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 16890

Title: Structure of G61-101   PubMed: 20599533

Deposition date: 2010-04-22 Original release date: 2010-07-27

Authors: S., Rishikesan; Gruber, Gerhard

Citation: Rishikesan, Sankaranarayanan; Manimekalai, Malathy; Gruber, Gerhard. "The NMR solution structure of subunit G (G(61)(-)(101)) of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae."  Biochim. Biophys. Acta 1798, 1961-1968 (2010).

Assembly members:
G61-101, polymer, 43 residues, 4604.364 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
G61-101: MDNAGGVGELEKKAEAGVQG ELAEIKKIAEKKKDDVVKIL IET

Data sets:
Data typeCount
13C chemical shifts122
15N chemical shifts43
1H chemical shifts296

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1G61-1011

Entities:

Entity 1, G61-101 43 residues - 4604.364 Da.

1   METASPASNALAGLYGLYVALGLYGLULEU
2   GLULYSLYSALAGLUALAGLYVALGLNGLY
3   GLULEUALAGLUILELYSLYSILEALAGLU
4   LYSLYSLYSASPASPVALVALLYSILELEU
5   ILEGLUTHR

Samples:

sample_1: D2O 7%; TFE, [U-100% 2H], 30%; sodium phosphate 25 mM; sodium chloride 200 mM; G61-101, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 308 K

Experiments:

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

Software:

SPARKY v2.1, Goddard - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA23755
EMBL CAY80326
GB AAA74570 AAB68921 AHY77737 AJP39136 AJU16333
REF NP_011905
SP P48836
TPG DAA06731

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