BMRB Entry 15640
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15640
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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, 19 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: XDSSLTAGYGSTQTARKGX
- assigned_chemical_shifts
- coupling_constants
Data type | Count |
1H chemical shifts | 102 |
coupling constants | 11 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | model peptide for INP | 1 |
Entities:
Entity 1, model peptide for INP 19 residues - Formula weight is not available
1 | ACE | ASP | SER | SER | LEU | THR | ALA | GLY | TYR | GLY | ||||
2 | SER | THR | GLN | THR | ALA | ARG | LYS | GLY | NH2 |
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