BMRB Entry 34169

Name: Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)
Published: 2019-03-28

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PDB ID: 5oqk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34169
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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:

Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)

Deposition date:

2017-08-12

Original release date:

2019-03-28

Authors:

Bayrhuber, M.; Maslennikov, I.; Kwiatowski, W.; Sobol, A.; Wierschem, C.; Eichmann, C.; Riek, R.

Citation:

Citation: Bayrhuber, Monika; Maslennikov, Innokentiy; Kwiatkowski, Witek; Sobol, Alexander; Wierschem, Christoph; Eichmann, Cedric; Frey, Lukas; Riek, Roland. "Nuclear Magnetic Resonance Solution Structure and Functional Behavior of the Human Proton Channel" Biochemistry 58, 4017-4027 (2019).
PubMed: 31365236

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 17352.062 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: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SHMRAPLDFRGMLRKLFSSH RFQVIIICLVVLDALLVLAE LILDLKIIQPDKNNYAAMVF HYMSITILVFFMMEIIFKLF VFRLEFFHHKFEILDAVVVV VSFILDIVLLFQEHQFEALG LLILLRLWRVARIINGIIIS VKTRSER

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	109
1H chemical shifts	711

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 147 residues - 17352.062 Da.

1

SER

HIS

MET

ARG

ALA

PRO

LEU

ASP

PHE

ARG

2

GLY

MET

LEU

ARG

LYS

LEU

PHE

SER

HIS

3

ARG

PHE

GLN

VAL

ILE

CYS

LEU

VAL

4

VAL

LEU

ASP

ALA

LEU

VAL

LEU

ALA

GLU

5

LEU

ILE

LEU

ASP

LEU

LYS

ILE

GLN

PRO

6

ASP

LYS

ASN

TYR

ALA

MET

VAL

PHE

7

HIS

TYR

MET

SER

ILE

THR

ILE

LEU

VAL

PHE

8

PHE

MET

GLU

ILE

PHE

LYS

LEU

PHE

9

VAL

PHE

ARG

LEU

GLU

PHE

HIS

LYS

10

PHE

GLU

ILE

LEU

ASP

ALA

VAL

11

VAL

SER

PHE

ILE

LEU

ASP

ILE

VAL

LEU

12

PHE

GLN

GLU

HIS

GLN

PHE

GLU

ALA

LEU

GLY

13

LEU

ILE

LEU

ARG

LEU

TRP

ARG

VAL

14

ALA

ARG

ILE

ASN

GLY

ILE

SER

15

VAL

LYS

THR

ARG

SER

GLU

ARG

Samples:

sample_1: Hv1/VSOP, [U-99% 13C; U-99% 15N; 50% 2H], 0.4 mM; MES 20 mM; BisTris 20 mM; FC-12 2 mM; LDAO 2 mM; TCEP 1 mM; ZnCl2 10 mM

sample_conditions_1: ionic strength: 30 mM; pH: 5.8; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	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

Software:

CYANA, Guntert P. - refinement

NMR spectrometers:

Bruker Avance 900 MHz

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