BMRB Entry 36288
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36288
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Title: Solution structure of Gaussia Liciferase by NMR
Deposition date: 2019-09-19 Original release date: 2019-11-20
Authors: Kobayashi, N.; Yamazaki, T.
Citation: Wu, N.; Kobayashi, N.; Tsuda, K.; Unzai, S.; Saotome, T.; Kuroda, Y.; Yamazaki, T.. "Solution structure of Gaussia Liciferase by NMR" .
Assembly members:
entity_1, polymer, 174 residues, 18851.838 Da.
Natural source: Common Name: Gaussia princeps Taxonomy ID: 148582 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gaussia princeps
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21c
Entity Sequences (FASTA):
entity_1: TGKPTENNEDFNIVAVASNF
ATTDLDADRGKLPGKKLPLE
VLKEMEANARKAGCTRGCLI
CLSHIKCTPKMKKFIPGRCH
TYEGDKESAQGGIGEAIVDI
PAIPRFKDLEPMEQFIAQVD
LCVDCTTGCLKGLANVQCSD
LLKKWLPQRCATFASKIQGQ
VDKIKGAGGDIEGR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 689 |
| 15N chemical shifts | 177 |
| 1H chemical shifts | 1094 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 174 residues - 18851.838 Da.
| 1 | THR | GLY | LYS | PRO | THR | GLU | ASN | ASN | GLU | ASP | ||||
| 2 | PHE | ASN | ILE | VAL | ALA | VAL | ALA | SER | ASN | PHE | ||||
| 3 | ALA | THR | THR | ASP | LEU | ASP | ALA | ASP | ARG | GLY | ||||
| 4 | LYS | LEU | PRO | GLY | LYS | LYS | LEU | PRO | LEU | GLU | ||||
| 5 | VAL | LEU | LYS | GLU | MET | GLU | ALA | ASN | ALA | ARG | ||||
| 6 | LYS | ALA | GLY | CYS | THR | ARG | GLY | CYS | LEU | ILE | ||||
| 7 | CYS | LEU | SER | HIS | ILE | LYS | CYS | THR | PRO | LYS | ||||
| 8 | MET | LYS | LYS | PHE | ILE | PRO | GLY | ARG | CYS | HIS | ||||
| 9 | THR | TYR | GLU | GLY | ASP | LYS | GLU | SER | ALA | GLN | ||||
| 10 | GLY | GLY | ILE | GLY | GLU | ALA | ILE | VAL | ASP | ILE | ||||
| 11 | PRO | ALA | ILE | PRO | ARG | PHE | LYS | ASP | LEU | GLU | ||||
| 12 | PRO | MET | GLU | GLN | PHE | ILE | ALA | GLN | VAL | ASP | ||||
| 13 | LEU | CYS | VAL | ASP | CYS | THR | THR | GLY | CYS | LEU | ||||
| 14 | LYS | GLY | LEU | ALA | ASN | VAL | GLN | CYS | SER | ASP | ||||
| 15 | LEU | LEU | LYS | LYS | TRP | LEU | PRO | GLN | ARG | CYS | ||||
| 16 | ALA | THR | PHE | ALA | SER | LYS | ILE | GLN | GLY | GLN | ||||
| 17 | VAL | ASP | LYS | ILE | LYS | GLY | ALA | GLY | GLY | ASP | ||||
| 18 | ILE | GLU | GLY | ARG |
Samples:
sample_1: GLuc, [U-100% 13C; U-100% 15N], 0.2 mM; MES 50 mM; sodium azide 2 mM; D2O, [U-2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | 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 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.98, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation
MAGRO v2.01.33, Kobayashi - data analysis
NMRPipe v2017, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v9.0, Johnson, One Moon Scientific - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
TopSpin v3.5, Bruker Biospin - collection
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts