BMRB Entry 51835
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51835
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Title: Binding of Rho GDP-dissociation inhibitor to its GTPase clients relies on preformed secondary structural properties of the binding interface PubMed: 38853146
Deposition date: 2023-02-16 Original release date: 2024-06-27
Authors: Medina-Gomez, Sara; Visco, Ilaria; Merino, Felipe; Bieling, Peter; Linser, Rasmus
Citation: Medina-Gomez, Sara; Visco, Ilaria; Merino, Felipe; Bieling, Peter; Linser, Rasmus. "Transient Structural Properties of the Rho GDP-Dissociation Inhibitor" Angew. Chem. Int. Ed. Engl. 63, e202403941-e202403941 (2024).
Assembly members:
entity_1, polymer, 208 residues, Formula weight is not available
Natural source: Common Name: cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6P
Entity Sequences (FASTA):
entity_1: GPLGMAEQEPTAEQLAQIAA
ENEEDEHSVNYKPPAQKSIQ
EIQELDKDDESLRKYKEALL
GRVAVSADPNVPNVVVTRLT
LVSSTAPGPLELDLTGDLES
FKKQSFVLKEGVEYRIKISF
RVNREIVSGMKYIQHTYRKG
VKIDKTDYMVGSYGPRAEEY
EFLTPMEEAPKGMLARGSYN
IKSRFTDDDRTDHLSWEWNL
TIKKEWKD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 505 |
15N chemical shifts | 156 |
1H chemical shifts | 156 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RhoGDI | 1 |
Entities:
Entity 1, RhoGDI 208 residues - Formula weight is not available
1 | GLY | PRO | LEU | GLY | MET | ALA | GLU | GLN | GLU | PRO | ||||
2 | THR | ALA | GLU | GLN | LEU | ALA | GLN | ILE | ALA | ALA | ||||
3 | GLU | ASN | GLU | GLU | ASP | GLU | HIS | SER | VAL | ASN | ||||
4 | TYR | LYS | PRO | PRO | ALA | GLN | LYS | SER | ILE | GLN | ||||
5 | GLU | ILE | GLN | GLU | LEU | ASP | LYS | ASP | ASP | GLU | ||||
6 | SER | LEU | ARG | LYS | TYR | LYS | GLU | ALA | LEU | LEU | ||||
7 | GLY | ARG | VAL | ALA | VAL | SER | ALA | ASP | PRO | ASN | ||||
8 | VAL | PRO | ASN | VAL | VAL | VAL | THR | ARG | LEU | THR | ||||
9 | LEU | VAL | SER | SER | THR | ALA | PRO | GLY | PRO | LEU | ||||
10 | GLU | LEU | ASP | LEU | THR | GLY | ASP | LEU | GLU | SER | ||||
11 | PHE | LYS | LYS | GLN | SER | PHE | VAL | LEU | LYS | GLU | ||||
12 | GLY | VAL | GLU | TYR | ARG | ILE | LYS | ILE | SER | PHE | ||||
13 | ARG | VAL | ASN | ARG | GLU | ILE | VAL | SER | GLY | MET | ||||
14 | LYS | TYR | ILE | GLN | HIS | THR | TYR | ARG | LYS | GLY | ||||
15 | VAL | LYS | ILE | ASP | LYS | THR | ASP | TYR | MET | VAL | ||||
16 | GLY | SER | TYR | GLY | PRO | ARG | ALA | GLU | GLU | TYR | ||||
17 | GLU | PHE | LEU | THR | PRO | MET | GLU | GLU | ALA | PRO | ||||
18 | LYS | GLY | MET | LEU | ALA | ARG | GLY | SER | TYR | ASN | ||||
19 | ILE | LYS | SER | ARG | PHE | THR | ASP | ASP | ASP | ARG | ||||
20 | THR | ASP | HIS | LEU | SER | TRP | GLU | TRP | ASN | LEU | ||||
21 | THR | ILE | LYS | LYS | GLU | TRP | LYS | ASP |
Samples:
sample_1: RhoGDI1, [U-13C; U-15N; U-2H], 600 uM; HEPES 20 mM; potassium chloride 150 mM; TCEP 0.5 mM; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 287 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v3.1.0 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts