Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15639

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

Data sets:
Data typeCount
1H chemical shifts103
coupling constants10

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1polymer chains1


Entity 1, polymer chains 17 residues - Formula weight is not available



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


NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1


Delta v4.3.2, JEOL - processing

NMR spectrometers:

  • JEOL ALPHA 500 MHz

Related Database Links:

BMRB 20010