BMRB Entry 34239

Title:
Gp36-MPER
Deposition date:
2018-02-22
Original release date:
2019-03-14
Authors:
D'Ursi, Anna Maria; Grimaldi, M.
Citation:

Citation: Grimaldi, Manuela; Stillitano, Ilaria; Amodio, Giuseppina; Santoro, Angelo; Buonocore, Michela; Moltedo, Ornella; Remondelli, Paolo; D'Ursi, Anna Maria. "Structural basis of antiviral activity of peptides from MPER of FIV gp36"  PLoS ONE 13, e0204042-e0204042 (2018).
PubMed: 30240422

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 6126.001 Da.

Natural source:

Natural source:   Common Name: isolate Petaluma   Taxonomy ID: 11673   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus FIV

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-31b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LQTKDLQQKFYEIILDIEQN NVQGKTGIQQLQKWEDWVRW IGNIPQYLKM

Data sets:
Data typeCount
13C chemical shifts71
15N chemical shifts48
1H chemical shifts262

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 50 residues - 6126.001 Da.

1   LEUGLNTHRLYSASPLEUGLNGLNLYSPHE
2   TYRGLUILEILELEUASPILEGLUGLNASN
3   ASNVALGLNGLYLYSTHRGLYILEGLNGLN
4   LEUGLNLYSTRPGLUASPTRPVALARGTRP
5   ILEGLYASNILEPROGLNTYRLEULYSMET

Samples:

sample_1: entity_1 mM; glucose, [U-95% 13C], 2 g/L; ammonium sulfate, [U-98% 15N], 1 g/L

sample_conditions_1: ionic strength: 0.15 Not defined; pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
3D NOESYsample_1isotropicsample_conditions_1
3D NOESY 13C-HSQCsample_1isotropicsample_conditions_1
NOESY 15N-HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3, Goddard - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS+, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

  • Bruker AvanceIII 900 MHz
  • Bruker AvanceIII 600 MHz

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