BMRB Entry 51620

Name: NMR assignment of NTD (44 - 180) of Nucleocapsid Protein of SARS-CoV-2
Published: 2022-10-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51620

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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:

NMR assignment of NTD (44 - 180) of Nucleocapsid Protein of SARS-CoV-2

Deposition date:

2022-09-09

Original release date:

2022-10-14

Authors:

Schiavina, Marco; Tagliaferro, Giuseppe; Pontoriero, Letizia; Pierattelli, Roberta; Felli, Isabella Caterina

Citation:

Citation: Schiavina, Marco; Pontoriero, Letizia; Tagliaferro, Giuseppe; Pierattelli, Roberta; Felli, Isabella Caterina. "The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin" Biomolecules 12, 1302-1302 (2022).
PubMed: 36139141

Assembly members:

Assembly members:
entity_1, polymer, 137 residues, 14850 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 coli Vector: pET28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GLPNNTASWFTALTQHGKED LKFPRGQGVPINTNSSPDDQ IGYYRRATRRIRGGDGKMKD LSPRWYFYYLGTGPEAGLPY GANKDGIIWVATEGALNTPK DHIGTRNPANNAAIVLQLPQ GTTLPKGFYAEGSRGGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	423
15N chemical shifts	145
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NTD	1

Entities:

Entity 1, NTD 137 residues - 14850 Da.

1

GLY

LEU

PRO

ASN

THR

ALA

SER

TRP

PHE

2

THR

ALA

LEU

THR

GLN

HIS

GLY

LYS

GLU

ASP

3

LEU

LYS

PHE

PRO

ARG

GLY

GLN

GLY

VAL

PRO

4

ILE

ASN

THR

ASN

SER

PRO

ASP

GLN

5

ILE

GLY

TYR

ARG

ALA

THR

ARG

6

ILE

ARG

GLY

ASP

GLY

LYS

MET

LYS

ASP

7

LEU

SER

PRO

ARG

TRP

TYR

PHE

TYR

LEU

8

GLY

THR

GLY

PRO

GLU

ALA

GLY

LEU

PRO

TYR

9

GLY

ALA

ASN

LYS

ASP

GLY

ILE

TRP

VAL

10

ALA

THR

GLU

GLY

ALA

LEU

ASN

THR

PRO

LYS

11

ASP

HIS

ILE

GLY

THR

ARG

ASN

PRO

ALA

ASN

12

ASN

ALA

ILE

VAL

LEU

GLN

LEU

PRO

GLN

13

GLY

THR

LEU

PRO

LYS

GLY

PHE

TYR

ALA

14

GLU

GLY

SER

ARG

GLY

SER

Samples:

sample_1: NTD (44-180) of N protein from SARS-CoV-2, [U-100% 13C; U-100% 15N], 450 uM; KPi 25 mM; KCl 150 mM; NaN3 0.03%

sample_conditions_1: ionic strength: 170 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
2D 13C CACO	sample_1	isotropic	sample_conditions_1
2D 13C CBCACO	sample_1	isotropic	sample_conditions_1
2D 13C CON	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 13C (H)CBCACON	sample_1	isotropic	sample_conditions_1

Software:

XEASY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz

UNP	P0DTC9
AlphaFold	P0DTC9