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 PubMed: 21213258
Deposition date: 2010-10-12 Original release date: 2011-01-12
Authors: Lee, Erinna; Yao, Shenggen; Norton, Raymond
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).
Assembly members:
R2_peptide, polymer, 20 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
R2_peptide: VFAEFLPLFSKFGSRLHILK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 18 |
| 1H chemical shifts | 148 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | R2 peptide | 1 |
Entities:
Entity 1, R2 peptide 20 residues - Formula weight is not available
| 1 | VAL | PHE | ALA | GLU | PHE | LEU | PRO | LEU | PHE | SER | |
| 2 | LYS | PHE | GLY | SER | ARG | LEU | HIS | ILE | LEU | LYS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts