BMRB Entry 19940

Title:
Chemical shifts and structural constraints of outer membrane protein A
Deposition date:
2014-04-24
Original release date:
2014-04-29
Authors:
Arora, Ashish; Abildgaard, Frits; Bushweller, John; Cierpicki, Tomasz; Liang, Binyong; Tamm, Lukas
Citation:

Citation: Arora, Ashish; Abildgaard, Frits; Bushweller, John; Tamm, Lukas. "Structure of outer membrane protein A transmembrane domain by NMR spectroscopy"  Nat. Struct. Biol. 8, 334-338 (2001).

Assembly members:

Assembly members:
OmpA, polymer, 176 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET14b

Data sets:
Data typeCount
13C chemical shifts463
15N chemical shifts143
1H chemical shifts143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ompa1

Entities:

Entity 1, ompa 176 residues - Formula weight is not available

1   ALAPROLYSASPASNTHRTRPTYRTHRGLY
2   ALALYSLEUGLYPHESERGLNTYRHISASP
3   THRGLYPHEILEASNASNASNGLYPROTHR
4   HISGLUASNGLNLEUGLYALAGLYALAPHE
5   GLYGLYTYRGLNVALASNPROTYRVALGLY
6   PHEGLUMETGLYTYRASPPHELEUGLYARG
7   METPROTYRLYSGLYSERVALGLUASNGLY
8   ALATYRLYSALAGLNGLYVALGLNLEUTHR
9   ALALYSLEUGLYTYRPROILETHRASPASP
10   LEUASPILETYRTHRARGLEUGLYGLYMET
11   VALPHEARGALAASPTHRLYSSERASNVAL
12   TYRGLYLYSASNHISASPTHRGLYVALSER
13   PROVALPHEALAGLYGLYVALGLUTYRALA
14   ILETHRPROGLUILEALATHRARGLEUGLU
15   TYRGLNPHETHRASNASNILEGLYASPALA
16   HISTHRILEGLYTHRARGPROASPASNGLY
17   METLEUSERLEUGLYVALSERTYRARGPHE
18   GLYGLNGLYGLUALAALA

Samples:

sample_1: OmpA, [U-13C; U-15N; U-2H], 1 mM; NaCl 50 mM; potassium phosphate 10 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 19410
PDB
DBJ BAA35715 BAB34464 BAG76542 BAI24400 BAI29850
EMBL CAA23588 CAQ31485 CAR02310 CAR12355 CAU96868
GB AAC74043 AAF37887 AAG55443 AAP74759 AAQ96072
REF NP_309068 NP_415477 WP_000315442 WP_000630860 WP_000750416
SP P0A910 P0A911
AlphaFold P0A910 P0A911

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