BMRB Entry 50955

Name: Backbone Chemical Shift Assignments of human glutathione peroxidase 4 (GPx4)
Published: 2021-09-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50955

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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 Chemical Shift Assignments of human glutathione peroxidase 4 (GPx4) PubMed: 34492183

Deposition date: 2021-05-28 Original release date: 2021-09-08

Authors: Labrecque, Courtney; Fuglestad, Brian

Citation: Labrecque, Courtney; Fuglestad, Brian. "Electrostatic Drivers of GPx4 Interactions with Membrane, Lipids, and DNA" Biochemistry 60, 2761-2772 (2021).

Assembly members:
entity_1, polymer, 164 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pNIC28-Bsa4

Entity Sequences (FASTA):
entity_1: SMRCARSMHEFSAKDIDGHM VNLDKYRGFVCIVTNVASQG GKTEVNYTQLVDLHARYAEC GLRILAFPCNQFGKQEPGSN EEIKEFAAGYNVKFDMFSKI CVNGDDAHPLWKWMKIQPKG KGILGNAIKWNFTKFLIDKN GCVVKRYGPMEEPLVIEKDL PHYF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	474
15N chemical shifts	154
1H chemical shifts	154

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GPx4	1

Entities:

Entity 1, GPx4 164 residues - Formula weight is not available

human, cytosolic GPx4, truncated at position 8, U46 mutated to G

1

SER

MET

ARG

CYS

ALA

ARG

SER

MET

HIS

GLU

2

PHE

SER

ALA

LYS

ASP

ILE

ASP

GLY

HIS

MET

3

VAL

ASN

LEU

ASP

LYS

TYR

ARG

GLY

PHE

VAL

4

CYS

ILE

VAL

THR

ASN

VAL

ALA

SER

GLN

GLY

5

GLY

LYS

THR

GLU

VAL

ASN

TYR

THR

GLN

LEU

6

VAL

ASP

LEU

HIS

ALA

ARG

TYR

ALA

GLU

CYS

7

GLY

LEU

ARG

ILE

LEU

ALA

PHE

PRO

CYS

ASN

8

GLN

PHE

GLY

LYS

GLN

GLU

PRO

GLY

SER

ASN

9

GLU

ILE

LYS

GLU

PHE

ALA

GLY

TYR

10

ASN

VAL

LYS

PHE

ASP

MET

PHE

SER

LYS

ILE

11

CYS

VAL

ASN

GLY

ASP

ALA

HIS

PRO

LEU

12

TRP

LYS

TRP

MET

LYS

ILE

GLN

PRO

LYS

GLY

13

LYS

GLY

ILE

LEU

GLY

ASN

ALA

ILE

LYS

TRP

14

ASN

PHE

THR

LYS

PHE

LEU

ILE

ASP

LYS

ASN

15

GLY

CYS

VAL

LYS

ARG

TYR

GLY

PRO

MET

16

GLU

PRO

LEU

VAL

ILE

GLU

LYS

ASP

LEU

17

PRO

HIS

TYR

PHE

Samples:

sample_1: GPx4, [U-98% 13C; U-98% 15N], 300 uM; Bis-Tris 20 mM; sodium chloride 100 mM; DTT 20 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRPipe v10.6 - processing

NMRFAM-SPARKY v1.470 - data analysis

NMR spectrometers:

Bruker AVANCE III 700 MHz
Bruker AVANCE III 600 MHz

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