BMRB Entry 34142
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34142
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Title: p130Cas SH3 domain PTP-PEST peptide chimera PubMed: 28808245
Deposition date: 2017-05-22 Original release date: 2017-09-14
Authors: Hexnerova, R.; Veverka, V.
Citation: Gemperle, J.; Hexnerova, R.; Lepsik, M.; Tesina, P.; Dibus, M.; Novotny, M.; Brabek, J.; Veverka, V.; Rosel, D.. "Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners." Sci. Rep. 7, 8057-8057 (2017).
Assembly members:
entity_1, polymer, 100 residues, 10847.371 Da.
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):
entity_1: GSMKYLNVLAKALYDNVAES
PDELSFRKGDIMTVLERDTQ
GLDGWWLCSLHGRQGIVPGN
RLKILVGMYDKKPAGSGGSG
SGSEKQDSPPPKPPRTRSCL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 385 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 633 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 100 residues - 10847.371 Da.
| 1 | GLY | SER | MET | LYS | TYR | LEU | ASN | VAL | LEU | ALA | |
| 2 | LYS | ALA | LEU | TYR | ASP | ASN | VAL | ALA | GLU | SER | |
| 3 | PRO | ASP | GLU | LEU | SER | PHE | ARG | LYS | GLY | ASP | |
| 4 | ILE | MET | THR | VAL | LEU | GLU | ARG | ASP | THR | GLN | |
| 5 | GLY | LEU | ASP | GLY | TRP | TRP | LEU | CYS | SER | LEU | |
| 6 | HIS | GLY | ARG | GLN | GLY | ILE | VAL | PRO | GLY | ASN | |
| 7 | ARG | LEU | LYS | ILE | LEU | VAL | GLY | MET | TYR | ASP | |
| 8 | LYS | LYS | PRO | ALA | GLY | SER | GLY | GLY | SER | GLY | |
| 9 | SER | GLY | SER | GLU | LYS | GLN | ASP | SER | PRO | PRO | |
| 10 | PRO | LYS | PRO | PRO | ARG | THR | ARG | SER | CYS | LEU |
Samples:
sample_1: entity_1, [U-13C; U-15N], 0.45 mM; TCEP 1 M; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 100 mM; 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
YASARA, Krieger - refinement
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts