BMRB Entry 50507

Name: 1H, 15N and 13C NMR assignments of the N-terminal domain of HKU1-bCoV nucleoprotein.
Published: 2021-10-01

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PDB ID: 7n45
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50507
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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:

1H, 15N and 13C NMR assignments of the N-terminal domain of HKU1-bCoV nucleoprotein.

Deposition date:

2020-10-10

Original release date:

2021-10-01

Authors:

Caruso, Icaro; Marques, Aline; Santana-Silva, Marcos; Araujo, Gabriela; Bezerra, Peter; Almeida, Fabio; Amorim, Gisele

Citation:

Citation: de Luna Marques, Aline; Caruso, Icaro Putinhon; Santana-Silva, Marcos Caique; Bezerra, Peter Reis; Araujo, Gabriela Rocha; Almeida, Fabio Ceneviva Lacerda; Amorim, Gisele Cardoso. "1H,15N and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the endemic human coronavirus HKU1" Biomol. NMR Assign. 15, 153-157 (2021).
PubMed: 33389548

Assembly members:

Assembly members:
HKU1-CoV nucleoprotein N-terminal domain, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: HKU1 betacoronavirus Taxonomy ID: 694002 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus HKU1 betacoronavirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HKU1-CoV nucleoprotein N-terminal domain: GNTIPHYSWFSGITQFQKGR DFKFSDGQGVPIAFGVPPSE AKGYWYRHSRRSFKTADGQQ KQLLPRWYFYYLGTGPYANA SYGESLEGVFWVANHQADTS TPSDVSSRDPTTQEAIPTRF PPGTILPQGYYVEGSGRS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	561
15N chemical shifts	135
1H chemical shifts	875

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-NTD	1

Entities:

Entity 1, N-NTD 138 residues - Formula weight is not available

1

GLY

ASN

THR

ILE

PRO

HIS

TYR

SER

TRP

PHE

2

SER

GLY

ILE

THR

GLN

PHE

GLN

LYS

GLY

ARG

3

ASP

PHE

LYS

PHE

SER

ASP

GLY

GLN

GLY

VAL

4

PRO

ILE

ALA

PHE

GLY

VAL

PRO

SER

GLU

5

ALA

LYS

GLY

TYR

TRP

TYR

ARG

HIS

SER

ARG

6

ARG

SER

PHE

LYS

THR

ALA

ASP

GLY

GLN

7

LYS

GLN

LEU

PRO

ARG

TRP

TYR

PHE

TYR

8

TYR

LEU

GLY

THR

GLY

PRO

TYR

ALA

ASN

ALA

9

SER

TYR

GLY

GLU

SER

LEU

GLU

GLY

VAL

PHE

10

TRP

VAL

ALA

ASN

HIS

GLN

ALA

ASP

THR

SER

11

THR

PRO

SER

ASP

VAL

SER

ARG

ASP

PRO

12

THR

GLN

GLU

ALA

ILE

PRO

THR

ARG

PHE

13

PRO

GLY

THR

ILE

LEU

PRO

GLN

GLY

TYR

14

TYR

VAL

GLU

GLY

SER

GLY

ARG

SER

Samples:

sample_1: N-NTD, [U-98% 13C; U-98% 15N], 250 uM; sodium phosphate 20 mM; PMSF 0.5 mM; sodium chloride 50 mM; sodium azide 3 mM; EDTA 3 mM

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
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6 - collection

NMRPipe v2020.084.12.02 - processing

NMRDraw v10.8 Rev 2020.072.12.11 - data analysis, processing

ANALYSIS v2.5.0 - chemical shift assignment, data analysis, peak picking, structure solution

ARIA2 v2.3.2 - refinement, structure solution

NMRbox v7.14 Rev 11801 - chemical shift assignment, data analysis, peak picking, processing, refinement, structure solution

NMR spectrometers:

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