BMRB Entry 52010

Name: SARS-CoV-2 Nucleocapsid protein NTD Y109A mutant
Published: 2023-11-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52010

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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:

SARS-CoV-2 Nucleocapsid protein NTD Y109A mutant

Deposition date:

2023-06-30

Original release date:

2023-11-15

Authors:

Estelle, Aidan; Forsythe, Heather; Yu, Zhen; Hughes, Kaitlyn; Lasher, Brittany; Allen, Patrick; Reardon, Patrick; Hendrix, David; Barbar, Elisar

Citation:

Citation: Estelle, Aidan; Forsythe, Heather; Yu, Zhen; Hughes, Kaitlyn; Lasher, Brittany; Allen, Patrick; Reardon, Patrick; Hendrix, David; Barbar, Elisar. "RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid" PNAS Nexus 2, pgad333-pgad333 (2023).
PubMed: 37901441

Assembly members:

Assembly members:
entity_1, polymer, 132 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: recombinant technology Host organism: Escherichia coli Vector: pET24d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAHMNNTASWFTALTQHGKE DLKFPRGQGVPINTNSSPDD QIGYYRRATRRIRGGDGKMK DLSPRWAFYYLGTGPEAGLP YGANKDGIIWVATEGALNTP KDHIGTRNPANNAAIVLQLP QGTTLPKGFYAE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	106
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NTD Y109A	1

Entities:

Entity 1, NTD Y109A 132 residues - Formula weight is not available

N-terminal domain of the nucleocapsid with a Y-to-A mutation at residue 109.

1

GLY

ALA

HIS

MET

ASN

THR

ALA

SER

TRP

2

PHE

THR

ALA

LEU

THR

GLN

HIS

GLY

LYS

GLU

3

ASP

LEU

LYS

PHE

PRO

ARG

GLY

GLN

GLY

VAL

4

PRO

ILE

ASN

THR

ASN

SER

PRO

ASP

5

GLN

ILE

GLY

TYR

ARG

ALA

THR

ARG

6

ARG

ILE

ARG

GLY

ASP

GLY

LYS

MET

LYS

7

ASP

LEU

SER

PRO

ARG

TRP

ALA

PHE

TYR

8

LEU

GLY

THR

GLY

PRO

GLU

ALA

GLY

LEU

PRO

9

TYR

GLY

ALA

ASN

LYS

ASP

GLY

ILE

TRP

10

VAL

ALA

THR

GLU

GLY

ALA

LEU

ASN

THR

PRO

11

LYS

ASP

HIS

ILE

GLY

THR

ARG

ASN

PRO

ALA

12

ASN

ALA

ILE

VAL

LEU

GLN

LEU

PRO

13

GLN

GLY

THR

LEU

PRO

LYS

GLY

PHE

TYR

14

ALA

GLU

Samples:

sample_1: NTD Y109A, [U-100% 15N], 500 uM; sodium chloride 20 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.04 M; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ v9.2.0-b27 - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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