 3 ASP B1112 OD2 61.9 99.0
REMARK 620 4 POP B2004 O5 116.6 78.6 177.4
REMARK 620 5 POP B2004 O2 151.6 155.9 91.6 90.3
REMARK 620 6 HOH B2201 O 70.9 100.0 90.7 90.7 101.5
REMARK 620 7 HOH B2202 O 106.2 83.0 81.0 97.6 77.3 171.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICP A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZP A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICP B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP B 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZP B 2006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2TPS RELATED DB: PDB
REMARK 900 THIAMIN PHOSPHATE SYNTHASE
REMARK 900 RELATED ID: 1G4S RELATED DB: PDB
REMARK 900 RELATED ID: 1G4P RELATED DB: PDB
REMARK 900 RELATED ID: 1G4E RELATED DB: PDB
REMARK 900 RELATED ID: 1G6C RELATED DB: PDB
REMARK 900 RELATED ID: 1G4T RELATED DB: PDB
REMARK 900 RELATED ID: 1G67 RELATED DB: PDB
DBREF 1G69 A 14 235 UNP P39594 THIE_BACSU 1 222
DBREF 1G69 B 1014 1235 UNP P39594 THIE_BACSU 1 222
SEQADV 1G69 HIS A 8 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 HIS A 9 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 HIS A 10 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 GLY A 11 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ILE A 12 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ARG A 13 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ALA A 130 UNP P39594 SER 117 ENGINEERED MUTATION
SEQADV 1G69 HIS B 1008 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 HIS B 1009 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 HIS B 1010 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 GLY B 1011 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ILE B 1012 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ARG B 1013 UNP P39594 CLONING ARTIFACT
SEQADV 1G69 ALA B 1130 UNP P39594 SER 117 ENGINEERED MUTATION
SEQRES 1 A 228 HIS HIS HIS GLY ILE ARG MET THR ARG ILE SER ARG GLU
SEQRES 2 A 228 MET MET LYS GLU LEU LEU SER VAL TYR PHE ILE MET GLY
SEQRES 3 A 228 SER ASN ASN THR LYS ALA ASP PRO VAL THR VAL VAL GLN
SEQRES 4 A 228 LYS ALA LEU LYS GLY GLY ALA THR LEU TYR GLN PHE ARG
SEQRES 5 A 228 GLU LYS GLY GLY ASP ALA LEU THR GLY GLU ALA ARG ILE
SEQRES 6 A 228 LYS PHE ALA GLU LYS ALA GLN ALA ALA CYS ARG GLU ALA
SEQRES 7 A 228 GLY VAL PRO PHE ILE VAL ASN ASP ASP VAL GLU LEU ALA
SEQRES 8 A 228 LEU ASN LEU LYS ALA ASP GLY ILE HIS ILE GLY GLN GLU
SEQRES 9 A 228 ASP ALA ASN ALA LYS GLU VAL ARG ALA ALA ILE GLY ASP
SEQRES 10 A 228 MET ILE LEU GLY VAL ALA ALA HIS THR MET SER GLU VAL
SEQRES 11 A 228 LYS GLN ALA GLU GLU ASP GLY ALA ASP TYR VAL GLY LEU
SEQRES 12 A 228 GLY PRO ILE TYR PRO THR GLU THR LYS LYS ASP THR ARG
SEQRES 13 A 228 ALA VAL GLN GLY VAL SER LEU ILE GLU ALA VAL ARG ARG
SEQRES 14 A 228 GLN GLY ILE SER ILE PRO ILE VAL GLY ILE GLY GLY ILE
SEQRES 15 A 228 THR ILE ASP ASN ALA ALA PRO VAL ILE GLN ALA GLY ALA
SEQRES 16 A 228 ASP GLY VAL SER MET ILE SER ALA ILE SER GLN ALA GLU
SEQRES 17 A 228 ASP PRO GLU SER ALA ALA ARG LYS PHE ARG GLU GLU ILE
SEQRES 18 A 228 GLN THR TYR LYS THR GLY ARG
SEQRES 1 B 228 HIS HIS HIS GLY ILE ARG MET THR ARG ILE SER ARG GLU
SEQRES 2 B 228 MET MET LYS GLU LEU LEU SER VAL TYR PHE ILE MET GLY
SEQRES 3 B 228 SER ASN ASN THR LYS ALA ASP PRO VAL THR VAL VAL GLN
SEQRES 4 B 228 LYS ALA LEU LYS GLY GLY ALA THR LEU TYR GLN PHE ARG
SEQRES 5 B 228 GLU LYS GLY GLY ASP ALA LEU THR GLY GLU ALA ARG ILE
SEQRES 6 B 228 LYS PHE ALA GLU LYS ALA GLN ALA ALA CYS ARG GLU ALA
SEQRES 7 B 228 GLY VAL PRO PHE ILE VAL ASN ASP ASP VAL GLU LEU ALA
SEQRES 8 B 228 LEU ASN LEU LYS ALA ASP GLY ILE HIS ILE GLY GLN GLU
SEQRES 9 B 228 ASP ALA ASN ALA LYS GLU VAL ARG ALA ALA ILE GLY ASP
SEQRES 10 B 228 MET ILE LEU GLY VAL ALA ALA HIS THR MET SER GLU VAL
SEQRES 11 B 228 LYS GLN ALA GLU GLU ASP GLY ALA ASP TYR VAL GLY LEU
SEQRES 12 B 228 GLY PRO ILE TYR PRO THR GLU THR LYS LYS ASP THR ARG
SEQRES 13 B 228 ALA VAL GLN GLY VAL SER LEU ILE GLU ALA VAL ARG ARG
SEQRES 14 B 228 GLN GLY ILE SER ILE PRO ILE VAL GLY ILE GLY GLY ILE
SEQRES 15 B 228 THR ILE ASP ASN ALA ALA PRO VAL ILE GLN ALA GLY ALA
SEQRES 16 B 228 ASP GLY VAL SER MET ILE SER ALA ILE SER GLN ALA GLU
SEQRES 17 B 228 ASP PRO GLU SER ALA ALA ARG LYS PHE ARG GLU GLU ILE
SEQRES 18 B 228 GLN THR TYR LYS THR GLY ARG
HET MG A2007 1
HET ICP A2001 9
HET POP A2003 9
HET TZP A2005 13
HET MG B2008 1
HET ICP B2002 9
HET POP B2004 9
HET TZP B2006 13
HETNAM MG MAGNESIUM ION
HETNAM ICP 2-METHYL-5-METHYLENE-5H-PYRIMIDIN-4-YLIDENEAMINE
HETNAM POP PYROPHOSPHATE 2-
HETNAM TZP 4-METHYL-5-HYDROXYETHYLTHIAZOLE PHOSPHATE
HETSYN ICP 4-IMINO-5-METHIDYL-2-METHYLPYRIMIDINE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ICP 2(C6 H7 N3)
FORMUL 5 POP 2(H2 O7 P2 2-)
FORMUL 6 TZP 2(C6 H10 N O4 P S)
FORMUL 11 HOH *279(H2 O)
HELIX 1 1 SER A 18 LEU A 26 1 9
HELIX 2 2 GLY A 33 THR A 37 5 5
HELIX 3 3 ASP A 40 GLY A 52 1 13
HELIX 4 4 THR A 67 GLY A 86 1 20
HELIX 5 5 ASP A 94 LYS A 102 1 9
HELIX 6 6 ASN A 114 GLY A 123 1 10
HELIX 7 7 THR A 133 GLY A 144 1 12
HELIX 8 8 VAL A 168 GLN A 177 1 10
HELIX 9 9 ALA A 194 ALA A 200 1 7
HELIX 10 10 ILE A 208 GLN A 213 1 6
HELIX 11 11 ASP A 216 GLY A 234 1 19
HELIX 12 12 SER B 1018 LEU B 1026 1 9
HELIX 13 13 GLY B 1033 THR B 1037 5 5
HELIX 14 14 ASP B 1040 GLY B 1052 1 13
HELIX 15 15 THR B 1067 GLY B 1086 1 20
HELIX 16 16 ASP B 1094 LYS B 1102 1 9
HELIX 17 17 ASN B 1114 ILE B 1122 1 9
HELIX 18 18 THR B 1133 GLY B 1144 1 12
HELIX 19 19 VAL B 1168 GLN B 1177 1 10
HELIX 20 20 ALA B 1194 ALA B 1200 1 7
HELIX 21 21 ILE B 1208 GLN B 1213 1 6
HELIX 22 22 ASP B 1216 THR B 1233 1 18
SHEET 1 A 9 VAL A 28 MET A 32 0
SHEET 2 A 9 LEU A 55 PHE A 58 1 O LEU A 55 N PHE A 30
SHEET 3 A 9 PHE A 89 ASN A 92 1 O ILE A 90 N PHE A 58
SHEET 4 A 9 GLY A 105 ILE A 108 1 O GLY A 105 N VAL A 91
SHEET 5 A 9 ILE A 126 ALA A 131 1 O ILE A 126 N ILE A 106
SHEET 6 A 9 TYR A 147 LEU A 150 1 O TYR A 147 N VAL A 129
SHEET 7 A 9 ILE A 183 ILE A 186 1 O VAL A 184 N LEU A 150
SHEET 8 A 9 VAL A 205 MET A 207 1 N SER A 206 O GLY A 185
SHEET 9 A 9 VAL A 28 MET A 32 1 N TYR A 29 O VAL A 205
SHEET 1 B 9 VAL B1028 MET B1032 0
SHEET 2 B 9 LEU B1055 PHE B1058 1 O LEU B1055 N PHE B1030
SHEET 3 B 9 PHE B1089 ASN B1092 1 O ILE B1090 N PHE B1058
SHEET 4 B 9 GLY B1105 ILE B1108 1 O GLY B1105 N VAL B1091
SHEET 5 B 9 ILE B1126 ALA B1131 1 O ILE B1126 N ILE B1106
SHEET 6 B 9 TYR B1147 LEU B1150 1 O TYR B1147 N VAL B1129
SHEET 7 B 9 ILE B1183 ILE B1186 1 O VAL B1184 N LEU B1150
SHEET 8 B 9 GLY B1204 MET B1207 1 O GLY B1204 N GLY B1185
SHEET 9 B 9 VAL B1028 MET B1032 1 N TYR B1029 O VAL B1205
LINK OD1 ASP A 93 MG MG A2007 1555 1555 2.42
LINK OD2 ASP A 93 MG MG A2007 1555 1555 3.09
LINK OD2 ASP A 112 MG MG A2007 1555 1555 2.33
LINK O2 POP A2003 MG MG A2007 1555 1555 2.26
LINK O5 POP A2003 MG MG A2007 1555 1555 2.44
LINK MG MG A2007 O HOH A2101 1555 1555 2.47
LINK MG MG A2007 O HOH A2102 1555 1555 2.29
LINK OD1 ASP B1093 MG MG B2008 1555 1555 2.35
LINK OD2 ASP B1093 MG MG B2008 1555 1555 2.86
LINK OD2 ASP B1112 MG MG B2008 1555 1555 2.53
LINK O5 POP B2004 MG MG B2008 1555 1555 2.00
LINK O2 POP B2004 MG MG B2008 1555 1555 2.65
LINK MG MG B2008 O HOH B2201 1555 1555 2.03
LINK MG MG B2008 O HOH B2202 1555 1555 2.25
CISPEP 1 GLY A 151 PRO A 152 0 0.06
CISPEP 2 GLY B 1151 PRO B 1152 0 -0.07
SITE 1 AC1 6 LYS A 61 ASP A 93 ASP A 112 POP A2003
SITE 2 AC1 6 HOH A2101 HOH A2102
SITE 1 AC2 6 LYS B1061 ASP B1093 ASP B1112 POP B2004
SITE 2 AC2 6 HOH B2201 HOH B2202
SITE 1 AC3 9 TYR A 29 ILE A 31 GLN A 57 HIS A 107
SITE 2 AC3 9 GLY A 149 VAL A 184 ILE A 186 POP A2003
SITE 3 AC3 9 TZP A2005
SITE 1 AC4 14 ARG A 59 LYS A 61 ASN A 92 HIS A 107
SITE 2 AC4 14 GLY A 109 ASP A 112 ALA A 130 LYS A 159
SITE 3 AC4 14 ICP A2001 TZP A2005 MG A2007 HOH A2101
SITE 4 AC4 14 HOH A2102 HOH A2105
SITE 1 AC5 14 ARG A 59 THR A 156 THR A 158 LYS A 159
SITE 2 AC5 14 ILE A 186 GLY A 188 MET A 207 ILE A 208
SITE 3 AC5 14 SER A 209 ICP A2001 POP A2003 HOH A2301
SITE 4 AC5 14 HOH A2302 HOH A2305
SITE 1 AC6 7 TYR B1029 ILE B1031 GLN B1057 HIS B1107
SITE 2 AC6 7 GLY B1149 POP B2004 TZP B2006
SITE 1 AC7 14 ARG B1059 LYS B1061 ASN B1092 ASP B1093
SITE 2 AC7 14 GLY B1109 GLU B1111 ALA B1130 LYS B1159
SITE 3 AC7 14 ICP B2002 MG B2008 HOH B2201 HOH B2202
SITE 4 AC7 14 HOH B2205 HOH B2207
SITE 1 AC8 13 ARG B1059 THR B1156 THR B1158 LYS B1159
SITE 2 AC8 13 ILE B1186 GLY B1188 MET B1207 ILE B1208
SITE 3 AC8 13 SER B1209 ICP B2002 HOH B2401 HOH B2402
SITE 4 AC8 13 HOH B2405
CRYST1 76.480 76.480 139.880 90.00 90.00 90.00 P 43 21 2 16
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 0.013075 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013075 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007149 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
