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 17438

Title: LAK160-P7   PubMed: 22869378

Deposition date: 2011-02-01 Original release date: 2012-01-30

Authors: Vermeer, Louic; Bui, Tam; Lan, Yun; Jumagulova, Elmira; Kozlowska, Justyna; McIntyre, Caitlin; Drake, Alex; Mason, James

Citation: Vermeer, Louic; Lan, Yun; Abbate, Vincenzo; Ruh, Emrah; Bui, Tam; Wilkinson, Louise; Kanno, Tokuwa; Jumagulova, Elmira; Kozlowska, Justyna; Patel, Jayneil; McIntyre, Caitlin; Yam, W.; Siu, Gilman; Atkinson, R.; Lam, Jenny; Bansal, Sukhvinder; Drake, Alex; Mitchell, Graham; Mason, A.. "Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides"  J. Biol. Chem. 287, 34120-34133 (2012).

Assembly members:
LAK160-P7, polymer, 24 residues, 2666.540 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: obtained from a vendor

Entity Sequences (FASTA):
LAK160-P7: KKLKLAPAKLALLWKALALK LKKA

Data sets:
Data typeCount
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LAK160-P71

Entities:

Entity 1, LAK160-P7 24 residues - 2666.540 Da.

1   LYSLYSLEULYSLEUALAPROALALYSLEU
2   ALALEULEUTRPLYSALALEUALALEULYS
3   LEULYSLYSALA

Samples:

sample_1: LAK160-P7 1 mM; SDS 100 mM; TRIS 5 mM; H2O 90%; D2O 10%

sample_conditions: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

ARIA v2.2, Linge, O, . - refinement, structure solution

TOPSPIN v3.0, Bruker Biospin - collection, processing

ProcheckNMR v3.5.4, Laskowski and MacArthur - data analysis

AQUA v3.2, Rullmann, Doreleijers and Kaptein - data analysis

CNSSOLVE v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Python v2.6.5, Python Software Foundation - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

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