BMRB Entry 16703
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16703
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Title: SPI2
Deposition date: 2010-02-03 Original release date: 2012-08-03
Authors: Lenarcic, Martina; Kludkiewicz, Barbara; Nowicka, Ursula; Grzelak, Krystina; Zagorski-Ostoja, Wlodzimierz; Zhukov, Igor
Citation: Lenarcic, Martina; Grzelak, Krystina; Zhukov, Igor; Zagorski-Ostoja, Wlodzimierz; Nowicka, Ursula. "High-resolution structure of atypical serine proteinase inhibitors by means of NMR spectroscopy" .
Assembly members:
spi2, polymer, 45 residues, 5033.501 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 Vector: pPICZalfaB
Entity Sequences (FASTA):
spi2: EAAVCTTEWDPVCGKDGKTY
SNLCWLNEAGVGLDHEGECH
HHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 111 |
15N chemical shifts | 38 |
1H chemical shifts | 244 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | spi2 | 1 |
Entities:
Entity 1, spi2 45 residues - 5033.501 Da.
additional two residues (EA) on N-termini; His-Tag6 on C-termini
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 | HIS | ||||
5 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: spi2 1.2 mM; H2O 90%; D2O 10%; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian Uniform NMR System 800 MHz
- Varian UnityPlus 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts