BMRB Entry 17253

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17253

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Title:
1H and backbone 15N chemical shifts of a peptide inhibitor for the Malaria surface protein, Apical Membrane Antigen 1
Deposition date:
2010-10-12
Original release date:
2011-01-12
Authors:
Lee, Erinna; Yao, Shenggen; Norton, Raymond
Citation:

Citation: Lee, Erinna; Yao, Shenggen; Sabo, Jennifer; Fairlie, W. Douglas; Stevenson, Rachel; Harris, Karen; Anders, Robin; Foley, Michael; Norton, Raymond. "Peptide inhibitors of the malaria surface protein, apical membrane antigen 1: Identification of key binding residues."  Biopolymers 95, 354-364 (2011).
PubMed: 21213258

Assembly members:

Assembly members:
R2_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: pET15b (modified)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R2_peptide: VFAEFLPLFSKFGSRLHILK

Data sets:
Data typeCount
15N chemical shifts18
1H chemical shifts148

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1R2 peptide1

Entities:

Entity 1, R2 peptide 20 residues - Formula weight is not available

1   VALPHEALAGLUPHELEUPROLEUPHESER
2   LYSPHEGLYSERARGLEUHISILELEULYS

Samples:

sample_1: sodium acetate 10 mM; sodium azide 0.03%; R2 peptide 2 mM; H2O 95%; D2O 5%

sample_2: sodium acetate 10 mM; sodium azide 0.03%; R2 peptide, [U-15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.1; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

XEASY v1.3, Bartels et al. - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 500 MHz

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