BMRB Entry 34753

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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/BMR34753
MolProbity Validation Chart

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Title:
Solution structure of TLR9 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, 5805.931 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: MEALSWDCFALSLLAVALGL GVPMLHHLCGWDLWYCFHLC LAWLPWRGRQ

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts53
1H chemical shifts336

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 50 residues - 5805.931 Da.

1   METGLUALALEUSERTRPASPCYSPHEALA
2   LEUSERLEULEUALAVALALALEUGLYLEU
3   GLYVALPROMETLEUHISHISLEUCYSGLY
4   TRPASPLEUTRPTYRCYSPHEHISLEUCYS
5   LEUALATRPLEUPROTRPARGGLYARGGLN

Samples:

sample_1: protein, [U-13C; U-15N], 1000 uM; LPPC 119 mM; LPPG 41 mM; potassium phosphate 20 mM; TCEP 5 mM; TSP 1 mM

sample_2: protein, [U-15N], 180 uM; LPPC 84 mM; LPPG 22 mM; potassium phosphate 30 mM; TCEP 5 mM; TSP 1 mM; dGpG 28 mg/mL; potassium chloride 80 mM; sodium azide 0.05 % w/v

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

sample_conditions_2: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

Experiments:

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

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - 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

PyMOL, Schrodinger, Inc. - data analysis

MOLMOL, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • 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