BMRB Entry 27334

Name: Ataxin7N10QT3N9 (Residues:1-62)
Published: 2018-02-07

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27334

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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:

Ataxin7N10QT3N9 (Residues:1-62)

Deposition date:

2017-12-07

Original release date:

2018-02-07

Authors:

Hu, Hongyu; Hong, Junye

Citation:

Citation: Hu, Hongyu; Hong, Junye; Wang, Dongdong; Xue, Wei; Yue, Hongwei; Yang, Hui; Jiang, Leilei; Wang, Wenning. "Structural and dynamic studies reveal that the alanine-rich region in the N-terminus of ataxin-7 initiates -helix formation of the polyglutamine tract but inhibits its amyloid aggregation" J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
Atx7N10QT3N9, polymer, 62 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: E. coli - cell free Vector: pET-32M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Atx7N10QT3N9: MSERAADDVRGEPRRAAAAA GGAAAAAARQQTQQQQQNQP PPPQPQRQQHPPPPPRRTRP ED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	158
15N chemical shifts	43
1H chemical shifts	179

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ataxin7N10QT3N9	1

Entities:

Entity 1, Ataxin7N10QT3N9 62 residues - Formula weight is not available

1

MET

SER

GLU

ARG

ALA

ASP

VAL

ARG

2

GLY

GLU

PRO

ARG

ALA

3

GLY

ALA

ARG

GLN

4

GLN

THR

GLN

ASN

GLN

PRO

5

PRO

GLN

PRO

GLN

ARG

GLN

HIS

6

PRO

ARG

THR

ARG

PRO

7

GLU

ASP

Samples:

sample_1: Atx7N10QT3N9, [U-13C; U-15N], 300 uM; Atx7N10QT3N9, [U-15N], 300 uM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Uniform NMR System 600 MHz

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