BMRB Entry 17441

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17441
MolProbity Validation Chart

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Title:
LAK160-P10
Deposition date:
2011-02-03
Original release date:
2012-02-14
Authors:
Vermeer, Louic; Bui, Tam; Lan, Yun; Jumagulova, Elmira; Kozlowska, Justyna; McIntyre, Caitlin; Drake, Alex; Mason, James
Citation:

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).
PubMed: 22869378

Assembly members:

Assembly members:
LAK160-P710, polymer, 24 residues, 2666.540 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LAK160-P710: KKLKLALAKPALLWKALALK LKKA

Data sets:
Data typeCount
1H chemical shifts49

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1LAK160-P7101

Entities:

Entity 1, LAK160-P710 24 residues - 2666.540 Da.

1   LYSLYSLEULYSLEUALALEUALALYSPRO
2   ALALEULEUTRPLYSALALEUALALEULYS
3   LEULYSLYSALA

Samples:

sample_1: LAK160-P710 1 mM; SDS 100 mM; TRIS 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

AQUA v2.2, Zimmerman, Moseley, Kulikowski and Montelione - data analysis

ARIA v2.2, Linge, O'Donoghue and Nilges - structure solution

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

ProcheckNMR v3.5.4, Laskowski and MacArthur - data analysis

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

Python v2.6.5, Python Software Foundation - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

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