BMRB Entry 51180

Name: 1H/13C/15N Assignments for the transmembrane domains of the potassium channel KcsA WT
Published: 2022-03-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51180

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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:

1H/13C/15N Assignments for the transmembrane domains of the potassium channel KcsA WT

Deposition date:

2021-11-16

Original release date:

2022-03-07

Authors:

Rohaim, Ahmed; Vermeulen, Bram; Li, Jing; Kummerer, Felix; Napoli, Federico; Blachowicz, Lydia; Medeiros-Silva, Joao; Roux, Benoit; Weingarth, Markus

Citation:

Citation: Rohaim, Ahmed; Vermeulen, Bram; Li, Jing; Kummerer, Felix; Napoli, Federico; Blachowicz, Lydia; Medeiros-Silva, Joao; Roux, Benoit; Weingarth, Markus. "A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V" Nat. Commun. 13, 1574-1574 (2022).
PubMed: 35322021

Assembly members:

Assembly members:
entity_1, polymer, 166 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptomyces lividans Taxonomy ID: 1916 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces lividans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPPMLSGLLARLVKLLLGRH GSALHWRAAGAATVLLVIVL LAGSYLAVLAERGAPGAQLI TYPRALWWSVETATTVGYGD LYPVTLWGRLVAVVVMVAGI TSFGLVTAALATWFVGREQE RRGHFVRHSEKAAEEAYTRT TRALHERFDRLERMLDDNRR HHHHHH

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	227
15N chemical shifts	82
1H chemical shifts	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KcsA WT monomer 1	1
2	KcsA WT monomer 2	1
3	KcsA WT monomer 3	1
4	KcsA WT monomer 4	1

Entities:

Entity 1, KcsA WT monomer 1 166 residues - Formula weight is not available

1

MET

PRO

MET

LEU

SER

GLY

LEU

ALA

2

ARG

LEU

VAL

LYS

LEU

GLY

ARG

HIS

3

GLY

SER

ALA

LEU

HIS

TRP

ARG

ALA

GLY

4

ALA

THR

VAL

LEU

VAL

ILE

VAL

LEU

5

LEU

ALA

GLY

SER

TYR

LEU

ALA

VAL

LEU

ALA

6

GLU

ARG

GLY

ALA

PRO

GLY

ALA

GLN

LEU

ILE

7

THR

TYR

PRO

ARG

ALA

LEU

TRP

SER

VAL

8

GLU

THR

ALA

THR

VAL

GLY

TYR

GLY

ASP

9

LEU

TYR

PRO

VAL

THR

LEU

TRP

GLY

ARG

LEU

10

VAL

ALA

VAL

MET

VAL

ALA

GLY

ILE

11

THR

SER

PHE

GLY

LEU

VAL

THR

ALA

LEU

12

ALA

THR

TRP

PHE

VAL

GLY

ARG

GLU

GLN

GLU

13

ARG

GLY

HIS

PHE

VAL

ARG

HIS

SER

GLU

14

LYS

ALA

GLU

ALA

TYR

THR

ARG

THR

15

THR

ARG

ALA

LEU

HIS

GLU

ARG

PHE

ASP

ARG

16

LEU

GLU

ARG

MET

LEU

ASP

ASN

ARG

17

HIS

Samples:

sample_1: KcsA WT, [U-100% 13C; U-100% 15N], 1.5 ± 0.3 mg; potassium phosphate 15 mM; potassium chloride 100 mM

sample_2: KcsA WT, [U-100% 13C; U-100% 15N], 1.5 ± 0.3 mg; HEPES 20 mM; barium chloride 5 mM

sample_3: KcsA WT, [U-100% 13C; U-100% 15N], 1.5 ± 0.3 mg; sodium citrate 20 mM

sample_conditions_1: pH: 7.4; temperature: 305 K

sample_conditions_2: pH: 7; temperature: 305 K

sample_conditions_3: pH: 4; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D CC	sample_1	isotropic	sample_conditions_1
2D NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_2
2D CC	sample_2	isotropic	sample_conditions_2
2D NH	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_3	isotropic	sample_conditions_3
2D CC	sample_3	isotropic	sample_conditions_3
2D NH	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_3	isotropic	sample_conditions_3

Software:

TOPSPIN v4.0.2 - collection, data analysis, processing

NMRFAM-SPARKY - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz MHz
Bruker Avance 800 MHz MHz
Bruker Avance 950 MHz MHz

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