BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15564

Title: GFT NMR based resonance assignment of membrane proteins: application to subunit c of E. coli F1F0 ATP synthase in LPPG micelles   PubMed: 18273680

Deposition date: 2007-11-26 Original release date: 2007-12-27

Authors: Zhang, Qi; Atreya, Hanudatta; Kamen, Doug; Girvin, Mark; Szypersk, Thomas

Citation: Zhang, Qi; Atreya, Hanudatta; Kamen, Douglas; Girvin, Mark; Szyperski, Thomas. "GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles"  J. Biomol. NMR 40, 157-163 (2008).

Assembly members:
subunit_c_of_E._coli_F1F0_ATP_synthas, polymer, 79 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEt 17b

Entity Sequences (FASTA):
subunit_c_of_E._coli_F1F0_ATP_synthas: MENLNMDLLYMAAAVMMGLA AIGAAIGIGILGGKFLEGAA RQPDLIPLLRTQFFIVMGLV NAIPMIAVGLGLYVMFAVA

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts80
1H chemical shifts575

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit c1

Entities:

Entity 1, subunit c 79 residues - Formula weight is not available

1   METGLUASNLEUASNMETASPLEULEUTYR
2   METALAALAALAVALMETMETGLYLEUALA
3   ALAILEGLYALAALAILEGLYILEGLYILE
4   LEUGLYGLYLYSPHELEUGLUGLYALAALA
5   ARGGLNPROASPLEUILEPROLEULEUARG
6   THRGLNPHEPHEILEVALMETGLYLEUVAL
7   ASNALAILEPROMETILEALAVALGLYLEU
8   GLYLEUTYRVALMETPHEALAVALALA

Samples:

sample_1: subunit c of E. coli F1F0 ATP synthas, [U-99% 13C; U-99% 15N], 0.9 mM; K-PO_4 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 320 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
(3,2)D HNNCOsample_1isotropicsample_conditions_1
(4,2)D HACA(CO)NHNsample_1isotropicsample_conditions_1
L-(4,3)D HNNCabCasample_1isotropicsample_conditions_1
L-(4,3)D HNN(CO)CabCasample_1isotropicsample_conditions_1
(4,3)D HCCHsample_1isotropicsample_conditions_1
3D 15N,13Calip,13Caro-resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
(5,3)D HN{N,CO}{CabCa}}sample_1isotropicsample_conditions_1
(5,3)D {CabCa}{CON}HNsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz

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