BMRB Entry 30909

Name: Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles
Published: 2021-08-09

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PDB ID: 7my8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30909
MolProbity Validation Chart

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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:

Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles

Deposition date:

2021-05-20

Original release date:

2021-08-09

Authors:

Koppisetti, R.; Fulcher, Y.; Van Doren, S.

Citation:

Citation: Koppisetti, R.; Fulcher, Y.; Van Doren, S.. "Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles" J. Am. Chem. Soc. 143, 13205-13211 (2021).
PubMed: 34375093

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4585.220 Da.

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: recombinant technology Host organism: Escherichia phage Ecwhy_1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SFIEDLLFNKVTLADAGFIK QYGDCLGDVAARDLICAQKF NG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	176
15N chemical shifts	41
1H chemical shifts	271

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 42 residues - 4585.220 Da.

1

SER

PHE

ILE

GLU

ASP

LEU

PHE

ASN

LYS

2

VAL

THR

LEU

ALA

ASP

ALA

GLY

PHE

ILE

LYS

3

GLN

TYR

GLY

ASP

CYS

LEU

GLY

ASP

VAL

ALA

4

ALA

ARG

ASP

LEU

ILE

CYS

ALA

GLN

LYS

PHE

5

ASN

GLY

Samples:

sample_1: Spike Fusion Peptide, Bicelles, [U-99% 15N], 0.4 mM

sample_2: Spike Fusion Peptide, Bicelles, [U-99% 13C; U-99% 15N], 0.4 mM

sample_conditions_1: ionic strength: 0 M; pH: 5.0; pressure: 0 Pa; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 15N Separated NOESY	sample_2	isotropic	sample_conditions_1
3D 13C Separated NOESY	sample_2	isotropic	sample_conditions_1
3D 13C TROSY edited NOESY	sample_2	isotropic	sample_conditions_1
2D 13C (Hb)Cb(CgCd)Hd	sample_2	isotropic	sample_conditions_1
2D 13C (Hb)Cb(CgCd)He	sample_2	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY, Woonghee Lee , Marco Tonelli , John L Markley - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

GROMACS, Berendsen - refinement

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 800 MHz

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