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Yorodumi- PDB-2gut: Solution structure of the trans-activation domain of the human co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2gut | ||||||
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Title | Solution structure of the trans-activation domain of the human co-activator ARC105 | ||||||
Components | ARC/MEDIATOR, Positive cofactor 2 glutamine/Q-rich-associated protein | ||||||
Keywords | TRANSCRIPTION / KIX / 3 HELICAL BUNDLE | ||||||
Function / homology | Function and homology information core mediator complex / Generic Transcription Pathway / somatic stem cell population maintenance / positive regulation of transcription initiation by RNA polymerase II / RNA polymerase II preinitiation complex assembly / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / PPARA activates gene expression / Transcriptional regulation of white adipocyte differentiation / nucleoplasm ...core mediator complex / Generic Transcription Pathway / somatic stem cell population maintenance / positive regulation of transcription initiation by RNA polymerase II / RNA polymerase II preinitiation complex assembly / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / PPARA activates gene expression / Transcriptional regulation of white adipocyte differentiation / nucleoplasm / membrane / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing using CYANA | ||||||
Authors | Vought, B.W. / Jim Sun, Z.-Y. / Hyberts, S.G. / Wagner, G. / Naar, A.M. | ||||||
Citation | Journal: Nature / Year: 2006 Title: An ARC/Mediator subunit required for SREBP control of cholesterol and lipid homeostasis. Authors: Yang, F. / Vought, B.W. / Satterlee, J.S. / Walker, A.K. / Jim Sun, Z.-Y. / Watts, J.L. / Debeaumont, R. / Mako Saito, R. / Hyberts, S.G. / Yang, S. / Macol, C. / Iyer, L. / Tjian, R. / van ...Authors: Yang, F. / Vought, B.W. / Satterlee, J.S. / Walker, A.K. / Jim Sun, Z.-Y. / Watts, J.L. / Debeaumont, R. / Mako Saito, R. / Hyberts, S.G. / Yang, S. / Macol, C. / Iyer, L. / Tjian, R. / van den Heuvel, S. / Hart, A.C. / Wagner, G. / Naar, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2gut.cif.gz | 419 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2gut.ent.gz | 367.3 KB | Display | PDB format |
PDBx/mmJSON format | 2gut.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/2gut ftp://data.pdbj.org/pub/pdb/validation_reports/gu/2gut | 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: 8791.069 Da / Num. of mol.: 1 / Fragment: ARC/MEDIATOR KIX domain, residues 5-78 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PCQAP, ARC105, CTG7A, TIG1 / Plasmid: pET24 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q96RN5 |
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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 arc105 U-15N, 13C, 30mM NaCl, 10mM phosphate buffer, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 30 mM NaCl / pH: 6.8 / 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 |
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-Processing
NMR software |
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Refinement | Method: simulated annealing using CYANA / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest NOE target function with no NOE violations > 0.5 A, and angular violations > 5 deg Conformers calculated total number: 20 / Conformers submitted total number: 15 |