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- PDB-2kis: Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker -

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Basic information

Entry
Database: PDB / ID: 2kis
TitleSolution structure of CA150 FF1 domain and FF1-FF2 interdomain linker
ComponentsTranscription elongation regulator 1
KeywordsTRANSCRIPTION REGULATOR / FF domain / extended helix / interdomain helix / linker peptide / interdomain dynamics / Activator / Alternative splicing / Coiled coil / Nucleus / Phosphoprotein / Repressor / Transcription / Transcription regulation
Function / homology
Function and homology information


transcription elongation factor activity / ubiquitin-like protein conjugating enzyme binding / RNA polymerase binding / negative regulation of transcription elongation by RNA polymerase II / mRNA Splicing - Major Pathway / RNA splicing / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / mRNA processing / transcription corepressor activity ...transcription elongation factor activity / ubiquitin-like protein conjugating enzyme binding / RNA polymerase binding / negative regulation of transcription elongation by RNA polymerase II / mRNA Splicing - Major Pathway / RNA splicing / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / mRNA processing / transcription corepressor activity / RNA polymerase II-specific DNA-binding transcription factor binding / transcription coactivator activity / nuclear speck / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / identical protein binding / nucleus
Similarity search - Function
FF domain / Transcription elongation regulator 1-like / FF domain / FF domain / FF domain superfamily / FF domain profile. / Contains two conserved F residues / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily ...FF domain / Transcription elongation regulator 1-like / FF domain / FF domain / FF domain superfamily / FF domain profile. / Contains two conserved F residues / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / Arc Repressor Mutant, subunit A / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Transcription elongation regulator 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing, distance geometry
Model detailslowest energy, model 1
AuthorsMurphy, J.M. / Hansen, D. / Wiesner, S. / Muhandiram, D. / Borg, M. / Smith, M.J. / Sicheri, F. / Kay, L.E. / Forman-Kay, J.D. / Pawson, T.
CitationJournal: J.Mol.Biol. / Year: 2009
Title: Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.
Authors: Murphy, J.M. / Hansen, D.F. / Wiesner, S. / Muhandiram, D.R. / Borg, M. / Smith, M.J. / Sicheri, F. / Kay, L.E. / Forman-Kay, J.D. / Pawson, T.
History
DepositionMay 8, 2009Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 26, 2020Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: pdbx_database_status / pdbx_nmr_software ...pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.3Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.4May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Transcription elongation regulator 1


Theoretical massNumber of molelcules
Total (without water)8,5781
Polymers8,5781
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)7 / 20structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Transcription elongation regulator 1 / / TATA box-binding protein-associated factor 2S / Transcription factor CA150 / CA150 / TCERG-1


Mass: 8577.958 Da / Num. of mol.: 1 / Fragment: FF1 domain: UNP residues 659-724
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: N-terminal 6xHis tag cleaved using TEV protease
Gene: CA150, TAF2S, TCERG-1, TCERG1 / Plasmid: pProEX Htb / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O14776

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D CBCA(CO)NH
1213D HN(CA)CB
1313D 1H-15N NOESY
1413D 1H-13C NOESY
1513D (H)CCH-TOCSY

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Sample preparation

DetailsContents: 1-1.7 mM [U-99% 13C; U-99% 15N] protein, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
SampleUnits: mM / Component: protein / Isotopic labeling: [U-99% 13C; U-99% 15N] / Conc. range: 1.0-1.7
Sample conditionsIonic strength: 0.137 / pH: 6.5 / Pressure: ambient / Temperature: 285 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
ARIA1.1Dr. Michael Nilges, Institut Pasteurautomated noe assignment
ARIA1.1Dr. Michael Nilges, Institut Pasteurrefinement
RefinementMethod: simulated annealing, distance geometry / Software ordinal: 1 / Details: As executed using Aria 1.1
NMR constraintsNOE constraints total: 3226 / NOE intraresidue total count: 1352 / NOE long range total count: 482 / NOE medium range total count: 549 / NOE sequential total count: 771
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 20 / Conformers submitted total number: 7
NMR ensemble rmsDistance rms dev: 0.018 Å / Distance rms dev error: 0.003 Å

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