BMRB

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 6859

Title: 1H chemical shift assignments for peptide P2   PubMed: 16460023

Deposition date: 2005-10-10 Original release date: 2006-04-24

Authors: Martins, Rafael; Sforca, Mauricio; Amino, Rogerio; Juliano, Maria; Juliano, Luiz; Pertinhez, Thelma; Spisni, Alberto; Schenkman, Sergio

Citation: Martins, Rafael; Sforca, Mauricio; Amino, Rogerio; Juliano, Maria; Oyama, Sergio; Juliano, Luiz; Pertinhez, Thelma; Spisni, Alberto; Schenkman, Sergio. "Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin"  Biochemistry 45, 1765-1774 (2006).

Assembly members:
P2, polymer, 27 residues, 2869.6 Da.

Natural source:   Common Name: triatomine bug   Taxonomy ID: 30076   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Triatoma infestans

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
P2: KQLKKVSAVAKVAMKKGAAL LKKMGVK

Data sets:
Data typeCount
1H chemical shifts163

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1P21

Entities:

Entity 1, P2 27 residues - 2869.6 Da.

1   LYSGLNLEULYSLYSVALSERALAVALALA
2   LYSVALALAMETLYSLYSGLYALAALALEU
3   LEULYSLYSMETGLYVALLYS

Samples:

sample_1: P2 1.2 mM; TFE 30%; D2O 5%

P2_conditions: pH: 4; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
1H_TOCSYsample_1not availableP2_conditions
1H_COSYsample_1not availableP2_conditions
1H_NOESYsample_1not availableP2_conditions
1H_ROESYsample_1not availableP2_conditions

Software:

NMRView5 v5, One Moon Scientific Inc. - spectrum analysis and chemical shift assignment

NMR spectrometers:

  • Varian Varian Unity 500 spectrometer 499.730 MHz

Related Database Links:

GB AAL82380 AAL82381 ABR27919 ABR27943