BMRB Entry 34617

Name: Solution NMR Structure of the Neh1 Domain of Human Nuclear factor erythroid 2-related factor 2 (NRF2)
Published: 2021-09-24

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PDB ID: 7o7b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34617
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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:

Solution NMR Structure of the Neh1 Domain of Human Nuclear factor erythroid 2-related factor 2 (NRF2)

Deposition date:

2021-04-13

Original release date:

2021-09-24

Authors:

Brueschweiler, S.

Citation:

Citation: Bruschweiler, Sven; Fuchs, Julian; Bader, Gerd; McConnell, Darryl; Konrat, Robert; Mayer, Moriz. "A Step toward NRF2-DNA Interaction Inhibitors by Fragment-Based NMR Methods" ChemMedChem 16, 3576-3587 (2021).
PubMed: 34524728

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9422.029 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAKHSSRLEAHLTRDELRAK ALHIPFPVEKIINLPVVDFN EMMSKEQFNEAQLALIRDIR RRGKNKVAAQNCRKRKLENI V

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	209
15N chemical shifts	61
1H chemical shifts	258

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 81 residues - 9422.029 Da.

1

GLY

ALA

LYS

HIS

SER

ARG

LEU

GLU

ALA

2

HIS

LEU

THR

ARG

ASP

GLU

LEU

ARG

ALA

LYS

3

ALA

LEU

HIS

ILE

PRO

PHE

PRO

VAL

GLU

LYS

4

ILE

ASN

LEU

PRO

VAL

ASP

PHE

ASN

5

GLU

MET

SER

LYS

GLU

GLN

PHE

ASN

GLU

6

ALA

GLN

LEU

ALA

LEU

ILE

ARG

ASP

ILE

ARG

7

ARG

GLY

LYS

ASN

LYS

VAL

ALA

GLN

8

ASN

CYS

ARG

LYS

ARG

LYS

LEU

GLU

ASN

ILE

9

VAL

Samples:

sample_1: neh1, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D (H)CCONNH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CCNMR, Skinner, Fogh, Boucher, Ragan, Mureddu, and Vuister - data analysis

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

Bruker AVANCE III HD 800 MHz
Bruker Avance NOE 600 MHz

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