BMRB Entry 10117
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR10117
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Title: The Confirmation of the Denatured Structure of Pyrrolidone carboxyl Peptidase under Non denaturing Conditions: Deference in Helix Propensity of Two Synthetic Peptides with Single Amino Acid Substitution 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:
mutant H6-peptide, polymer, 18 residues, 2049 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):
mutant H6-peptide: SYEMELEAVKVPIEVALE
- 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 - 2049 Da.
1 | SER | TYR | GLU | MET | GLU | LEU | GLU | ALA | VAL | LYS | ||||
2 | VAL | PRO | ILE | GLU | VAL | ALA | LEU | GLU |
Samples:
sample_1: mutant 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
Related Database Links:
PDB |