BMRB Entry 19994

Title:
3D NMR structure of the transmembrane domain of the full-length inner membrane protein YgaP from Escherichia coli   PubMed: 24958726
Deposition date:
2014-05-29
Original release date:
2014-09-10
Authors:
Eichmann, Cedric; Tzitzilonis, Christos; Bordignon, Enrica; Maslennikov, Innokentiy; Choe, Senyon; Riek, Roland
Citation:

Citation: Eichmann, Cedric; Tzitzilonis, Christos; Bordignon, Enrica; Maslennikov, Innokentiy; Choe, Senyon; Riek, Roland. "Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli."  J. Biol. Chem. 289, 23482-23503 (2014).

Assembly members:

Assembly members:
entity, polymer, 68 residues, 7157.559 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a-LIC

Experimental source:

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a-LIC

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts298
15N chemical shifts61
13C chemical shifts12

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 68 residues - 7157.559 Da.

1   LYSSERGLNPROLEUPROLEUMETARGGLN
2   VALGLNILEALAALAGLYGLYLEUILELEU
3   ILEGLYVALVALLEUGLYTYRTHRVALASN
4   SERGLYPHEPHELEULEUSERGLYPHEVAL
5   GLYALAGLYLEULEUPHEALAGLYILESER
6   GLYPHESERGLYMETALAARGLEULEUASP
7   LYSMETPROTRPASNGLNARGALA

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; H2O 95%; D2O 5%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 273 K; pH: 7.0; pressure: 1 atm; ionic strength: 0 M

sample_conditions_2: temperature: 273 K; pH: 7.0; pressure: 1 atm; ionic strength: 0 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2

Software:

XEASY, Bartels et al. - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAB36952 BAE76780 BAG78445 BAI26930 BAI31960
EMBL CAP77107 CAQ33005 CAQ99590 CAR04179 CAR09287
GB AAC75715 AAG57776 AAN44189 AAN81669 AAP18017
REF NP_311556 NP_417154 NP_708482 WP_001229436 WP_001229438
SP P55734
AlphaFold P55734

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