BMRB Entry 34027

Name: NMR spatial structure of Tk-hefu peptide
Published: 2017-08-11

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PDB ID: 5lm0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34027
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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:

NMR spatial structure of Tk-hefu peptide

Deposition date:

2016-07-28

Original release date:

2017-08-11

Authors:

Mineev, K.; Berkut, A.; Novikova, E.; Oparin, P.; Grishin, E.; Arseniev, A.; Vassilevski, A.

Citation:

Citation: Berkut, Antonina; Chugunov, Anton; Mineev, Konstantin; Peigneur, Steve; Tabakmakher, Valentin; Krylov, Nikolay; Oparin, Peter; Lihonosova, Alyona; Novikova, Ekaterina; Arseniev, Alexander; Grishin, Eugene; Tytgat, Jan; Efremov, Roman; Vassilevski, Alexander. "Protein surface topography as a tool to enhance the selective activity of a potassium channel blocker" J. Biol. Chem. 294, 18349-18359 (2019).
PubMed: 31533989

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 3565.082 Da.

Natural source:

Natural source: Common Name: Wheat Taxonomy ID: 376535 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum kiharae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADDRCYRMCQRYHDRREKKQ CKEGCRYG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	10
15N chemical shifts	34
1H chemical shifts	174

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 28 residues - 3565.082 Da.

1

ALA

ASP

ARG

CYS

TYR

ARG

MET

CYS

GLN

2

ARG

TYR

HIS

ASP

ARG

GLU

LYS

GLN

3

CYS

LYS

GLU

GLY

CYS

ARG

TYR

GLY

Samples:

sample_1: Tk-hefu, [U-99% 15N], 1 mM; sodium azide 0.001%

sample_conditions_1: ionic strength: 20 mM; pH: 5.7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9.4, Keller and Wuthrich - chemical shift assignment

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.2, Bruker Biospin - processing

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