BMRB Entry 19864

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19864

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Title:
H, N, Halpha, Calpha and Cbeta assignments of R1 peptide at pH 5 and 313 K
Deposition date:
2014-03-18
Original release date:
2019-07-12
Authors:
Wang, Geqing; MacRaild, Christopher; Mohanty, Biswaranjan; Mobli, Mehdi; Norton, Raymond; Scanlon, Martin
Citation:

Citation: Wang, Geqing; MacRaild, Christopher; Mohanty, Biswaranjan; Mobli, Mehdi; McGowen, Sheena; Cowieson, Nathan; Anders, Robin; Simpson, Jamie; Norton, Raymond; Scanlon, Martin. "Molecular insights into the interaction between Plasmodium falciparum apical membrane antigen 1 and an invasion-inhibitory peptide"  PLoS ONE 9, e109674-e109674 (2014).
PubMed: 25343578

Assembly members:

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

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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 shifts65
15N chemical shifts18
1H chemical shifts137

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, 90% 15N], 0.4 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 0.01 % (w/v); complete protease inhibitor cocktail (Roche) 0.2 % (w/v)

sample_conditions_1: ionic strength: 20 mM; pH: 5.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN v3.2, BRUKER - collection, processing

NMR spectrometers:

  • Bruker Avance 500 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