BMRB Entry 54046
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR54046
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Blejec, Katerina; Smith, Colin. "Deamidation and isomerization to elusive isoaspartate in a computationally designed miniprotein
" Protein Sci. 35, e70508-e70508 (2026).
PubMed: 41725062
Assembly members:
EHEE_rd2_0005 N31D, polymer, 61 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28b
Entity Sequences (FASTA):
EHEE_rd2_0005 N31D: MGSSHHHHHHSSGLVPRGSH
MTTRYRFTDEEEARRAAKEW
ARRGYQVHVTQDGTYWEVEV
R
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 67 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EHEE_rd2_0005 N31D | 1 |
Entities:
Entity 1, EHEE_rd2_0005 N31D 61 residues - Formula weight is not available
21 residue N-term tag + 40 residue protein
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | THR | THR | ARG | TYR | ARG | PHE | THR | ASP | GLU | ||||
| 4 | GLU | GLU | ALA | ARG | ARG | ALA | ALA | LYS | GLU | TRP | ||||
| 5 | ALA | ARG | ARG | GLY | TYR | GLN | VAL | HIS | VAL | THR | ||||
| 6 | GLN | ASP | GLY | THR | TYR | TRP | GLU | VAL | GLU | VAL | ||||
| 7 | ARG |
Samples:
sample_1: EHEE_rd2_0005 N31D, [U-100% 15N], 250 uM; sodium chloride 150 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 343 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
Software:
NMRPipe - processing
FitNMR - data analysis, peak picking, peak assignment
NMR spectrometers:
- Bruker Avance 600 MHz MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks