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 6499

Title: NMR structure of antimicrobial peptide distinctin in water   PubMed: 15840728

Authors: Amodeo, P.; Raimondo, D.; Andreotti, G.; Motta, A.; Scaloni, A.

Citation: Raimondo, D.; Andreotti, G.; Saint, N.; Amodeo, P.; Renzone, G.; Sanseverino, M.; Zocchi, I.; Molle, G.; Motta, A.; Scaloni, A.. "A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin."  Proc. Natl. Acad. Sci. U. S. A. ., .-..

Assembly members:
Distinctin chain A, polymer, 22 residues, Formula weight is not available
Distinctin chain B, polymer, 25 residues, Formula weight is not available

Natural source:   Common Name: tree frog   Taxonomy ID: 164618   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Phyllomedusa distincta

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Distinctin chain A: ENREVPPGFTALIKTLRKCK II
Distinctin chain B: NLVSGLIEARKYLEQLHRKL KNCKV

Data sets:
Data typeCount
1H chemical shifts413

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Distinctin chain A monomer 11
2Distinctin chain B monomer 12
3Distinctin chain A monomer 21
4Distinctin chain B monomer 22

Entities:

Entity 1, Distinctin chain A monomer 1 22 residues - Formula weight is not available

1   GLUASNARGGLUVALPROPROGLYPHETHR
2   ALALEUILELYSTHRLEUARGLYSCYSLYS
3   ILEILE

Entity 2, Distinctin chain B monomer 1 25 residues - Formula weight is not available

1   ASNLEUVALSERGLYLEUILEGLUALAARG
2   LYSTYRLEUGLUGLNLEUHISARGLYSLEU
3   LYSASNCYSLYSVAL

Samples:

sample_1: Distinctin chain A0.05 – 3.8 mM; Distinctin chain B0.05 – 3.8 mM; Phosphate 20 mM; NaCl 100 mM

sample_cond_1: ionic strength: 0.15 M; pH: 5.8; pressure: 1 atm; temperature: 300 K

sample_cond_2: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available

Software:

AMBER v5 - refinement, structure solution

Molmol v2K.2 - data analysis

xwinnmr v3.5 - processing

NMR spectrometers:

  • Bruker DRX 500 MHz

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