BMRB Entry 36080

Name: NMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion
Published: 2018-02-06

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PDB ID: 5xjk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR36080
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion PubMed: 28988778

Deposition date: 2017-05-02 Original release date: 2018-02-06

Authors: Bhattacharjya, S.; Chatterjee, D.

Citation: Mahajan, Mukesh; Chatterjee, Deepak; Bhuvaneswari, Kannaian; Pillay, Shubhadra; Bhattacharjya, Surajit. "NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion" Biochim. Biophys. Acta 1860, 407-415 (2018).

Assembly members:
Spike protein S2, polymer, 65 residues, 7544.744 Da.

Natural source: Common Name: HCoV-SARS Taxonomy ID: 227859 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus SARS-related coronavirus

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

Entity Sequences (FASTA):
Spike protein S2: PRNTREVFAQVKQMYKTPTL KYFGGFNFSQILPSPLKPTK RSFIEDLLFNKVTLADAGFM KQYGE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	56
15N chemical shifts	56
1H chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 65 residues - 7544.744 Da.

1

PRO

ARG

ASN

THR

ARG

GLU

VAL

PHE

ALA

GLN

2

VAL

LYS

GLN

MET

TYR

LYS

THR

PRO

THR

LEU

3

LYS

TYR

PHE

GLY

PHE

ASN

PHE

SER

GLN

4

ILE

LEU

PRO

SER

PRO

LEU

LYS

PRO

THR

LYS

5

ARG

SER

PHE

ILE

GLU

ASP

LEU

PHE

ASN

6

LYS

VAL

THR

LEU

ALA

ASP

ALA

GLY

PHE

MET

7

LYS

GLN

TYR

GLY

GLU

Samples:

sample_1: Large Fragment of the SARS-CoV Fusion Protein, [U-13C; U-15N], 0.2 M; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
Hetronuclear NOE	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

Bruker DRX 600 MHz

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