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 17000

Title: Structure of E1-69 of Yeast V-ATPase   PubMed: 21399923

Deposition date: 2010-06-14 Original release date: 2011-03-24

Authors: Sankaranarayanan, Rishikesan; Gruber, Gerhard

Citation: Rishikesan, Sankaranarayanan; Thaker, Youg; Gruber, Gerhard. "NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase."  J. Bioenerg. Biomembr. 43, 187-193 (2011).

Assembly members:
entity, polymer, 69 residues, 7908.008 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
entity: MASAITALTPNQVNDELNKM QAFIRKEAEEKAKEIQLKAD QEYEIEKTNIVRNETNNIDG NFKSKLKKA

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts68
1H chemical shifts427

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E1-691

Entities:

Entity 1, E1-69 69 residues - 7908.008 Da.

1   METALASERALAILETHRALALEUTHRPRO
2   ASNGLNVALASNASPGLULEUASNLYSMET
3   GLNALAPHEILEARGLYSGLUALAGLUGLU
4   LYSALALYSGLUILEGLNLEULYSALAASP
5   GLNGLUTYRGLUILEGLULYSTHRASNILE
6   VALARGASNGLUTHRASNASNILEASPGLY
7   ASNPHELYSSERLYSLEULYSLYSALA

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 2 mM; Na2PO4 25 mM; NaCl 200 mM; EDTA 5 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

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

Molmol, Koradi, Billeter and Wuthrich - structure solution

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA26638
EMBL CAA89978 CAA99654 CAY86613
GB AAA35209 AHY77605 AJP41835 AJT71258 AJT71746
REF NP_014977
SP P22203
TPG DAA11094

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