BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 34750

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PDB ID:
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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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: 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:
entity_1, polymer, 50 residues, 5852.218 Da.

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

Entity Sequences (FASTA):
entity_1: MSVSECHRTALVSGMCCALF LLILLTGVLCHRFHGLWYMK MMWAWLQAKR

Data sets:
Data typeCount
13C chemical shifts222
15N chemical shifts50
1H chemical shifts359

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 50 residues - 5852.218 Da.

1   METSERVALSERGLUCYSHISARGTHRALA
2   LEUVALSERGLYMETCYSCYSALALEUPHE
3   LEULEUILELEULEUTHRGLYVALLEUCYS
4   HISARGPHEHISGLYLEUTRPTYRMETLYS
5   METMETTRPALATRPLEUGLNALALYSARG

Samples:

sample_1: protein, [U-13C; U-15N], 200 uM; DMPC 23.27 mM; DMPG 5.87 mM; DHPC 78.16 mM; potassium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05 % w/v; TSP 1 mM

sample_2: protein, [U-15N], 188 uM; DMPC 24.23 mM; DMPG 5.50 mM; DHPC 80.18 mM; potassium phosphate 50 mM; TCEP 4 mM; sodium azide 0.05 % w/v; TSP 1 mM; dGpG 30 mg/mL; potassium chloride 100 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

sample_conditions_2: ionic strength: 235 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic constant timesample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSY aromaticsample_1isotropicsample_conditions_1
2D CBHD aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic constant timesample_1isotropicsample_conditions_1
3D hCCH-TOCSY constant timesample_1isotropicsample_conditions_1
3D HCcH-TOCSY constant timesample_1isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_2anisotropicsample_conditions_2
2D 1H-15N HSQCsample_2anisotropicsample_conditions_2

Software:

CYANA v3.98.13, Peter Guentert - structure calculation

TopSpin v3.0, Bruker Biospin - processing

CARA v1.9.7.1, Keller and Wuthrich - chemical shift assignment, peak picking

qMDD v3.2, Maxim Mayzel, Krzysztof Kazimierczuk, Vladislav Orekhov - processing

MOLMOL, Koradi, Billeter and Wuthrich - data analysis

PyMOL, Schrodinger, Inc. - data analysis

NMR spectrometers:

  • 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