HEADER TRANSFERASE 16-APR-01 1IG3
TITLE MOUSE THIAMIN PYROPHOSPHOKINASE COMPLEXED WITH THIAMIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIAMIN PYROPHOSPHOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.6.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA BARREL, ALPHA/BETA/ALPHA SANDWICH, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.TIMM,J.LIU,L.-J.BAKER,R.A.HARRIS
REVDAT 5 07-FEB-24 1IG3 1 REMARK SEQADV HETSYN
REVDAT 4 24-FEB-09 1IG3 1 VERSN
REVDAT 3 01-APR-03 1IG3 1 JRNL
REVDAT 2 04-JUL-01 1IG3 1 JRNL
REVDAT 1 25-APR-01 1IG3 0
JRNL AUTH D.E.TIMM,J.LIU,L.J.BAKER,R.A.HARRIS
JRNL TITL CRYSTAL STRUCTURE OF THIAMIN PYROPHOSPHOKINASE.
JRNL REF J.MOL.BIOL. V. 310 195 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11419946
JRNL DOI 10.1006/JMBI.2001.4727
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 52413
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2606
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3887
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 413
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.10
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.427
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52413
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, HEPES
REMARK 280 BUFFER, PH 7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.03333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 94.06667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 94.06667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.03333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -362.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 155.53816
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 94.06667
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 44.90000
REMARK 350 BIOMT2 3 0.866025 -0.500000 0.000000 77.76908
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 47.03333
REMARK 350 BIOMT1 4 -0.500000 -0.866025 0.000000 44.90000
REMARK 350 BIOMT2 4 -0.866025 0.500000 0.000000 77.76908
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 47.03333
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -400.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 155.53816
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 94.06667
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 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 HIS B 20
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLN B 164 O2 SO4 B 607 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 719 O HOH B 788 6665 2.10
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 ASP A 66 -122.57 42.67
REMARK 500 GLU A 79 30.53 -140.31
REMARK 500 ASP A 115 103.79 -4.03
REMARK 500 LYS A 178 -112.38 57.53
REMARK 500 ASP B 66 -121.67 38.75
REMARK 500 GLU B 79 28.00 -149.29
REMARK 500 LYS B 178 -114.25 57.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VIB B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VIB A 502
DBREF 1IG3 A 21 263 UNP Q9R0M5 TPK1_MOUSE 1 243
DBREF 1IG3 B 21 263 UNP Q9R0M5 TPK1_MOUSE 1 243
SEQADV 1IG3 MET A 1 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY A 2 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER A 3 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER A 4 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 5 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 6 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 7 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 8 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 9 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 10 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER A 11 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER A 12 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY A 13 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 LEU A 14 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 VAL A 15 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 PRO A 16 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 ARG A 17 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY A 18 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER A 19 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS A 20 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 MET B 1 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY B 2 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER B 3 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER B 4 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 5 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 6 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 7 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 8 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 9 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 10 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER B 11 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER B 12 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY B 13 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 LEU B 14 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 VAL B 15 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 PRO B 16 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 ARG B 17 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 GLY B 18 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 SER B 19 UNP Q9R0M5 EXPRESSION TAG
SEQADV 1IG3 HIS B 20 UNP Q9R0M5 EXPRESSION TAG
SEQRES 1 A 263 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 263 LEU VAL PRO ARG GLY SER HIS MET GLU HIS ALA PHE THR
SEQRES 3 A 263 PRO LEU GLU PRO LEU LEU PRO THR GLY ASN LEU LYS TYR
SEQRES 4 A 263 CYS LEU VAL VAL LEU ASN GLN PRO LEU ASP ALA ARG PHE
SEQRES 5 A 263 ARG HIS LEU TRP LYS LYS ALA LEU LEU ARG ALA CYS ALA
SEQRES 6 A 263 ASP GLY GLY ALA ASN HIS LEU TYR ASP LEU THR GLU GLY
SEQRES 7 A 263 GLU ARG GLU SER PHE LEU PRO GLU PHE VAL SER GLY ASP
SEQRES 8 A 263 PHE ASP SER ILE ARG PRO GLU VAL LYS GLU TYR TYR THR
SEQRES 9 A 263 LYS LYS GLY CYS ASP LEU ILE SER THR PRO ASP GLN ASP
SEQRES 10 A 263 HIS THR ASP PHE THR LYS CYS LEU GLN VAL LEU GLN ARG
SEQRES 11 A 263 LYS ILE GLU GLU LYS GLU LEU GLN VAL ASP VAL ILE VAL
SEQRES 12 A 263 THR LEU GLY GLY LEU GLY GLY ARG PHE ASP GLN ILE MET
SEQRES 13 A 263 ALA SER VAL ASN THR LEU PHE GLN ALA THR HIS ILE THR
SEQRES 14 A 263 PRO VAL PRO ILE ILE ILE ILE GLN LYS ASP SER LEU ILE
SEQRES 15 A 263 TYR LEU LEU GLN PRO GLY LYS HIS ARG LEU HIS VAL ASP
SEQRES 16 A 263 THR GLY MET GLU GLY SER TRP CYS GLY LEU ILE PRO VAL
SEQRES 17 A 263 GLY GLN PRO CYS ASN GLN VAL THR THR THR GLY LEU LYS
SEQRES 18 A 263 TRP ASN LEU THR ASN ASP VAL LEU GLY PHE GLY THR LEU
SEQRES 19 A 263 VAL SER THR SER ASN THR TYR ASP GLY SER GLY LEU VAL
SEQRES 20 A 263 THR VAL GLU THR ASP HIS PRO LEU LEU TRP THR MET ALA
SEQRES 21 A 263 ILE LYS SER
SEQRES 1 B 263 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 263 LEU VAL PRO ARG GLY SER HIS MET GLU HIS ALA PHE THR
SEQRES 3 B 263 PRO LEU GLU PRO LEU LEU PRO THR GLY ASN LEU LYS TYR
SEQRES 4 B 263 CYS LEU VAL VAL LEU ASN GLN PRO LEU ASP ALA ARG PHE
SEQRES 5 B 263 ARG HIS LEU TRP LYS LYS ALA LEU LEU ARG ALA CYS ALA
SEQRES 6 B 263 ASP GLY GLY ALA ASN HIS LEU TYR ASP LEU THR GLU GLY
SEQRES 7 B 263 GLU ARG GLU SER PHE LEU PRO GLU PHE VAL SER GLY ASP
SEQRES 8 B 263 PHE ASP SER ILE ARG PRO GLU VAL LYS GLU TYR TYR THR
SEQRES 9 B 263 LYS LYS GLY CYS ASP LEU ILE SER THR PRO ASP GLN ASP
SEQRES 10 B 263 HIS THR ASP PHE THR LYS CYS LEU GLN VAL LEU GLN ARG
SEQRES 11 B 263 LYS ILE GLU GLU LYS GLU LEU GLN VAL ASP VAL ILE VAL
SEQRES 12 B 263 THR LEU GLY GLY LEU GLY GLY ARG PHE ASP GLN ILE MET
SEQRES 13 B 263 ALA SER VAL ASN THR LEU PHE GLN ALA THR HIS ILE THR
SEQRES 14 B 263 PRO VAL PRO ILE ILE ILE ILE GLN LYS ASP SER LEU ILE
SEQRES 15 B 263 TYR LEU LEU GLN PRO GLY LYS HIS ARG LEU HIS VAL ASP
SEQRES 16 B 263 THR GLY MET GLU GLY SER TRP CYS GLY LEU ILE PRO VAL
SEQRES 17 B 263 GLY GLN PRO CYS ASN GLN VAL THR THR THR GLY LEU LYS
SEQRES 18 B 263 TRP ASN LEU THR ASN ASP VAL LEU GLY PHE GLY THR LEU
SEQRES 19 B 263 VAL SER THR SER ASN THR TYR ASP GLY SER GLY LEU VAL
SEQRES 20 B 263 THR VAL GLU THR ASP HIS PRO LEU LEU TRP THR MET ALA
SEQRES 21 B 263 ILE LYS SER
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 612 5
HET SO4 A 613 5
HET SO4 A 616 5
HET VIB A 502 18
HET SO4 B 606 5
HET SO4 B 607 5
HET SO4 B 608 5
HET SO4 B 611 5
HET SO4 B 615 5
HET VIB B 501 18
HETNAM SO4 SULFATE ION
HETNAM VIB 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-
HETNAM 2 VIB ETHYL)-4-METHYL-THIAZOL-3-IUM
HETSYN VIB THIAMIN; VITAMIN B1
FORMUL 3 SO4 14(O4 S 2-)
FORMUL 12 VIB 2(C12 H17 N4 O S 1+)
FORMUL 19 HOH *413(H2 O)
HELIX 1 1 LEU A 28 LEU A 32 5 5
HELIX 2 2 ARG A 51 ALA A 59 1 9
HELIX 3 3 GLY A 67 LEU A 75 1 9
HELIX 4 4 GLU A 79 PHE A 83 5 5
HELIX 5 5 ARG A 96 LYS A 106 1 11
HELIX 6 6 THR A 119 LYS A 135 1 17
HELIX 7 7 ARG A 151 ALA A 165 1 15
HELIX 8 8 THR A 166 ILE A 168 5 3
HELIX 9 9 LEU B 28 LEU B 32 5 5
HELIX 10 10 ARG B 51 ALA B 59 1 9
HELIX 11 11 GLY B 67 THR B 76 1 10
HELIX 12 12 GLU B 79 PHE B 83 5 5
HELIX 13 13 ASP B 91 ILE B 95 5 5
HELIX 14 14 ARG B 96 LYS B 106 1 11
HELIX 15 15 THR B 119 LYS B 135 1 17
HELIX 16 16 ARG B 151 THR B 169 1 19
SHEET 1 A 5 HIS A 23 PHE A 25 0
SHEET 2 A 5 GLY A 188 HIS A 193 1 O LYS A 189 N HIS A 23
SHEET 3 A 5 LEU A 246 THR A 251 -1 O VAL A 247 N LEU A 192
SHEET 4 A 5 CYS A 212 THR A 218 -1 O THR A 216 N GLU A 250
SHEET 5 A 5 ASP A 227 LEU A 229 -1 N ASP A 227 O VAL A 215
SHEET 1 B10 ASP A 109 SER A 112 0
SHEET 2 B10 PHE A 87 GLY A 90 1 O VAL A 88 N ILE A 111
SHEET 3 B10 LEU A 61 ALA A 65 1 O ARG A 62 N PHE A 87
SHEET 4 B10 TYR A 39 VAL A 43 1 O TYR A 39 N LEU A 61
SHEET 5 B10 VAL A 141 LEU A 145 1 O VAL A 141 N CYS A 40
SHEET 6 B10 ILE A 173 GLN A 177 1 O ILE A 174 N THR A 144
SHEET 7 B10 SER A 180 LEU A 185 -1 N SER A 180 O GLN A 177
SHEET 8 B10 LEU A 255 ILE A 261 -1 O LEU A 255 N LEU A 185
SHEET 9 B10 GLU A 199 ILE A 206 -1 N GLY A 200 O ALA A 260
SHEET 10 B10 SER A 236 ASN A 239 -1 N SER A 236 O LEU A 205
SHEET 1 C 5 GLU B 22 PHE B 25 0
SHEET 2 C 5 GLY B 188 HIS B 193 1 O LYS B 189 N HIS B 23
SHEET 3 C 5 LEU B 246 THR B 251 -1 O VAL B 247 N LEU B 192
SHEET 4 C 5 CYS B 212 THR B 218 -1 O THR B 216 N GLU B 250
SHEET 5 C 5 ASP B 227 LEU B 229 -1 N ASP B 227 O VAL B 215
SHEET 1 D10 ASP B 109 SER B 112 0
SHEET 2 D10 PHE B 87 GLY B 90 1 N VAL B 88 O ASP B 109
SHEET 3 D10 LEU B 61 ALA B 65 1 O ARG B 62 N PHE B 87
SHEET 4 D10 TYR B 39 VAL B 43 1 O TYR B 39 N LEU B 61
SHEET 5 D10 VAL B 141 LEU B 145 1 O VAL B 141 N CYS B 40
SHEET 6 D10 ILE B 173 GLN B 177 1 O ILE B 174 N THR B 144
SHEET 7 D10 SER B 180 LEU B 185 -1 N SER B 180 O GLN B 177
SHEET 8 D10 LEU B 255 ILE B 261 -1 O LEU B 255 N LEU B 185
SHEET 9 D10 GLU B 199 ILE B 206 -1 N GLY B 200 O ALA B 260
SHEET 10 D10 SER B 236 ASN B 239 -1 O SER B 236 N LEU B 205
SITE 1 AC1 4 GLY A 78 GLU A 79 ARG A 80 HOH A 691
SITE 1 AC2 3 LYS A 105 LYS A 106 HOH A 753
SITE 1 AC3 7 ASP A 117 HIS A 118 THR A 119 THR A 122
SITE 2 AC3 7 ASN A 160 GLN A 164 HOH A 650
SITE 1 AC4 3 ASN A 45 HOH A 668 HOH A 745
SITE 1 AC5 6 GLY B 78 GLU B 79 ARG B 80 TYR B 102
SITE 2 AC5 6 HOH B 761 HOH B 809
SITE 1 AC6 9 HIS B 118 THR B 119 THR B 122 ASN B 160
SITE 2 AC6 9 THR B 161 GLN B 164 HOH B 617 HOH B 698
SITE 3 AC6 9 HOH B 786
SITE 1 AC7 4 ASN B 45 HOH B 635 HOH B 677 HOH B 708
SITE 1 AC8 3 SER A 238 VIB A 502 ARG B 151
SITE 1 AC9 4 ARG A 151 HOH A 752 SER B 238 VIB B 501
SITE 1 BC1 5 GLY B 200 SER B 201 LYS B 262 SER B 263
SITE 2 BC1 5 HOH B 644
SITE 1 BC2 5 GLY A 200 SER A 201 LYS A 262 SER A 263
SITE 2 BC2 5 HOH A 623
SITE 1 BC3 7 GLN A 46 GLY A 150 HOH A 648 HOH A 713
SITE 2 BC3 7 HOH A 715 HOH A 729 HOH A 772
SITE 1 BC4 4 ALA B 24 ARG B 191 HIS B 193 HOH B 781
SITE 1 BC5 8 ASN A 213 HIS A 253 HOH A 676 HOH A 747
SITE 2 BC5 8 HOH A 756 PRO B 33 GLY B 35 LYS B 58
SITE 1 BC6 9 GLN A 116 ASP A 117 SO4 A 610 TRP B 222
SITE 2 BC6 9 SER B 236 THR B 237 SER B 238 ASN B 239
SITE 3 BC6 9 HOH B 616
SITE 1 BC7 12 TRP A 222 SER A 236 THR A 237 SER A 238
SITE 2 BC7 12 ASN A 239 SO4 A 609 HOH A 631 HOH A 644
SITE 3 BC7 12 GLN B 116 ASP B 117 HIS B 118 HOH B 786
CRYST1 89.800 89.800 141.100 90.00 90.00 120.00 P 31 2 1 12
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 0.011136 0.006429 0.000000 0.00000
SCALE2 0.000000 0.012859 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
