BMRB Entry 50961
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50961
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Title: 1H, 15N and 13C chemical shift assignments of the PYK2(728-839) polypeptide PubMed: 35945264
Deposition date: 2021-06-05 Original release date: 2022-10-12
Authors: Momin, Afaque Ahmad; Mendes, Tiago; Barthe, Philippe; Faure, Camille; Hong, SeungBeom; Jaremko, Mariusz; Girault, Jean-Antoine; Jaremko, Lukasz; Arold, Stefan
Citation: Momin, Afaque; Mendes, Tiago; Barthe, Philippe; Faure, Camille; Hong, SeungBeom; Yu, Piao; Kadare, Gress; Jaremko, Mariusz; Girault, Jean-Antoine; Jaremko, Lukasz; Arold, Stefan. "PYK2 senses calcium through a disordered dimerization and calmodulin-binding element" Commun. Biol. 5, 800-800 (2022).
Assembly members:
entity_1, polymer, 128 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 Vector: pET32a
Entity Sequences (FASTA):
entity_1: MHHHHHHSSGLVPRGSTNLL
APKLQFQVPEGLCASSPTLT
SPMEYPSPVNSLHTPPLHRH
NVFKRHSMREEDFIQPSSRE
EAQQLWEAEKVKMRQILDKQ
QKQMVEDYQWLRQEEKSLDP
MVYMNDKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 331 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 708 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PYK2(728-839) polypeptide | 1 |
Entities:
Entity 1, PYK2(728-839) polypeptide 128 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | LEU | VAL | PRO | ARG | GLY | SER | THR | ASN | LEU | LEU | ||||
| 3 | ALA | PRO | LYS | LEU | GLN | PHE | GLN | VAL | PRO | GLU | ||||
| 4 | GLY | LEU | CYS | ALA | SER | SER | PRO | THR | LEU | THR | ||||
| 5 | SER | PRO | MET | GLU | TYR | PRO | SER | PRO | VAL | ASN | ||||
| 6 | SER | LEU | HIS | THR | PRO | PRO | LEU | HIS | ARG | HIS | ||||
| 7 | ASN | VAL | PHE | LYS | ARG | HIS | SER | MET | ARG | GLU | ||||
| 8 | GLU | ASP | PHE | ILE | GLN | PRO | SER | SER | ARG | GLU | ||||
| 9 | GLU | ALA | GLN | GLN | LEU | TRP | GLU | ALA | GLU | LYS | ||||
| 10 | VAL | LYS | MET | ARG | GLN | ILE | LEU | ASP | LYS | GLN | ||||
| 11 | GLN | LYS | GLN | MET | VAL | GLU | ASP | TYR | GLN | TRP | ||||
| 12 | LEU | ARG | GLN | GLU | GLU | LYS | SER | LEU | ASP | PRO | ||||
| 13 | MET | VAL | TYR | MET | ASN | ASP | LYS | SER |
Samples:
sample_1: PYK2KFL, [U-100% 15N], 0.25 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM
sample_2: PYK2KFL, [U-100% 13C; U-100% 15N], 0.25 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.6.2 - processing
CINDY v2.1 - data analysis
NMR spectrometers:
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts