BMRB Entry 27549

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for TDP-43 RRM2 at 6M urea
Published: 2018-11-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27549

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for TDP-43 RRM2 at 6M urea

Deposition date:

2018-07-17

Original release date:

2018-11-15

Authors:

Mackness, Brian; Morgan, Brittany; Deveau, Laura; Kathuria, Sagar; Tavella, Davide; Massi, Francesca; Zitzewitz, Jill

Citation:

Citation: Tavella, Davide; Zitzewitz, Jill; Massi, Francesca. "Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis." Biophys. J. 115, 1673-1680 (2018).
PubMed: 30309612

Assembly members:

Assembly members:
TDP-43_RRM2, polymer, 76 residues, 8506.6182 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: pGEX-6p1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TDP-43_RRM2: GPLGSRKVFVGRCTEDMTED ELREFFSQYGDVMDVFIPKP FRAFAFVTFADDQIAQSLCG EDLIIKGISVHISNAE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	119
15N chemical shifts	68
1H chemical shifts	68

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TDP-43 RRM2	1

Entities:

Entity 1, TDP-43 RRM2 76 residues - 8506.6182 Da.

The first two residues (GP) are left after cleavege by PreScission protease. The following three residues (LGS) are required for cloning.

1

GLY

PRO

LEU

GLY

SER

ARG

LYS

VAL

PHE

VAL

2

GLY

ARG

CYS

THR

GLU

ASP

MET

THR

GLU

ASP

3

GLU

LEU

ARG

GLU

PHE

SER

GLN

TYR

GLY

4

ASP

VAL

MET

ASP

VAL

PHE

ILE

PRO

LYS

PRO

5

PHE

ARG

ALA

PHE

ALA

PHE

VAL

THR

PHE

ALA

6

ASP

GLN

ILE

ALA

GLN

SER

LEU

CYS

GLY

7

GLU

ASP

LEU

ILE

LYS

GLY

ILE

SER

VAL

8

HIS

ILE

SER

ASN

ALA

GLU

Samples:

sample_1: MOPS 20 mM; potassium chloride 25 mM; beta-mercaptoethanol 1 mM; TDP-43 RRM2, [U-100% 13C; U-100% 15N], .47 mM; urea 6 M

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ v2.2, Varian - collection

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz

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