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- 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 | ||||||
![]() | GH1 | ||||||
![]() | CHROMOSOMAL PROTEIN | ||||||
Function / homology | ![]() : / : / negative regulation of DNA recombination / chromosome condensation / nucleosomal DNA binding / nucleosome / nucleosome assembly / double-stranded DNA binding / regulation of DNA-templated transcription / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Cerf, C. / Lippens, G. / Ramakrishnan, V. / Muyldermans, S. / Segers, A. / Wyns, L. / Wodak, S.J. / Hallenga, K. | ||||||
![]() | ![]() 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. Authors: Cerf, C. / Lippens, G. / Ramakrishnan, V. / Muyldermans, S. / Segers, A. / Wyns, L. / Wodak, S.J. / Hallenga, K. #1: ![]() Title: 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: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 310.8 KB | Display | ![]() |
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PDB format | ![]() | 256.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 341.3 KB | Display | ![]() |
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Full document | ![]() | 552.3 KB | Display | |
Data in XML | ![]() | 49.1 KB | Display | |
Data in CIF | ![]() | 66 KB | Display | |
Arichive directory | ![]() ![]() | 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
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 14 |