BMRB Entry 50124
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50124
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NMR-STAR v3 text file.
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Title: Complete sequential assignment of the protein K1-CanA from Pyrodictium abyssi PubMed: 32052266
Deposition date: 2019-12-12 Original release date: 2020-12-14
Authors: Munte, Claudia; Kalbitzer, Hans Robert; Kreitner, Raphael; Singer, Katrin; Stetter, Karl; Horn, Gudrun; Kremer, Werner
Citation: Kreitner, Raphael; Munte, Claudia; Singer, Katrin; Stetter, Karl; Horn, Gudrun; Kremer, Werner; Kalbitzer, Hans Robert. "Complete sequential assignment and secondary structure prediction of the cannulae forming protein CanA from the hyperthermophilic archebacterium Pyrodictium abyssi" Biomol. NMR Assign. 14, 141-146 (2020).
Assembly members:
entity_1, polymer, 172 residues, 18706.21 Da.
Natural source: Common Name: Pyrodictium abyssi Taxonomy ID: 54256 Superkingdom: Archaea Kingdom: not available Genus/species: Pyrodictium abyssi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET17b
Entity Sequences (FASTA):
entity_1: ATGTAQAVSEPIDVESHLGS
ITPAAGAQGSDDIGYAIVWI
KDQVNDVKLKVTLANAEQLK
PYFKYLQIQITSGYETNSTA
LGNFSETKAVISLDNPSAVI
VLDKEDIAVLYPDKTGYTNT
SIWVPGEPDKIIVYNETKPV
AILNFKAFYEAKEGMLFDSL
PVIFNFQVLQVG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 756 |
| 15N chemical shifts | 187 |
| 1H chemical shifts | 1227 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | K1-CanA monomer | 1 |
Entities:
Entity 1, K1-CanA monomer 172 residues - 18706.21 Da.
Residues 1-10 from CanA have been removed
| 1 | ALA | THR | GLY | THR | ALA | GLN | ALA | VAL | SER | GLU | ||||
| 2 | PRO | ILE | ASP | VAL | GLU | SER | HIS | LEU | GLY | SER | ||||
| 3 | ILE | THR | PRO | ALA | ALA | GLY | ALA | GLN | GLY | SER | ||||
| 4 | ASP | ASP | ILE | GLY | TYR | ALA | ILE | VAL | TRP | ILE | ||||
| 5 | LYS | ASP | GLN | VAL | ASN | ASP | VAL | LYS | LEU | LYS | ||||
| 6 | VAL | THR | LEU | ALA | ASN | ALA | GLU | GLN | LEU | LYS | ||||
| 7 | PRO | TYR | PHE | LYS | TYR | LEU | GLN | ILE | GLN | ILE | ||||
| 8 | THR | SER | GLY | TYR | GLU | THR | ASN | SER | THR | ALA | ||||
| 9 | LEU | GLY | ASN | PHE | SER | GLU | THR | LYS | ALA | VAL | ||||
| 10 | ILE | SER | LEU | ASP | ASN | PRO | SER | ALA | VAL | ILE | ||||
| 11 | VAL | LEU | ASP | LYS | GLU | ASP | ILE | ALA | VAL | LEU | ||||
| 12 | TYR | PRO | ASP | LYS | THR | GLY | TYR | THR | ASN | THR | ||||
| 13 | SER | ILE | TRP | VAL | PRO | GLY | GLU | PRO | ASP | LYS | ||||
| 14 | ILE | ILE | VAL | TYR | ASN | GLU | THR | LYS | PRO | VAL | ||||
| 15 | ALA | ILE | LEU | ASN | PHE | LYS | ALA | PHE | TYR | GLU | ||||
| 16 | ALA | LYS | GLU | GLY | MET | LEU | PHE | ASP | SER | LEU | ||||
| 17 | PRO | VAL | ILE | PHE | ASN | PHE | GLN | VAL | LEU | GLN | ||||
| 18 | VAL | GLY |
Samples:
sample_1: K1-CanA 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_2: K1-CanA 1.8 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_3: K1-CanA 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_4: K1-CanA, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_5: K1-CanA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_6: K1-CanA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM
sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_3 | isotropic | sample_conditions_1 |
| 3D HCAN | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_6 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D (HB)CB(CGCC-TOCSY)Har | sample_3 | isotropic | sample_conditions_1 |
| 3D (HB)CB(CGCD)HD | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
TOPSPIN, Bruker Biospin - processing
AUREMOL, Bruker Biospin - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts