BMRB Entry 15677

Title:
Solubilization of transmembrane proteins in water: structural studies of a water-soluble analogue of the potassium channel KcsA
Deposition date:
2008-02-29
Original release date:
2008-11-10
Authors:
Ma, Dejian; Xu, Yan; Tillman, Tommy; Tang, Pei; Meirovitch, Eva; Eckenhoff, Roderic; Carnini, Anna
Citation:

Citation: Ma, Dejian; Tillman, Tommy; Tang, Pei; Meirovitch, Eva; Eckenhoff, Roderic; Carnini, Anna; Xu, Yan. "NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA"  Proc. Natl. Acad. Sci. U. S. A. 105, 16537-16542 (2008).
PubMed: 18948596

Assembly members:

Assembly members:
WSK3, polymer, 103 residues, 11404.746 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24a

Data sets:
Data typeCount
13C chemical shifts411
15N chemical shifts113
1H chemical shifts744

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41

Entities:

Entity 1, entity_1 103 residues - 11404.746 Da.

This is the water-soluble analogue of transmembrane domain of potassium channel KcsA

1   SERALAASPHISGLUARGGLUALAGLNLYS
2   ALAGLUGLUGLULEUGLNLYSVALLEUGLU
3   GLUALASERLYSLYSALAVALGLUALAGLU
4   ARGGLYALAPROGLYALAALALEUILESER
5   TYRPROASPALAILETRPTRPSERVALGLU
6   THRALATHRTHRVALGLYTYRGLYASPARG
7   TYRPROVALTHRGLUGLUGLYARGLYSVAL
8   ALAGLUGLNVALMETLYSALAGLYILEGLU
9   VALPHEALALEUVALTHRALAALALEUALA
10   THRASPPHEVALARGARGGLUGLUGLUARG
11   ARGGLYHIS

Samples:

wsk3_15N: WSK3_15N, [U-15N], 0.2 mM; D2O, [U-2H], 55 M; DSS 0.2 mM

wsk3_13C15N: wsk3, [U-13C; U-15N], 0.2 mM; D2O, [U-2H], 55 M; DSS 0.2 mM

sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCwsk3_13C15Nisotropicsample_conditions_1
3D CBCA(CO)NHwsk3_13C15Nisotropicsample_conditions_1
3D HNCOwsk3_13C15Nisotropicsample_conditions_1
3D HNCAwsk3_13C15Nisotropicsample_conditions_1
3D HNCACBwsk3_13C15Nisotropicsample_conditions_1
3D HCCH-TOCSYwsk3_13C15Nisotropicsample_conditions_1
T1, T2, hetNOEwsk3_13C15Nisotropicsample_conditions_1
R2 dispersionwsk3_13C15Nisotropicsample_conditions_1
diffusion measurementwsk3_13C15Nisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TOPSPIN v1.3, Bruker Biospin - collection

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, peak picking, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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