+
Open data
-
Basic information
Entry | Database: PDB / ID: 1tey | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of human histone chaperone, ASF1A | ||||||
![]() | ASF1 anti-silencing function 1 homolog A | ||||||
![]() | CHAPERONE / BETA-SANDWICH / DISTORTED IMMUNOGLOBULIN-LIKE | ||||||
Function / homology | ![]() histone chaperone activity / muscle cell differentiation / 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 ...histone chaperone activity / muscle cell differentiation / 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 | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, cartesian dynamics | ||||||
![]() | Mousson, F. / Lautrette, A. / Thuret, J.Y. / Agez, M. / Amigues, B. / Courbeyrette, R. / Neumann, J.M. / Guerois, R. / Mann, C. / Ochsenbein, F. | ||||||
![]() | ![]() 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: ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 887.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 481.9 KB | Display | |
Data in XML | ![]() | 63.8 KB | Display | |
Data in CIF | ![]() | 84.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
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.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||
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 |
---|---|
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 |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |