BMRB Entry 50127

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50127

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Title:
Influenza A virus M2 cytoplasmic tail at pH 5.5
Deposition date:
2019-12-13
Original release date:
2020-06-09
Authors:
Claridge, Jolyon; Schnell, Jason
Citation:

Citation: Claridge, Jolyon; Mohd-Kipli, Faiz; Florea, Andrei; Gate, Thomas; Schnell, Jason. "pH-dependent Secondary Structure Propensity of the Influenza A Virus M2 Cytoplasmic Tail"  Biomol. NMR Assignments 14, 157-161 (2020).
PubMed: 32157574

Assembly members:

Assembly members:
entity_1, polymer, 58 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Influenza A   Taxonomy ID: 11320   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alphainfluenzavirus Influenza A

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSDRLFFKCIYRRFKYGL KRGPSTEGVPESMREEYQQE QQSAVDVDDGHFVNIELE

Data sets:
Data typeCount
13C chemical shifts97
15N chemical shifts36
1H chemical shifts36

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Influenza A virus matrix 2 protein1

Entities:

Entity 1, Influenza A virus matrix 2 protein 58 residues - Formula weight is not available

1   GLYPROGLYSERASPARGLEUPHEPHELYS
2   CYSILETYRARGARGPHELYSTYRGLYLEU
3   LYSARGGLYPROSERTHRGLUGLYVALPRO
4   GLUSERMETARGGLUGLUTYRGLNGLNGLU
5   GLNGLNSERALAVALASPVALASPASPGLY
6   HISPHEVALASNILEGLULEUGLU

Samples:

sample_1: Influenza A virus matrix protein 2, [U-99% 13C; U-99% 15N], 0.225 mM; NaPO4 20 mM; Na acetate 20 mM; NaCl 137 mM; KCl 2.7 mM

sample_conditions_1: ionic strength: 0.180 M; pH: 5.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

NMRPipe v8.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNMR v2, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

Uniprot J9V8B5
AlphaFold J9V8B5

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