BMRB Entry 15639
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15639
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Title: 1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris PubMed: 18361918
Deposition date: 2008-01-25 Original release date: 2008-05-28
Authors: Kumaki, Yasuhiro; Kawano, Keiichi; Hikichi, Kunio; Matsumoto, Takeshi; Matsushima, Norio
Citation: Kumaki, Yasuhiro; Kawano, Keiichi; Hikichi, Kunio; Matsumoto, Takeshi; Matsushima, Norio. "A circular loop of the sixteen-residue repeating unit in ice nucleation protein" Biochem. Biophys. Res. Commun. 371, 5-9 (2008).
Assembly members:
model_peptide_for_INP, polymer, 17 residues, Formula weight is not available
Natural source: Common Name: Xanthomonas campestris Taxonomy ID: 339 Superkingdom: Bacteria Kingdom: not available Genus/species: Xanthomonas campestris
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
model_peptide_for_INP: XTARKGSDLTTGYGSTX
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 1H chemical shifts | 103 |
| coupling constants | 10 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | polymer chains | 1 |
Entities:
Entity 1, polymer chains 17 residues - Formula weight is not available
| 1 | NLQ | THR | ALA | ARG | LYS | GLY | SER | ASP | LEU | THR | ||||
| 2 | THR | GLY | TYR | GLY | SER | THR | SET |
Samples:
sample_1: model peptide for INP 3 mM; DSS 1 mM
sample_conditions_1: ionic strength: 0 M; pH: 4.4; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
Delta v4.3.2, JEOL - processing
NMR spectrometers:
- JEOL ALPHA 500 MHz