BMRB Entry 31288
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31288
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Yang, Yanwu; Dhayalan, Balamurugan; Ehnbom, Andreas; Weil-Ktorza, Orit; Metanis, Norman; Weiss, Michael. "Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge
" Protein Sci. 35, e70697-e70697 (2026).
PubMed: 42478539
Assembly members:
entity_1, polymer, 21 residues, 2326.647 Da.
entity_2, polymer, 32 residues, 3748.340 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: GIVEQCCTSICSLYQLENYC
G
entity_2: FVNQHLCGSHLVEALYLVCG
ERGFFYTPKTRR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 186 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 360 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
Entities:
Entity 1, unit_1 21 residues - 2326.647 Da.
| 1 | GLY | ILE | VAL | GLU | GLN | CYS | CYS | THR | SER | ILE | ||||
| 2 | CYS | SER | LEU | TYR | GLN | LEU | GLU | ASN | TYR | CYS | ||||
| 3 | GLY |
Entity 2, unit_2 32 residues - 3748.340 Da.
| 1 | PHE | VAL | ASN | GLN | HIS | LEU | CYS | GLY | SER | HIS | ||||
| 2 | LEU | VAL | GLU | ALA | LEU | TYR | LEU | VAL | CYS | GLY | ||||
| 3 | GLU | ARG | GLY | PHE | PHE | TYR | THR | PRO | LYS | THR | ||||
| 4 | ARG | ARG |
Samples:
sample_1: glargine insulin 0.3 ± 0.01 mM
sample_2: glargine insulin 0.3 ± 0.01 mM
sample_conditions_1: ionic strength: 0.1 Not defined; pH: 2.1; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1 Not defined; pH: 2.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
TopSpin, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker AVANCE NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks