BMRB Entry 18153
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18153
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Title: The solution structure of thermomacin
Deposition date: 2011-12-20 Original release date: 2012-02-28
Authors: Jung, sascha; Soennichsen, Frank; Hung, Chien-Wen; Thoely, Andreas; Boidin-Wichlacz, Celine; Gelhaus, Christoph; Podschun, Rainer; Tasiemski, Aurelie; Leippe, Matthias; Groetzinger, Joachim
Citation: Jung, sascha; Soennichsen, Frank; Hung, Chien-Wen; Thoely, Andreas; Boidin-Wichlacz, Celine; Gelhaus, Christoph; Podschun, Rainer; Tasiemski, Aurelie; Leippe, Matthias; Groetzinger, Joachim. "The Macin Family of Antimicrobial Proteins Combines Antimicrobial and Nerve-Repair Activities" J. Biol. Chem. ., .-..
Assembly members:
entity, polymer, 75 residues, 8465.560 Da.
Natural source: Common Name: medicinal leech Taxonomy ID: 6421 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hirudo medicinalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GCFEDWSRCSPSTASATGVL
WRSCDSYCKVCFKADRGECY
DSPSLNCPHRLPNNKQCRCI
NARTAKDNRNPTCWA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 125 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 306 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | thermomacin | 1 |
Entities:
Entity 1, thermomacin 75 residues - 8465.560 Da.
| 1 | GLY | CYS | PHE | GLU | ASP | TRP | SER | ARG | CYS | SER | ||||
| 2 | PRO | SER | THR | ALA | SER | ALA | THR | GLY | VAL | LEU | ||||
| 3 | TRP | ARG | SER | CYS | ASP | SER | TYR | CYS | LYS | VAL | ||||
| 4 | CYS | PHE | LYS | ALA | ASP | ARG | GLY | GLU | CYS | TYR | ||||
| 5 | ASP | SER | PRO | SER | LEU | ASN | CYS | PRO | HIS | ARG | ||||
| 6 | LEU | PRO | ASN | ASN | LYS | GLN | CYS | ARG | CYS | ILE | ||||
| 7 | ASN | ALA | ARG | THR | ALA | LYS | ASP | ASN | ARG | ASN | ||||
| 8 | PRO | THR | CYS | TRP | ALA |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; H2O 93%; D2O 7%; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 7.4; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Brunger, Adams, Clore, Gros, Nilges and Read, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Guntert, Mumenthaler and Wuthrich, Johnson, One Moon Scientific - chemical shift assignment, processing, refinement, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
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