BMRB Entry 15042
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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/BMR15042
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Title: DPC micelle-bound NMR structures of Tritrp5 PubMed: 16997878
Deposition date: 2006-11-20 Original release date: 2007-10-30
Authors: Schibli, D.; Nguyen, L.
Citation: Schibli, D.; Nguyen, L.; Kernaghan, S.; Rekdal, O.; Vogel, H.. "Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions and their micelle-bound NMR structures" Biophys. J. 91, 4413-4426 (2006).
Assembly members:
Tritrp5, polymer, 14 residues, Formula weight is not available
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):
Tritrp5: VRRYPWWWPYLRRX
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 102 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Tritrp5 | 1 |
Entities:
Entity 1, Tritrp5 14 residues - Formula weight is not available
1 | VAL | ARG | ARG | TYR | PRO | TRP | TRP | TRP | PRO | TYR | ||||
2 | LEU | ARG | ARG | NH2 |
Samples:
sample: Tritrp51 2 mM; DPC-d38 150 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 4.8; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H NOESY | sample | isotropic | sample_conditions_1 |
1H TOCSY | sample | isotropic | sample_conditions_1 |
1H COSY | sample | isotropic | sample_conditions_1 |
Software:
ARIA, J Linge, S O, . - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz