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- PDB-1thi: CRYSTAL STRUCTURES OF TWO INTENSELY SWEET PROTEINS -

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Basic information

Entry
Database: PDB / ID: 1thi
TitleCRYSTAL STRUCTURES OF TWO INTENSELY SWEET PROTEINS
ComponentsTHAUMATIN I
KeywordsSWEET TASTING PROTEIN
Function / homologyThaumatin, conserved site / Thaumatin family signature. / Thaumatin family / Thaumatin family / Thaumatin family profile. / Thaumatin family / Osmotin/thaumatin-like superfamily / cytoplasmic vesicle / Thaumatin I
Function and homology information
Biological speciesThaumatococcus daniellii (katemfe)
MethodX-RAY DIFFRACTION / Resolution: 3.2 Å
AuthorsKim, S.-H.
Citation
Journal: Trends Biochem.Sci. / Year: 1988
Title: Crystal structures of two intensely sweet proteins.
Authors: Kim, S.H. / de Vos, A. / Ogata, C.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1985
Title: Three-Dimensional Structure of Thaumatin I, an Intensely Sweet Protein
Authors: Devos, A.M. / Hatada, M. / Van Derwel, H. / Krabbendam, H. / Peerdeman, A.F. / Kim, S.-H.
#2: Journal: FEBS Lett. / Year: 1975
Title: Crystallization and Crystal Data of Thaumatin I, a Sweet-Tasting Protein from Thaumatococcus Daniellii Benth
Authors: Van Derwel, H. / Vansoest, T.C. / Royers, E.C.
#3: Journal: Eur.J.Biochem. / Year: 1979
Title: The Complete Amino-Acid Sequence of the Sweet Protein Thaumatin I
Authors: Iyengar, R.B. / Smits, P. / Van Derouderaa, F. / Van Derwel, H. / Van Brouwershaven, J. / Ravestein, P. / Richters, G. / Vanwassenaar, P.D.
History
DepositionMay 24, 1989Processing site: BNL
Revision 1.0Oct 15, 1989Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: THAUMATIN I


Theoretical massNumber of molelcules
Total (without water)22,2271
Polymers22,2271
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)74.420, 53.320, 52.250
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein THAUMATIN I / Coordinate model: Cα atoms only


Mass: 22227.059 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thaumatococcus daniellii (katemfe) / References: UniProt: P02883

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.33 Å3/Da / Density % sol: 47.23 %
Crystal grow
*PLUS
pH: 7 / Method: vapor-phase equilibrium
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 mg/mlprotein 11
250 mMHEPES11
32.0-2.5 Mammonium sulfate12

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Processing

RefinementHighest resolution: 3.2 Å
Refinement stepCycle: LAST / Highest resolution: 3.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms207 0 0 0 207
Refinement
*PLUS
Highest resolution: 3.2 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS

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