BMRB Entry 25544

Title:
Solution structure of human Myosin VI isoform3 (1050-1131)
Deposition date:
2015-03-20
Original release date:
2016-03-07
Authors:
He, Fahu; Walters, Kylie
Citation:

Citation: He, Fahu; Wollscheid, Hans-Peter; Nowicka, Urszula; Biancospino, Matteo; Valentini, Eleonora; Ehlinger, Aaron; Acconcia, Filippo; Magistrati, Elisa; Polo, Simona; Walters, Kylie. "Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains"  Cell Rep. 14, 2683-2694 (2016).
PubMed: 26971995

Assembly members:

Assembly members:
entity, polymer, 82 residues, 9580.269 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6p

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts89
1H chemical shifts607

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 82 residues - 9580.269 Da.

1   ARGPROLYSMETTHRPROGLUGLNMETALA
2   LYSGLUMETSERGLUPHELEUSERARGGLY
3   PROALAVALLEUALATHRLYSALAALAALA
4   GLYTHRLYSLYSTYRASPLEUSERLYSTRP
5   LYSTYRALAGLULEUARGASPTHRILEASN
6   THRSERCYSASPILEGLULEULEUALAALA
7   CYSARGGLUGLUPHEHISARGARGLEULYS
8   VALTYRHISALATRPLYSSERLYSASNLYS
9   LYSARG

Samples:

sample_1: entity, [U-13C; U-15N], 0.7 mM; sodium phosphate buffer 20 mM; NaCl 50 mM; DTT 2 mM; NaN3 0.1%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Kujira, Naohiro Kobayashi - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks