BMRB Entry 53381

Name: 1H, 15N, CA Chemical Shift Assignments for the region 300-360 for TDP-43 C-terminal domain at pH 7
Published: 2025-10-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53381

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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, CA Chemical Shift Assignments for the region 300-360 for TDP-43 C-terminal domain at pH 7

Deposition date:

2025-10-06

Original release date:

2025-10-31

Authors:

Krishnashenoy Padmabai, Jayakrishna Shenoy; Fawzi, Nicolas L.

Citation:

Citation: Krishnashenoy Padmabai, Jayakrishna Shenoy; Fawzi, Nicolas L.. "Structural details of helix-mediated multimerization of the conserved region of TDP-43 C-terminal domain" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMNRQLERSGRFGGNPGGF GNQGGFGNSRGGGAGLGNNQ GSNMGGGMNFGAFSINPAMM AAAQAALQSSWGMMGMLASQ QNQSGPSGNNQNQGNMQREP NQAFGSGNNSYSGSNSGAAI GWGSASNAGSGSGFNGGFGS SMDSKSSGWGM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	58
15N chemical shifts	58
1H chemical shifts	58

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, TDP-43_CTD 151 residues - Formula weight is not available

1

GLY

HIS

MET

ASN

ARG

GLN

LEU

GLU

ARG

SER

2

GLY

ARG

PHE

GLY

ASN

PRO

GLY

PHE

3

GLY

ASN

GLN

GLY

PHE

GLY

ASN

SER

ARG

4

GLY

ALA

GLY

LEU

GLY

ASN

GLN

5

GLY

SER

ASN

MET

GLY

MET

ASN

PHE

6

GLY

ALA

PHE

SER

ILE

ASN

PRO

ALA

MET

7

ALA

GLN

ALA

LEU

GLN

SER

8

TRP

GLY

MET

GLY

MET

LEU

ALA

SER

GLN

9

GLN

ASN

GLN

SER

GLY

PRO

SER

GLY

ASN

10

GLN

ASN

GLN

GLY

ASN

MET

GLN

ARG

GLU

PRO

11

ASN

GLN

ALA

PHE

GLY

SER

GLY

ASN

SER

12

TYR

SER

GLY

SER

ASN

SER

GLY

ALA

ILE

13

GLY

TRP

GLY

SER

ALA

SER

ASN

ALA

GLY

SER

14

GLY

SER

GLY

PHE

ASN

GLY

PHE

GLY

SER

15

SER

MET

ASP

SER

LYS

SER

GLY

TRP

GLY

16

MET

Samples:

sample_1: TDP-43_CTD, [U-100% 13C; U-100% 15N], 13 uM; DSS 10 uM; HEPES 20 uM; sodium chloride 150 mM; D2O, [U-99% 2H], 2.76 M

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 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

Software:

TOPSPIN - collection, processing

NMRPipe - processing

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 850 MHz

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