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 19658

Title: The solution NMR structure of maximin-4 in SDS micelles   PubMed: 21234559

Deposition date: 2013-12-05 Original release date: 2013-12-23

Authors: Toke, Orsolya; Banoczi, Zoltan; Kiraly, Peter; Heinzmann, Ralf; Burck, Jochen; Ulrich, Anne; Hudecz, Ferenc

Citation: Toke, Orsolya; Banoczi, Zoltan; Kiraly, Peter; Heinzmann, Ralf; Burck, Jochen; Ulrich, Anne; Hudecz, Ferenc. "A kinked antimicrobial peptide fromBombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments"  Eur. Biophys. J. 40, 447-462 (2011).

Assembly members:
maximin-4, polymer, 27 residues, 2617.163 Da.

Natural source:   Common Name: large-webbed bell toad   Taxonomy ID: 161274   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bombina maxima

Experimental source:   Production method: chemical synthesis   Host organism: not applicable

Entity Sequences (FASTA):
maximin-4: GIGGVLLSAGKAALKGLAKV LAEKYAN

Data sets:
Data typeCount
1H chemical shifts188

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1maximin-41

Entities:

Entity 1, maximin-4 27 residues - 2617.163 Da.

1   GLYILEGLYGLYVALLEULEUSERALAGLY
2   LYSALAALALEULYSGLYLEUALALYSVAL
3   LEUALAGLULYSTYRALAASN

Samples:

maximin-4-SDS: maximin-41 – 1.2 mM; sodium-phosphate 10 mM; d25-sodium-dodecyl-sulfate, [U-100% 2H], 200 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 220 mM; pH: 5.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYmaximin-4-SDSisotropicsample_conditions_1
2D 1H-1H NOESYmaximin-4-SDSisotropicsample_conditions_1
2D 1H-15N HSQCmaximin-4-SDSisotropicsample_conditions_1
2D 1H-13C HSQCmaximin-4-SDSisotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

FELIX, Accelrys - peak picking, processing

ARIA, Linge, O'Donoghue and Nilges - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Varian Varian NMR System 600 MHz

Related Database Links:

APD AP00061