BMRB Entry 34737

Name: Structure of the low complexity domain of TDP-43 (fragment 309-350) with methionine sulfoxide modifications
Published: 2023-01-30

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PDB ID: 8a6i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34737
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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:

Structure of the low complexity domain of TDP-43 (fragment 309-350) with methionine sulfoxide modifications

Deposition date:

2022-06-17

Original release date:

2023-01-30

Authors:

Carrasco, J.; Anton, R.; Pantoja-Uceda, D.; Laurents, D.; Oroz, J.

Citation:

Citation: Carrasco, J.; Anton, R.; Valbuena, A.; Pantoja-Uceda, D.; Mukhi, M.; Hervas, R.; Laurents, D.; Gasset, M.; Oroz, J.. "Metamorphism in TDP-43 prion-like domain determines chaperone recognition" Nat. Commun. 14, 466-466 (2023).
PubMed: 36709343

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4331.803 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 BL21(DE3) Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGXNFGAFSINPAXXAAAQA ALQSSWGXXGXLASQQNQSG PS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	40
1H chemical shifts	214

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 42 residues - 4331.803 Da.

1

GLY

MHO

ASN

PHE

GLY

ALA

PHE

SER

ILE

2

ASN

PRO

ALA

MHO

ALA

GLN

ALA

3

ALA

LEU

GLN

SER

TRP

GLY

MHO

GLY

4

MHO

LEU

ALA

SER

GLN

ASN

GLN

SER

GLY

5

PRO

SER

Samples:

sample_1: TDP-43 fragment 309-350, [U-13C; U-15N], 500 uM; HEPES 20 mM; potassium chloride 10 mM; MgCl2 5 mM; ATP 1 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNNH	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-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

Sparky v3.190, Goddard - chemical shift assignment

TopSpin v4.0.8, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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