BMRB Entry 19085
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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/BMR19085
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Title: Novel method of protein purification for structural research. Example of ultra high resolution structure of SPI-2 inhibitor by X-ray and NMR spectroscopy.
Deposition date: 2013-03-12 Original release date: 2014-03-10
Authors: Lenarcic Zivkovic, Martina; Dvornyk, Angela; Kludkiewicz, Barbara; Kopera, Edyta; Zagorski-Ostoja, Wlodzimierz; Grzelak, Krystyna; Zhukov, Igor; Bal, Wojciech
Citation: Kopera, Edyta; Krzywda, Szymon; Lenarcic Zivkovic, Martina; Dvornyk, Angela; Kludkiewicz, Barbara; Grzelak, Krystyna; Zhukov, Igor; Zagorski-Ostoja, Wlodzimierz; Jaskolski, Mariusz; Bal, Wojciech. "Ultrahigh resolution protein structure enabled by a non-enzymatic tag removal method. X-ray and NMR study of SPI-2 inhibitor" Not known ., .-..
Assembly members:
GmSPI_2, polymer, 40 residues, 4317.768 Da.
Natural source: Common Name: Greater wax moth Taxonomy ID: 7137 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Galleria mellonella
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
GmSPI_2: EAAVCTTEWDPVCGKDGKTY
SNLCWLNEAGVGLDHEGECL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 96 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 241 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SPI-2 inhibitor | 1 |
Entities:
Entity 1, SPI-2 inhibitor 40 residues - 4317.768 Da.
Non-native residues 1-3 and 40 originated from cloning procedures and protein processing in Pichia pastoris.
| 1 | GLU | ALA | ALA | VAL | CYS | THR | THR | GLU | TRP | ASP | |
| 2 | PRO | VAL | CYS | GLY | LYS | ASP | GLY | LYS | THR | TYR | |
| 3 | SER | ASN | LEU | CYS | TRP | LEU | ASN | GLU | ALA | GLY | |
| 4 | VAL | GLY | LEU | ASP | HIS | GLU | GLY | GLU | CYS | LEU |
Samples:
sample_1: GmSPI 2 0.5 mM
sample_conditions_1: ionic strength: 50 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
No software information available
NMR spectrometers:
- Varian Uniform NMR System 800 MHz
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts