BMRB Entry 34090
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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/BMR34090
MolProbity Validation Chart
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NMR-STAR v3 text file.
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RDF gzip file.
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Citation: Stutz, Katharina; Muller, Alex; Hiss, Jan; Schneider, Petra; Blatter, Markus; Pfeiffer, Bernhard; Posselt, Gernot; Kanfer, Gil; Kornmann, Benoit; Wrede, Paul; Altmann, Karl-Heinz; Wessler, Silja; Schneider, Gisbert. "Peptide-Membrane Interaction between Targeting and Lysis." ACS Chem. Biol. 12, 2254-2259 (2017).
PubMed: 28763193
Assembly members:
entity_1, polymer, 15 residues, 1415.743 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: synthetic construct
Entity Sequences (FASTA):
entity_1: GLFDIVKKVVGALGX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 49 |
| 1H chemical shifts | 108 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 15 residues - 1415.743 Da.
| 1 | GLY | LEU | PHE | ASP | ILE | VAL | LYS | LYS | VAL | VAL | ||||
| 2 | GLY | ALA | LEU | GLY | NH2 |
Samples:
sample_1: peptide 1%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0 pH*; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY STRUCTURE a DETERMINATION. | sample_1 | anisotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker Avance III 500 MHz