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 11002

Title: NMR structure of the antimicrobial peptide RP-1 bound to SDS micelles   PubMed: 18712851

Deposition date: 2007-07-07 Original release date: 2008-08-25

Authors: Bourbigot, Sarah; Booth, Valerie; Dodd, Erin; Horwood, Chrystal; Welch, William; Sharma, Shantanu; Waring, Alan; Yeaman, Michael

Citation: Bourbigot, Sarah; Dodd, Erin; Horwood, Chrystal; Cumby, Nichole; Fardy, Liam; Welch, William; Ramjan, Zachary; Sharma, Shantanu; Waring, Alan; Yeaman, Michael; Booth, Valerie. "Antimicrobial peptide RP-1 structure and interactions with anionic versus zwitterionic micelles"  Biopolymers 91, 1-13 (2009).

Assembly members:
antimicrobial peptide RP-1 subunit 1, polymer, 18 residues, 2170.836 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: chemical synthesis

Entity Sequences (FASTA):
antimicrobial peptide RP-1 subunit 1: ALYKKFKKKLLKSLKRLG

Data sets:
Data typeCount
15N chemical shifts5
1H chemical shifts167

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 18 residues - 2170.836 Da.

1   ALALEUTYRLYSLYSPHELYSLYSLYSLEU
2   LEULYSSERLEULYSARGLEUGLY

Samples:

sample_1: entity, [U-15N]-Leu, 1.5 mM; DSS 0.4 mM; SDS, [U-99% 2H], 150 mM; sodium azide 0.4 mM

sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

SPARKY v3.110, Goddard - data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 11003
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts