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Yorodumi- PDB-1thu: THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN -
+Open data
-Basic information
Entry | Database: PDB / ID: 1thu | ||||||
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Title | THE STRUCTURES OF THREE CRYSTAL FORMS OF THE SWEET PROTEIN THAUMATIN | ||||||
Components | THAUMATIN ISOFORM B | ||||||
Keywords | SWEET TASTING PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thaumatococcus daniellii (katemfe) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Ko, T.-P. / Day, J. / Greenwood, A. / McPherson, A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1994 Title: Structures of three crystal forms of the sweet protein thaumatin. Authors: Ko, T.P. / Day, J. / Greenwood, A. / McPherson, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1thu.cif.gz | 45.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1thu.ent.gz | 36.4 KB | Display | PDB format |
PDBx/mmJSON format | 1thu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/th/1thu ftp://data.pdbj.org/pub/pdb/validation_reports/th/1thu | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 84 |
-Components
#1: Protein | Mass: 22243.119 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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Sequence details | CROSS REFERENCE TO SEQUENCE DATABASE SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME THM1_THADA SEQUENCE ...CROSS REFERENCE TO SEQUENCE DATABASE SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME THM1_THADA SEQUENCE ADVISORY NOTICE DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.34 % |
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Crystal grow | *PLUS Method: vapor diffusion |
Components of the solutions | *PLUS Common name: PEG3350 |
-Data collection
Reflection | *PLUS Highest resolution: 2.61 Å / Num. obs: 8350 / % possible obs: 70.8 % / Num. measured all: 27736 / Rmerge(I) obs: 0.1062 |
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Reflection shell | *PLUS Highest resolution: 2.61 Å / Lowest resolution: 2.81 Å / % possible obs: 38.1 % / Num. unique obs: 892 / Num. measured obs: 1854 / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 4.84 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.6→8 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.184 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.76 Å2 | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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