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- PDB-1ust: YEAST HISTONE H1 GLOBULAR DOMAIN I, HHO1P GI, SOLUTION NMR STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1ust
TitleYEAST HISTONE H1 GLOBULAR DOMAIN I, HHO1P GI, SOLUTION NMR STRUCTURES
ComponentsHISTONE H1
KeywordsDNA BINDING PROTEIN / LINKER HISTONE / DNA BINDING DOMAIN / WINGED HELIX FOLD
Function / homology
Function and homology information


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 / chromatin / regulation of DNA-templated transcription / DNA binding / nucleus
Similarity search - Function
Linker histone H1/H5 / linker histone H1 and H5 family / Linker histone H1/H5, domain H15 / Linker histone H1/H5 globular (H15) domain profile. / Domain in histone families 1 and 5 / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodSOLUTION NMR / DISTANCE GEOMETRY, BOND ANGLE GEOMETRY
AuthorsAli, T. / Coles, P. / Stevens, T.J. / Stott, K. / Thomas, J.O.
CitationJournal: J.Mol.Biol. / Year: 2004
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
DepositionNov 30, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 1, 2004Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 15, 2020Group: Other / Category: pdbx_database_status / Item: _pdbx_database_status.status_code_cs
Revision 1.4May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HISTONE H1


Theoretical massNumber of molelcules
Total (without water)10,2781
Polymers10,2781
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100MINIMUM ENERGY
RepresentativeModel #1

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Components

#1: Protein HISTONE H1 /


Mass: 10277.848 Da / Num. of mol.: 1 / Fragment: GLOBULAR DOMAIN I, RESIDUES 38-130
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Plasmid: PET17B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P53551
Compound detailsCOULD ACT AS AN H1-TYPE LINKER HISTONE. HAS BEEN SHOWN TO BIND DNA.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 7.0 / Pressure: 1 atm / Temperature: 288 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
ARIAstructure solution
CNSstructure solution
RefinementMethod: DISTANCE GEOMETRY, BOND ANGLE GEOMETRY / Software ordinal: 1
NMR ensembleConformer selection criteria: MINIMUM ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 10

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