BMRB Entry 10116
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR10116
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Title: The Confirmation of the Denatured Structure of Pyrrolidone Carboxyl Peptidase under Non denaturing Conditions: Helix Propensity of wild-type H6-peptide PubMed: 17979195
Deposition date: 2007-02-16 Original release date: 2008-06-27
Authors: Umezaki, Taro; Iimura, Satoshi; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide
Citation: Umezaki, Taro; Iimura, Satoshi; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide. "The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution." Proteins 71, 737-742 (2008).
Assembly members:
wild-type H6-peptide, polymer, 18 residues, 2023 Da.
Natural source: Common Name: Pyrococcus furiosus Taxonomy ID: 2261 Superkingdom: Archaea Kingdom: not available Genus/species: Pyrococcus furiosus
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
wild-type H6-peptide: SYEMELEAVKVAIEVALE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 117 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 1 |
| 3 | subunit 3 | 1 |
| 4 | subunit 4 | 1 |
Entities:
Entity 1, subunit 1 18 residues - 2023 Da.
| 1 | SER | TYR | GLU | MET | GLU | LEU | GLU | ALA | VAL | LYS | ||||
| 2 | VAL | ALA | ILE | GLU | VAL | ALA | LEU | GLU |
Samples:
sample_1: wild-type H6-peptide 0.7 mM; 2.2.2 trifluoroethanol-d2 30%
condition_1: pH: 7.0; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-1H NOESY | sample_1 | not available | condition_1 |
| HOHAHA | sample_1 | not available | condition_1 |
| DQF-COSY | sample_1 | not available | condition_1 |
Software:
xwinnmr - collection
SPARKY v3.110 - peak assignments
NMR spectrometers:
- Bruker DRX 600 MHz