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Yorodumi- PDB-1trl: NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THER... -
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-Basic information
Entry | Database: PDB / ID: 1trl | ||||||
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Title | NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS HAVING THE NATIVE STRUCTURE | ||||||
Components | THERMOLYSIN FRAGMENT 255 - 316 | ||||||
Keywords | HYDROLASE (METALLOPROTEASE) | ||||||
Function / homology | Function and homology information thermolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus thermoproteolyticus (bacteria) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Rico, M. / Jimenez, M.A. / Gonzalez, C. / De Filippis, V. / Fontana, A. | ||||||
Citation | Journal: Biochemistry / Year: 1994 Title: NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure. Authors: Rico, M. / Jimenez, M.A. / Gonzalez, C. / De Filippis, V. / Fontana, A. #1: Journal: Eur.J.Biochem. / Year: 1993 Title: Cd and H-NMR Studies on the Conformational Properties of Peptide Fragments from the C-Terminal Domain of Thermolysin Authors: Jimenez, M.A. / Bruix, M. / Gonzalez, C. / Blanco, F.J. / Nieto, J.L. / Herranz, J. / Rico, M. #2: Journal: J.Mol.Biol. / Year: 1985 Title: Folding of Thermolysin Fragments: Identification of the Minimum Size of a Carboxyl-Terminal Fragment that Can Fold Into a Stable Native-Like Structure Authors: Dalzoppo, D. / Vita, C. / Fontana, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1trl.cif.gz | 168.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1trl.ent.gz | 141 KB | Display | PDB format |
PDBx/mmJSON format | 1trl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tr/1trl ftp://data.pdbj.org/pub/pdb/validation_reports/tr/1trl | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6631.481 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus thermoproteolyticus (bacteria) References: UniProt: P00800, thermolysin |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
NMR software | Name: GROMOS / Developer: VAN GUNSTEREN,BERENDSEN / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 8 |