BMRB Entry 52112

Name: Amide backbone chemical shift assignments for human glutathione peroxidase 4 I129S,L130S mutant (GPX4-U46C-I129S-L130S)
Published: 2025-12-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52112

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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:

Amide backbone chemical shift assignments for human glutathione peroxidase 4 I129S,L130S mutant (GPX4-U46C-I129S-L130S)

Deposition date:

2023-09-04

Original release date:

2025-12-02

Authors:

Bostock, Mark; Mourao, Andre; Popowicz, Grzegorz; Sattler, Michael

Citation:

Citation: Lorenz, Svenja; Wahida, Adam; Bostock, Mark; Mourao, Andre; Sattler, Michael; Popowicz, Grzegorz; Conrad, Marcus. "An ultra-rare variant of GPX4 reveals the structural basis to avert neurodegeneration" .

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, 19554.44 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: pET-M11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMCASRDDWRCARSMHEFS AKDIDGHMVNLDKYRGFVCI VTNVASQCGKTEVNYTQLVD LHARYAECGLRILAFPCNQF GKQEPGSNEEIKEFAAGYNV KFDMFSKICVNGDDAHPLWK WMKIQPKGKGSSGNAIKWNF TKFLIDKNGCVVKRYGPMEE PLVIEKDLPHYF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	155
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GPX4 I129S,L130S	1

Entities:

Entity 1, GPX4 I129S,L130S 172 residues - 19554.44 Da.

1

GLY

ALA

MET

CYS

ALA

SER

ARG

ASP

TRP

2

ARG

CYS

ALA

ARG

SER

MET

HIS

GLU

PHE

SER

3

ALA

LYS

ASP

ILE

ASP

GLY

HIS

MET

VAL

ASN

4

LEU

ASP

LYS

TYR

ARG

GLY

PHE

VAL

CYS

ILE

5

VAL

THR

ASN

VAL

ALA

SER

GLN

CYS

GLY

LYS

6

THR

GLU

VAL

ASN

TYR

THR

GLN

LEU

VAL

ASP

7

LEU

HIS

ALA

ARG

TYR

ALA

GLU

CYS

GLY

LEU

8

ARG

ILE

LEU

ALA

PHE

PRO

CYS

ASN

GLN

PHE

9

GLY

LYS

GLN

GLU

PRO

GLY

SER

ASN

GLU

10

ILE

LYS

GLU

PHE

ALA

GLY

TYR

ASN

VAL

11

LYS

PHE

ASP

MET

PHE

SER

LYS

ILE

CYS

VAL

12

ASN

GLY

ASP

ALA

HIS

PRO

LEU

TRP

LYS

13

TRP

MET

LYS

ILE

GLN

PRO

LYS

GLY

LYS

GLY

14

SER

GLY

ASN

ALA

ILE

LYS

TRP

ASN

PHE

15

THR

LYS

PHE

LEU

ILE

ASP

LYS

ASN

GLY

CYS

16

VAL

LYS

ARG

TYR

GLY

PRO

MET

GLU

17

PRO

LEU

VAL

ILE

GLU

LYS

ASP

LEU

PRO

HIS

18

TYR

PHE

Samples:

sample_1: GPX4 I129S,L130S, [U-100% 15N], 0.5 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; D2O, [U-99% 2H], 10 % v/v; DTT 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

AZARA v2.8 - processing

TOPSPIN v3.5 pl7 - collection

CcpNMR v2.5 - data analysis

NMR spectrometers:

Bruker AVANCE III 900 MHz
Bruker AVANCE III 800 MHz

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