BMRB Entry 26826

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for TDP-43 C-terminal domain ALS-associated variant A321G
Published: 2016-08-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26826

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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 C-terminal domain ALS-associated variant A321G

Deposition date:

2016-06-21

Original release date:

2016-08-19

Authors:

Conicella, Alexander; Fawzi, Nicolas

Citation:

Citation: Conicella, Alexander; Zerze, Gul; Mittal, Jeetain; Fawzi, Nicolas. "ALS Mutations Disrupt Phase Separation Mediated by alpha-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain" Structure (Cambridge, MA, U.S.) 24, 1537-1549 (2016).
PubMed: 27545621

Assembly members:

Assembly members:
A321G_TDP-43_267-414, polymer, 151 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: Escherichia coli Vector: pJ411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A321G_TDP-43_267-414: GHMNRQLERSGRFGGNPGGF GNQGGFGNSRGGGAGLGNNQ GSNMGGGMNFGAFSINPGMM AAAQAALQSSWGMMGMLASQ QNQSGPSGNNQNQGNMQREP NQAFGSGNNSYSGSNSGAAI GWGSASNAGSGSGFNGGFGS SMDSKSSGWGM

Data sets:

assigned_chemical_shifts
- cs-A321G_TDP-43_267-414

Data type	Count
13C chemical shifts	255
15N chemical shifts	136
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	A321G TDP-43_267-414 Monomer	1

Entities:

Entity 1, A321G TDP-43_267-414 Monomer 151 residues - Formula weight is not available

Residues 1-3 comprise the cloning artifact left after removal of the N-terminal affinity tag by cleavage with TEV protease.

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

GLY

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: A321G TDP-43_267-414, [U-99% 13C; U-99% 15N], 20 uM; MES 20 mM

283_K: pH: 6.1; pressure: 1 atm; temperature: 283 K

298_K: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample-1	isotropic	298_K
3D HNCACB	sample-1	isotropic	298_K
3D CBCA(CO)NH	sample-1	isotropic	298_K

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 850 MHz
Bruker Avance 500 MHz

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