BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27357

Title: AC12 peptide from Hypsiboas raniceps   PubMed: 30610885

Deposition date: 2018-01-11 Original release date: 2019-01-07

Authors: Popov, Claudia; Magalhaes, Beatriz; Goodfellow, Brian; Pereira, Pedro; Rodrigues, Joao; Rezende, Taia

Citation: Popov, Claudia; Magalhaes, Beatriz; Goodfellow, Brian; Bocca, Anamelia; Pereira, David; Andrade, Paula; Valentao, Patricia; Pereira, Pedro; Rodrigues, Joao; Veloso, Paulo; Rezende, Taia. "Host-defense peptides AC12, DK16 and RC11 with immunomodulatory activity isolated from Hypsiboas raniceps skin secretion"  Peptides 113, 11-21 (2019).

Assembly members:
Peptide_AC12, polymer, 12 residues, Formula weight is not available

Natural source:   Common Name: Chaco treefrog   Taxonomy ID: 192750   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Hypsiboas raniceps

Experimental source:   Production method: chemical synthesis   Host organism: Hypsiboas raniceps

Entity Sequences (FASTA):
Peptide_AC12: ACFLTRLGTYVC

Data sets:
Data typeCount
1H chemical shifts85

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AC121

Entities:

Entity 1, AC12 12 residues - Formula weight is not available

1   ALACYSPHELEUTHRARGLEUGLYTHRTYR
2   VALCYS

Samples:

sample_1: Peptide AC12 1 mM

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

NMRFAM-Sparky v1.412, Goddard, NMRFAM, Lee, W et. al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz