Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17999
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Citation: Mayer, Christina; Slater, Leanne; Erat, Michele; Konrat, Robert; Vakonakis, Ioannis. "Structural Analysis of the Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Intracellular Domain Reveals a Conserved Interaction Epitope." J. Biol. Chem. 287, 7182-7189 (2012).
PubMed: 22249178
Assembly members:
ATS-FL, polymer, 403 residues, Formula weight is not available
Natural source: Common Name: malaria parasite P. falciparum Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET16-3c
Data type | Count |
13C chemical shifts | 935 |
15N chemical shifts | 312 |
1H chemical shifts | 636 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ATS-FL | 1 |
Entity 1, ATS-FL 403 residues - Formula weight is not available
Residues -10 to -1 represent a cloning artefact. Remaining sequence is the cytoplasmic domain of PfEMP1
1 | GLY | PRO | LEU | GLY | SER | PRO | GLY | ILE | PRO | GLY | ||||
2 | LYS | LYS | LYS | PRO | LYS | SER | PRO | VAL | ASP | LEU | ||||
3 | ILE | ARG | VAL | LEU | ASP | ILE | HIS | LYS | GLY | ASP | ||||
4 | TYR | GLY | MET | PRO | THR | LEU | LYS | SER | LYS | ASN | ||||
5 | ARG | TYR | ILE | PRO | TYR | ALA | SER | ASP | THR | TYR | ||||
6 | LYS | GLY | LYS | THR | TYR | ILE | TYR | MET | GLU | GLY | ||||
7 | ASP | SER | ASP | SER | GLY | HIS | TYR | TYR | GLU | ASP | ||||
8 | THR | THR | ASP | ILE | THR | SER | SER | GLU | SER | GLU | ||||
9 | TYR | GLU | GLU | MET | ASP | ILE | ASN | ASP | ILE | TYR | ||||
10 | VAL | PRO | ASP | SER | PRO | LYS | TYR | LYS | THR | LEU | ||||
11 | ILE | GLU | VAL | VAL | LEU | GLU | PRO | SER | LYS | ARG | ||||
12 | ASP | THR | PRO | SER | SER | ASP | ALA | PRO | MET | ASN | ||||
13 | LYS | PHE | THR | ASP | ASP | GLU | TRP | ASN | GLN | LEU | ||||
14 | LYS | GLN | ASP | PHE | ILE | SER | GLY | ILE | LEU | GLU | ||||
15 | ASN | GLU | GLN | LYS | ASP | LEU | PRO | LYS | ASN | ASN | ||||
16 | ILE | SER | GLY | ASN | THR | PRO | MET | ASN | THR | GLN | ||||
17 | PRO | ASN | THR | LEU | TYR | PHE | ASN | LYS | PRO | GLU | ||||
18 | GLU | LYS | PRO | PHE | ILE | THR | SER | ILE | HIS | ASP | ||||
19 | ARG | ASP | LEU | TYR | SER | GLY | GLU | GLU | ILE | ASN | ||||
20 | TYR | ASN | ILE | ASN | MET | SER | THR | ASN | SER | MET | ||||
21 | ASP | ASP | THR | SER | TYR | VAL | SER | ASN | ASN | VAL | ||||
22 | TYR | SER | GLY | ILE | ASP | LEU | ILE | ASN | ASP | THR | ||||
23 | LEU | SER | GLY | ASN | GLN | HIS | ILE | ASP | ILE | TYR | ||||
24 | ASP | GLU | VAL | LEU | LYS | ARG | LYS | GLU | ASN | GLU | ||||
25 | LEU | PHE | GLY | THR | ASN | TYR | LYS | LYS | ASN | THR | ||||
26 | SER | ASN | ASN | ASN | VAL | ALA | LYS | LEU | THR | ASN | ||||
27 | SER | ASP | PRO | ILE | MET | ASN | GLN | LEU | ASP | LEU | ||||
28 | LEU | HIS | LYS | TRP | LEU | ASP | ARG | HIS | ARG | ASP | ||||
29 | MET | CYS | GLU | LYS | TRP | LYS | SER | LYS | GLU | ASP | ||||
30 | ILE | LEU | HIS | LYS | LEU | ASN | GLU | GLN | TRP | ASN | ||||
31 | LYS | ASP | ASN | ASP | GLY | GLY | ASN | VAL | PRO | ILE | ||||
32 | ASP | ASN | ARG | SER | LEU | ASN | THR | ASP | VAL | TRP | ||||
33 | ILE | GLU | ILE | ASP | MET | ASP | ASP | PRO | LYS | GLY | ||||
34 | LYS | LYS | GLU | PHE | SER | ASN | MET | ASP | THR | ILE | ||||
35 | LEU | ASP | ASP | ILE | GLU | ASP | ASP | ILE | TYR | TYR | ||||
36 | ASP | VAL | ASN | ASP | ASP | GLU | ASN | PRO | SER | VAL | ||||
37 | ASP | ASN | ILE | PRO | MET | ASP | HIS | ASN | LYS | VAL | ||||
38 | ASP | VAL | PRO | LYS | LYS | VAL | HIS | VAL | GLU | MET | ||||
39 | LYS | ILE | LEU | ASN | ASN | THR | SER | ASN | GLY | SER | ||||
40 | LEU | GLU | PRO | GLU | PHE | PRO | ILE | SER | ASP | VAL | ||||
41 | TRP | ASN | ILE |
sample_1: ATS-FL, [U-99% 13C; U-99% 15N], 0.2-0.5 mM; NaCl 50 mM; Na2HPO4 20 mM; NaN3 0.01%; DSS 0.1 mM
sample_conditions_1: ionic strength: 0.11 M; pH: 7; pressure: 1 atm; temperature: 273 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNHAHB | sample_1 | isotropic | sample_conditions_1 |
3D HACACO | sample_1 | isotropic | sample_conditions_1 |
3D HACA(CO)N | sample_1 | isotropic | sample_conditions_1 |
Omega Spectrometer Operating Software vBeta 6.03b2, Ge/Bruker - collection
NMRPipe v2.4 Rev 2006.095.11.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP v4.3.7, Garrett - data analysis
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks