BMRB Entry 15330
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15330
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Citation: Mysliwy, Justyna; Dingley, Andrew; Stanisak, Mareike; Jung, Sascha; Lorenzen, Inken; Roeder, Thomas; Leippe, Matthias; Grotzinger, Joachim. "Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans." Dev. Comp. Immunol. 34, 323-330 (2010).
PubMed: 19917307
Assembly members:
caenopore-5, polymer, 99 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pIVEX2.4a
Entity Sequences (FASTA):
caenopore-5: MSGSHHHHHHSSGIEGRGRS
ALSCQMCELVVKKYEGSADK
DANVIKKDFDAECKKLFHTI
PFGTRECDHYVNSKVDPIIH
ELEGGTAPKDVCTKLNECP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 529 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | caenopore-5 Pro cis conformer | 1 |
Entities:
Entity 1, caenopore-5 Pro cis conformer 99 residues - Formula weight is not available
Residues 1-18 a non-native affinity tag
| 1 | MET | SER | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | ILE | GLU | GLY | ARG | GLY | ARG | SER | ||||
| 3 | ALA | LEU | SER | CYS | GLN | MET | CYS | GLU | LEU | VAL | ||||
| 4 | VAL | LYS | LYS | TYR | GLU | GLY | SER | ALA | ASP | LYS | ||||
| 5 | ASP | ALA | ASN | VAL | ILE | LYS | LYS | ASP | PHE | ASP | ||||
| 6 | ALA | GLU | CYS | LYS | LYS | LEU | PHE | HIS | THR | ILE | ||||
| 7 | PRO | PHE | GLY | THR | ARG | GLU | CYS | ASP | HIS | TYR | ||||
| 8 | VAL | ASN | SER | LYS | VAL | ASP | PRO | ILE | ILE | HIS | ||||
| 9 | GLU | LEU | GLU | GLY | GLY | THR | ALA | PRO | LYS | ASP | ||||
| 10 | VAL | CYS | THR | LYS | LEU | ASN | GLU | CYS | PRO |
Samples:
sample_1: caenopore-5, [U-99% 13C; U-99% 15N], 1-2 mM; sodium phosphate 50 mM
sample1_conditions: ionic strength: 0.05 M; pH: 5.2; pressure: 1 atm; temperature: 297 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample1_conditions |
| 3D HNCA | sample_1 | isotropic | sample1_conditions |
| 3D H(CCO)NH | sample_1 | isotropic | sample1_conditions |
| 3D C(CO)NH | sample_1 | isotropic | sample1_conditions |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample1_conditions |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample1_conditions |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample1_conditions |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample1_conditions |
Software:
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks