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Open data
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Basic information
Entry | Database: PDB / ID: 1kkx | ||||||
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Title | Solution structure of the DNA-binding domain of ADR6 | ||||||
![]() | Transcription regulatory protein ADR6 | ||||||
![]() | DNA BINDING PROTEIN / ARID / ADR6 / DNA-binding domain | ||||||
Function / homology | ![]() carbon catabolite activation of transcription from RNA polymerase II promoter / positive regulation of mating type switching / HDACs deacetylate histones / SWI/SNF complex / DNA-templated DNA replication / RNA polymerase II-specific DNA-binding transcription factor binding / transcription cis-regulatory region binding / chromatin remodeling / chromatin / regulation of transcription by RNA polymerase II ...carbon catabolite activation of transcription from RNA polymerase II promoter / positive regulation of mating type switching / HDACs deacetylate histones / SWI/SNF complex / DNA-templated DNA replication / RNA polymerase II-specific DNA-binding transcription factor binding / transcription cis-regulatory region binding / chromatin remodeling / chromatin / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Tu, X. / Wu, J. / Xu, Y. / Shi, Y. | ||||||
![]() | ![]() Title: 1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain. Authors: Tu, X. / Wu, J. / Xu, Y. / Shi, Y. #1: ![]() Title: 1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain Authors: Tu, X. / Wu, J. / Xu, Y. / Shi, Y. #2: ![]() Title: 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 346.5 KB | Display | ![]() |
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PDB format | ![]() | 283.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346.7 KB | Display | ![]() |
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Full document | ![]() | 492.9 KB | Display | |
Data in XML | ![]() | 44 KB | Display | |
Data in CIF | ![]() | 57.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kn5C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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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: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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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 |
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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 |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
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Processing
NMR software | Name: CNS / Version: v 1.0 / Developer: A.T. Brunger / Classification: refinement |
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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 |