+Open data
-Basic information
Entry | Database: PDB / ID: 6zv3 | ||||||
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Title | TFIIS N-terminal domain (TND) from human MED26 | ||||||
Components | Mediator of RNA polymerase II transcription subunit 26 | ||||||
Keywords | TRANSCRIPTION / transcription elongation | ||||||
Function / homology | Function and homology information core mediator complex / mediator complex / Generic Transcription Pathway / RSV-host interactions / positive regulation of transcription initiation by RNA polymerase II / RNA polymerase II preinitiation complex assembly / transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / PPARA activates gene expression ...core mediator complex / mediator complex / Generic Transcription Pathway / RSV-host interactions / positive regulation of transcription initiation by RNA polymerase II / RNA polymerase II preinitiation complex assembly / transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / PPARA activates gene expression / Transcriptional regulation of white adipocyte differentiation / transcription coactivator activity / positive regulation of gene expression / regulation of transcription by RNA polymerase II / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics / molecular dynamics | ||||||
Authors | Veverka, V. | ||||||
Citation | Journal: Science / Year: 2021 Title: A ubiquitous disordered protein interaction module orchestrates transcription elongation. Authors: Cermakova, K. / Demeulemeester, J. / Lux, V. / Nedomova, M. / Goldman, S.R. / Smith, E.A. / Srb, P. / Hexnerova, R. / Fabry, M. / Madlikova, M. / Horejsi, M. / De Rijck, J. / Debyser, Z. / ...Authors: Cermakova, K. / Demeulemeester, J. / Lux, V. / Nedomova, M. / Goldman, S.R. / Smith, E.A. / Srb, P. / Hexnerova, R. / Fabry, M. / Madlikova, M. / Horejsi, M. / De Rijck, J. / Debyser, Z. / Adelman, K. / Hodges, H.C. / Veverka, V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6zv3.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6zv3.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 6zv3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6zv3_validation.pdf.gz | 561.5 KB | Display | wwPDB validaton report |
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Full document | 6zv3_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6zv3_validation.xml.gz | 123.6 KB | Display | |
Data in CIF | 6zv3_validation.cif.gz | 147.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zv/6zv3 ftp://data.pdbj.org/pub/pdb/validation_reports/zv/6zv3 | HTTPS FTP |
-Related structure data
Related structure data | 6zuyC 6zuzC 6zv0C 6zv1C 6zv2C 6zv4C 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: 10183.872 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MED26, ARC70, CRSP7 / Production host: Escherichia coli (E. coli) / References: UniProt: O95402 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 0.5 mM [U-13C; U-15N] MED26, 25 mM [U-2H] TRIS, 200 mM sodium chloride, 1 mM TCEP, 95% H2O/5% D2O Label: s1 / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 225 mM / Label: c1 / pH: 7.4 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 850 MHz |
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-Processing
NMR software |
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Refinement |
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NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 50 |