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 50428

Title: 1H, 13C, 15N solid-state MAS NMR assignments of influenza virus hemagglutinin stalk long alpha helix (LAH) antigen   PubMed: 33750007

Deposition date: 2020-08-06 Original release date: 2021-07-27

Authors: Jaudzems, Kristaps; Kirsteina, Anna; Schubeis, Tobias; Kazaks, Andris; Tars, Kaspars; Lesage, Anne; Pintacuda, Guido

Citation: Jaudzems, Kristaps; Kirsteina, Anna; Schubeis, Tobias; Casano, Gilles; Ouari, Olivier; Bogans, Janis; Kazaks, Andris; Tars, Kaspars; Lesage, Anne; Pintacuda, Guido. "Structural Analysis of an Antigen Chemically Coupled on Virus-Like Particles in Vaccine Formulation"  Angew. Chem. Int. Ed. Engl. 60, 12847-12851 (2021).

Assembly members:
entity_1, polymer, 58 residues, Formula weight is not available

Natural source:   Common Name: Influenza virus   Taxonomy ID: 11309   Superkingdom: Viruses   Kingdom: not available   Genus/species: Influenza Influenza virus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETDuet-1

Entity Sequences (FASTA):
entity_1: MEKRIENLNKKVDDGFLDIW TYNAELLVLLENERTLDYHD SNVKNLYEKVRSQLKNNA

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts48
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1stalk protein, chain 11
2stalk protein, chain 21
3stalk protein, chain 31

Entities:

Entity 1, stalk protein, chain 1 58 residues - Formula weight is not available

1   METGLULYSARGILEGLUASNLEUASNLYS
2   LYSVALASPASPGLYPHELEUASPILETRP
3   THRTYRASNALAGLULEULEUVALLEULEU
4   GLUASNGLUARGTHRLEUASPTYRHISASP
5   SERASNVALLYSASNLEUTYRGLULYSVAL
6   ARGSERGLNLEULYSASNASNALA

Samples:

sample_1: stalk protein, [U-100% 13C; U-100% 15N], 500 ± 200 mg/mL; ammonium sulfate saturated na

sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 283 K; temperature controller setting: 273 K

sample_conditions_2: pH: 8; pressure: 1 atm; temperature: 283 K; temperature controller setting: 265 K

Experiments:

NameSampleSample stateSample conditions
3D NCOCXsample_1isotropicsample_conditions_1
3D NCACXsample_1isotropicsample_conditions_1
3D CONCAsample_1isotropicsample_conditions_1
3D CANCOsample_1isotropicsample_conditions_1
2D DARRsample_1isotropicsample_conditions_1
2D RFDRsample_1isotropicsample_conditions_1
2D C(HH)Csample_1isotropicsample_conditions_1
3D N(HH)Csample_1isotropicsample_conditions_1
2D NCOsample_1isotropicsample_conditions_1
2D NCAsample_1isotropicsample_conditions_1
3D (H)NCAHsample_1isotropicsample_conditions_2
3D (H)CBCAHsample_1isotropicsample_conditions_2
3D (H)COCAHsample_1isotropicsample_conditions_2
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_2
2D 1H-13C CP-HSQCsample_1isotropicsample_conditions_2

Software:

TOPSPIN v3.5.7 - collection, processing

CARA v1.9.1 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III 1000 MHz

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