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Open data
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Basic information
Entry | Database: PDB / ID: 6zv2 | ||||||
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Title | TFIIS N-terminal domain (TND) from human PPP1R10 | ||||||
![]() | Serine/threonine-protein phosphatase 1 regulatory subunit 10 | ||||||
![]() | TRANSCRIPTION / transcription elongation | ||||||
Function / homology | ![]() negative regulation of mitotic DNA damage checkpoint / PTW/PP1 phosphatase complex / positive regulation of telomere maintenance / protein phosphatase inhibitor activity / negative regulation of cardiac muscle cell apoptotic process / protein import into nucleus / nuclear body / chromatin / DNA binding / RNA binding ...negative regulation of mitotic DNA damage checkpoint / PTW/PP1 phosphatase complex / positive regulation of telomere maintenance / protein phosphatase inhibitor activity / negative regulation of cardiac muscle cell apoptotic process / protein import into nucleus / nuclear body / chromatin / DNA binding / RNA binding / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics / molecular dynamics | ||||||
![]() | Veverka, V. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.9 MB | Display | ![]() |
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PDB format | ![]() | 1.6 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 563.1 KB | Display | ![]() |
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Full document | ![]() | 1001.1 KB | Display | |
Data in XML | ![]() | 144.4 KB | Display | |
Data in CIF | ![]() | 165.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6zuyC ![]() 6zuzC ![]() 6zv0C ![]() 6zv1C ![]() 6zv3C ![]() 6zv4C C: citing same article ( |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 17221.992 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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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: 0.7 mM [U-13C; U-15N] PPP1R10, 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
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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: 40 |