BMRB Entry 15075
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15075
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Title: Merozoite surface protein 2 (MSP2) of Plasmodium falciparum: expression, structure and amyloid formation of the conserved N-terminal domain PubMed: 17516503
Deposition date: 2006-12-12 Original release date: 2007-10-17
Authors: Low, Andrew; Chandrashekaran, Indu; Adda, Christopher; Yao, Shenggan; Sabo, Jennifer; Zhang, Xuecheng; Soetopo, Alfreda; Anders, Robin; Norton, Raymond
Citation: Low, Andrew; Chandrashekaran, Indu; Adda, Christopher; Yao, Shenggan; Sabo, Jennifer; Zhang, Xuecheng; Soetopo, Alfreda; Anders, Robin; Norton, Raymond. "Merozoite surface protein 2 of Plasmodium falciparum: expression, structure, dynamics, and fibril formation of the conserved N-terminal domain" Biopolymers 87, 12-22 (2007).
Assembly members:
1-25MSP2, polymer, 28 residues, 3228 Da.
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
1-25MSP2: GSMIKNESKYSNTFINNAYN
MSIRRSMA
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 15N chemical shifts | 30 |
| 1H chemical shifts | 166 |
| coupling constants | 11 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | 1-25MSP2 | 1 |
Entities:
Entity 1, 1-25MSP2 28 residues - 3228 Da.
Residues -3 to -1 are from the cleavage site. Residues 1 to 25 are the N-terminal region of MSP2
| 1 | GLY | SER | MET | ILE | LYS | ASN | GLU | SER | LYS | TYR | ||||
| 2 | SER | ASN | THR | PHE | ILE | ASN | ASN | ALA | TYR | ASN | ||||
| 3 | MET | SER | ILE | ARG | ARG | SER | MET | ALA |
Samples:
sample_1: 1-25MSP2, [U-15N], 1.2 mM; D2O 5%; Acetic Acid 10 mM
sample_conditions_1: ionic strength: 10 mM; pH: 3.4; 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 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - Data collection, Data processing
XEASY v1.3, Bartels et al. - Peak assignments
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts