+Open data
-Basic information
Entry | Database: PDB / ID: 1kkx | ||||||
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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 information carbon catabolite activation of transcription from RNA polymerase II promoter / 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 / chromatin ...carbon catabolite activation of transcription from RNA polymerase II promoter / 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 / 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 | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tu, X. / Wu, J. / Xu, Y. / Shi, Y. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2001 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: Journal: J.BIOMOL.NMR / Year: 2001 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: Journal: BIOCHIM.BIOPHYS.ACTA / Year: 2000 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kkx.cif.gz | 346.5 KB | Display | PDBx/mmCIF format |
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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
Summary document | 1kkx_validation.pdf.gz | 346.7 KB | Display | wwPDB validaton report |
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Full document | 1kkx_full_validation.pdf.gz | 492.9 KB | Display | |
Data in XML | 1kkx_validation.xml.gz | 44 KB | Display | |
Data in CIF | 1kkx_validation.cif.gz | 57.7 KB | Display | |
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 (ref.) |
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Similar structure data | |
Other databases |
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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: 14566.800 Da / Num. of mol.: 1 / Fragment: ARID domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: adr6 / Plasmid: pREP-4 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P09547 |
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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 |
-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 |