BMRB Entry 34294
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34294
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Title: Solution structure of rat RIP2 caspase recruitment domain PubMed: 30352081
Deposition date: 2018-06-25 Original release date: 2018-10-29
Authors: Mineev, K.; Goncharuk, S.; Artemieva, L.; Arseniev, A.
Citation: Goncharuk, S.; Artemieva, L.; Tabakmakher, V.; Arseniev, A.; Mineev, K.. "CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions." PLoS ONE 13, e0206244-e0206244 (2018).
Assembly members:
entity_1, polymer, 125 residues, 14075.079 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MHHHHHHGSGSGLVPRGSGI
AQQWIQSKREAIVSQMTEAC
LNQSLDALLSRDLIMKEDYE
LISTKPTRTAKVRQLLDTSD
IQGEEFARVIVQKLKDNKQM
GLQPYPEVLLVSRTPSSNVL
QNKTL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 530 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 881 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 125 residues - 14075.079 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | GLY | SER | GLY | ||||
| 2 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | GLY | ILE | ||||
| 3 | ALA | GLN | GLN | TRP | ILE | GLN | SER | LYS | ARG | GLU | ||||
| 4 | ALA | ILE | VAL | SER | GLN | MET | THR | GLU | ALA | CYS | ||||
| 5 | LEU | ASN | GLN | SER | LEU | ASP | ALA | LEU | LEU | SER | ||||
| 6 | ARG | ASP | LEU | ILE | MET | LYS | GLU | ASP | TYR | GLU | ||||
| 7 | LEU | ILE | SER | THR | LYS | PRO | THR | ARG | THR | ALA | ||||
| 8 | LYS | VAL | ARG | GLN | LEU | LEU | ASP | THR | SER | ASP | ||||
| 9 | ILE | GLN | GLY | GLU | GLU | PHE | ALA | ARG | VAL | ILE | ||||
| 10 | VAL | GLN | LYS | LEU | LYS | ASP | ASN | LYS | GLN | MET | ||||
| 11 | GLY | LEU | GLN | PRO | TYR | PRO | GLU | VAL | LEU | LEU | ||||
| 12 | VAL | SER | ARG | THR | PRO | SER | SER | ASN | VAL | LEU | ||||
| 13 | GLN | ASN | LYS | THR | LEU |
Samples:
sample_1: CARD domain of rat RIP2, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; TCEP 1 mM; sodium azide 0.001%
sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert P. - structure calculation
CARA v1.9.4, Keller and Wuthrich - chemical shift assignment
TOPSPIN v3.2, Bruker Biospin - processing
NMR spectrometers:
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts