BMRB Entry 34609
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34609
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR structure of GIPC1-GH2 domain PubMed: 33808390
Deposition date: 2021-03-04 Original release date: 2021-04-11
Authors: Barthe, P.; Roumestand, C.
Citation: Dubois, Cecile; Planelles-Herrero, Vicente; Tillatte-Tripodi, Camille; Delbecq, Stephane; Mammri, Lea; Sirkia, Elena; Ropars, Virginie; Roumestand, Christian; Barthe, Philippe. "Pressure and Chemical Unfolding of an alpha-Helical Bundle Protein: the GH2 Domain of the Protein Adaptor GIPC1" Int. J. Mol. Sci. 22, 3597-3597 (2021).
Assembly members:
entity_1, polymer, 83 residues, 9181.199 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GAMGDLPSAFEEKAIEKVDD
LLESYMGIRDTELAATMVEL
GKDKRNPDELAEALDERLGD
FAFPDEFVFDVWGAIGDAKV
GRY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 222 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 532 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 83 residues - 9181.199 Da.
| 1 | GLY | ALA | MET | GLY | ASP | LEU | PRO | SER | ALA | PHE | ||||
| 2 | GLU | GLU | LYS | ALA | ILE | GLU | LYS | VAL | ASP | ASP | ||||
| 3 | LEU | LEU | GLU | SER | TYR | MET | GLY | ILE | ARG | ASP | ||||
| 4 | THR | GLU | LEU | ALA | ALA | THR | MET | VAL | GLU | LEU | ||||
| 5 | GLY | LYS | ASP | LYS | ARG | ASN | PRO | ASP | GLU | LEU | ||||
| 6 | ALA | GLU | ALA | LEU | ASP | GLU | ARG | LEU | GLY | ASP | ||||
| 7 | PHE | ALA | PHE | PRO | ASP | GLU | PHE | VAL | PHE | ASP | ||||
| 8 | VAL | TRP | GLY | ALA | ILE | GLY | ASP | ALA | LYS | VAL | ||||
| 9 | GLY | ARG | TYR |
Samples:
sample_1: GIPC1-GH2, [U-15N], 1.0 mM; TRIS 20 mM; EDTA 0.1 mM; PMSF 0.1 mM
sample_2: GIPC1-GH2, [U-13C; U-15N], 1.0 mM; TRIS 20 mM; EDTA 0.1 mM; PMSF 0.1 mM
sample_3: GIPC1-GH2 1.0 mM; TRIS 20 mM; EDTA 0.1 mM; PMSF 0.1 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
CINDY, Padilla - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts