BMRB Entry 36243
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36243
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Mouse receptor-interacting protein kinase 3 (RIP3) amyloid structure by solid-state NMR PubMed: 33712586
Deposition date: 2019-03-26 Original release date: 2023-02-23
Authors: Wu, X.; Hu, H.; Zhang, J.; Dong, X.; Wang, J.; Schwieters, C.; Wang, H.; Lu, J.
Citation: Wu, Xia-Lian; Hu, Hong; Dong, Xing-Qi; Zhang, Jing; Wang, Jian; Schwieters, Charles; Liu, Jing; Wu, Guo-Xiang; Li, Bing; Lin, Jing-Yu; Wang, Hua-Yi; Lu, Jun-Xia. "The amyloid structure of mouse RIPK3 (receptor interacting protein kinase 3) in cell necroptosis." Nat. Commun. 12, 1627-1627 (2021).
Assembly members:
Receptor-interacting serine/threonine-protein kinase 3, polymer, 84 residues, 9454.359 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 BL21(DE3)
Entity Sequences (FASTA):
Receptor-interacting serine/threonine-protein kinase 3: HHHHHHGPHPQRNQGDGRHG
TPWYPWTPPNPMTGPPALVF
NNCSEVQIGNYNSLVAPPRT
TASSSAKYDQAQFGRGRGWQ
PFHK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 90 |
| 15N chemical shifts | 22 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, chain 1 | 1 |
| 2 | entity_1, chain 2 | 1 |
| 3 | entity_1, chain 3 | 1 |
| 4 | entity_1, chain 4 | 1 |
| 5 | entity_1, chain 5 | 1 |
Entities:
Entity 1, entity_1, chain 1 84 residues - 9454.359 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | GLY | PRO | HIS | PRO | ||||
| 2 | GLN | ARG | ASN | GLN | GLY | ASP | GLY | ARG | HIS | GLY | ||||
| 3 | THR | PRO | TRP | TYR | PRO | TRP | THR | PRO | PRO | ASN | ||||
| 4 | PRO | MET | THR | GLY | PRO | PRO | ALA | LEU | VAL | PHE | ||||
| 5 | ASN | ASN | CYS | SER | GLU | VAL | GLN | ILE | GLY | ASN | ||||
| 6 | TYR | ASN | SER | LEU | VAL | ALA | PRO | PRO | ARG | THR | ||||
| 7 | THR | ALA | SER | SER | SER | ALA | LYS | TYR | ASP | GLN | ||||
| 8 | ALA | GLN | PHE | GLY | ARG | GLY | ARG | GLY | TRP | GLN | ||||
| 9 | PRO | PHE | HIS | LYS |
Samples:
sample_1: mouse rip3 fibril, [U-99% 13C; U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%
sample_2: mouse rip3 fibril, [99% 2-13C Glycerol, U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%
sample_3: mouse rip3 fibril, [99% 1,3-13C Glycerol; U-99% 15N], 0.95 – 1.05 mg/mL; H2O 100%
sample_4: mouse rip3 fibril, [U-50% 13C; natural abundance N][natural abundance C13, U-50% N15], 0.95 – 1.05 mg/mL; H2O 100%
sample_conditions_1: ionic strength: 0 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D CC DARR | sample_1 | anisotropic | sample_conditions_1 |
| 2D NCaCX | sample_1 | anisotropic | sample_conditions_1 |
| 2D NCoCX | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | anisotropic | sample_conditions_1 |
| 2D CC DARR | sample_4 | anisotropic | sample_conditions_1 |
| 2D NC TEDOR | sample_4 | anisotropic | sample_conditions_1 |
| 2D NCoCX | sample_3 | anisotropic | sample_conditions_1 |
| 2D NCaCX | sample_3 | anisotropic | sample_conditions_1 |
| 2D CC DARR | sample_3 | anisotropic | sample_conditions_1 |
| 2D NCoCX | sample_2 | anisotropic | sample_conditions_1 |
| 2D NCaCX | sample_2 | anisotropic | sample_conditions_1 |
| 2D CC DARR | sample_2 | anisotropic | sample_conditions_1 |
| 2D NC TEDOR | sample_2 | anisotropic | sample_conditions_1 |
| 2D NC TEDOR | sample_1 | anisotropic | sample_conditions_1 |
| 2D NC TEDOR | sample_3 | anisotropic | sample_conditions_1 |
| 2D ChhC | sample_4 | anisotropic | sample_conditions_1 |
| 2D NCaCX | sample_1 | anisotropic | sample_conditions_1 |
| 2D CC DARR | sample_1 | anisotropic | sample_conditions_1 |
| 2D NCoCX | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | anisotropic | sample_conditions_1 |
Software:
Sparky, Goddard - peak picking
TopSpin, Bruker Biospin - collection
X-PLOR NIH v2.50, Schwieters, Kuszewski, Tjandra and Clore - refinement
xplor-nih v2.48, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 700 MHz
- Agilent DD2 700 MHz