BMRB Entry 34750

Name: Solution structure of TLR2 transmembrane and cytoplasmic juxtamembrane regions
Published: 2023-03-14

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PDB ID: 8ar0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34750
MolProbity Validation Chart

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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 structure of TLR2 transmembrane and cytoplasmic juxtamembrane regions

Deposition date:

2022-08-15

Original release date:

2023-03-14

Authors:

Kornilov, F.; Shabalkina, A.; Goncharuk, M.; Goncharuk, S.; Arseniev, A.; Mineev, K.

Citation:

Citation: Kornilov, F.; Shabalkina, A.; Cong, L.; Volynsky, P.; Kot, E.; Kayushin, A.; Lushpa, V.; Goncharuk, M.; Arseniev, A.; Goncharuk, S.; Xiaohui, W.; Mineev, K.. "The Architecture of Transmembrane and Cytoplasmic Juxtamembrane regions of Toll-like receptors" .

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 5852.218 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: MSVSECHRTALVSGMCCALF LLILLTGVLCHRFHGLWYMK MMWAWLQAKR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	222
15N chemical shifts	50
1H chemical shifts	359

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 50 residues - 5852.218 Da.

1	MET	SER	VAL	SER	GLU	CYS	HIS	ARG	THR	ALA
2	LEU	VAL	SER	GLY	MET	CYS	CYS	ALA	LEU	PHE
3	LEU	LEU	ILE	LEU	LEU	THR	GLY	VAL	LEU	CYS
4	HIS	ARG	PHE	HIS	GLY	LEU	TRP	TYR	MET	LYS
5	MET	MET	TRP	ALA	TRP	LEU	GLN	ALA	LYS	ARG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic constant time	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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-COSY aromatic	sample_1	isotropic	sample_conditions_1
2D CBHD aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic constant time	sample_1	isotropic	sample_conditions_1
3D hCCH-TOCSY constant time	sample_1	isotropic	sample_conditions_1
3D HCcH-TOCSY constant time	sample_1	isotropic	sample_conditions_1
2D 1H-15N IPAP-HSQC	sample_2	anisotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	anisotropic	sample_conditions_2

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

BMRB Entry 34750

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	SER	VAL	SER	GLU	CYS	HIS	ARG	THR	ALA
2	LEU	VAL	SER	GLY	MET	CYS	CYS	ALA	LEU	PHE
3	LEU	LEU	ILE	LEU	LEU	THR	GLY	VAL	LEU	CYS
4	HIS	ARG	PHE	HIS	GLY	LEU	TRP	TYR	MET	LYS
5	MET	MET	TRP	ALA	TRP	LEU	GLN	ALA	LYS	ARG

1	MET	SER	VAL	SER	GLU	CYS	HIS	ARG	THR	ALA
2	LEU	VAL	SER	GLY	MET	CYS	CYS	ALA	LEU	PHE
3	LEU	LEU	ILE	LEU	LEU	THR	GLY	VAL	LEU	CYS
4	HIS	ARG	PHE	HIS	GLY	LEU	TRP	TYR	MET	LYS
5	MET	MET	TRP	ALA	TRP	LEU	GLN	ALA	LYS	ARG

1	MET	SER	VAL	SER	GLU	CYS	HIS	ARG	THR	ALA
2	LEU	VAL	SER	GLY	MET	CYS	CYS	ALA	LEU	PHE
3	LEU	LEU	ILE	LEU	LEU	THR	GLY	VAL	LEU	CYS
4	HIS	ARG	PHE	HIS	GLY	LEU	TRP	TYR	MET	LYS
5	MET	MET	TRP	ALA	TRP	LEU	GLN	ALA	LYS	ARG