BMRB Entry 25872

Name: TrkA transmembrane domain NMR structure in DPC micelles
Published: 2016-11-03

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PDB ID: 2n90
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25872
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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:

TrkA transmembrane domain NMR structure in DPC micelles

Deposition date:

2015-10-29

Original release date:

2016-11-03

Authors:

Nadezhdin, Kirill; Goncharuk, Sergey; Arseniev, Alexander

Citation:

Citation: Nadezhdin, Kirill; Goncharuk, Sergey; Arseniev, Alexander; Vilar, Marcial. "TrkA transmembrane domain NMR structure in DPC micelles" .

Assembly members:

Assembly members:
entity, polymer, 39 residues, 4214.127 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: cell free synthesis Host organism: E. coli - cell free Vector: pGEMEX-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKKDETPFGVSVAVGLAVFA CLFLSTLLLVLNKAGRRNK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	154
15N chemical shifts	37
1H chemical shifts	277

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 39 residues - 4214.127 Da.

1

MET

LYS

ASP

GLU

THR

PRO

PHE

GLY

VAL

2

SER

VAL

ALA

VAL

GLY

LEU

ALA

VAL

PHE

ALA

3

CYS

LEU

PHE

LEU

SER

THR

LEU

VAL

4

LEU

ASN

LYS

ALA

GLY

ARG

ASN

LYS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; entity 1 mM; DPC, [U-100% 2H], 40 mM; potassium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - visualization

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

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