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- PDB-1e0l: FBP28WW domain from Mus musculus -

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Basic information

Entry
Database: PDB / ID: 1e0l
TitleFBP28WW domain from Mus musculus
ComponentsFORMIN BINDING PROTEIN
KeywordsSH3 DOMAIN / WW DOMAIN / FBP28 / SIGNAL TRANSDUCTION
Function / homology
Function and homology information


mRNA Splicing - Major Pathway / proline-rich region binding / RNA polymerase binding / transcription coregulator activity / DNA-binding transcription factor activity / DNA-templated transcription / nucleoplasm / nucleus
Similarity search - Function
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. ...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
Similarity search - Domain/homology
Transcription elongation regulator 1 / Transcription elongation regulator 1
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsMacias, M.J. / Gervais, V. / Civera, C. / Oschkinat, H.
CitationJournal: Nat.Struct.Biol. / Year: 2000
Title: Structural Analysis of Ww Domains and Design of a Ww Prototype
Authors: Macias, M.J. / Gervais, V. / Civera, C. / Oschkinat, H.
History
DepositionMar 30, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 20, 2000Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FORMIN BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)4,3651
Polymers4,3651
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 20LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein/peptide FORMIN BINDING PROTEIN


Mass: 4364.709 Da / Num. of mol.: 1 / Fragment: DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q61051, UniProt: Q8CGF7*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR NMR SPECTROSCOPY

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 285 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
ARIA/CNS1. NILGES, M.refinement
ARIA CNSCNSstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 20 / Conformers submitted total number: 10

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