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Yorodumi- PDB-2cuj: Solution structure of SWIRM domain of mouse transcriptional adapt... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2cuj | ||||||
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Title | Solution structure of SWIRM domain of mouse transcriptional adaptor 2-like | ||||||
Components | transcriptional adaptor 2-like | ||||||
Keywords | TRANSCRIPTION / Transcriptional regulation / Nuclear protein / ADA2 / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Formation of WDR5-containing histone-modifying complexes / : / SAGA-type complex / ATAC complex / SAGA complex / regulation of tubulin deacetylation / regulation of cell division / regulation of embryonic development / regulation of protein phosphorylation / regulation of protein stability ...Formation of WDR5-containing histone-modifying complexes / : / SAGA-type complex / ATAC complex / SAGA complex / regulation of tubulin deacetylation / regulation of cell division / regulation of embryonic development / regulation of protein phosphorylation / regulation of protein stability / mitotic spindle / chromatin organization / mitotic cell cycle / transcription coactivator activity / regulation of cell cycle / chromatin remodeling / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleus Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Yoneyama, M. / Umehara, T. / Sato, M. / Tochio, N. / Koshiba, S. / Inoue, M. / Tanaka, A. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural and Functional Differences of SWIRM Domain Subtypes Authors: Yoneyama, M. / Tochio, N. / Umehara, T. / Koshiba, S. / Inoue, M. / Yabuki, T. / Aoki, M. / Seki, E. / Matsuda, T. / Watanabe, S. / Tomo, Y. / Nishimura, Y. / Harada, T. / Terada, T. / ...Authors: Yoneyama, M. / Tochio, N. / Umehara, T. / Koshiba, S. / Inoue, M. / Yabuki, T. / Aoki, M. / Seki, E. / Matsuda, T. / Watanabe, S. / Tomo, Y. / Nishimura, Y. / Harada, T. / Terada, T. / Shirouzu, M. / Hayashizaki, Y. / Ohara, O. / Tanaka, A. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2cuj.cif.gz | 649.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2cuj.ent.gz | 543 KB | Display | PDB format |
PDBx/mmJSON format | 2cuj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cu/2cuj ftp://data.pdbj.org/pub/pdb/validation_reports/cu/2cuj | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11676.451 Da / Num. of mol.: 1 / Fragment: SWIRM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: Tada2l / Plasmid: P041018-15 / References: UniProt: Q8BNK0, UniProt: Q8CHV6*PLUS |
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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: 1.36mM SWIRM domain U-15N, 13C; 20mM d-Tris-HCl2 (pH7.0), 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120 / pH: 7.0 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function, structures with the lowest energy, structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |