BMRB Entry 34610

Name: Solution structure of toll like receptor 1 (TLR1) TIR domain
Published: 2021-08-17

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PDB ID: 7nt7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34610
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 toll like receptor 1 (TLR1) TIR domain

Deposition date:

2021-03-09

Original release date:

2021-08-17

Authors:

Mineev, K.; Lushpa, V.; Goncharuk, M.

Citation:

Citation: Lushpa, Vladislav; Goncharuk, Marina; Lin, Cong; Zalevsky, Arthur; Talyzina, Irina; Luginina, Aleksandra; Vakhrameev, Daniil; Shevtsov, Mikhail; Goncharuk, Sergey; Arseniev, Alexander; Borshchevskiy, Valentin; Wang, Xiaohui; Mineev, Konstantin. "Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn 2+ ions" Commun. Biol. 4, 1003-1003 (2021).
PubMed: 34429510

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 19204.139 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: SNIPLEELQRNLQFHAFISY SGHDSFWVKNELLPNLEKEG MQICLHERNFVPGKSIVENI ITCIEKSYKSIFVLSPNFVQ SEWCHYELYFAHHNLFHEGS NSLILILLEPIPQYSIPSSY HKLKSLMARRTYLEWPKEKS KRGLFWANLRAAINIKLTEQ AKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	729
15N chemical shifts	160
1H chemical shifts	1192

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_1 163 residues - 19204.139 Da.

1

SER

ASN

ILE

PRO

LEU

GLU

LEU

GLN

ARG

2

ASN

LEU

GLN

PHE

HIS

ALA

PHE

ILE

SER

TYR

3

SER

GLY

HIS

ASP

SER

PHE

TRP

VAL

LYS

ASN

4

GLU

LEU

PRO

ASN

LEU

GLU

LYS

GLU

GLY

5

MET

GLN

ILE

CYS

LEU

HIS

GLU

ARG

ASN

PHE

6

VAL

PRO

GLY

LYS

SER

ILE

VAL

GLU

ASN

ILE

7

ILE

THR

CYS

ILE

GLU

LYS

SER

TYR

LYS

SER

8

ILE

PHE

VAL

LEU

SER

PRO

ASN

PHE

VAL

GLN

9

SER

GLU

TRP

CYS

HIS

TYR

GLU

LEU

TYR

PHE

10

ALA

HIS

ASN

LEU

PHE

HIS

GLU

GLY

SER

11

ASN

SER

LEU

ILE

LEU

ILE

LEU

GLU

PRO

12

ILE

PRO

GLN

TYR

SER

ILE

PRO

SER

TYR

13

HIS

LYS

LEU

LYS

SER

LEU

MET

ALA

ARG

14

THR

TYR

LEU

GLU

TRP

PRO

LYS

GLU

LYS

SER

15

LYS

ARG

GLY

LEU

PHE

TRP

ALA

ASN

LEU

ARG

16

ALA

ILE

ASN

ILE

LYS

LEU

THR

GLU

GLN

17

ALA

LYS

Samples:

sample_1: TLR1-TIR, [U-100% 13C; U-100% 15N], 0.8 mM; PIPES 20 mM; sodium chloride 25 mM; TCEP 3 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

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

qMDD v2.7, Orekhov, Mayzel - processing

TopSpin, Bruker Biospin - processing

NMR spectrometers:

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