BMRB Entry 27680

Name: 1H/13C/15N Assignments for the TM domains of the KcsA potassium channel
Published: 2019-11-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27680

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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 TM domains of the KcsA potassium channel

Deposition date:

2018-11-05

Original release date:

2019-11-05

Authors:

Medeiros-Silva, Joao; Jekhmane, Shehrazade; Li, Jing; Kummerer, Felix; Muller-Hermes, Christoph; Baldus, Marc; Roux, Benoit; Weingarth, Markus

Citation:

Citation: Jekhmane, Shehrazade; Medeiros-Silva, Joao; Li, Jing; Kummerer, Felix; Muller-Hermes, Christoph; Baldus, Marc; Roux, Benoit; Weingarth, Markus. "Shifts in the selectivity filter dynamics cause modal gating in K+ channels" Nat. Commun. 10, 123-123 (2019).
PubMed: 30631074

Assembly members:

Assembly members:
KcsA_E71Q, polymer, 166 residues, 17694 Da.

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):
KcsA_E71Q: MPPMLSGLLARLVKLLLGRH GSALHWRAAGAATVLLVIVL LAGSYLAVLAERGAPGAQLI TYPRALWWSVQTATTVGYGD LYPVTLWGRLVAVVVMVAGI TSFGLVTAALATWFVGREQE RRGHFVRHSEKAAEEAYTRT TRALHERFDRLERMLDDNRR HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	77
15N chemical shifts	30
1H chemical shifts	31

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KcsA Monomer E71Q, 1	1
2	KcsA Monomer E71Q, 2	1
3	KcsA Monomer E71Q, 3	1
4	KcsA Monomer E71Q, 4	1

Entities:

Entity 1, KcsA Monomer E71Q, 1 166 residues - 17694 Da.

Residues 1-27; 51-61; 82-87; 112-160 are in contact with the cytoplasmic/extracellular environment Residues 28-50; 62-81;88-111 are embedded in the membrane Residues 74-80 form the filter Residues 161-166 form the His-Tag

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

GLN

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 E71Q, [U-100% 13C; U-100% 15N], 1.5 ± 0.3 mg; Potassium phosphate 15 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.0.2, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

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

UNP	P0A334
EMBL	1f6g
NCBI	1916
PIR	S60172
PDB	1BL8
AlphaFold	Q54397