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- PDB-1yqa: Engineering the structural stability and functional properties of... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yqa | ||||||
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Title | Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p | ||||||
![]() | Histone H1 | ||||||
![]() | DNA BINDING PROTEIN / Winged-helix | ||||||
Function / homology | ![]() negative regulation of DNA recombination / supercoiled DNA binding / chromosome condensation / phosphate ion binding / nucleosomal DNA binding / protein-DNA complex / chromatin DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly ...negative regulation of DNA recombination / supercoiled DNA binding / chromosome condensation / phosphate ion binding / nucleosomal DNA binding / protein-DNA complex / chromatin DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly / double-stranded DNA binding / nucleic acid binding / molecular adaptor activity / regulation of DNA-templated transcription / chromatin / DNA binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / see journal citation | ||||||
![]() | Sanderson, A. / Stott, K. / Stevens, T.J. / Thomas, J.O. | ||||||
![]() | ![]() Title: Engineering the Structural Stability and Functional Properties of the GI Domain into the Intrinsically Unfolded GII Domain of the Yeast Linker Histone Hho1p. Authors: Sanderson, A. / Stott, K. / Stevens, T.J. / Thomas, J.O. #1: ![]() Title: Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p Authors: Ali, T. / Coles, P. / Stevens, T.J. / Stott, K. / Thomas, J.O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 249.1 KB | Display | ![]() |
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PDB format | ![]() | 206.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 338.7 KB | Display | ![]() |
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Full document | ![]() | 397.4 KB | Display | |
Data in XML | ![]() | 15.7 KB | Display | |
Data in CIF | ![]() | 25.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9553.217 Da / Num. of mol.: 1 / Fragment: GII loop mutant (GII-L), Residues 171-258 Mutation: F210Y, S211P, delta-S212, K213I, L214V, K215G, T216S, S217A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: HHO1 / Plasmid: pET17b / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1mM GII-L U-15N,13C; 100mM phosphate buffer; 1mM EDTA; 1-2mM DTT Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 100mM phosphate / pH: 7.0 / Pressure: 1 atm / Temperature: 288 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: see journal citation / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |