BMRB Entry 51355

Name: Backbone and side-chain NMR assignment of the human TRPV3 ion channel N-terminal intrinsically disordered region
Published: 2022-06-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51355

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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:

Backbone and side-chain NMR assignment of the human TRPV3 ion channel N-terminal intrinsically disordered region

Deposition date:

2022-03-09

Original release date:

2022-06-06

Authors:

Wiedemann, Christoph; Goretzki, Benedikt; Merz, Zoe; Schmitt, Pauline; Tebbe, Frederike; 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, 118 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: KAHPKEMVPLMGKRVAAPSG NPAILPEKRPAEITPTKKSA HFFLEIEGFEPNPTVAKTSP PVFSKPMDSNIRQCISGNCD DMDSPQSPQDDVTETPSNPN SPSAQLAKEEQRRKKRRL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	458
15N chemical shifts	99
1H chemical shifts	620

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hsTRPV3-IDR	1

Entities:

Entity 1, hsTRPV3-IDR 118 residues - Formula weight is not available

1

LYS

ALA

HIS

PRO

LYS

GLU

MET

VAL

PRO

LEU

2

MET

GLY

LYS

ARG

VAL

ALA

PRO

SER

GLY

3

ASN

PRO

ALA

ILE

LEU

PRO

GLU

LYS

ARG

PRO

4

ALA

GLU

ILE

THR

PRO

THR

LYS

SER

ALA

5

HIS

PHE

LEU

GLU

ILE

GLU

GLY

PHE

GLU

6

PRO

ASN

PRO

THR

VAL

ALA

LYS

THR

SER

PRO

7

PRO

VAL

PHE

SER

LYS

PRO

MET

ASP

SER

ASN

8

ILE

ARG

GLN

CYS

ILE

SER

GLY

ASN

CYS

ASP

9

ASP

MET

ASP

SER

PRO

GLN

SER

PRO

GLN

ASP

10

ASP

VAL

THR

GLU

THR

PRO

SER

ASN

PRO

ASN

11

SER

PRO

SER

ALA

GLN

LEU

ALA

LYS

GLU

12

GLN

ARG

LYS

ARG

LEU

Samples:

sample_1: hsTRPV3-IDR, [U-99% 13C; U-99% 15N], 300 uM; D2O, [U-99% 2H], 10%; DSS 0.1 mM; H2O 90%; sodium phosphate 10 mM; sodium chloride 300 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.31 M; pH: 6.2; 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 (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

UNP	Q8NET8-1
AlphaFold	Q8NFH2