BMRB Entry 16964
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16964
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Citation: Schuetz, Anne; Wasmer, Christian; Habenstein, Birgit; Verel, Rene; Greenwald, Jason; Riek, Roland; Bockmann, Anja; Meier, Beat. "Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227)." Chembiochem 11, 1543-1551 (2010).
PubMed: 20572250
Assembly members:
HET-s, polymer, 229 residues, 25470 Da.
Natural source: Common Name: ascomycetes Taxonomy ID: 5145 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Podospora anserina
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 817 |
| 15N chemical shifts | 205 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HET-s(1-227) | 1 |
Entities:
Entity 1, HET-s(1-227) 229 residues - 25470 Da.
The first two residues represent non-native remainders of a cleaved HIS-tag. This is the globular domain of a prion protein.
| 1 | GLY | SER | MET | SER | GLU | PRO | PHE | GLY | ILE | VAL | ||||
| 2 | ALA | GLY | ALA | LEU | ASN | VAL | ALA | GLY | LEU | PHE | ||||
| 3 | ASN | ASN | CYS | VAL | ASP | CYS | PHE | GLU | TYR | VAL | ||||
| 4 | GLN | LEU | GLY | ARG | PRO | PHE | GLY | ARG | ASP | TYR | ||||
| 5 | GLU | ARG | CYS | GLN | LEU | ARG | LEU | ASP | ILE | ALA | ||||
| 6 | LYS | ALA | ARG | LEU | SER | ARG | TRP | GLY | GLU | ALA | ||||
| 7 | VAL | LYS | ILE | ASN | ASP | ASP | PRO | ARG | PHE | HIS | ||||
| 8 | SER | SER | ALA | PRO | THR | ASP | LYS | SER | VAL | GLN | ||||
| 9 | LEU | ALA | LYS | SER | ILE | VAL | GLU | GLU | ILE | LEU | ||||
| 10 | LEU | LEU | PHE | GLU | SER | ALA | GLN | LYS | THR | SER | ||||
| 11 | LYS | ARG | TYR | GLU | LEU | VAL | ALA | ASP | GLN | GLN | ||||
| 12 | ASP | LEU | VAL | VAL | PHE | GLU | ASP | LYS | ASP | MET | ||||
| 13 | LYS | PRO | ILE | GLY | ARG | ALA | LEU | HIS | ARG | ARG | ||||
| 14 | LEU | ASN | ASP | LEU | VAL | SER | ARG | ARG | GLN | LYS | ||||
| 15 | GLN | THR | SER | LEU | ALA | LYS | LYS | THR | ALA | TRP | ||||
| 16 | ALA | LEU | TYR | ASP | GLY | LYS | SER | LEU | GLU | LYS | ||||
| 17 | ILE | VAL | ASP | GLN | VAL | ALA | ARG | PHE | VAL | ASP | ||||
| 18 | GLU | LEU | GLU | LYS | ALA | PHE | PRO | ILE | GLU | ALA | ||||
| 19 | VAL | CYS | HIS | LYS | LEU | ALA | GLU | ILE | GLU | ILE | ||||
| 20 | GLU | GLU | VAL | GLU | ASP | GLU | ALA | SER | LEU | THR | ||||
| 21 | ILE | LEU | LYS | ASP | ALA | ALA | GLY | GLY | ILE | ASP | ||||
| 22 | ALA | ALA | MET | SER | ASP | ALA | ALA | ALA | GLN | LYS | ||||
| 23 | ILE | ASP | ALA | ILE | VAL | GLY | ARG | ASN | SER |
Samples:
sample_1: HET-s, [U-100% 13C; U-100% 15N], 25 mg; DTT 0.5 mM; sodium azide 0.02%; DSS 1 mg; TRIS 20 mM; H2O 100%
sample_conditions_1: ionic strength: 20 mM; pH: 8.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D NCACO | sample_1 | solid | sample_conditions_1 |
| 3D NCOCA | sample_1 | solid | sample_conditions_1 |
| 3D CANCO | sample_1 | solid | sample_conditions_1 |
| 3D NCACB-DREAM | sample_1 | solid | sample_conditions_1 |
| 3D N(CO)CACB | sample_1 | solid | sample_conditions_1 |
| 3D CAN(CO)CA | sample_1 | solid | sample_conditions_1 |
| 3D CCC | sample_1 | solid | sample_conditions_1 |
| 3D NCACX-DARR | sample_1 | solid | sample_conditions_1 |
| 3D N(CA)CBCX | sample_1 | solid | sample_conditions_1 |
Software:
SPARKY v3.115, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
- Bruker Avance 600 MHz