BMRB Entry 51663

Name: Backbone resonance assignments for a 21-residue peptide corresponding to the SARS-CoV-2 spike C-terminal tail
Published: 2023-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51663

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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:

Backbone resonance assignments for a 21-residue peptide corresponding to the SARS-CoV-2 spike C-terminal tail

Deposition date:

2022-10-14

Original release date:

2023-12-19

Authors:

He, Yanan; Chen, Yihong; Dey, Debajit; Hasan, Saif; Orban, John

Citation:

Citation: Dey, Debajit; Qing, Enya; Chen, Yihong; He, Yanan; Jennings, Benjamin; Cohn, Whitaker; Singh, Suruchi; Gakhar, Lokesh; Schnicker, Nicholas; Pierce, Brian; Whitelegge, Julian; Doray, Balraj; Orban, John; Gallagher, Tom; Hasan, Saif. "A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs" Nat. Commun. 14, 8358-8358 (2023).
PubMed: 38102143

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, Formula weight is not available

Natural source:

Natural source: Common Name: SARS-CoV-2 Taxonomy ID: 2697049 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus HCoV-SARS

Experimental source:

Experimental source: Production method: bacterial expression Host organism: E. coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: CCKFDEDDSEPVLKGVKLHY T

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	57
15N chemical shifts	19
1H chemical shifts	19

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cov2	1

Entities:

Entity 1, cov2 21 residues - Formula weight is not available

1

CYS

LYS

PHE

ASP

GLU

ASP

SER

GLU

2

PRO

VAL

LEU

LYS

GLY

VAL

LYS

LEU

HIS

TYR

3

THR

Samples:

sample_1: 21-residue peptide corresponding to the SARS-CoV-2 spike C-terminal tail, [U-100% 13C 15N], 300 uM; potassium phosphate 100 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - data collection

NMRPipe - data processiing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

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