BMRB Entry 25134

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25134

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Title:
H, N, Calpha assignments of AMA1-bound R1 peptide at pH 7 and 313k
Deposition date:
2014-08-07
Original release date:
2019-07-11
Authors:
Wang, Geqing; MacRaild, Christopher; Mohanty, Biswaranjan; Mobli, Mehdi; Norton, Raymond; Scanlon, Martin
Citation:

Citation: Akter, Mansura; Drinkwater, Nyssa; Devine, Shane; Drew, Simon; Krishnarjuna, Bankala; Debono, Cael; Wang, Geqing; Scanlon, Martin; Scammells, Peter; McGowan, Sheena; MacRaild, Christopher; Norton, Raymond. "Identification of the Binding Site of Apical Membrane Antigen 1 (AMA1) Inhibitors Using a Paramagnetic Probe"  ChemMedChem 14, 603-612 (2019).
PubMed: 30653832

Assembly members:

Assembly members:
R1_peptide, polymer, 20 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R1_peptide: VFAEFLPLFSKFGSRMHILK

Data sets:
Data typeCount
13C chemical shifts15
15N chemical shifts12
1H chemical shifts12

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1R1 peptide1

Entities:

Entity 1, R1 peptide 20 residues - Formula weight is not available

1   VALPHEALAGLUPHELEUPROLEUPHESER
2   LYSPHEGLYSERARGMETHISILELEULYS

Samples:

sample_1: R1 peptide, [U-95% 13C; U-90% 15N; U-72% 2H], 0.3 mM; AMA1, [U-72% 2H], 0.32 mM; sodium phosphate 20 mM; sodium azide 0.01 % w/v; Roche protease inhibitor cocktail 0.2 % w/v; Arginine 50 mM; Glutamic acid 50 mM; D2O 5 % v/v; H2O 90%

sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

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