BMRB Entry 51344

Name: TrkA-eJTM-TMD-5PG
Published: 2022-05-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51344

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

TrkA-eJTM-TMD-5PG

Deposition date:

2022-03-02

Original release date:

2022-05-27

Authors:

Kot, Erik; Vasilieva, Ekaterina; Shabalkina, Alexandra; 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: GSDNPFEFNGEDGIGVSFSG VDTNSTSGDGVEKKDETPFG VSVAVGLAVFACLFLSTLLL VLNKAGRRNK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	158
15N chemical shifts	64
1H chemical shifts	64

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TrkA-eJTM-TMD-5PG	1

Entities:

Entity 1, TrkA-eJTM-TMD-5PG 70 residues - Formula weight is not available

1	GLY	SER	ASP	ASN	PRO	PHE	GLU	PHE	ASN	GLY
2	GLU	ASP	GLY	ILE	GLY	VAL	SER	PHE	SER	GLY
3	VAL	ASP	THR	ASN	SER	THR	SER	GLY	ASP	GLY
4	VAL	GLU	LYS	LYS	ASP	GLU	THR	PRO	PHE	GLY
5	VAL	SER	VAL	ALA	VAL	GLY	LEU	ALA	VAL	PHE
6	ALA	CYS	LEU	PHE	LEU	SER	THR	LEU	LEU	LEU
7	VAL	LEU	ASN	LYS	ALA	GLY	ARG	ARG	ASN	LYS

Samples:

sample_1: TrkA-eJTM-TMD-5PG, [U-100% 13C; U-100% 15N], 0.30 mM; DMPC 25.0 mM; CHAPS 55.4 mM; sodium phosphate buffer 50 mM; D2O, [U-2H], 5 % v/v; TSP, d4, 0.5 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 6.4; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_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

1	GLY	SER	ASP	ASN	PRO	PHE	GLU	PHE	ASN	GLY
2	GLU	ASP	GLY	ILE	GLY	VAL	SER	PHE	SER	GLY
3	VAL	ASP	THR	ASN	SER	THR	SER	GLY	ASP	GLY
4	VAL	GLU	LYS	LYS	ASP	GLU	THR	PRO	PHE	GLY
5	VAL	SER	VAL	ALA	VAL	GLY	LEU	ALA	VAL	PHE
6	ALA	CYS	LEU	PHE	LEU	SER	THR	LEU	LEU	LEU
7	VAL	LEU	ASN	LYS	ALA	GLY	ARG	ARG	ASN	LYS

1	GLY	SER	ASP	ASN	PRO	PHE	GLU	PHE	ASN	GLY
2	GLU	ASP	GLY	ILE	GLY	VAL	SER	PHE	SER	GLY
3	VAL	ASP	THR	ASN	SER	THR	SER	GLY	ASP	GLY
4	VAL	GLU	LYS	LYS	ASP	GLU	THR	PRO	PHE	GLY
5	VAL	SER	VAL	ALA	VAL	GLY	LEU	ALA	VAL	PHE
6	ALA	CYS	LEU	PHE	LEU	SER	THR	LEU	LEU	LEU
7	VAL	LEU	ASN	LYS	ALA	GLY	ARG	ARG	ASN	LYS

1	GLY	SER	ASP	ASN	PRO	PHE	GLU	PHE	ASN	GLY
2	GLU	ASP	GLY	ILE	GLY	VAL	SER	PHE	SER	GLY
3	VAL	ASP	THR	ASN	SER	THR	SER	GLY	ASP	GLY
4	VAL	GLU	LYS	LYS	ASP	GLU	THR	PRO	PHE	GLY
5	VAL	SER	VAL	ALA	VAL	GLY	LEU	ALA	VAL	PHE
6	ALA	CYS	LEU	PHE	LEU	SER	THR	LEU	LEU	LEU
7	VAL	LEU	ASN	LYS	ALA	GLY	ARG	ARG	ASN	LYS