BMRB Entry 26905

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26905

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
backbone chemical shift assignment of S23C mutant of the Respiratory Syncytail Virus phosphoprotein
Deposition date:
2016-09-22
Original release date:
2017-02-15
Authors:
Cardone, Christophe; Lassoued, Safa; Galloux, Marie; Eleouet, Jean-Francois; Sizun, Christina
Citation:

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).
PubMed: 28031463

Assembly members:

Assembly members:
P-S23C, polymer, 244 residues, 27413.0335 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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
  • Hide all

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
AlphaFold P12579

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