BMRB Entry 28017

Name: QBP1+TDP-43 POLYPEPTIDE
Published: 2019-10-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28017

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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:

QBP1+TDP-43 POLYPEPTIDE

Deposition date:

2019-09-15

Original release date:

2019-10-03

Authors:

Laurents, Douglas; Mompean, Miguel

Citation:

Citation: Mompean, Miguel; Ramirez de Mingo, Daniel; Hervas, Ruben; Fernandez-Ramirez, Maria Del Carmen; Carrion-Vazquez, Mariano; Laurents, Douglas. "Molecular mechanism of the inhibition of TDP-43 amyloidogenesis by QBP1" Arch. Biochem. Biophys. 675, 108113-108113 (2019).
PubMed: 31568752

Assembly members:

Assembly members:
QBP1+TDP-43, polymer, 28 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: chemical synthesis Vector: n.a.

Entity Sequences (FASTA):

Entity Sequences (FASTA):
QBP1+TDP-43: WKWWPGIFGGGASQQNQSGP SGNNQNQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	64
15N chemical shifts	37
1H chemical shifts	176

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	QBP1+TDP-43	1

Entities:

Entity 1, QBP1+TDP-43 28 residues - Formula weight is not available

1

TRP

LYS

TRP

PRO

GLY

ILE

PHE

GLY

2

GLY

ALA

SER

GLN

ASN

GLN

SER

GLY

PRO

3

SER

GLY

ASN

GLN

ASN

GLN

GLY

Samples:

sample_1: QBP1+TDP-43 0.94 ± 0.03 mM; potassium hydrogen phosphate 10 mM

sample_2: QBP1+TDP-43 0.94 ± 0.03 mM; potassium hydrogen phosphate 10 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.8; pressure: 1 atm; temperature: 278.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

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