+
Open data
-
Basic information
| Entry | Database: PDB / ID: 1kkx | ||||||
|---|---|---|---|---|---|---|---|
| Title | Solution structure of the DNA-binding domain of ADR6 | ||||||
Components | Transcription regulatory protein ADR6 | ||||||
Keywords | DNA BINDING PROTEIN / ARID / ADR6 / DNA-binding domain | ||||||
| Function / homology | Function and homology informationpositive regulation of mating type switching / HDACs deacetylate histones / SWI/SNF complex / cellular response to amino acid starvation / DNA-templated DNA replication / RNA polymerase II-specific DNA-binding transcription factor binding / transcription cis-regulatory region binding / chromatin remodeling / regulation of transcription by RNA polymerase II / chromatin ...positive regulation of mating type switching / HDACs deacetylate histones / SWI/SNF complex / cellular response to amino acid starvation / DNA-templated DNA replication / RNA polymerase II-specific DNA-binding transcription factor binding / transcription cis-regulatory region binding / chromatin remodeling / regulation of transcription by RNA polymerase II / chromatin / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tu, X. / Wu, J. / Xu, Y. / Shi, Y. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2001Title: 1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain. Authors: Tu, X. / Wu, J. / Xu, Y. / Shi, Y. #1: Journal: J.BIOMOL.NMR / Year: 2001Title: 1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain Authors: Tu, X. / Wu, J. / Xu, Y. / Shi, Y. #2: Journal: BIOCHIM.BIOPHYS.ACTA / Year: 2000Title: Expression and purification of a recombinant DNA-binding domain of ADR6 protein from Escherichia coli and its secondary structure characterization Authors: Tu, X. / Xiao, Y. / Zeng, W. / Shi, Y. | ||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 1kkx.cif.gz | 346.5 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb1kkx.ent.gz | 283.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1kkx.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kk/1kkx ftp://data.pdbj.org/pub/pdb/validation_reports/kk/1kkx | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 1kn5C C: citing same article ( |
|---|---|
| Similar structure data | |
| Other databases |
|
-
Links
-
Assembly
| Deposited unit | ![]()
| |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| 1 |
| |||||||||
| NMR ensembles |
|
-
Components
| #1: Protein | Mass: 14566.800 Da / Num. of mol.: 1 / Fragment: ARID domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: adr6 / Plasmid: pREP-4 / Species (production host): Escherichia coli / Production host: ![]() |
|---|
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| NMR experiment |
|
-
Sample preparation
| Details | Contents: 1mM ADR6 ARID domain U-15N, U-13C, 50mM phosphate buffer at pH4.9, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
|---|---|
| Sample conditions | Ionic strength: 50mM phosphate buffer / pH: 4.9 / Pressure: ambient / Temperature: 300 K |
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
|---|---|
| Radiation wavelength | Relative weight: 1 |
| NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
-
Processing
| NMR software | Name: CNS / Version: v 1.0 / Developer: A.T. Brunger / Classification: refinement |
|---|---|
| Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
| NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |
Movie
Controller
About Yorodumi






Citation










PDBj

