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 17986

Title: Solution structure of cyclic gomesin peptide   PubMed: 23426877

Deposition date: 2011-10-08 Original release date: 2013-04-02

Authors: CHAN, LAI YUE; ZHANG, MINQUAN; HUANG, YEN-HUA; WATERS, NORMAN; BANSAL, PARAMJIT; CRAIK, DAVID; DALY, NORELLE

Citation: CHAN, LAI YUE; ZHANG, MINQUAN; HUANG, YEN-HUA; WATERS, NORMAN; BANSAL, PARAMJIT; CRAIK, DAVID; DALY, NORELLE. "Cyclization of the antimicrobial Peptide gomesin with native chemical ligation: influences on stability and bioactivity"  Chembiochem 14, 617-624 (2013).

Assembly members:
cyclic_gomesin, polymer, 18 residues, 2199.7 Da.

Natural source:   Common Name: Spiders   Taxonomy ID: 6896   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Aphonopelma not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
cyclic_gomesin: GCRRLCYKQRCVTYCRGR

Data sets:
Data typeCount
1H chemical shifts105

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1cyclic gomesin1

Entities:

Entity 1, cyclic gomesin 18 residues - 2199.7 Da.

1   GLYCYSARGARGLEUCYSTYRLYSGLNARG
2   CYSVALTHRTYRCYSARGGLYARG

Samples:

sample_1: cyclic gomesin 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

XEASY, Keller and Wuthrich - chemical shift assignment

SPARKY v3.114, Goddard - chemical shift assignment

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, data analysis, refinement

MolProbity, Richardson - data analysis

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAD67587
SP P82358