BMRB Entry 34109

Name: NMR structure of TLR4 transmembrane domain (624-657) in DPC micelles
Published: 2018-03-16

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PDB ID: 5nao
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34109
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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:

NMR structure of TLR4 transmembrane domain (624-657) in DPC micelles

Deposition date:

2017-02-28

Original release date:

2018-03-16

Authors:

Mineev, K.; Goncharuk, S.; Goncharuk, M.; Arseniev, A.

Citation:

Citation: Mineev, K.; Goncharuk, S.; Goncharuk, M.; Volynsky, P.; Novikova, E.; Aresinev, A.. "Spatial structure of TLR4 transmembrane domain in bicelles provides the insight into the receptor activation mechanism." Sci. Rep. 7, 6864-6864 (2017).
PubMed: 28761155

Assembly members:

Assembly members:
entity_1, polymer, 35 residues, 3903.716 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: MNITSQMNKTIIGVSVLSVL VVSVVAVLVYKFYFH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	158
15N chemical shifts	34
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	entity_1	1

Entities:

Entity 1, entity_1 35 residues - 3903.716 Da.

1

MET

ASN

ILE

THR

SER

GLN

MET

ASN

LYS

THR

2

ILE

GLY

VAL

SER

VAL

LEU

SER

VAL

LEU

3

VAL

SER

VAL

ALA

VAL

LEU

VAL

TYR

4

LYS

PHE

TYR

PHE

HIS

Samples:

sample_1: TLR4-TM, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; DPC, [U-99% 2H], 100 ± 1 mM; sodium phosphate 20 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment

TOPSPIN v3.5, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 800 MHz

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