+Open data
-Basic information
Entry | Database: PDB / ID: 1dfe | ||||||
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Title | NMR STRUCTURE OF RIBOSOMAL PROTEIN L36 FROM THERMUS THERMOPHILUS | ||||||
Components | L36 RIBOSOMAL PROTEIN | ||||||
Keywords | RIBOSOME / ANTI-PARALLEL BETA SHEET / ZINC BINDING | ||||||
Function / homology | Function and homology information ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | SOLUTION NMR | ||||||
Model type details | minimized average | ||||||
Authors | Hard, T. / Rak, A. / Allard, P. / Kloo, L. / Garber, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: The solution structure of ribosomal protein L36 from Thermus thermophilus reveals a zinc-ribbon-like fold. Authors: Hard, T. / Rak, A. / Allard, P. / Kloo, L. / Garber, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dfe.cif.gz | 23.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dfe.ent.gz | 14.8 KB | Display | PDB format |
PDBx/mmJSON format | 1dfe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dfe_validation.pdf.gz | 287.9 KB | Display | wwPDB validaton report |
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Full document | 1dfe_full_validation.pdf.gz | 287.7 KB | Display | |
Data in XML | 1dfe_validation.xml.gz | 2.3 KB | Display | |
Data in CIF | 1dfe_validation.cif.gz | 2.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/df/1dfe ftp://data.pdbj.org/pub/pdb/validation_reports/df/1dfe | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4435.411 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P80256 |
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#2: Chemical | ChemComp-ZN / |
-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 representative | Selection criteria: minimized average structure |
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NMR ensemble | Conformers submitted total number: 1 |