BMRB Entry 26773
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26773
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Title: Chemical shift assignments of Spectrin repeat a17 PubMed: 28806784
Deposition date: 2016-04-01 Original release date: 2017-08-01
Authors: Cutts, Erin; Vakonakis, Ioannis
Citation: Cutts, Erin; Laasch, Niklas; Reiter, Dirk; Trenker, Raphael; Slater, Leanne; Stansfeld, Phillip; Vakonakis, Ioannis. "Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions" PLoS Pathog. 13, e1006552-e1006552 (2017).
Assembly members:
a17, polymer, 126 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
a17: GPGAHHEKLKEAYALFQFFQ
DLDDEESWIEEKLIRVSSQD
YGRDLQGVQNLLKKHKRLEG
ELVAHEPAIQNVLDMAEKLK
DKAAVGQEEIQLRLAQFVEH
WEKLKELAKARGLKLEESLE
YLQFMQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 368 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 240 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | a17 | 1 |
Entities:
Entity 1, a17 126 residues - Formula weight is not available
Residues 1-3 correspond to cloning artifacts
| 1 | GLY | PRO | GLY | ALA | HIS | HIS | GLU | LYS | LEU | LYS | ||||
| 2 | GLU | ALA | TYR | ALA | LEU | PHE | GLN | PHE | PHE | GLN | ||||
| 3 | ASP | LEU | ASP | ASP | GLU | GLU | SER | TRP | ILE | GLU | ||||
| 4 | GLU | LYS | LEU | ILE | ARG | VAL | SER | SER | GLN | ASP | ||||
| 5 | TYR | GLY | ARG | ASP | LEU | GLN | GLY | VAL | GLN | ASN | ||||
| 6 | LEU | LEU | LYS | LYS | HIS | LYS | ARG | LEU | GLU | GLY | ||||
| 7 | GLU | LEU | VAL | ALA | HIS | GLU | PRO | ALA | ILE | GLN | ||||
| 8 | ASN | VAL | LEU | ASP | MET | ALA | GLU | LYS | LEU | LYS | ||||
| 9 | ASP | LYS | ALA | ALA | VAL | GLY | GLN | GLU | GLU | ILE | ||||
| 10 | GLN | LEU | ARG | LEU | ALA | GLN | PHE | VAL | GLU | HIS | ||||
| 11 | TRP | GLU | LYS | LEU | LYS | GLU | LEU | ALA | LYS | ALA | ||||
| 12 | ARG | GLY | LEU | LYS | LEU | GLU | GLU | SER | LEU | GLU | ||||
| 13 | TYR | LEU | GLN | PHE | MET | GLN |
Samples:
sample_1: a17, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 300 mM; sodium phosphate 20 mM; DTT 1 mM; DSS 0.05 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.34 M; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CCPN_Analysis, Prof. Geerten Vuister - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts