BMRB Entry 25317
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25317
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Citation: Platzer, Gerald; Okon, Mark; McIntosh, Lawrence. "pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements" J. Biomol. NMR 60, 109-129 (2014).
PubMed: 25239571
Assembly members:
ACE-GLY-ASP-GLY-NH2 peptide, polymer, 5 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: chemical synthesis
Entity Sequences (FASTA):
ACE-GLY-ASP-GLY-NH2 peptide: XGDGX
- pH_titration
- pH_param_list
| Data type | Count |
| pKa values | 24 |
| pH NMR parameter values | 201 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ACE-GLY-ASP-GLY-NH2 peptide | 1 |
Entities:
Entity 1, ACE-GLY-ASP-GLY-NH2 peptide 5 residues - Formula weight is not available
| 1 | ACE | GLY | ASP | GLY | NH2 |
Samples:
sample_1: blocked tripeptide, [U-13C; U-15N], 10 mM; NaCl 50 mM
sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 50 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H-NMR | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| multiple-bond 13C HMBC | sample_1 | isotropic | sample_conditions_1 |
| multiple-bond 15N HMBC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3, Bruker Biospin - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz