BMRB Entry 19943

Title:
3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli
Deposition date:
2014-04-26
Original release date:
2014-06-23
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).
PubMed: 24958726

Assembly members:

Assembly members:
YgaP, polymer, 108 residues, 11716.429 Da.

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: pET3a-LIC

Data sets:
Data typeCount
1H chemical shifts707
13C chemical shifts306
15N chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YgaP1

Entities:

Entity 1, YgaP 108 residues - 11716.429 Da.

1   ALALEUTHRTHRILESERPROHISASPALA
2   GLNGLULEUILEALAARGGLYALALYSLEU
3   ILEASPILEARGASPALAASPGLUTYRLEU
4   ARGGLUHISILEPROGLUALAASPLEUALA
5   PROLEUSERVALLEUGLUGLNSERGLYLEU
6   PROALALYSLEUARGHISGLUGLNILEILE
7   PHEHISCYSGLNALAGLYLYSARGTHRSER
8   ASNASNALAASPLYSLEUALAALAILEALA
9   ALAPROALAGLUILEPHELEULEUGLUASP
10   GLYILEASPGLYTRPLYSLYSALAGLYLEU
11   PROVALALAVALASNLYSSERGLN

Samples:

sample_1: YgaP, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Herrmann, Guntert and Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 17137 19946 25085
PDB
DBJ BAB36952 BAE76780 BAG78445 BAI26930 BAI31960
EMBL CAP77107 CAQ33005 CAQ87965 CAQ99590 CAR04179
GB AAC75715 AAG57776 AAN44189 AAN81669 AAP18017
REF NP_311556 NP_417154 NP_708482 WP_001229433 WP_001229436
SP P55734
AlphaFold P55734

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