BMRB Entry 51343

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51343

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Title:
TrkA_eJTM_TMD_wt
Deposition date:
2022-03-02
Original release date:
2022-05-27
Authors:
Kot, Erik; Vasilieva, Ekaterina; Shabalkina, Alexandra; Goncharuk, Sergey; Mineev, Konstantin
Citation:

Citation: Kot, Erik; Franco, Maria; Vasilieva, Ekaterina; Shabalkina, Alexandra; Arseniev, Alexander; Goncharuk, Sergey; Mineev, Konstantin; Vilar, Marcal. "Intrinsically disordered regions couple the ligand binding and kinase activation of Trk neurotrophin receptors"  iScience 25, 104348-104348 (2022).
PubMed: 35601915

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli   Vector: pGEMEX-1/H6tag

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDNPFEFNPEDPIPVSFSP VDTNSTSGDPVEKKDETPFG VSVAVGLAVFACLFLSTLLL VLNKAGRRNK

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts58
1H chemical shifts58

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TrkA-eJTM-TMD1

Entities:

Entity 1, TrkA-eJTM-TMD 70 residues - Formula weight is not available

1   GLYSERASPASNPROPHEGLUPHEASNPRO
2   GLUASPPROILEPROVALSERPHESERPRO
3   VALASPTHRASNSERTHRSERGLYASPPRO
4   VALGLULYSLYSASPGLUTHRPROPHEGLY
5   VALSERVALALAVALGLYLEUALAVALPHE
6   ALACYSLEUPHELEUSERTHRLEULEULEU
7   VALLEUASNLYSALAGLYARGARGASNLYS

Samples:

sample_1: TrkA-eJTM-TMD, [U-100% 13C; U-100% 15N], 0.30 mM; DMPC 21.5 mM; CHAPS 49.9 mM; Sodium phosphate buffer 50 mM; D2O, [U-2H], 5 % v/v; NaN3 0.01%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.4; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1

Software:

CARA - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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