BMRB Entry 51193

Name: Backbone resonance assignments of transmembrane domain of SARS-CoV-2 spike protein
Published: 2022-03-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51193

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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 of transmembrane domain of SARS-CoV-2 spike protein PubMed: 35162961

Deposition date: 2021-11-25 Original release date: 2022-03-10

Authors: Huang, Qiwei; Li, Qingxin; Kang, Congbao

Citation: Li, Qingxin; Huang, Qiwei; Kang, Congbao. "Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles" Int. J. Mol. Sci. 23, 1040-1040 (2022).

Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MQELGKYEQYIKWPWYIWLG FIAGLIAIVMVTIMLSSMTS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	113
15N chemical shifts	38
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S-TM	1

Entities:

Entity 1, S-TM 60 residues - Formula weight is not available

MGSSHHHHHHSSGLVPRGSHM are fusion tag. QEL.. (1201, 1202, 1203).

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	GLN	GLU	LEU	GLY	LYS	TYR	GLU	GLN	TYR
4	ILE	LYS	TRP	PRO	TRP	TYR	ILE	TRP	LEU	GLY
5	PHE	ILE	ALA	GLY	LEU	ILE	ALA	ILE	VAL	MET
6	VAL	THR	ILE	MET	LEU	SER	SER	MET	THR	SER

Samples:

sample_1: S-TM, [U-100% 13C; U-100% 15N], 0.8 ± 0.2 mM; sodium phosphate 20 mM; DPC 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRView - chemical shift assignment

CYANA - structure solution

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz

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

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	GLN	GLU	LEU	GLY	LYS	TYR	GLU	GLN	TYR
4	ILE	LYS	TRP	PRO	TRP	TYR	ILE	TRP	LEU	GLY
5	PHE	ILE	ALA	GLY	LEU	ILE	ALA	ILE	VAL	MET
6	VAL	THR	ILE	MET	LEU	SER	SER	MET	THR	SER

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	GLN	GLU	LEU	GLY	LYS	TYR	GLU	GLN	TYR
4	ILE	LYS	TRP	PRO	TRP	TYR	ILE	TRP	LEU	GLY
5	PHE	ILE	ALA	GLY	LEU	ILE	ALA	ILE	VAL	MET
6	VAL	THR	ILE	MET	LEU	SER	SER	MET	THR	SER

1	MET	GLY	SER	SER	HIS	HIS	HIS	HIS	HIS	HIS
2	SER	SER	GLY	LEU	VAL	PRO	ARG	GLY	SER	HIS
3	MET	GLN	GLU	LEU	GLY	LYS	TYR	GLU	GLN	TYR
4	ILE	LYS	TRP	PRO	TRP	TYR	ILE	TRP	LEU	GLY
5	PHE	ILE	ALA	GLY	LEU	ILE	ALA	ILE	VAL	MET
6	VAL	THR	ILE	MET	LEU	SER	SER	MET	THR	SER