BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 26904

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26904

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Title: Backbone chemical shift assignment of a tetrameric N-terminal fragment of Respiratory Syncytial Virus phosphoprotein (residues M1-R163)   PubMed: 28031463

Deposition date: 2016-09-22 Original release date: 2017-02-15

Authors: Lassoued, Safa; Pereira, Nelson; Fix, Jenna; Galloux, Marie; Eleouet, Jean-Francois; Sizun, Christina

Citation: Pereira, Nelson; Cardone, Christophe; Lassoued, Safa; Galloux, Marie; Fix, Jenna; Assrir, Nadine; Lescop, Ewen; Bontems, Francois; Eleouet, Jean-Francois; Sizun, Christina. "New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners"  J. Biol. Chem. 292, 2120-2131 (2017).

Assembly members:
P1-163, polymer, 165 residues, 18438.1606 Da.

Natural source:   Common Name: human RSV   Taxonomy ID: 11250   Superkingdom: Viruses   Kingdom: not available   Genus/species: Orthopneumovirus HRSV

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

Entity Sequences (FASTA):
P1-163: GSMEKFAPEFHGEDANNRAT KFLESIKGKFTSPKDPKKKD SIISVNSIDIEVTKESPITS NSTIINPTNETDDNAGNKPN YQRKPLVSFKEDPIPSDNPF SKLYKETIETFDNNEEESSY SYEEINDQTNDNITARLDRI DEKLSEILGMLHTLVVASAG PTSAR

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts121
1H chemical shifts269

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P1-163, chain 11
2P1-163, chain 21
3P1-163, chain 31
4P1-163, chain 41

Entities:

Entity 1, P1-163, chain 1 165 residues - 18438.1606 Da.

P1-163 is a phosphoprotein fragment that contains residues M1-R163 and two N-terminal residues (GS) that are left over from a cleaved GST-tag.

1   GLYSERMETGLULYSPHEALAPROGLUPHE
2   HISGLYGLUASPALAASNASNARGALATHR
3   LYSPHELEUGLUSERILELYSGLYLYSPHE
4   THRSERPROLYSASPPROLYSLYSLYSASP
5   SERILEILESERVALASNSERILEASPILE
6   GLUVALTHRLYSGLUSERPROILETHRSER
7   ASNSERTHRILEILEASNPROTHRASNGLU
8   THRASPASPASNALAGLYASNLYSPROASN
9   TYRGLNARGLYSPROLEUVALSERPHELYS
10   GLUASPPROILEPROSERASPASNPROPHE
11   SERLYSLEUTYRLYSGLUTHRILEGLUTHR
12   PHEASPASNASNGLUGLUGLUSERSERTYR
13   SERTYRGLUGLUILEASNASPGLNTHRASN
14   ASPASNILETHRALAARGLEUASPARGILE
15   ASPGLULYSLEUSERGLUILELEUGLYMET
16   LEUHISTHRLEUVALVALALASERALAGLY
17   PROTHRSERALAARG

Samples:

sample_P1-163: P1-163, [U-13C; U-15N], 0.3 ± 3e-05 mM; sodium phosphate 20.0 ± 0.002 mM; sodium chloride 100.0 ± 0.01 mM

CondSet1: ionic strength: 0.100 M; pH: 6.500; pressure: 1.000 atm; temperature: 288.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_P1-163isotropicCondSet1
3D HNCAsample_P1-163isotropicCondSet1
3D HN(CO)CAsample_P1-163isotropicCondSet1
3D HNCACBsample_P1-163isotropicCondSet1
3D CBCA(CO)NHsample_P1-163isotropicCondSet1
3D HNHAsample_P1-163isotropicCondSet1
3D 1H-15N NOESYsample_P1-163isotropicCondSet1
2D 1H-15N HSQCsample_P1-163isotropicCondSet1

Software:

CcpNmr_Analysis v2.2, Bruker Biospin, CCPN - chemical shift assignment, collection, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UniProt P12579

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts