BMRB Entry 51147

Name: Backbone NMR assignments of the human TRPV4 intrinsically disordered N-terminus
Published: 2022-05-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51147

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 assignments of the human TRPV4 intrinsically disordered N-terminus

Deposition date:

2021-10-19

Original release date:

2022-05-05

Authors:

Goretzki, Benedikt; Tebbe, Frederike; Hellmich, Ute; Mitrovic, Sarah-Ana

Citation:

Citation: Goretzki, Benedikt; Tebbe, Frederike; Mitrovic, Sarah-Ana; Hellmich, Ute. "Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation" Biomol. NMR Assignments 16, 205-212 (2022).
PubMed: 35451798

Assembly members:

Assembly members:
entity_1, polymer, 147 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: ADSSEGPRAGPGEVAELPGD ESGTPGGEAFPLSSLANLFE GEDGSLSPSPADASRPAGPG DGRPNLRMKFQGAFRKGVPN PIDLLESTLYESSVVPGPKK APMDSLFDYGTYRHHSSDNK RWRKKIIEKQPQSPKAPAPQ PPPILKV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	419
15N chemical shifts	124
1H chemical shifts	467

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRPV4-IDR	1

Entities:

Entity 1, TRPV4-IDR 147 residues - Formula weight is not available

1

ALA

ASP

SER

GLU

GLY

PRO

ARG

ALA

GLY

2

PRO

GLY

GLU

VAL

ALA

GLU

LEU

PRO

GLY

ASP

3

GLU

SER

GLY

THR

PRO

GLY

GLU

ALA

PHE

4

PRO

LEU

SER

LEU

ALA

ASN

LEU

PHE

GLU

5

GLY

GLU

ASP

GLY

SER

LEU

SER

PRO

SER

PRO

6

ALA

ASP

ALA

SER

ARG

PRO

ALA

GLY

PRO

GLY

7

ASP

GLY

ARG

PRO

ASN

LEU

ARG

MET

LYS

PHE

8

GLN

GLY

ALA

PHE

ARG

LYS

GLY

VAL

PRO

ASN

9

PRO

ILE

ASP

LEU

GLU

SER

THR

LEU

TYR

10

GLU

SER

VAL

PRO

GLY

PRO

LYS

11

ALA

PRO

MET

ASP

SER

LEU

PHE

ASP

TYR

GLY

12

THR

TYR

ARG

HIS

SER

ASP

ASN

LYS

13

ARG

TRP

ARG

LYS

ILE

GLU

LYS

GLN

14

PRO

GLN

SER

PRO

LYS

ALA

PRO

ALA

PRO

GLN

15

PRO

ILE

LEU

LYS

VAL

Samples:

sample_1: TRPV4-IDR, [U-100% 13C; U-100% 15N], 200 uM; DSS 100 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 4.5; pressure: 1 atm; temperature: 298 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9.1.4 - chemical shift assignment

TOPSPIN v4.1 - processing

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 900 MHz