BMRB Entry 51353

Name: Backbone NMR assignment of the human TRPV1 ion channel N-terminal intrinsically disordered region
Published: 2022-06-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51353

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:

Backbone NMR assignment of the human TRPV1 ion channel N-terminal intrinsically disordered region

Deposition date:

2022-03-09

Original release date:

2022-06-06

Authors:

Goretzki, Benedikt; Wiedemann, Christoph; Hellmich, Ute

Citation:

Citation: Wiedemann, Christoph; Goretzki, Benedikt; Merz, Zoe; Tebbe, Frederike; Schmitt, Pauline; Hellmich, Ute. "Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels" Biomol. NMR Assignments 16, 289-296 (2022).
PubMed: 35666427

Assembly members:

Assembly members:
entity_1, polymer, 99 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: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKWSSTDLGAAADPLQKDTC PDPLDGDPNSRPPPAKPQLS TAKSRTRLFGKGDSEEAFPV DCPHEEGELDSCPTITVSPV ITIQRPGDGPTGARLLSQD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	280
15N chemical shifts	84
1H chemical shifts	319

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hsTRPV1-IDR	1

Entities:

Entity 1, hsTRPV1-IDR 99 residues - Formula weight is not available

1

LYS

TRP

SER

THR

ASP

LEU

GLY

ALA

2

ALA

ASP

PRO

LEU

GLN

LYS

ASP

THR

CYS

3

PRO

ASP

PRO

LEU

ASP

GLY

ASP

PRO

ASN

SER

4

ARG

PRO

ALA

LYS

PRO

GLN

LEU

SER

5

THR

ALA

LYS

SER

ARG

THR

ARG

LEU

PHE

GLY

6

LYS

GLY

ASP

SER

GLU

ALA

PHE

PRO

VAL

7

ASP

CYS

PRO

HIS

GLU

GLY

GLU

LEU

ASP

8

SER

CYS

PRO

THR

ILE

THR

VAL

SER

PRO

VAL

9

ILE

THR

ILE

GLN

ARG

PRO

GLY

ASP

GLY

PRO

10

THR

GLY

ALA

ARG

LEU

SER

GLN

ASP

Samples:

sample_1: hsTRPV1-IDR, [U-99% 13C; U-99% 15N], 300 uM; D2O, [U-99% 2H], 10%; DSS 0.1 mM; H2O 90%; TRIS 10 mM; sodium chloride 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.11 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CARA - chemical shift assignment

TOPSPIN - collection, processing

CcpNMR - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

UNP	Q8NER1-1
AlphaFold	Q9NY22