BMRB Entry 15051
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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/BMR15051
MolProbity Validation Chart
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NMR-STAR v3 text file.
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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).
PubMed: 16997878
Assembly members:
Prophenin1, 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):
Prophenin1: VRRFPWWWPFLRRX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Prophenin1 | 1 |
Entities:
Entity 1, Prophenin1 14 residues - Formula weight is not available
| 1 | VAL | ARG | ARG | PHE | PRO | TRP | TRP | TRP | PRO | PHE | ||||
| 2 | LEU | ARG | ARG | NH2 |
Samples:
sample: Tritrp11 – 3 mM; DPC-d38 150 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 4.5; 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'Donoghue and M Nilges - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz