BMRB Entry 25705

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25705

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Title:
Backbone assignment of the N-terminal domain of human respiratory syncytial virus nucleoprotein
Deposition date:
2015-07-14
Original release date:
2017-08-16
Authors:
Pereira, Nelson; Galloux, Marie; Eleouet, Jean-Francois; Sizun, Christina
Citation:

Citation: Ouizougun-Oubari, Mohamed; Pereira, Nelson; Tarus, Bogdan; Galloux, Marie; Lassoued, Safa; Fix, Jenna; Tortorici, M Alejandra; Hoos, Sylviane; Baron, Bruno; England, Patrick; Desmaele, Didier; Couvreur, Patrick; Bontems, Francois; Rey, Felix; Eleouet, Jean-Francois; Sizun, Christina; Slama-Schwok, Anny; Duquerroy, Stephane. "A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of Human Respiratory Syncytial Virus"  J. Virol. 89, 11129-11143 (2015).
PubMed: 26246564

Assembly members:

Assembly members:
Nucleoprotein, polymer, 233 residues, 26238.2629 Da.

Natural source:

Natural source:   Common Name: RSV   Taxonomy ID: 11260   Superkingdom: Viruses   Kingdom: not available   Genus/species: Pneumovirus Human respiratory syncytial virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nucleoprotein: MGSDSIDTPNYDVQKHINKL CGMLLITEDANHKFTGLIGM LYAMSRLGREDTIKILRDAG YHVKANGVDVTTHRQDINGK EMKFEVLTLASLTTEIQINI EIESRKSYKKMLKEMGEVAP EYRHDSPDCGMIILCIAALV ITKLAAGDRSGLTAVIRRAN NVLKNEMKRYKGLLPKDIAN SFYEVFEKHPHFIDVFVHFG IAQSSTRGGSRVEGIFAGLF MNAYGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts637
15N chemical shifts212
1H chemical shifts212

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1N-NTD1

Entities:

Entity 1, N-NTD 233 residues - 26238.2629 Da.

Residues M1-S3 were introduced during cloning of the nucleoprotein fragment D3-G252. Residues L253-H260 constitute the C-terminal his-tag.

1   METGLYSERASPSERILEASPTHRPROASN
2   TYRASPVALGLNLYSHISILEASNLYSLEU
3   CYSGLYMETLEULEUILETHRGLUASPALA
4   ASNHISLYSPHETHRGLYLEUILEGLYMET
5   LEUTYRALAMETSERARGLEUGLYARGGLU
6   ASPTHRILELYSILELEUARGASPALAGLY
7   TYRHISVALLYSALAASNGLYVALASPVAL
8   THRTHRHISARGGLNASPILEASNGLYLYS
9   GLUMETLYSPHEGLUVALLEUTHRLEUALA
10   SERLEUTHRTHRGLUILEGLNILEASNILE
11   GLUILEGLUSERARGLYSSERTYRLYSLYS
12   METLEULYSGLUMETGLYGLUVALALAPRO
13   GLUTYRARGHISASPSERPROASPCYSGLY
14   METILEILELEUCYSILEALAALALEUVAL
15   ILETHRLYSLEUALAALAGLYASPARGSER
16   GLYLEUTHRALAVALILEARGARGALAASN
17   ASNVALLEULYSASNGLUMETLYSARGTYR
18   LYSGLYLEULEUPROLYSASPILEALAASN
19   SERPHETYRGLUVALPHEGLULYSHISPRO
20   HISPHEILEASPVALPHEVALHISPHEGLY
21   ILEALAGLNSERSERTHRARGGLYGLYSER
22   ARGVALGLUGLYILEPHEALAGLYLEUPHE
23   METASNALATYRGLYLEUGLUHISHISHIS
24   HISHISHIS

Samples:

DCN: N-NTD, [U-100% 13C; U-100% 15N; U-70% 2H], 80.0 ± 8.00 uM; MES 20.0 ± 2.0 mM; NaCl 250.0 ± 1.0 mM; TCEP 1.5 ± 0.00015 mM; H2O 93%; D2O 7%

Cond1: ionic strength: 0.250 M; pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCDCNisotropicCond1
3D HNCADCNisotropicCond1
3D HN(CO)CADCNisotropicCond1
3D HNCODCNisotropicCond1
3D HNCACBDCNisotropicCond1
3D HN(CO)CACBDCNisotropicCond1

Software:

CcpNmr_Analysis v2.2, CCPN - Assignment, Data analysis

NmrPipe v1.0, Frank Delaglio - Data processing

TopSpin v3.1, Bruker - Data processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UniProt P03418
AlphaFold P88810

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