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- PDB-1uzc: THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11 -

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Basic information

Entry
Database: PDB / ID: 1uzc
TitleTHE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11
ComponentsHYPOTHETICAL PROTEIN FLJ21157Hypothesis
KeywordsNUCLEAR PROTEIN / TRANSCRIPTION / PHOSPHOPEPTIDE RECOGNITION / RNA POLYMERASE II CARBOXYL-TERMINAL DOMAIN
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 / cytosol
Similarity search - Function
FF domain / 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 ...FF domain / 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 / Arc Repressor Mutant, subunit A / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Pre-mRNA-processing factor 40 homolog A / Pre-mRNA-processing factor 40 homolog A
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING
AuthorsAllen, M.D. / Jemth, P. / Friedler, A. / Schon, O. / Bycroft, M.
CitationJournal: J.Mol.Biol. / Year: 2002
Title: The Structure of an Ff Domain from Human Hypa/Fbp11.
Authors: Allen, M.D. / Friedler, A. / Schon, O. / Bycroft, M.
History
DepositionMar 9, 2004Deposition site: PDBE / Processing site: PDBE
SupersessionApr 5, 2004ID: 1H40
Revision 1.0Apr 5, 2004Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Database references / Category: citation / Item: _citation.page_last
Revision 1.4Jan 24, 2018Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name ..._entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.5May 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 / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HYPOTHETICAL PROTEIN FLJ21157


Theoretical massNumber of molelcules
Total (without water)8,2511
Polymers8,2511
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)23 / 30NO DISTANCE VIOLATION 0.25A AND NO ANGLE VIOLATIONS > 5 DEGREES
RepresentativeModel #1

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Components

#1: Protein HYPOTHETICAL PROTEIN FLJ21157 / Hypothesis / HUNTINGTIN-INTERACTING PROTEIN HYPA/FBP11


Mass: 8251.467 Da / Num. of mol.: 1 / Fragment: FF DOMAIN, RESIDUES 250-319
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PRSET-GROEL / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q9H782, UniProt: O75400*PLUS
Compound detailsTHE FF DOMAIN MAY BE INVOLVED IN PROTEIN-PROTEIN INTERACTION AND OFTEN OCCURS IN CONJUNCTION WITH WW DOMAINS
Sequence detailsTHE SEQUENCE OF THIS ENTRY ALSO MATCHES FRAGMENTS OF FORMIN BINDING PROTEIN 11 (SWISS-PROT ...THE SEQUENCE OF THIS ENTRY ALSO MATCHES FRAGMENTS OF FORMIN BINDING PROTEIN 11 (SWISS-PROT ACCESSION Q9R1C7) AND HUNTINGTIN-INTERACTING PROTEIN HYPA/FBP11 (SWISS-PROT ACCESSION O75404, 98% IDENTITY)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111STANDARD 13C
12115N
1311H EXPERIMENTS
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED FF DOMAIN)

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Sample preparation

Sample conditionspH: 6.0 / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLORBRUNGERrefinement
ANSIG3.3structure solution
RefinementMethod: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: NO DISTANCE VIOLATION 0.25A AND NO ANGLE VIOLATIONS > 5 DEGREES
Conformers calculated total number: 30 / Conformers submitted total number: 23

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