BMRB Entry 27029

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignment for Human TRPV1 Sensing Domain
Published: 2021-11-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27029

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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 1H, 13C, and 15N Chemical Shift Assignment for Human TRPV1 Sensing Domain

Deposition date:

2017-02-09

Original release date:

2021-11-17

Authors:

Kim, Minjoo; Sisco, Nicholas; Van Horn, Wade

Citation:

Citation: Kim, Minjoo; Sisco, Nicholas; Hilton, Jacob; Montano, Camila; Castro, Manuel; Cherry, Brian; Levitus, Marcia; Van Horn, Wade. "Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing" Nat. Commun. 11, 4169-4169 (2020).
PubMed: 32820172

Assembly members:

Assembly members:
hV1-SD, polymer, 143 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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hV1-SD: GSPLNRLLQDKWDRFVKRIF YFNFLVYCLYMIIFTMAAYY RPVDGLPPFKMEKTGDYFRV TGEILSVLGGVYFFFRGIQY FLQRRPSMKTLFVDSYSEML FFLQSLFMLATVVLYFSHLK EYVASMVFSLALGWTNMLYY TRG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	328
15N chemical shifts	118
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hV1-SD monomer	1

Entities:

Entity 1, hV1-SD monomer 143 residues - Formula weight is not available

1

GLY

SER

PRO

LEU

ASN

ARG

LEU

GLN

ASP

2

LYS

TRP

ASP

ARG

PHE

VAL

LYS

ARG

ILE

PHE

3

TYR

PHE

ASN

PHE

LEU

VAL

TYR

CYS

LEU

TYR

4

MET

ILE

PHE

THR

MET

ALA

TYR

5

ARG

PRO

VAL

ASP

GLY

LEU

PRO

PHE

LYS

6

MET

GLU

LYS

THR

GLY

ASP

TYR

PHE

ARG

VAL

7

THR

GLY

GLU

ILE

LEU

SER

VAL

LEU

GLY

8

VAL

TYR

PHE

ARG

GLY

ILE

GLN

TYR

9

PHE

LEU

GLN

ARG

PRO

SER

MET

LYS

THR

10

LEU

PHE

VAL

ASP

SER

TYR

SER

GLU

MET

LEU

11

PHE

LEU

GLN

SER

LEU

PHE

MET

LEU

ALA

12

THR

VAL

LEU

TYR

PHE

SER

HIS

LEU

LYS

13

GLU

TYR

VAL

ALA

SER

MET

VAL

PHE

SER

LEU

14

ALA

LEU

GLY

TRP

THR

ASN

MET

LEU

TYR

15

THR

ARG

GLY

Samples:

sample_1: hV1-SD, [U-100% 13C; U-100% 15N], 0.9 mM; LPPG 2.5 % w/v; sodium phosphate 2.5 mM; EDTA 0.5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 850 MHz

UNP	Q8NER1
AlphaFold	Q9NY22