+Open data
-Basic information
Entry | Database: PDB / ID: 6zuz | ||||||
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Title | TFIIS N-terminal domain (TND) from human Elongin-A | ||||||
Components | Elongin-A | ||||||
Keywords | TRANSCRIPTION / elongation factor | ||||||
Function / homology | Function and homology information elongin complex / site of DNA damage / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation ...elongin complex / site of DNA damage / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / regulation of transcription by RNA polymerase II / extracellular space / nucleoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / 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 | 6zuz.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6zuz.ent.gz | 916 KB | Display | PDB format |
PDBx/mmJSON format | 6zuz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zu/6zuz ftp://data.pdbj.org/pub/pdb/validation_reports/zu/6zuz | HTTPS FTP |
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-Related structure data
Related structure data | 6zuyC 6zv0C 6zv1C 6zv2C 6zv3C 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: 9705.288 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOA, TCEB3, MSTP059 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14241 |
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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] ELOA, 25 mM deuterated 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 / Manufacturer: Bruker / Model: AVANCE / Field strength: 850 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||
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: 40 |