BMRB Entry 34703

Name: Solution structure of Tk-hefu-11
Published: 2022-09-21

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PDB ID: 7qxj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34703
MolProbity Validation Chart

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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 structure of Tk-hefu-11

Deposition date:

2022-01-26

Original release date:

2022-09-21

Authors:

Mineev, K.; Lushpa, V.; Vassilevski, A.; Gigolaev, A.

Citation:

Citation: Gigolaev, Andrei; Lushpa, Vladislav; Pinheiro-Junior, Ernesto; Tabakmakher, Valentin; Peigneur, Steve; Ignatova, Anastasija; Feofanov, Alexey; Efremov, Roman; Mineev, Konstantin; Tytgat, Jan; Vassilevski, Alexander. "Artificial pore blocker acts specifically on voltage-gated potassium channel isoform K V 1.6" J. Biol. Chem. 298, 102467-102467 (2022).
PubMed: 36087839

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 3647.324 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: synthetic construct

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADKRCYRMCQRYHQRRQRRQ CKKGCRYG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	66
15N chemical shifts	35
1H chemical shifts	195

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 28 residues - 3647.324 Da.

1

ALA

ASP

LYS

ARG

CYS

TYR

ARG

MET

CYS

GLN

2

ARG

TYR

HIS

GLN

ARG

GLN

ARG

GLN

3

CYS

LYS

GLY

CYS

ARG

TYR

GLY

Samples:

sample_1: Tk-hefu-11 1 mM; sodium azide 0.0001%; sodium chloride 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	anisotropic	sample_conditions_1
2D TOCSY	sample_1	anisotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D HNHA	sample_1	anisotropic	sample_conditions_1
3D HNHB	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	anisotropic	sample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE 700 MHz

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