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 15463

Title: Spatial Structure and Hydrophobic Organization Determine Membrane Activity of Latarcins, Spider Antimicrobial Peptides   PubMed: 18293934

Deposition date: 2007-09-10 Original release date: 2008-07-08

Authors: Dubovskii, P.; Volynsky, P.; Polyansky, A.; Chupin, V.; Efremov, R.; Arseniev, A.

Citation: Dubovskii, P.; Volynsky, P.; Polyansky, A.; Karpunin, D.; Chupin, V.; Efremov, R.; Arseniev, A.. "Three-dimensional structure/hydrophobicity of latarcins specifies their mode of membrane activity"  Biochemistry 47, 3525-3533 (2008).

Assembly members:
Latarcin-1, polymer, 26 residues, Formula weight is not available

Natural source:   Common Name: Lachesana tarabaevi   Taxonomy ID: 379576   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lachesana tarabaevi

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Latarcin-1: SMWSGMWRRKLKKLRNALKK KLKGEK

Data sets:
Data typeCount
1H chemical shifts156

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Latarcin-11

Entities:

Entity 1, Latarcin-1 26 residues - Formula weight is not available

1   SERMETTRPSERGLYMETTRPARGARGLYS
2   LEULYSLYSLEUARGASNALALEULYSLYS
3   LYSLEULYSGLYGLULYS

Samples:

sample_1: Latarcin-1 2 ± 0.1 mM; perdeuterated SDS 120 mM; H2O 90%; D2O 10%

sample_2: Latarcin-1 2 ± 0.1 mM; perdeuterated SDS 120 mM; D2O 100%

sample_conditions_1: pH: 7.1; pressure: 0.99 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D TOCSYsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
DQF-COSYsample_2isotropicsample_conditions_1

Software:

CYANA v1.0.6., Guentert P. - refinement

xwinnmr v3.1.a, BRUKER - collection

XEASY v40300000, Xia & Bartels - data analysis

FANMEM v4.1, Nolde, Arseniev, Vergoten, Efremov - refinement

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB
EMBL CAJ81660
SP Q1ELT9