BMRB Entry 26903

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26903

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Title:
Backbone chemical shift assignment of a deletion mutant of Respiratory Syncytial Virus phosphoprotein without oligomerization domain
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:

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_delta_122-160, polymer, 205 residues, 23169.4 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_delta_122-160: GSIMEKFAPEFHGEDANNRA TKFLESIKGKFTSPKDPKKK DSIISVNSIDIEVTKESPIT SNSTIINPTNETDDNAGNKP NYQRKPLVSFKEDPIPSDNP FSKLYKETIETFDNNEEESS YSYESARDGIRDAMVGLREE MIEKIRTEALMTNDRLEAMA RLRNEESEKMAKDTSDEVSL NPTSEKLNNLLEGNDSDNDL SLEDF

Data sets:
Data typeCount
13C chemical shifts592
15N chemical shifts193
1H chemical shifts645

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1P_delta[122-160]1

Entities:

Entity 1, P_delta[122-160] 205 residues - 23169.4 Da.

P_delta[122-160] corresponds to the sequence of the hRSV phosphoprotein deleted of its oligomerization domain (E122-T160). The three N-terminal residues (GSI) are left over from a cleaved GST-tag.

1   GLYSERILEMETGLULYSPHEALAPROGLU
2   PHEHISGLYGLUASPALAASNASNARGALA
3   THRLYSPHELEUGLUSERILELYSGLYLYS
4   PHETHRSERPROLYSASPPROLYSLYSLYS
5   ASPSERILEILESERVALASNSERILEASP
6   ILEGLUVALTHRLYSGLUSERPROILETHR
7   SERASNSERTHRILEILEASNPROTHRASN
8   GLUTHRASPASPASNALAGLYASNLYSPRO
9   ASNTYRGLNARGLYSPROLEUVALSERPHE
10   LYSGLUASPPROILEPROSERASPASNPRO
11   PHESERLYSLEUTYRLYSGLUTHRILEGLU
12   THRPHEASPASNASNGLUGLUGLUSERSER
13   TYRSERTYRGLUSERALAARGASPGLYILE
14   ARGASPALAMETVALGLYLEUARGGLUGLU
15   METILEGLULYSILEARGTHRGLUALALEU
16   METTHRASNASPARGLEUGLUALAMETALA
17   ARGLEUARGASNGLUGLUSERGLULYSMET
18   ALALYSASPTHRSERASPGLUVALSERLEU
19   ASNPROTHRSERGLULYSLEUASNASNLEU
20   LEUGLUGLYASNASPSERASPASNASPLEU
21   SERLEUGLUASPPHE

Samples:

P_delta_122-160_15N13C: P_delta[122-160], [U-13C; U-15N], 0.14 ± 1.5e-05 mM; sodium phosphate 20.00 ± 0.002 mM; sodium chloride 100.00 ± 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 HNCOP_delta_122-160_15N13CisotropicCondSet1
3D HNCACBP_delta_122-160_15N13CisotropicCondSet1
3D HNCOCACBP_delta_122-160_15N13CisotropicCondSet1
3D HNCAP_delta_122-160_15N13CisotropicCondSet1
3D HN(CO)CAP_delta_122-160_15N13CisotropicCondSet1
3D HBHA(CO)NHP_delta_122-160_15N13CisotropicCondSet1
2D 1H-15N HSQCP_delta_122-160_15N13CisotropicCondSet1

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
AlphaFold P12579

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