BMRB Entry 25543

Name: Solution structure of human Myosin VI isoform3 (998-1071)
Published: 2016-03-07

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PDB ID: 2n11
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25543
MolProbity Validation Chart

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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:

Solution structure of human Myosin VI isoform3 (998-1071)

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, 74 residues, 8399.430 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):

Entity Sequences (FASTA):
entity: QQQAVLEQERRDRELALRIA QSEAELISDEAQADLALRRS LDSYPVSKNDGTRPKMTPEQ MAKEMSEFLSRGPA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	294
15N chemical shifts	82
1H chemical shifts	525

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 74 residues - 8399.430 Da.

1

GLN

ALA

VAL

LEU

GLU

GLN

GLU

ARG

2

ARG

ASP

ARG

GLU

LEU

ALA

LEU

ARG

ILE

ALA

3

GLN

SER

GLU

ALA

GLU

LEU

ILE

SER

ASP

GLU

4

ALA

GLN

ALA

ASP

LEU

ALA

LEU

ARG

SER

5

LEU

ASP

SER

TYR

PRO

VAL

SER

LYS

ASN

ASP

6

GLY

THR

ARG

PRO

LYS

MET

THR

PRO

GLU

GLN

7

MET

ALA

LYS

GLU

MET

SER

GLU

PHE

LEU

SER

8

ARG

GLY

PRO

ALA

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_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 800 MHz
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