BMRB Entry 52062

Name: Backbone 1H and 15N Chemical Shift Assignments for the region 310-350 for TDP-43 C-terminal domain engineered variant 5M to A outside CR
Published: 2023-10-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52062

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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 and 15N Chemical Shift Assignments for the region 310-350 for TDP-43 C-terminal domain engineered variant 5M to A outside CR

Deposition date:

2023-07-30

Original release date:

2023-10-28

Authors:

Krishnashenoy Padmabai, Jayakrishna Shenoy; Mohanty, Priyesh; Rizuan, Azamat; Mercado Ortiz, Jose; Fawzi, Nicolas; Mittal, Jeetain

Citation:

Citation: Mohanty, Priyesh; Krishnashenoy Padmabai, Jayakrishna Shenoy; Rizuan, Azamat; Mercado Ortiz, Jose; Fawzi, Nicolas; Mittal, Jeetain. "A synergy between site-specific and transient interactions drives the phase separation of a disordered, low-complexity domain" Proc. Natl. Acad. Sci. U. S. A. 120, e2305625120-e2305625120 (2023).
PubMed: 37579155

Assembly members:

Assembly members:
entity_1, polymer, 148 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):
entity_1: NRQLERSGRFGGNPGGFGNQ GGFGNSRGGGAGLGNNQGSN AGGGANFGAFSINPAMMAAA QAALQSSWGMMGMLASQQNQ SGPSGNNQNQGNAQREPNQA FGSGNNSYSGSNSGAAIGWG SASNAGSGSGFNGGFGSSAD SKSSGWGA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	39
1H chemical shifts	39

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	5M to A IDR	1

Entities:

Entity 1, 5M to A IDR 148 residues - Formula weight is not available

1

ASN

ARG

GLN

LEU

GLU

ARG

SER

GLY

ARG

PHE

2

GLY

ASN

PRO

GLY

PHE

GLY

ASN

GLN

3

GLY

PHE

GLY

ASN

SER

ARG

GLY

4

ALA

GLY

LEU

GLY

ASN

GLN

GLY

SER

ASN

5

ALA

GLY

ALA

ASN

PHE

GLY

ALA

PHE

6

SER

ILE

ASN

PRO

ALA

MET

ALA

7

GLN

ALA

LEU

GLN

SER

TRP

GLY

MET

8

MET

GLY

MET

LEU

ALA

SER

GLN

ASN

GLN

9

SER

GLY

PRO

SER

GLY

ASN

GLN

ASN

GLN

10

GLY

ASN

ALA

GLN

ARG

GLU

PRO

ASN

GLN

ALA

11

PHE

GLY

SER

GLY

ASN

SER

TYR

SER

GLY

12

SER

ASN

SER

GLY

ALA

ILE

GLY

TRP

GLY

13

SER

ALA

SER

ASN

ALA

GLY

SER

GLY

SER

GLY

14

PHE

ASN

GLY

PHE

GLY

SER

ALA

ASP

15

SER

LYS

SER

GLY

TRP

GLY

ALA

Samples:

sample_1: 5M to A IDR TDP-43 mutant, [U-100% 15N], 20 uM

sample_conditions_1: ionic strength: 0 M; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

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