BMRB Entry 34314
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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/BMR34314
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Citation: Blatter, M.; Schneider, G.. "Peptide-membrane interaction between targeting and lysis" .
Assembly members:
entity_1, polymer, 15 residues, 1616.106 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: Escherichia coli
Entity Sequences (FASTA):
entity_1: GLFDIVKKVLKLLKX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 61 |
| 1H chemical shifts | 130 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 15 residues - 1616.106 Da.
| 1 | GLY | LEU | PHE | ASP | ILE | VAL | LYS | LYS | VAL | LEU | ||||
| 2 | LYS | LEU | LEU | LYS | NH2 |
Samples:
sample_1: peptide 10 mM
sample_conditions_1: ionic strength: 0 mM; pH: 5; pressure: 1 Pa; temperature: 291 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker AvanceIII 500 MHz