BMRB Entry 19892

Title:
REFINED STRUCTURE OF OUTER MEMBRANE PROTEIN X IN NANODISC BY MEASURING RESIDUAL DIPOLAR COUPLINGS   PubMed: 24752984
Deposition date:
2014-04-05
Original release date:
2015-03-16
Authors:
Bibow, S.; Carneiro, M.; Sabo, T.; Schwiegk, C.; Becker, S.; Riek, R.; Lee, D.
Citation:

Citation: Bibow, S.; Carneiro, M.; Sabo, T.; Schwiegk, C.; Becker, S.; Riek, R.; Lee, D.. "Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings"  Protein Sci. 23, .-851 (856).

Assembly members:

Assembly members:
OUTER_MEMBRANE_PROTEIN_X, polymer, 148 residues, 16371.898 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET3b

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET3b

Data sets:
Data typeCount
15N chemical shifts117
1H chemical shifts118

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OUTER MEMBRANE PROTEIN X1

Entities:

Entity 1, OUTER MEMBRANE PROTEIN X 148 residues - 16371.898 Da.

1   ALATHRSERTHRVALTHRGLYGLYTYRALA
2   GLNSERASPALAGLNGLYGLNMETASNLYS
3   METGLYGLYPHEASNLEULYSTYRARGTYR
4   GLUGLUASPASNSERPROLEUGLYVALILE
5   GLYSERPHETHRTYRTHRGLULYSSERARG
6   THRALASERSERGLYASPTYRASNLYSASN
7   GLNTYRTYRGLYILETHRALAGLYPROALA
8   TYRARGILEASNASPTRPALASERILETYR
9   GLYVALVALGLYVALGLYTYRGLYLYSPHE
10   GLNTHRTHRGLUTYRPROTHRTYRLYSASN
11   ASPTHRSERASPTYRGLYPHESERTYRGLY
12   ALAGLYLEUGLNPHEASNPROMETGLUASN
13   VALALALEUASPPHESERTYRGLUGLNSER
14   ARGILEARGSERVALASPVALGLYTHRTRP
15   ILEALAGLYVALGLYTYRARGPHE

Samples:

sample_1: OUTER MEMBRANE PROTEIN X, [U-100% 13C; U-100% 15N], 0.5 mM; Tris-HCl 10 mM; sodium azide 0.05%; NaCl 100 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N COCAINEsample_1isotropicsample_conditions_1

Software:

X-_PLOR_NIH, SCHWIETERS, KUSZEWSKI, TJ - refinement

NMRPIPE, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - structure solution

TOPSPIN, Bruker Biospin - structure solution

SPARKY, Goddard - structure solution

NMR spectrometers:

  • BRUKER AVANCE I and AVANCE III 700. 800, 900 MHz

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