BMRB Entry 50381
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50381
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Title: The Structural Basis of PTEN Regulation by Multi-Site Phosphorylation PubMed: 34625746
Deposition date: 2020-07-08 Original release date: 2021-10-10
Authors: Dempsey, Daniel; Viennet, Thibault; Arthanari, Haribabu; Cole, Philipp
Citation: Dempsey, Daniel; Viennet, Thibault; Iwase, Reina; Park, Eunyoung; Henriquez, Stephanie; Chen, Zan; Jeliazkov, Jeliazko; Palanski, Brad; Phan, Kim; Coote, Paul; Gray, Jeffrey; Eck, Michael; Gabelli, Sandra; Arthanari, Haribabu; Cole, Philip. "The Structural Basis of PTEN Regulation by Multi-Site Phosphorylation" Nat. Struct. Mol. Biol. 28, 858-868 (2021).
Assembly members:
entity_1, polymer, 336 residues, Formula weight is not available
entity_2, polymer, 18 residues, Formula weight is not available
Natural source: Common Name: vase tunicate Taxonomy ID: 7719 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ciona intestinalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: KASSRRTISQNKRRYRKDGF
DLDLTYVTDHVIAMSFPSSG
RQSLFRNPIGEVSRFFKTKH
PDKFRIYNLCSERGYDETKF
DNHVYRVMIDDHNVPTLVDL
LKFIDDAKVWMTSDPDHVIA
IHSKGGKGRTGTLVSSWLLE
DGKFDTAKEALEYFGSRRTD
FEVGDVFQGVETASQIRYVG
YFEKIKKNYGGQLPPMKKLK
VTGVTITAIQGVGRGNGSDL
SMQIVSERQEVLLCKFAEGY
NCALQYDATDDCVTCEVKNC
PVLAGDIKVRFMSTSKSLPR
GYDNCPFYFWFNTSLVEGDH
VTLKREEIDNPHKKKTWKIY
RDNFTVKLTFSDAEDI
entity_2: CYXDXXDXDPENEPFDED
- assigned_chemical_shifts
- chem_shift_perturbation
| Data type | Count |
| 13C chemical shifts | 165 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 91 |
| molecule interaction chemical shift values | 180 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VSP | 1 |
| 2 | 4P PTEN C-tail | 2 |
Entities:
Entity 1, VSP 336 residues - Formula weight is not available
VSP soluble domain, aa 241-576
| 1 | LYS | ALA | SER | SER | ARG | ARG | THR | ILE | SER | GLN | ||||
| 2 | ASN | LYS | ARG | ARG | TYR | ARG | LYS | ASP | GLY | PHE | ||||
| 3 | ASP | LEU | ASP | LEU | THR | TYR | VAL | THR | ASP | HIS | ||||
| 4 | VAL | ILE | ALA | MET | SER | PHE | PRO | SER | SER | GLY | ||||
| 5 | ARG | GLN | SER | LEU | PHE | ARG | ASN | PRO | ILE | GLY | ||||
| 6 | GLU | VAL | SER | ARG | PHE | PHE | LYS | THR | LYS | HIS | ||||
| 7 | PRO | ASP | LYS | PHE | ARG | ILE | TYR | ASN | LEU | CYS | ||||
| 8 | SER | GLU | ARG | GLY | TYR | ASP | GLU | THR | LYS | PHE | ||||
| 9 | ASP | ASN | HIS | VAL | TYR | ARG | VAL | MET | ILE | ASP | ||||
| 10 | ASP | HIS | ASN | VAL | PRO | THR | LEU | VAL | ASP | LEU | ||||
| 11 | LEU | LYS | PHE | ILE | ASP | ASP | ALA | LYS | VAL | TRP | ||||
| 12 | MET | THR | SER | ASP | PRO | ASP | HIS | VAL | ILE | ALA | ||||
| 13 | ILE | HIS | SER | LYS | GLY | GLY | LYS | GLY | ARG | THR | ||||
| 14 | GLY | THR | LEU | VAL | SER | SER | TRP | LEU | LEU | GLU | ||||
| 15 | ASP | GLY | LYS | PHE | ASP | THR | ALA | LYS | GLU | ALA | ||||
| 16 | LEU | GLU | TYR | PHE | GLY | SER | ARG | ARG | THR | ASP | ||||
| 17 | PHE | GLU | VAL | GLY | ASP | VAL | PHE | GLN | GLY | VAL | ||||
| 18 | GLU | THR | ALA | SER | GLN | ILE | ARG | TYR | VAL | GLY | ||||
| 19 | TYR | PHE | GLU | LYS | ILE | LYS | LYS | ASN | TYR | GLY | ||||
| 20 | GLY | GLN | LEU | PRO | PRO | MET | LYS | LYS | LEU | LYS | ||||
| 21 | VAL | THR | GLY | VAL | THR | ILE | THR | ALA | ILE | GLN | ||||
| 22 | GLY | VAL | GLY | ARG | GLY | ASN | GLY | SER | ASP | LEU | ||||
| 23 | SER | MET | GLN | ILE | VAL | SER | GLU | ARG | GLN | GLU | ||||
| 24 | VAL | LEU | LEU | CYS | LYS | PHE | ALA | GLU | GLY | TYR | ||||
| 25 | ASN | CYS | ALA | LEU | GLN | TYR | ASP | ALA | THR | ASP | ||||
| 26 | ASP | CYS | VAL | THR | CYS | GLU | VAL | LYS | ASN | CYS | ||||
| 27 | PRO | VAL | LEU | ALA | GLY | ASP | ILE | LYS | VAL | ARG | ||||
| 28 | PHE | MET | SER | THR | SER | LYS | SER | LEU | PRO | ARG | ||||
| 29 | GLY | TYR | ASP | ASN | CYS | PRO | PHE | TYR | PHE | TRP | ||||
| 30 | PHE | ASN | THR | SER | LEU | VAL | GLU | GLY | ASP | HIS | ||||
| 31 | VAL | THR | LEU | LYS | ARG | GLU | GLU | ILE | ASP | ASN | ||||
| 32 | PRO | HIS | LYS | LYS | LYS | THR | TRP | LYS | ILE | TYR | ||||
| 33 | ARG | ASP | ASN | PHE | THR | VAL | LYS | LEU | THR | PHE | ||||
| 34 | SER | ASP | ALA | GLU | ASP | ILE |
Entity 2, 4P PTEN C-tail 18 residues - Formula weight is not available
| 1 | CYS | TYR | SEP | ASP | TPO | TPO | ASP | SEP | ASP | PRO | ||||
| 2 | GLU | ASN | GLU | PRO | PHE | ASP | GLU | ASP |
Samples:
sample_1: Voltage Sensing Phosphatase, [U-13C; U-15N; U-2H], 175 uM; Tetra-phosphorylated PTEN C-tail 800 uM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; 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_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3 - collection
NMRPipe - processing
CcpNMR v2.4 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
- Bruker AVANCE NEO 900 MHz
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts