BMRB Entry 15641

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15641

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Title:
1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 24-residue peptide corresponding to the segment within ice nucleation protein of Erwinia uredovora, Erwinia herbicola
Deposition date:
2008-01-25
Original release date:
2008-05-28
Authors:
Kumaki, Yasuhiro; Kawano, Keiichi; Hikichi, Kunio; Matsumoto, Takeshi; Matsushima, Norio
Citation:

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).
PubMed: 18361918

Assembly members:

Assembly members:
model_peptide_for_INP, polymer, 24 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Erwinia herbicola   Taxonomy ID: 553   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pantoea ananatis

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
model_peptide_for_INP: SGLRSVLTAGYGSSLISGRR SSLT

Data sets:
Data typeCount
1H chemical shifts151
coupling constants12

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1polymer chains1

Entities:

Entity 1, polymer chains 24 residues - Formula weight is not available

1   SERGLYLEUARGSERVALLEUTHRALAGLY
2   TYRGLYSERSERLEUILESERGLYARGARG
3   SERSERLEUTHR