BMRB Entry 30591

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30591
MolProbity Validation Chart

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Title:
Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy
Deposition date:
2019-03-20
Original release date:
2019-06-07
Authors:
Barnes, A.; Shen, Y.; Ying, J.; Takagi, Y.; Torchia, D.; Sellers, J.; Bax, A.
Citation:

Citation: Barnes, C.; Shen, Y.; Ying, J.; Takagi, Y.; Torchia, D.; Sellers, J.; Bax, A.. "Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy."  J. Am. Chem. Soc. 22, 9004-9017 (2019).
PubMed: 31117653

Assembly members:

Assembly members:
entity_1, polymer, 68 residues, 8939.936 Da.

Natural source:

Natural source:   Common Name: Mongolian gerbil   Taxonomy ID: 10047   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Meriones unguiculatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KQQEEEAERLRRIQEEMEKE RKRREEDEQRRRKEEEERRM KLEMEAKRKQEEEERKKRED DEKRIQAE

Data sets:
Data typeCount
13C chemical shifts118
15N chemical shifts67
1H chemical shifts67

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 68 residues - 8939.936 Da.

1   LYSGLNGLNGLUGLUGLUALAGLUARGLEU
2   ARGARGILEGLNGLUGLUMETGLULYSGLU
3   ARGLYSARGARGGLUGLUASPGLUGLNARG
4   ARGARGLYSGLUGLUGLUGLUARGARGMET
5   LYSLEUGLUMETGLUALALYSARGLYSGLN
6   GLUGLUGLUGLUARGLYSLYSARGGLUASP
7   ASPGLULYSARGILEGLNALAGLU

Samples:

sample_1: entity_1, [U-15N; U-13C; U-2H], 1 mM

sample_2: entity_1, [U-15N; U-2H], 1 mM

sample_3: entity_1, [U-15N; U-13C; U-2H], 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.3; pressure: 1 bar; temperature: 293 K

sample_conditions_2: ionic strength: 25 mM; pH: 7.8; pressure: 1 bar; temperature: 293 K

sample_conditions_3: ionic strength: 25 mM; pH: 6.3; pressure: 1 bar; temperature: 293 K

sample_conditions_4: ionic strength: 25 mM; pH: 6.3; pressure: 1 bar; temperature: 293 K

sample_conditions_5: ionic strength: 100 mM; pH: 6.3; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
4D 1H-15N-15N-1H HMQC-NOESY-TROSY-HSQCsample_1isotropicsample_conditions_1
TROSY-HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
ARTSY-Jsample_2isotropicsample_conditions_1
WEX-III TROSYsample_2isotropicsample_conditions_2
ARTSYsample_1anisotropicsample_conditions_3
E.COSY-HSQC-TROSYsample_1anisotropicsample_conditions_3
ARTSYsample_3anisotropicsample_conditions_4
Heteronuclear TROSY-based relaxationsample_2isotropicsample_conditions_1
Heteronuclear TROSY-based relaxationsample_2isotropicsample_conditions_1
ARTSYsample_1anisotropicsample_conditions_5

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker 900-MHz Bruker Avance-II 900 MHz
  • Bruker 800-MHz Bruker 800 MHz
  • Bruker 600-MHz Bruker 600 MHz

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