BMRB Entry 25718
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25718
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Title: Regnase-1 N-terminal domain PubMed: 26927947
Deposition date: 2015-07-18 Original release date: 2016-03-14
Authors: Yokogawa, Mariko; Tsushima, Takashi; Noda, Nobuo; Kumeta, Hiroyuki; Adachi, Wakana; Enokizono, Yoshiaki; Yamashita, Kazuo; Standley, Daron; Takeuchi, Osamu; Akira, Shizuo; Inagaki, Fuyuhiko
Citation: Yokogawa, Mariko; Tsushima, Takashi; Noda, Nobuo; Kumeta, Hiroyuki; Adachi, Wakana; Enokizono, Yoshiaki; Yamashita, Kazuo; Standley, Daron; Takeuchi, Osamu; Akira, Shizuo; Inagaki, Fuyuhiko. "Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions" Sci. Rep. 6, 22324-22324 (2016).
Assembly members:
Reg1_NTD, polymer, 49 residues, 5422.245 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Reg1_NTD: GPHMTSELQMKVDFFRKLGY
SSSEIHSVLQKLGVQADTNT
VLGELVKHG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 214 |
| 15N chemical shifts | 50 |
| 1H chemical shifts | 336 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 49 residues - 5422.245 Da.
| 1 | GLY | PRO | HIS | MET | THR | SER | GLU | LEU | GLN | MET | ||||
| 2 | LYS | VAL | ASP | PHE | PHE | ARG | LYS | LEU | GLY | TYR | ||||
| 3 | SER | SER | SER | GLU | ILE | HIS | SER | VAL | LEU | GLN | ||||
| 4 | LYS | LEU | GLY | VAL | GLN | ALA | ASP | THR | ASN | THR | ||||
| 5 | VAL | LEU | GLY | GLU | LEU | VAL | LYS | HIS | GLY |
Samples:
sample_1: Reg1_NTD, [U-99% 13C; U-99% 15N], 1.1 mM; DSS 5 ug; D2O, [U-2H], 10 % v/v; HEPES 20 mM; sodium chloride 150 mM; H2O 90 % v/v
sample_conditions_1: ionic strength: 170 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)HA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR v6.1C, Varian - collection
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Olivia, Masashi Yokochi - chemical shift assignment, data analysis, peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
rnmrtk vv.3, JC Hoch and AS Sterm - processing
NMR spectrometers:
- Agilent INOVA 800 MHz
- Agilent INOVA 600 MHz
- Agilent INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts