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 18861

Title: NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles   PubMed: 23681729

Authors: Shenkarev, Zakhar; Paramonov, Alexander; Gizatullina, Albina

Citation: Shenkarev, Zakhar; Paramonov, Alexander; Lyukmanova, Ekaterina; Gizatullina, Albina; Zhuravleva, Anastasia; Tagaev, Andrey; Yakimenko, Zoya; Telezhinskaya, Irina; Kirpichnikov, Mikhail; Ovchinnikova, Tatiana; Arseniev, Alexander. "Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model."  Chem. Biodivers. 10, 838-863 (2013).

Assembly members:
ANTIAMOEBIN_I, polymer, 17 residues, 1628.970 Da.

Natural source:   Common Name: Emericellopsis minima   Taxonomy ID: 45245   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Emericellopsis Minima

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):
ANTIAMOEBIN_I: XFXXXXGLXXXQXXXPX

Data sets:
Data typeCount
13C chemical shifts64
15N chemical shifts14
1H chemical shifts113

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Antiamoebin I1

Entities:

Entity 1, Antiamoebin I 17 residues - 1628.970 Da.

1   ACEPHEAIBAIBAIBDIVGLYLEUAIBAIB
2   HYPGLNDIVHYPAIBPROPHL

Samples:

sample_1: DHPC 120 mM; DMPC 30 mM; acetic acid 7.5 mM; sodium acetate 2.5 mM; ANTIAMOEBIN I, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: pH: 5.1; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

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