BMRB Entry 50428

Name: 1H, 13C, 15N solid-state MAS NMR assignments of influenza virus hemagglutinin stalk long alpha helix (LAH) antigen
Published: 2021-07-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50428

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

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:

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).
PubMed: 33750007

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEKRIENLNKKVDDGFLDIW TYNAELLVLLENERTLDYHD SNVKNLYEKVRSQLKNNA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	232
15N chemical shifts	48
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	stalk protein, chain 1	1
2	stalk protein, chain 2	1
3	stalk protein, chain 3	1

Entities:

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

1

MET

GLU

LYS

ARG

ILE

GLU

ASN

LEU

ASN

LYS

2

LYS

VAL

ASP

GLY

PHE

LEU

ASP

ILE

TRP

3

THR

TYR

ASN

ALA

GLU

LEU

VAL

LEU

4

GLU

ASN

GLU

ARG

THR

LEU

ASP

TYR

HIS

ASP

5

SER

ASN

VAL

LYS

ASN

LEU

TYR

GLU

LYS

VAL

6

ARG

SER

GLN

LEU

LYS

ASN

ALA

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:

Name	Sample	Sample state	Sample conditions
3D NCOCX	sample_1	isotropic	sample_conditions_1
3D NCACX	sample_1	isotropic	sample_conditions_1
3D CONCA	sample_1	isotropic	sample_conditions_1
3D CANCO	sample_1	isotropic	sample_conditions_1
2D DARR	sample_1	isotropic	sample_conditions_1
2D RFDR	sample_1	isotropic	sample_conditions_1
2D C(HH)C	sample_1	isotropic	sample_conditions_1
3D N(HH)C	sample_1	isotropic	sample_conditions_1
2D NCO	sample_1	isotropic	sample_conditions_1
2D NCA	sample_1	isotropic	sample_conditions_1
3D (H)NCAH	sample_1	isotropic	sample_conditions_2
3D (H)CBCAH	sample_1	isotropic	sample_conditions_2
3D (H)COCAH	sample_1	isotropic	sample_conditions_2
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C CP-HSQC	sample_1	isotropic	sample_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 peaks
SPARKY: Backbone or all simulated peaks