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Yorodumi- PDB-2eqj: Solution structure of the TUDOR domain of Metal-response element-... -
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-Basic information
Entry | Database: PDB / ID: 2eqj | ||||||
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Title | Solution structure of the TUDOR domain of Metal-response element-binding transcription factor 2 | ||||||
Components | Metal-response element-binding transcription factor 2 | ||||||
Keywords | TRANSCRIPTION / structure genomics / TUDOR domain / Metal-response element-binding transcription factor 2 / Zinc-regulated factor 1 / ZiRF1 / Metal-response element DNA-binding protein M96 / Metal-regulatory transcription factor 2 / PCL2 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information PRC2 methylates histones and DNA / segment specification / stem cell population maintenance / epigenetic regulation of gene expression / methylated histone binding / cellular response to leukemia inhibitory factor / transcription corepressor binding / stem cell differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-binding transcription repressor activity, RNA polymerase II-specific ...PRC2 methylates histones and DNA / segment specification / stem cell population maintenance / epigenetic regulation of gene expression / methylated histone binding / cellular response to leukemia inhibitory factor / transcription corepressor binding / stem cell differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / chromatin organization / chromatin binding / regulation of DNA-templated transcription / DNA binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Dang, W. / Muto, Y. / Isono, K. / Watanabe, S. / Tarada, T. / Kigawa, T. / Koseki, H. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the TUDOR domain of Metal-response element-binding transcription factor 2 Authors: Dang, W. / Muto, Y. / Isono, K. / Watanabe, S. / Tarada, T. / Kigawa, T. / Koseki, H. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eqj.cif.gz | 393.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eqj.ent.gz | 343.7 KB | Display | PDB format |
PDBx/mmJSON format | 2eqj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/2eqj ftp://data.pdbj.org/pub/pdb/validation_reports/eq/2eqj | 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: 7311.332 Da / Num. of mol.: 1 / Fragment: TUDOR domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: cell-free protein synthesis / Gene: Mtf2 / Plasmid: P061002-01 / References: UniProt: Q02395 |
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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: 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 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: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |