BMRB Entry 25877
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25877
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Title: Solution structure of cecropin P1 with LPS PubMed: 26939541
Deposition date: 2015-11-04 Original release date: 2016-06-15
Authors: Baek, Mihwa; Kamiya, Masakatsu; Kushibiki, Takahiro; Nakazumi, Taichi; Tomisawa, Satoshi; Abe, Chiharu; Kumaki, Yasuhiro; Kushibiki, Takahiro; Kikukawa, Takashi; Demura, Makoto; Kawano, Keiichi; Aizawa, Tomoyasu
Citation: Baek, Mihwa; Kamiya, Masakatsu; Kushibiki, Takahiro; Nakazumi, Taichi; Tomisawa, Satoshi; Abe, Chiharu; Kumaki, Yasuhiro; Kushibiki, Takahiro; Kikukawa, Takashi; Demura, Makoto; Kawano, Keiichi; Aizawa, Tomoyasu. "Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy" J. Pep. Sci. 22, 214-221 (2016).
Assembly members:
cp1, polymer, 31 residues, 3345.946 Da.
Natural source: Common Name: pig Taxonomy ID: 9823 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Sus scrofa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
cp1: SWLSKTAKKLENSAKKRISE
GIAIAIQGGPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 100 |
| 15N chemical shifts | 29 |
| 1H chemical shifts | 217 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cp1 | 1 |
Entities:
Entity 1, cp1 31 residues - 3345.946 Da.
| 1 | SER | TRP | LEU | SER | LYS | THR | ALA | LYS | LYS | LEU | ||||
| 2 | GLU | ASN | SER | ALA | LYS | LYS | ARG | ILE | SER | GLU | ||||
| 3 | GLY | ILE | ALA | ILE | ALA | ILE | GLN | GLY | GLY | PRO | ||||
| 4 | ARG |
Samples:
natural_CP1: cp1 1 mM; H2O 90%; D2O 10%
13C15N-CP1: cp1, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%
15N-CP1: cp1, [U-15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15N-CP1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | natural_CP1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | natural_CP1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 3D HNCA | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C15N-CP1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N-CP1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 15N-CP1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 13C15N-CP1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts