BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16354

Title: NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii   PubMed: 19760172

Authors: Gayen, Shovanlal; Balakrishna, Asha; Gruber, Gerhard

Citation: Gayen, Shovanlal; Balakrishna, Asha; Gruber, Gerhard. "NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii."  J. Bioenerg. Biomembr. 41, 343-348 (2009).

Assembly members:
E(1-52), polymer, 52 residues, Formula weight is not available

Natural source:   Common Name: Methanococcus jannaschii   Taxonomy ID: 2190   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanococcus jannaschii

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

Entity Sequences (FASTA):
E(1-52): MAVKLMGVDKIKSKILDDAK AEANKIISEAEAEKAKILEK AKEEAEKRKAEI

Data sets:
Data typeCount
13C chemical shifts155
15N chemical shifts52
1H chemical shifts377

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E subunit1

Entities:

Entity 1, E subunit 52 residues - Formula weight is not available

1   METALAVALLYSLEUMETGLYVALASPLYS
2   ILELYSSERLYSILELEUASPASPALALYS
3   ALAGLUALAASNLYSILEILESERGLUALA
4   GLUALAGLULYSALALYSILELEUGLULYS
5   ALALYSGLUGLUALAGLULYSARGLYSALA
6   GLUILE

Samples:

sample_1: sodium phosphate 25 mM; D2O 10%; sodium azide 0.1 mM; TFE 60%; H2O 90%

sample_conditions_1: ionic strength: 0 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

TOPSPIN v2.1, Bruker Biospin - collection

Molmol, Koradi, Billeter and Wuthrich - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAB98203 AIJ06424
REF WP_048202497
SP Q57673