BMRB Entry 16876
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16876
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1HN, 1HA, 13CA, 13CB, 13CO and 15N Chemical Shift Assignments for Intrinsically Disordered Dehydrin ERD14 PubMed: 21336827
Deposition date: 2010-04-16 Original release date: 2011-05-05
Authors: Szalaine Agoston, Bianka; Tompa, Peter; Perczel, Andras
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).
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
Entity Sequences (FASTA):
ERD14: MAEEIKNVPEQEVPKVATEE
SSAEVTDRGLFDFLGKKKDE
TKPEETPIASEFEQKVHISE
PEPEVKHESLLEKLHRSDSS
SSSSSEEEGSDGEKRKKKKE
KKKPTTEVEVKEEEKKGFME
KLKEKLPGHKKPEDGSAVAA
APVVVPPPVEEAHPVEKKGI
LEKIKEKLPGYHPKTTVEEE
KKDKE
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T1rho_relaxation
- heteronucl_T2_relaxation
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 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ERD14 | 1 |
Entities:
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 |
Samples:
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
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 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 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Swiss NMR - chemical shift assignment
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Bruker DRX 600 MHz
Related Database Links:
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 shifts
SPARKY: Backbone
or all simulated shifts