BMRB Entry 30591

Name: Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy
Published: 2019-06-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30591

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy PubMed: 31117653

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: 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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	118
15N chemical shifts	67
1H chemical shifts	67

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 68 residues - 8939.936 Da.

1

LYS

GLN

GLU

ALA

GLU

ARG

LEU

2

ARG

ILE

GLN

GLU

MET

GLU

LYS

GLU

3

ARG

LYS

ARG

GLU

ASP

GLU

GLN

ARG

4

ARG

LYS

GLU

ARG

MET

5

LYS

LEU

GLU

MET

GLU

ALA

LYS

ARG

LYS

GLN

6

GLU

ARG

LYS

ARG

GLU

ASP

7

ASP

GLU

LYS

ARG

ILE

GLN

ALA

GLU

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:

Name	Sample	Sample state	Sample conditions
4D 1H-15N-15N-1H HMQC-NOESY-TROSY-HSQC	sample_1	isotropic	sample_conditions_1
TROSY-HSQC	sample_1	isotropic	sample_conditions_1
3D TROSY-HNCACB	sample_1	isotropic	sample_conditions_1
ARTSY-J	sample_2	isotropic	sample_conditions_1
WEX-III TROSY	sample_2	isotropic	sample_conditions_2
ARTSY	sample_1	anisotropic	sample_conditions_3
E.COSY-HSQC-TROSY	sample_1	anisotropic	sample_conditions_3
ARTSY	sample_3	anisotropic	sample_conditions_4
Heteronuclear TROSY-based relaxation	sample_2	isotropic	sample_conditions_1
Heteronuclear TROSY-based relaxation	sample_2	isotropic	sample_conditions_1
ARTSY	sample_1	anisotropic	sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts