+Open data
-Basic information
Entry | Database: PDB / ID: 1tey | ||||||
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Title | NMR structure of human histone chaperone, ASF1A | ||||||
Components | ASF1 anti-silencing function 1 homolog A | ||||||
Keywords | CHAPERONE / BETA-SANDWICH / DISTORTED IMMUNOGLOBULIN-LIKE | ||||||
Function / homology | Function and homology information muscle cell differentiation / histone chaperone activity / DNA replication-dependent chromatin assembly / DNA repair-dependent chromatin remodeling / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / replication fork processing / osteoblast differentiation / nucleosome assembly / site of double-strand break / histone binding ...muscle cell differentiation / histone chaperone activity / DNA replication-dependent chromatin assembly / DNA repair-dependent chromatin remodeling / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / 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 | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, cartesian dynamics | ||||||
Authors | Mousson, 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tey.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1tey.ent.gz | 914.3 KB | Display | PDB format |
PDBx/mmJSON format | 1tey.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/1tey ftp://data.pdbj.org/pub/pdb/validation_reports/te/1tey | HTTPS FTP |
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-Related structure data
Similar structure data |
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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: 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
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 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 |
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Sample conditions | Ionic strength: 20 mM / pH: 7.4 / Pressure: ambient / Temperature: 298 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: 600 MHz |
-Processing
NMR software |
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Refinement | Method: 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 representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |