BMRB Entry 19589
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19589
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Title: NMR assignment of the RhoGAP domain from the Rgd1 protein of Saccharomyces cerevisiae PubMed: 29280056
Deposition date: 2013-10-29 Original release date: 2014-11-10
Authors: Martinez, Denis; Prouzet-mauleon, Valerie; Hugues, Michel; Claveres, Annie; Doignon, Francois; Odaert, Benoit
Citation: Martinez, Denis; Prouzet-Mauleon, Valerie; Hugues, Michel; Doignon, Francois; Odaert, Benoit. "Assignment of 1H, 13C and 15N resonances and secondary structure of the Rgd1-RhoGAP domain" Biomol. NMR Assign. 12, 129-132 (2018).
Assembly members:
Rgd1p-RhoGAP_domain, polymer, 226 residues, 25692 Da.
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Rgd1p-RhoGAP_domain: MISHIQTNNNMPPGVQKNFK
TFGVPLESLIEFEQDMVPAI
VRQCIYVIDKFGLDQEGIYR
KSANVLDVSKLKEEIDKDPA
NISMILPSKPHSDSDIYLVG
SLLKTFFASLPDSVLPKALS
SEIKVCLQIEDPTTRKNFMH
GLIYNLPDAQYWTLRALVFH
LKRVLAHEAQNRMNLRALCI
IWGPTIAPANPDDANDVNFQ
IMAMEVLLEVSDQAFEPELE
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 853 |
| 15N chemical shifts | 210 |
| 1H chemical shifts | 1431 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RhoGAP | 1 |
Entities:
Entity 1, RhoGAP 226 residues - 25692 Da.
The His-tag involve residues 219 to 226.
| 1 | MET | ILE | SER | HIS | ILE | GLN | THR | ASN | ASN | ASN | ||||
| 2 | MET | PRO | PRO | GLY | VAL | GLN | LYS | ASN | PHE | LYS | ||||
| 3 | THR | PHE | GLY | VAL | PRO | LEU | GLU | SER | LEU | ILE | ||||
| 4 | GLU | PHE | GLU | GLN | ASP | MET | VAL | PRO | ALA | ILE | ||||
| 5 | VAL | ARG | GLN | CYS | ILE | TYR | VAL | ILE | ASP | LYS | ||||
| 6 | PHE | GLY | LEU | ASP | GLN | GLU | GLY | ILE | TYR | ARG | ||||
| 7 | LYS | SER | ALA | ASN | VAL | LEU | ASP | VAL | SER | LYS | ||||
| 8 | LEU | LYS | GLU | GLU | ILE | ASP | LYS | ASP | PRO | ALA | ||||
| 9 | ASN | ILE | SER | MET | ILE | LEU | PRO | SER | LYS | PRO | ||||
| 10 | HIS | SER | ASP | SER | ASP | ILE | TYR | LEU | VAL | GLY | ||||
| 11 | SER | LEU | LEU | LYS | THR | PHE | PHE | ALA | SER | LEU | ||||
| 12 | PRO | ASP | SER | VAL | LEU | PRO | LYS | ALA | LEU | SER | ||||
| 13 | SER | GLU | ILE | LYS | VAL | CYS | LEU | GLN | ILE | GLU | ||||
| 14 | ASP | PRO | THR | THR | ARG | LYS | ASN | PHE | MET | HIS | ||||
| 15 | GLY | LEU | ILE | TYR | ASN | LEU | PRO | ASP | ALA | GLN | ||||
| 16 | TYR | TRP | THR | LEU | ARG | ALA | LEU | VAL | PHE | HIS | ||||
| 17 | LEU | LYS | ARG | VAL | LEU | ALA | HIS | GLU | ALA | GLN | ||||
| 18 | ASN | ARG | MET | ASN | LEU | ARG | ALA | LEU | CYS | ILE | ||||
| 19 | ILE | TRP | GLY | PRO | THR | ILE | ALA | PRO | ALA | ASN | ||||
| 20 | PRO | ASP | ASP | ALA | ASN | ASP | VAL | ASN | PHE | GLN | ||||
| 21 | ILE | MET | ALA | MET | GLU | VAL | LEU | LEU | GLU | VAL | ||||
| 22 | SER | ASP | GLN | ALA | PHE | GLU | PRO | GLU | LEU | GLU | ||||
| 23 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Rgd1p-RhoGAP domain, [U-13C; U-15N], 400 uM; Tris 20 mM; DTT 2 mM; NaN3 0.1 mM
sample_2: Rgd1p-RhoGAP domain, [U-13C; U-15N], 400 uM; Rgd1p-RhoGAP domain, [U-13C; U-15N], 300 uM; d11-Tris 20 mM; DTT 5 mM; NaN3 0.1 mM
sample_3: Rgd1p-RhoGAP domain, [U-15N], 250 uM; Tris 20 mM; DTT 5 mM; NaN3 1 mM
sample_4: Rgd1p-RhoGAP domain, [U-13C; U-15N], 700 uM; Tris 20 mM; DTT 5 mM; NaN3 1 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.35; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts