BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26905

Title: backbone chemical shift assignment of S23C mutant of the Respiratory Syncytail Virus phosphoprotein   PubMed: 28031463

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

Authors: Cardone, Christophe; Lassoued, Safa; 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:
P-S23C, polymer, 244 residues, 27413.0335 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):
P-S23C: GSIMEKFAPEFHGEDANNRA TKFLECIKGKFTSPKDPKKK DSIISVNSIDIEVTKESPIT SNSTIINPTNETDDNAGNKP NYQRKPLVSFKEDPIPSDNP FSKLYKETIETFDNNEEESS YSYEEINDQTNDNITARLDR IDEKLSEILGMLHTLVVASA GPTSARDGIRDAMVGLREEM IEKIRTEALMTNDRLEAMAR LRNEESEKMAKDTSDEVSLN PTSEKLNNLLEGNDSDNDLS LEDF

Data sets:
Data typeCount
13C chemical shifts451
15N chemical shifts149
1H chemical shifts514

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1P-S23C, chain 11
2P-S23C, chain 21
3P-S23C, chain 31
4P-S23C, chain 41

Entities:

Entity 1, P-S23C, chain 1 244 residues - 27413.0335 Da.

hRSV phosphoprotein with S23C mutation. The three N-terminal residues (GSI) are left over from a cleaved GST-tag.

1   GLYSERILEMETGLULYSPHEALAPROGLU
2   PHEHISGLYGLUASPALAASNASNARGALA
3   THRLYSPHELEUGLUCYSILELYSGLYLYS
4   PHETHRSERPROLYSASPPROLYSLYSLYS
5   ASPSERILEILESERVALASNSERILEASP
6   ILEGLUVALTHRLYSGLUSERPROILETHR
7   SERASNSERTHRILEILEASNPROTHRASN
8   GLUTHRASPASPASNALAGLYASNLYSPRO
9   ASNTYRGLNARGLYSPROLEUVALSERPHE
10   LYSGLUASPPROILEPROSERASPASNPRO
11   PHESERLYSLEUTYRLYSGLUTHRILEGLU
12   THRPHEASPASNASNGLUGLUGLUSERSER
13   TYRSERTYRGLUGLUILEASNASPGLNTHR
14   ASNASPASNILETHRALAARGLEUASPARG
15   ILEASPGLULYSLEUSERGLUILELEUGLY
16   METLEUHISTHRLEUVALVALALASERALA
17   GLYPROTHRSERALAARGASPGLYILEARG
18   ASPALAMETVALGLYLEUARGGLUGLUMET
19   ILEGLULYSILEARGTHRGLUALALEUMET
20   THRASNASPARGLEUGLUALAMETALAARG
21   LEUARGASNGLUGLUSERGLULYSMETALA
22   LYSASPTHRSERASPGLUVALSERLEUASN
23   PROTHRSERGLULYSLEUASNASNLEULEU
24   GLUGLYASNASPSERASPASNASPLEUSER
25   LEUGLUASPPHE

Samples:

P-S23C-15N13C: P-S23C, [U-13C; U-15N; U-2H], 0.1 ± 1e-05 mM; sodium phosphate 20.0 ± 0.002 mM; sodium chloride 100.0 ± 0.01 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCP-S23C-15N13CisotropicCondition
3D HNCOP-S23C-15N13CisotropicCondition
3D HN(CO)CAP-S23C-15N13CisotropicCondition
3D HNCAP-S23C-15N13CisotropicCondition
3D HNCACBP-S23C-15N13CisotropicCondition
3D HN(CO)CACBP-S23C-15N13CisotropicCondition
3D HBHA(CO)NHP-S23C-15N13CisotropicCondition

Software:

CcpNmr_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking

Topspin v3.1, Bruker - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP P12579

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