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- PDB-1tey: NMR structure of human histone chaperone, ASF1A -

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Basic information

Entry
Database: PDB / ID: 1tey
TitleNMR structure of human histone chaperone, ASF1A
ComponentsASF1 anti-silencing function 1 homolog A
KeywordsCHAPERONE / BETA-SANDWICH / DISTORTED IMMUNOGLOBULIN-LIKE
Function / homology
Function and homology information


histone chaperone activity / DNA replication-dependent chromatin assembly / muscle cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / replication fork processing / osteoblast differentiation / nucleosome assembly / site of double-strand break / histone binding ...histone chaperone activity / DNA replication-dependent chromatin assembly / muscle cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / replication fork processing / osteoblast differentiation / nucleosome assembly / site of double-strand break / histone binding / DNA repair / chromatin binding / chromatin / protein-containing complex / nucleoplasm / nucleus
Similarity search - Function
Histone chaperone ASF1-like / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Histone chaperone ASF1A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics, cartesian dynamics
AuthorsMousson, F. / Lautrette, A. / Thuret, J.Y. / Agez, M. / Amigues, B. / Courbeyrette, R. / Neumann, J.M. / Guerois, R. / Mann, C. / Ochsenbein, F.
Citation
Journal: Proc.Natl.Acad.Sci.Usa / Year: 2005
Title: Structural basis for the interaction of Asf1 with histone H3 and its functional implications.
Authors: Mousson, F. / Lautrette, A. / Thuret, J.Y. / Agez, M. / Courbeyrette, R. / Amigues, B. / Becker, E. / Neumann, J.M. / Guerois, R. / Mann, C. / Ochsenbein, F.
#1: Journal: To be Published
Title: 1H, 13C and 15N resonance assignments of the conserved core of hAsf1A
Authors: Mousson, F. / Couprie, J. / Thuret, J.Y. / Neumann, J.M. / Mann, C. / Ochsenbein, F.
History
DepositionMay 26, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 12, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

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Assembly

Deposited unit
A: ASF1 anti-silencing function 1 homolog A


Theoretical massNumber of molelcules
Total (without water)17,9281
Polymers17,9281
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20all calculated structures submitted
RepresentativeModel #1closest to the average

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Components

#1: Protein ASF1 anti-silencing function 1 homolog A


Mass: 17927.998 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN (residues 1-156)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ASF1A / Plasmid: PETM30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 GOLD DE3 / References: UniProt: Q9Y294

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY
131HNHA
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

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Sample preparation

DetailsContents: 1mM Asf1A U-15N,13C; 20mM tris-D11; 1mM EDTA; 0.1mM DSS; 0.1 mM NaN3; 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 20 mM / pH: 7.4 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.1Brukercollection
XwinNMR3.1Brukerprocessing
Sparky3.106T. D. Goddard and D. G. Knellerdata analysis
ARIA1.1J.Linge, S.O'Donoghue, M.Nilgesrefinement
RefinementMethod: simulated annealing, torsion angle dynamics, cartesian dynamics
Software ordinal: 1
Details: the structures are based on a total of 4489 restraints, 4257 are NOE-derived distance constraints, 170 dihedral angle restraints from J coupling measurements and Talos,62 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 20 / Conformers submitted total number: 20

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