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- PDB-2l5f: Solution structure of the tandem WW domains from HYPA/FBP11 -

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Basic information

Entry
Database: PDB / ID: 2l5f
TitleSolution structure of the tandem WW domains from HYPA/FBP11
ComponentsPre-mRNA-processing factor 40 homolog A
KeywordsPROTEIN BINDING / 2WW / HYPA / FBP11
Function / homology
Function and homology information


mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape ...mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape / nuclear speck / cell cycle / cell division / RNA binding / nucleoplasm / membrane
Similarity search - Function
Pre-mRNA-processing factor Prp40 / 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. ...Pre-mRNA-processing factor Prp40 / 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
Pre-mRNA-processing factor 40 homolog A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsJiang, Y. / Hu, H.
CitationJournal: To be Published
Title: Interaction with polyglutamine expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA)
Authors: Jiang, Y. / Che, M. / Yuan, J. / Xie, Y. / Yan, X. / Hu, H.
History
DepositionNov 1, 2010Deposition site: BMRB / Processing site: PDBJ
Revision 1.0May 11, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Pre-mRNA-processing factor 40 homolog A


Theoretical massNumber of molelcules
Total (without water)10,5491
Polymers10,5491
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Pre-mRNA-processing factor 40 homolog A / Fas ligand-associated factor 1 / Formin-binding protein 11 / Formin-binding protein 3 / Huntingtin ...Fas ligand-associated factor 1 / Formin-binding protein 11 / Formin-binding protein 3 / Huntingtin yeast partner A / Huntingtin-interacting protein 10 / HIP-10 / Huntingtin-interacting protein A / Renal carcinoma antigen NY-REN-6


Mass: 10549.498 Da / Num. of mol.: 1 / Fragment: WW domains (UNP RESIDUES 133-220) / Mutation: P67T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 / Production host: Escherichia coli (E. coli) / References: UniProt: O75400

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D 1H-13C NOESY
1313D C(CO)NH
1413D HNCO
1513D H(CCO)NH
1613D HN(CA)CB
1713D 1H-15N NOESY
1813D CBCA(CO)NH
1913D (H)CCH-TOCSY

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Sample preparation

DetailsContents: 10 mM sodium phosphate-1, 100 mM sodium chloride-2, 5 mM DTT-3, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
10 mMsodium phosphate-11
100 mMsodium chloride-21
5 mMDTT-31
Sample conditionsIonic strength: 0.11 / pH: 6.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR softwareName: CNS / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 1

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