BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27680

Title: 1H/13C/15N Assignments for the TM domains of the KcsA potassium channel   PubMed: 30631074

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: 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).

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

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PQE60

Entity Sequences (FASTA):
KcsA_E71Q: MPPMLSGLLARLVKLLLGRH GSALHWRAAGAATVLLVIVL LAGSYLAVLAERGAPGAQLI TYPRALWWSVQTATTVGYGD LYPVTLWGRLVAVVVMVAGI TSFGLVTAALATWFVGREQE RRGHFVRHSEKAAEEAYTRT TRALHERFDRLERMLDDNRR HHHHHH

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts30
1H chemical shifts31

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1KcsA Monomer E71Q, 11
2KcsA Monomer E71Q, 21
3KcsA Monomer E71Q, 31
4KcsA Monomer E71Q, 41

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   METPROPROMETLEUSERGLYLEULEUALA
2   ARGLEUVALLYSLEULEULEUGLYARGHIS
3   GLYSERALALEUHISTRPARGALAALAGLY
4   ALAALATHRVALLEULEUVALILEVALLEU
5   LEUALAGLYSERTYRLEUALAVALLEUALA
6   GLUARGGLYALAPROGLYALAGLNLEUILE
7   THRTYRPROARGALALEUTRPTRPSERVAL
8   GLNTHRALATHRTHRVALGLYTYRGLYASP
9   LEUTYRPROVALTHRLEUTRPGLYARGLEU
10   VALALAVALVALVALMETVALALAGLYILE
11   THRSERPHEGLYLEUVALTHRALAALALEU
12   ALATHRTRPPHEVALGLYARGGLUGLNGLU
13   ARGARGGLYHISPHEVALARGHISSERGLU
14   LYSALAALAGLUGLUALATYRTHRARGTHR
15   THRARGALALEUHISGLUARGPHEASPARG
16   LEUGLUARGMETLEUASPASPASNARGARG
17   HISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
NHsample_1isotropicsample_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

Related Database Links:

UNP P0A334
EMBL 1f6g
NCBI 1916
PIR S60172
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts