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Yorodumi- PDB-6hq1: Solution structure of the globular domain from human histone H1.0 -
+Open data
-Basic information
Entry | Database: PDB / ID: 6hq1 | ||||||
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Title | Solution structure of the globular domain from human histone H1.0 | ||||||
Components | Histone H1.0 | ||||||
Keywords | DNA BINDING PROTEIN / alpha-helical / nucleosome assembly | ||||||
Function / homology | Function and homology information negative regulation of DNA recombination / positive regulation of transcription regulatory region DNA binding / Apoptosis induced DNA fragmentation / chromosome condensation / nucleosomal DNA binding / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / minor groove of adenine-thymine-rich DNA binding / heterochromatin formation / transcription repressor complex / euchromatin ...negative regulation of DNA recombination / positive regulation of transcription regulatory region DNA binding / Apoptosis induced DNA fragmentation / chromosome condensation / nucleosomal DNA binding / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / minor groove of adenine-thymine-rich DNA binding / heterochromatin formation / transcription repressor complex / euchromatin / chromatin DNA binding / nucleosome assembly / structural constituent of chromatin / nucleosome / actin cytoskeleton / double-stranded DNA binding / nuclear body / chromatin / Golgi apparatus / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Martinsen, J.H. / Bugge, K. / Kragelund, B.B. | ||||||
Funding support | Denmark, 1items
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Citation | Journal: To Be Published Title: Micromolar affinity association of an IDP and a folded protein without the involvement of persistent binding sites Authors: Bugge, K. / Martinsen, J.H. / Fernandes, C.B. / Borgia, A. / Schuler, B. / Best, R. / Kragelund, B.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hq1.cif.gz | 455.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hq1.ent.gz | 382.8 KB | Display | PDB format |
PDBx/mmJSON format | 6hq1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hq/6hq1 ftp://data.pdbj.org/pub/pdb/validation_reports/hq/6hq1 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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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: 8163.378 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: H1F0, H1FV / Production host: Escherichia coli (E. coli) / References: UniProt: P07305 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 165 mM / Label: 13C15N / pH: 7.4 / Pressure: 1 atm / Temperature: 283 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 2 | ||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |