BMRB Entry 25756
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25756
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Morando, Maria; Saladino, Giorgio; D'Amelio, Nicola; Pucheta-Martinez, Encarna; Lovera, Silvia; Lelli, Moreno; Lopez-Mendez, Blanca; Marenchino, Marco; Campos-Olivas, Ramon; Gervasio, Francesco. "Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase" Sci. Rep. 6, 24439-24439 (2016).
PubMed: 27087366
Assembly members:
Src_catalytic_domain, polymer, 286 residues, 32689.6 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus Gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: modified pET28
Entity Sequences (FASTA):
Src_catalytic_domain: GHMQTQGLAKDAWEIPRESL
RLEVKLGQGCFGEVWMGTWN
GTTRVAIKTLKPGTMSPEAF
LQEAQVMKKLRHEKLVQLYA
VVSEEPIYIVTEYMSKGSLL
DFLKGEMGKYLRLPQLVDMA
AQIASGMAYVERMNYVHRDL
RAANILVGENLVCKVADFGL
ARLIEDNEYTARQGAKFPIK
WTAPEAALYGRFTIKSDVWS
FGILLTELTTKGRVPYPGMV
NREVLDQVERGYRMPCPPEC
PESLHDLMCQCWRKDPEERP
TFEYLQAFLEDYFTSTEPQY
QPGENL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 540 |
| 15N chemical shifts | 179 |
| 1H chemical shifts | 179 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Src catalytic domain | 1 |
Entities:
Entity 1, Src catalytic domain 286 residues - 32689.6 Da.
| 1 | GLY | HIS | MET | GLN | THR | GLN | GLY | LEU | ALA | LYS | ||||
| 2 | ASP | ALA | TRP | GLU | ILE | PRO | ARG | GLU | SER | LEU | ||||
| 3 | ARG | LEU | GLU | VAL | LYS | LEU | GLY | GLN | GLY | CYS | ||||
| 4 | PHE | GLY | GLU | VAL | TRP | MET | GLY | THR | TRP | ASN | ||||
| 5 | GLY | THR | THR | ARG | VAL | ALA | ILE | LYS | THR | LEU | ||||
| 6 | LYS | PRO | GLY | THR | MET | SER | PRO | GLU | ALA | PHE | ||||
| 7 | LEU | GLN | GLU | ALA | GLN | VAL | MET | LYS | LYS | LEU | ||||
| 8 | ARG | HIS | GLU | LYS | LEU | VAL | GLN | LEU | TYR | ALA | ||||
| 9 | VAL | VAL | SER | GLU | GLU | PRO | ILE | TYR | ILE | VAL | ||||
| 10 | THR | GLU | TYR | MET | SER | LYS | GLY | SER | LEU | LEU | ||||
| 11 | ASP | PHE | LEU | LYS | GLY | GLU | MET | GLY | LYS | TYR | ||||
| 12 | LEU | ARG | LEU | PRO | GLN | LEU | VAL | ASP | MET | ALA | ||||
| 13 | ALA | GLN | ILE | ALA | SER | GLY | MET | ALA | TYR | VAL | ||||
| 14 | GLU | ARG | MET | ASN | TYR | VAL | HIS | ARG | ASP | LEU | ||||
| 15 | ARG | ALA | ALA | ASN | ILE | LEU | VAL | GLY | GLU | ASN | ||||
| 16 | LEU | VAL | CYS | LYS | VAL | ALA | ASP | PHE | GLY | LEU | ||||
| 17 | ALA | ARG | LEU | ILE | GLU | ASP | ASN | GLU | TYR | THR | ||||
| 18 | ALA | ARG | GLN | GLY | ALA | LYS | PHE | PRO | ILE | LYS | ||||
| 19 | TRP | THR | ALA | PRO | GLU | ALA | ALA | LEU | TYR | GLY | ||||
| 20 | ARG | PHE | THR | ILE | LYS | SER | ASP | VAL | TRP | SER | ||||
| 21 | PHE | GLY | ILE | LEU | LEU | THR | GLU | LEU | THR | THR | ||||
| 22 | LYS | GLY | ARG | VAL | PRO | TYR | PRO | GLY | MET | VAL | ||||
| 23 | ASN | ARG | GLU | VAL | LEU | ASP | GLN | VAL | GLU | ARG | ||||
| 24 | GLY | TYR | ARG | MET | PRO | CYS | PRO | PRO | GLU | CYS | ||||
| 25 | PRO | GLU | SER | LEU | HIS | ASP | LEU | MET | CYS | GLN | ||||
| 26 | CYS | TRP | ARG | LYS | ASP | PRO | GLU | GLU | ARG | PRO | ||||
| 27 | THR | PHE | GLU | TYR | LEU | GLN | ALA | PHE | LEU | GLU | ||||
| 28 | ASP | TYR | PHE | THR | SER | THR | GLU | PRO | GLN | TYR | ||||
| 29 | GLN | PRO | GLY | GLU | ASN | LEU |
Samples:
sample_1: Src catalytic domain, [U-99% 13C; U-99% 15N; U>70% 2H], 0.4 mM; magnesium chloride 1 mM; sodium chloride 500 mM; sodium azide 0.03%; TCEP 1 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 0.541 M; pH: 6.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - aid in the analysis of NMR spectra for assignment
xwinnmr, Bruker Biospin - spectra processing
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 1000 MHz
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks