BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25541

Title: Solution structure of MyUb (1080-1122) of human Myosin VI   PubMed: 26971995

Deposition date: 2015-03-20 Original release date: 2016-03-07

Authors: He, Fahu; Walters, Kylie

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).

Assembly members:
entity, polymer, 51 residues, 5213.026 Da.

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

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

Entity Sequences (FASTA):
entity: GPLGSPNSGTKKYDLSKWKY AELRDTINTSCDIELLAACR EEFHRRLKVYH

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts55
1H chemical shifts364

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 51 residues - 5213.026 Da.

The first 8 residues (GPLGSPNS) are a tag

1   GLYPROLEUGLYSERPROASNSERGLYTHR
2   LYSLYSTYRASPLEUSERLYSTRPLYSTYR
3   ALAGLULEUARGASPTHRILEASNTHRSER
4   CYSASPILEGLULEULEUALAALACYSARG
5   GLUGLUPHEHISARGARGLEULYSVALTYR
6   HIS

Samples:

sample_1: entity, [U-13C; U-15N], 0.3 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:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

Kujira, Naohiro Kobayashi - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

Uniprot Q9UM54

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts