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Yorodumi- PDB-1ghc: HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULA... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1ghc | ||||||
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| Title | HOMO-AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5 | ||||||
Components | GH1 | ||||||
Keywords | CHROMOSOMAL PROTEIN | ||||||
| Function / homology | Function and homology informationnegative regulation of DNA recombination / chromosome condensation / nucleosomal DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly / double-stranded DNA binding / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Cerf, C. / Lippens, G. / Ramakrishnan, V. / Muyldermans, S. / Segers, A. / Wyns, L. / Wodak, S.J. / Hallenga, K. | ||||||
Citation | Journal: Biochemistry / Year: 1994Title: Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5. Authors: Cerf, C. / Lippens, G. / Ramakrishnan, V. / Muyldermans, S. / Segers, A. / Wyns, L. / Wodak, S.J. / Hallenga, K. #1: Journal: Biochemistry / Year: 1993Title: Homo-and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Sequential Assignment and Secondary Structure Authors: Cerf, C. / Lippens, G. / Muyldermans, S. / Segers, A. / Ramakrishnan, V. / Wodak, S.J. / Hallenga, K. / Wyns, L. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1ghc.cif.gz | 310.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1ghc.ent.gz | 256.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1ghc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1ghc_validation.pdf.gz | 341.3 KB | Display | wwPDB validaton report |
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| Full document | 1ghc_full_validation.pdf.gz | 552.3 KB | Display | |
| Data in XML | 1ghc_validation.xml.gz | 49.1 KB | Display | |
| Data in CIF | 1ghc_validation.cif.gz | 66 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gh/1ghc ftp://data.pdbj.org/pub/pdb/validation_reports/gh/1ghc | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein | Mass: 7691.005 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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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
| Software |
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| NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
| NMR ensemble | Conformers submitted total number: 14 |
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