BMRB Entry 11003
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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/BMR11003
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Title: NMR structure of the antimicrobial peptide RP-1 bound to DPC 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
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 5 |
| 1H chemical shifts | 161 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 18 residues - 2170.836 Da.
| 1 | ALA | LEU | TYR | LYS | LYS | PHE | LYS | LYS | LYS | LEU | ||||
| 2 | LEU | LYS | SER | LEU | LYS | ARG | LEU | GLY |
Samples:
sample_1: entity, [U-15N]-Leu, 1.5 mM; DSS 0.4 mM; DPC, [U-99% 2H], 150 mM; sodium azide 0.4 mM
sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts