Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16876
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Citation: Szalaine Agoston, Bianka; Kovacs, Denes; Tompa, Peter; Perczel, Andras. "Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14." Biomol. NMR Assignments 5, 189-193 (2011).
PubMed: 21336827
Assembly members:
ERD14, polymer, 185 residues, 20786.3 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET23b
| Data type | Count |
| 13C chemical shifts | 532 |
| 15N chemical shifts | 182 |
| 1H chemical shifts | 328 |
| heteronuclear NOE values | 167 |
| T1 relaxation values | 167 |
| T1rho relaxation values | 167 |
| T2 relaxation values | 167 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ERD14 | 1 |
Entity 1, ERD14 185 residues - 20786.3 Da.
| 1 | MET | ALA | GLU | GLU | ILE | LYS | ASN | VAL | PRO | GLU | ||||
| 2 | GLN | GLU | VAL | PRO | LYS | VAL | ALA | THR | GLU | GLU | ||||
| 3 | SER | SER | ALA | GLU | VAL | THR | ASP | ARG | GLY | LEU | ||||
| 4 | PHE | ASP | PHE | LEU | GLY | LYS | LYS | LYS | ASP | GLU | ||||
| 5 | THR | LYS | PRO | GLU | GLU | THR | PRO | ILE | ALA | SER | ||||
| 6 | GLU | PHE | GLU | GLN | LYS | VAL | HIS | ILE | SER | GLU | ||||
| 7 | PRO | GLU | PRO | GLU | VAL | LYS | HIS | GLU | SER | LEU | ||||
| 8 | LEU | GLU | LYS | LEU | HIS | ARG | SER | ASP | SER | SER | ||||
| 9 | SER | SER | SER | SER | SER | GLU | GLU | GLU | GLY | SER | ||||
| 10 | ASP | GLY | GLU | LYS | ARG | LYS | LYS | LYS | LYS | GLU | ||||
| 11 | LYS | LYS | LYS | PRO | THR | THR | GLU | VAL | GLU | VAL | ||||
| 12 | LYS | GLU | GLU | GLU | LYS | LYS | GLY | PHE | MET | GLU | ||||
| 13 | LYS | LEU | LYS | GLU | LYS | LEU | PRO | GLY | HIS | LYS | ||||
| 14 | LYS | PRO | GLU | ASP | GLY | SER | ALA | VAL | ALA | ALA | ||||
| 15 | ALA | PRO | VAL | VAL | VAL | PRO | PRO | PRO | VAL | GLU | ||||
| 16 | GLU | ALA | HIS | PRO | VAL | GLU | LYS | LYS | GLY | ILE | ||||
| 17 | LEU | GLU | LYS | ILE | LYS | GLU | LYS | LEU | PRO | GLY | ||||
| 18 | TYR | HIS | PRO | LYS | THR | THR | VAL | GLU | GLU | GLU | ||||
| 19 | LYS | LYS | ASP | LYS | GLU |
sample_1: ERD14, [U-99% 13C; U-99% 15N], 1 mM; MES 10 mM; H2O 90%; D2O 10%
sample_2: ERD14, [U-99% 15N], 1 mM; MES 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 10 mM; pH: 6.54; pressure: 1 atm; temperature: 288 K
| 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNN | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)N | sample_1 | isotropic | sample_conditions_1 |
| 3D HNN-COSY | sample_1 | isotropic | sample_conditions_1 |
| 13C-det. H(CA)CON | sample_1 | isotropic | sample_conditions_1 |
| R1-measurement | sample_2 | isotropic | sample_conditions_1 |
| hetNOE measurement | sample_2 | isotropic | sample_conditions_1 |
| R2 measurement | sample_2 | isotropic | sample_conditions_1 |
| R1rho measurement | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - collection, processing
CARA, Swiss NMR - chemical shift assignment
SPARKY, Goddard - data analysis
| BMRB | 26636 |
| DBJ | BAA04569 BAE98985 |
| GB | AAF17644 AAG40050 AAG41486 AAK00404 AAK62649 |
| REF | NP_001185408 NP_177745 |
| SP | P42763 |
| AlphaFold | P42763 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks