BMRB Entry 50507

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):

Data sets:
Data typeCount
13C chemical shifts561
15N chemical shifts135
1H chemical shifts875

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-NTD1

Entities:

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

1   GLYASNTHRILEPROHISTYRSERTRPPHE
2   SERGLYILETHRGLNPHEGLNLYSGLYARG
3   ASPPHELYSPHESERASPGLYGLNGLYVAL
4   PROILEALAPHEGLYVALPROPROSERGLU
5   ALALYSGLYTYRTRPTYRARGHISSERARG
6   ARGSERPHELYSTHRALAASPGLYGLNGLN
7   LYSGLNLEULEUPROARGTRPTYRPHETYR
8   TYRLEUGLYTHRGLYPROTYRALAASNALA
9   SERTYRGLYGLUSERLEUGLUGLYVALPHE
10   TRPVALALAASNHISGLNALAASPTHRSER
11   THRPROSERASPVALSERSERARGASPPRO
12   THRTHRGLNGLUALAILEPROTHRARGPHE
13   PROPROGLYTHRILELEUPROGLNGLYTYR
14   TYRVALGLUGLYSERGLYARGSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_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