BMRB Entry 50888

Name: 1H 15N 13C chemical shift assignment of the construct of human ataxin-3 including residues 182-291
Published: 2021-08-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50888

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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:

1H 15N 13C chemical shift assignment of the construct of human ataxin-3 including residues 182-291

Deposition date:

2021-04-10

Original release date:

2021-08-16

Authors:

Invernizzi, Gaetano; Lambrughi, Matteo; Lindorff-Larsen, Kresten; Papaleo, Elena; Teilum, Kaare

Citation:

Citation: Lambrughi, Matteo; Maiani, Emiliano; Fas, Burcu; Shaw, Gary; Kragelund, Birthe; Lindorff-Larsen, Kresten; Teilum, Kaare; Invernizzi, Gaetano; Papaleo, Elena. "Ubiquitin Interacting Motifs: duality between structured and disordered motifs" Front. Mol. Biosci. 8, 676235-676235 (2021).
PubMed: 34262938

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available

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: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSVQQMHRPKLIGEELA QLKEQRVHKTDLERMLEAND GSGMLDEDEEDLQRALALSR QEIDMEDEEADLRRAIQLSM QGSSRNISQDMTQTSGTNLT SEELRKRREAYFEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	375
15N chemical shifts	104
1H chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ataxin-3	1

Entities:

Entity 1, ataxin-3 114 residues - Formula weight is not available

Residues 1-5 are residuals from the glutathione S-transferase (GST) tag. The sequence includes the disordered region between the Josephin domain and the polyglutamine tract of ataxin-3.

1

GLY

PRO

LEU

GLY

SER

VAL

GLN

MET

HIS

2

ARG

PRO

LYS

LEU

ILE

GLY

GLU

LEU

ALA

3

GLN

LEU

LYS

GLU

GLN

ARG

VAL

HIS

LYS

THR

4

ASP

LEU

GLU

ARG

MET

LEU

GLU

ALA

ASN

ASP

5

GLY

SER

GLY

MET

LEU

ASP

GLU

ASP

GLU

6

ASP

LEU

GLN

ARG

ALA

LEU

ALA

LEU

SER

ARG

7

GLN

GLU

ILE

ASP

MET

GLU

ASP

GLU

ALA

8

ASP

LEU

ARG

ALA

ILE

GLN

LEU

SER

MET

9

GLN

GLY

SER

ARG

ASN

ILE

SER

GLN

ASP

10

MET

THR

GLN

THR

SER

GLY

THR

ASN

LEU

THR

11

SER

GLU

LEU

ARG

LYS

ARG

GLU

ALA

12

TYR

PHE

GLU

LYS

Samples:

sample_1: ataxin-3, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 150 mM; D2O 10%; Phosphate Buffered Saline buffer 90%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

CcpNMR - chemical shift assignment

VNMRj - collection

NMR spectrometers:

Varian INOVA 800 MHz

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